MOLECULES AND CHIMERIC MOLECULES THEREOF BACKGROUND OF THE INVENTION FIELD OF THE INVENTION The present invention relates generally to the fields of proteins, diagnostics, therapeutics and nutrition. More particularly, the present invention provides an isolated protein molecule in or related to the tumour necrosis factor (TNTF) superfamily such as TNF-a, Lymphotoxin-a (LT-a)r TNFRI, TNFRII, 0X40, BAFF, NGFR, Fas Ligand or chimeric molecules thereof comprising ai least a portion of the protein molecule, such as TNF-a-Fc, LT-a-Fc, TNFRJ-Fc. TNFRI]-Fc. OX40-Fc. BAFF-Fc, NGFR-Fc, Fas Ligand-Fc; wherein the protein or chimeric molecule thereof has a profile of measurable physiochemical parameters, wherein the profile is indicative of. associated with or forms the basis of one or more pharmacological traits. The present invention further contemplates the use of the isolated protein or chimeric molecule, thereof in a range of diagnostic, prophylactic, therapeutic, nutritional and/or research applications. DESCRIPTION OF THE PRIOR ART Reference tc any prior art in this specification is not, and should not be taken as an acknowledgment or any form of suggestion that this prior art form? a part of the common general Icnowiedge. The TNF' superfamily is associated with the regulation of cell growth, survival, apoptosis and necrosis, as well a? inflammatory responses. Significantly, TNF molecules have a selective cytoloxK effect on tumour cells as well as inducing apcptosis in non-cancerous cells Receptors in the TNF superfamily contain cysteine-rich repeat? in the extra-cellular domain, Members of the TNF superfamily include TNF-a, LT-a: TNFRI, TNFRH. OX40,. BAFF, NGFR and Fas Ligand. TNF-a fTNF-alpha, tumour necrosis factor ligand superfamily member 2, TNFSF2) is a 233 amino acid membrane-hound protein that forms a biologically active homotrimer. The structural:} related molecule, lymphotoxin alpha (LT-a, TNF beta, TNFSF2j is synthesised as a 205 ammo acid peptide including a 34 amino acid signal sequence that, unlike the other TNF superfamiiy ligands, directs the secretion of its mature peptide. TNF-a and LT-a mediate necrosis or apoptosis particularly in transformed cells, as well as the induction of inflammatory processes, cell proliferation, C3tokine release and activation of T and B lymphocytes. Additionally, localized, low-level expression of TNF-a and LT-a participates in tissue re-modelling and host defence responses, including the destruction virus infected cells and enhancement of antibacterial activities of granulocytes. Additionally, during embryonic development TNF-a and LT-a have been identified as a key component in the organogenesis of the peripheral lymphatic organ system, such as lymph nodes, spieer. and Fever? patches. Uncontrolled regulation of TNF-a or LT-a expression plays u major role in the development of autoimmune diseases such as rheumatoid arthritis, and inflammatory bowel diseases, such as CromT's disease and multiple sclerosis (MS). The effects of TNF-a and LT-a are mediated through the TNF receptors, tumor necrosis factor receptor 1 (TNFRI) and tumor necrosis factor receptor II (TNFRII). Both TNF receptors omc TMF-s and LT-a with high affinity and are present on virtually all cell types except for red blood cells. Deletion analysis in the C terminal intracellular region of TNFRI has revealed the existence of a death domain, which is involved in signalling processes leading to programmed cell death. The death domain of TNFRI interacts with a variety of other signalling adaptor molecules, including TRADD and RIP. TNFRII is more a bun dam on endolhelial cells and cells of hematopoietic lineage. Soluble forms of TNFRII have been characterized in human urine as 30kDa and 45kDa proteins. These soluble TNF receptor proteins exhibit TNF" inhibitor)' qualities and result from the proteolytic cleavage of the membrane bound receptor. Notably, many of the stimuli that induce expression of TNF-a also induced expression of soluble TNF receptors suggesting the soluble receptors may play a role in regulating TNF activity. In particular, TNFRJ and TNFRII may be useful for treating & disease state in a subject which is characterized by an excess of TNF-ii, for example, psonasis. Psoriasis is currently affecting approximately 2-3% of the population worldwide (Nickoloff ei al. J Clin Invest. 773:1664-1675, 2004). Not only can skin lesions be pruritic and disfiguring in psoriasis patients, 10-30% of patients can also have nail dystrophy accompanied by psoriatic arthritis. Hence, psoriasis is much more than a dermatologicai nuisance, as it interferes with many normal daily activities, such as the use of hands, walking, sleeping, and sexual activity. It is reported that at least 30% of psoriasis paiients actually contemplate suicide (Nickoloff er al, supra. 2004). Other inflammatory skin conditions characterized by an excess level of TNF-a include Behcet's disease, bullous dermatitis, eczema, fungal infection, leprosy, neutrophilic dermatitis, pitynasis macuiara (or pityriasis rosea), pityriasis nigra (or tinea nigra), pityriasis rubra pilaris. systemic lupus erythematosus, systemic vascularitis and toxic epidermal necrolysis (Evereklioglu Expert Opin Pharmacother 5(2:317-28, 2004; Lipozecic er al. Ada Dermatovenero! Croat 72(7j:35-41, 2004; Mahe el al.. Ann Dermatol Venereal J29H2): 1374-9, 2002; Tec er al.. Microbes Infect 4(11): 1193-202, 2002). In addition, an excess level of 7NF-a ma}' be induced by the use of other medications. For instance, patients using the Aldara cream (Imiquimod) may develop skin reactions including erythema, erosion, ulceration. flaking, scaling, dry/ness,, scabbing, crusting, weeping or exudating of skin. Human 0X40 (tumor necrosis factor receptor superfamily member 4, TNFSF4) is a 50 kDa transmembrane protein expressed primarily on the surface of activated CD4-r T cells. 0X40 is a co-stimulatory molecule involved in the T cell dependent immune response, namely. T cell activation and proliferation, the induction of cytokine production by effector T cells, generation of memory T cells, and arresting peripheral T cell tolerance in vivo. Expression of OX40 is induced hours or days following the initiation of a CD28 signal, h ha? been reported that the interaction of 0X40 with its ligand plays a role in the expansion of! ce.F. numbers at the heigh: of the immune response as well as the generation of memory T ceils. OX40-OX40L interactions also mediate T-cell proliferation and IL-2 production in the absence of CD28. However, activated 0X40 deficient T cells are highly susceptible to apopiosis despite having relatively normal IL-2 production, cell division and expansion. 1; has been proposed that manipulating the levels of OX40 or OX40-OX40L interaction during inflammatory responses ma)1 be therapeutically beneficial in T-cell mediated diseases especially allergic, inflammatory and autoimmune diseases. Recently, several groups have reduced clinical signs of autoimmunity in animal models by blocking the OX40-OX40-hgand interaction. BAFF (also known as tumor necrosis factor ligand superfamily member 13B, TNFSF13B) is a 285 ami no acici type II membrane glycoprotein. BAFF is expressed by B cells, T cells, dendritic cells., macrophages and neutrophils. BAFF is a B cell survival factor and specifically promotes the proliferation of activated B cells, Immunoglobulin switching to IgD" B cells, the survival of immunoglobulin secreting cells and is involved in B cell maturation. This suggests BAFF is an important mediator of the humoral immune response. Studies indicate that treatment of B cells with BAFF results in the expression of pro-survival oncogenes including Bcl-xL. Bel-2 and Mcl-1. Because BAFF is a B cell survival factor, its de-regulation can promote the survival of auto-reactive B cells and the pathogenesis of autoimmune disease. Additionally, elevated levels of BAFF have also been detected in patients with autoimmune disease, including in the joints of patients with rheumatoid arthritis fRA) and inflammatory arthritis where the synovial levels of BAFF are higher than serum levels. BAFF is useful for regulating biological processes mediated by B cells. T cells, dendritic cells, macrophages and neutrophils. in particular for activating the BAFFR e.g to increase B-lymphocyte proliferation, activation and survival. In particular. BAFT can be used as a treatment for immune deficiency, e.g. patients who have inadequate B lymphocyte proliferation, activation or survival, or who have Common Variable Immune Deficiency (CVID), or IgA deficiency. BAFF can also be used to enhance antibod) production in vaccination procedures. Additionally, BAFF linked to radionuclides can be as therapy for targetting and killing B-cell malignancies. Nerve growth factor receptor (NGFR) also is tumour necrosis factor receptor superfamily member 16 TNFRSF16. NGFR is a type 1 membrane protein that is synthesised as a 427 ammo acid giycoproteir. consisting of a 28 arnino acid signal peptide. "NGFR binds with equal affinity all neurotrophins. but higher affinity binding is achieved by association of 'NGFR with TncA, B and C. Ligand binding to the NGFR can promote either survival or apoptosis of neurons. The effects neurotrophins on cells involves a complex interplay between the "NGFR receptor and the Trk A, B and C receptors that is not completely understood, However. NGF treatment of neurons induces apoptosis, which is not seen in neurons deficient in NGFR. while Trk A predominantly inhibits NGFR apoptotic activity. A further complexity is that both the pro-apoptotic and anti-apoptotic pathways induced by NGFR signalling are dependent upon the type and functional state of the cell. There are various possible clirucal applications for NGFR in neurological disorders including Alzheimer's disease, Parkinson's disease, neuromuscular and motor neuron disorders. multiple sclerosis, cerebral palsy, diabetic neuropathies and pain management as the interaction of Trk A and NGFR on sensory neurons is involved in the development of chronic pain. A soluble NGFR can also be used to inhibit breast cancer growth and other tumours for which NGF and other NGFR ligands are mitogens. Fas Ligand (Fasl. or TNF ligand superfamily member 6, TNFSF6) is a 281 amino acid type II membrane protein, FasL also exist as a soluble protein resulting from proteolytic cleavage of the BCD or by alternative splicing. The active form of FasL is homotrimeric. FasL is involved in the regulation of programmed cell death (apoptosis), immune homeostasis and immune privilege and tumor cell survival. Initial experiments showed that activated CD4- T cells induced cytolytic activity in cells expressing Fas. FasL was subsequently cloaed and was demonstrated to induce apoptosis via interaction with Fas. This binding of FasL to its receptor Fas results in the assembly of a death inducing signalling complex (DISC) which initiates the apoptosis signalling cascade. DISC includes Fas associated death domain (FADD) proteins and recruits and activates caspases 8 and 10 which initiate the caspase cascade and the apoptotic death of the cell. FasL plays an important role in normal immune homeostasis as FasL deficient animal models develop systemic autoimmune disease. FasL has been identified as being involved in three types of apoptosis: the removal of activated T cells at the end of an immune response; the killing of virally infected or cancerous cells by cytolytic T cells or natural killer cells; and the killing of inflammatory cells by non-lymphoid cells in the eye and testis. Additionally, FasL expression car; also promote neutrophil-mediated inflammatory responses via a neutrophilic chemotactic activity. Additionally, FasL is involved in erythroid differentiation, angiogenesis e.g. in the eye and skin homeostasis and the response to cellular stress. The biological effector functions exerted by proteins via interaction with their respective binding proteins means that the TNF superfamily and its related proteins and their respective ligands or receptors may have significant potential as therapeutic agents to modulate physiological processes. However, minor changes to the molecule such as primary, secondary, tertiary or quaternary structure and co- or post-translational modification patterns can have a significant impact on the activity, secretion, antigenicty and clearance of the protein. It is possible, therefore, that the proteins can be generated with specific primary, secondary, tertiary or quaternary structure, or co- or post-translational structure or make-up that confer unique or particularly useful properties. There is consequently a need to evaluate the physiochemical properties of proteins under different conditions of production to determine whether they have useful physiochemical characteristics or other pharmacological traits. The problem to date is that production of commercially available proteins are carried out in cells derived from species that are evolutionary distant to humans, cells such as bacteria, yeast, fungi, and insect. These cells express proteins that either lack glycosylation or exhibit glycosylation repertoires that are distinct to human cells and this impacts substantially on their clinical utility. For example, proteins expressed in yeast or fungi systems such as AspergUlus possess a high density of mannose which makes the protein therapeutical useless (Herscovics etal. FASEB J 7:540-550, 1993). Even in non-human mammalian expression systems such as Chinese hamster ovary (CHO) cells, significant differences in the glycosylation patterns are documented compared with thai of human cells. For example, most mammals, including rodents, express the enzyme (a 1,3) galactotransferase, which generates Gal (ex l,3)-Gal (}3 l,4)-GlcNAc oligosaccharides on glycoproteins. However in humans, apes and Old World monkeys, the expression of this enzyme has become inactivated through a frameshift mutation in the gene, (Larsen e; al J Biol Cherrt 2(55:7055-706 3, 1990) Although most of the CHO cell lines used for recombinant protein synthesis, such as Dux-Ell, have inactivated the gene expressing (a 3,3) Galactotransferase, they still lack a functional (a 2, 6) sialyltransferase enzyme for synthesis of fa 2, 6)-linked terminal sialic acids which are present in humancells. Furthermore., the sialic acid motifs present on CHO cell expressed glycoproteins proteins are prone to degradation by a CHO cell endogenous sialidase (Gramer ei al. Biotechnology- 73(7;:692-8, 1995). As a result, proteins produced from these non-human expression systems will exhibit physiochemical and pharmacological characteristics such as half-life, antigenicky..stability and functional potency that are distinct from human cell-derived proteins, The recent advancement of stem cell technology has substantially increased the potential for utilizing stem cells in applications such as transplantation therapy, drug screening, toxicology studies and functional genomics. However, stem cells are routinely maintained in culture medium that contains non-human proteins and are therefore not suitable for clinical applications due to the possibility of contamination with non-human infectious material. Furthermore, culturing of stem cells in non-human derived media may result in the incorporation of non-human carbohydrate moieties thus compromising transplant application. (Martin et al. Nature Medicine 11 (2).'228-232, 2005). Hence, the use of specific human-derived proteins in the maintenance and/or differenttiation of stem cells will ameliorate the incorporation of xenogeneic proteins and enhance stem cell clinical utility. Accordingly, there is a need to develop proteins and their receptors which have particularly desired physiochemical and pharmacological properties for use in diagnostic, prophylactic, therapeutic and/or nutritional research applications and the present invention provides proteins belonging to the TNF superfamily and its related proteins for clinical, commercial and research applications, SUMMARY OF THE INMSNTION Throughout this specification, unless the context requires otherwise, the word "comprise", or variations such as "comprises" or "comprising", will be understood to imply the inclusion of a stated element or integer or group of elements or integers but not the exclusion of any other element or integer or group of elements or integers. Nucleotide and ammo acid sequences are referred to by a sequence identifier number (SEQ ID NO:). The SEQ ID NOs: correspond numerically to the sequence identifiers 400>1 (SEQ ID N0:l), 400>2 (SEQ ID N0:2j, etc. A summary of the sequence identifiers is provided in Table 1. A sequence listing is provided after the claims. The present invention relates generally to an isolated protein or chimeric molecule thereof in or related to the TNF superfamily comprising a profile of physiochemical parameters. wherein the profile is indicative of. associated with, or forms the basis of one or more distinctive pharmacological traits. More particularly, the present invention provides an isolated protein or chimeric molecule thereof selected from the list of TNF-a, TNF-a-Fc. LT-a, LT-a-Fc, TNFRL TNFRI-Fc, TNFRII, TNFRE-Fc, 0X40, OX40-Fc, BAFF, BAFF-Fc, NGFR. NGFR-Fc, Fas Ligand, Fas Ligand-Fc comprising a physiochemical profile comprising a number of measurable physiochemical parameters, {[Px]i. P3x]2,--.[Px]n,}J wherein Px represents a measurable physiochemical parameter and "n" is an integer >1. wherein each parameter between and including [Px]i to [Px]n is a different measurable physiochemical parameter, wherein the value of any one or more of the measurable physiochemical characteristics is indicative of, associated with, or forms the basis of, a distinctive pharmacological trait. Ty, or series of distinctive pharmacological traits {[Ty]i, [Ty]i, ....[Tyjm} wherein Ty represents a distinctive pharmacological trait and m is an integer >] and each of [T,,]; to [Ty]m is a different pharmacological trait. As used herein the term "distinctive" with regard to a phannacological trait of a protein or chimeric molecule thereof of the present invention refers to one or more pharmacological traits of a protein or chimeric molecule thereof which are distinctive for the particular physiochemical profile. In a particular embodiment, one or more of the pharmacological trails of an isolated protein or chimeric molecule thereof is different from, or distinctive relative to a form of the same protein or chimeric molecule thereof produced in a prokaryotic or lower eukaryotic cell or even a higher eukaryotic cell of a non-human species. In another embodiment, the pharmacological traits of a subject isolated protein or chimeric molecule thereof contribute to a desired functional outcome. As used herein, the term "measurable physiochemical parameters" or Px refers to one or more measurable characteristics of the isolated protein or chimeric molecule thereof. In a particular embodiment of the present invention, the measurable physiochemical parameters of a subject isolated protein or chimeric molecule thereof contribute to or are otherwise responsible for the derived pharmacological trait, Ty. An isolated protein or chimeric molecule of the present invention comprises physiochemical parameters (Px) which taken as a whole define protein molecule or chimeric molecule. The physiochemical parameters may be selected from the group consisting of apparent molecular weight (Pi), isoelectric point (pi) (P2)3 number of isoforms (Pi)., relative intensities of the different number of isoforms (?). percentage by weight carbohydrate (Pj). observed molecular weight following N-linked oligosaccharide deglycosylation (Pe)-. observed molecular weight following N-linked and O-linked oligosaccharide deglycosylation (Pi), percentage acidic monosaccharide content (P8), monosaccharide content (P?), sialic acid content (Pjo).- sulfate and phosphate content (Pn), Ser/Thr: GalNAc ratio (Pn): neutral percentage of N-linked oligosaccharide content (Pn), acidic percentage of N-linked oligosaccharide content (Pi 4), neutral percentage of O-linked oligosaccharide content (P), acidic percentage of O-linked oligosaccharide content (Pie), ratio of N-linked oiigosaccharides (Pn). ratio of O-linked oligosaccharides (Pig), structure of N-linked oligosaccharide fraction (Pig), structure of O-linked oligosaccharide fraction (P2o); position and make up of N-linked oligosaccharides (PiiX position and make up of O-linked oligosaccharides 22), co-translational modification (Pza), post-translational modification (PjO. acylation (P), acetylation (Pze), amidation (Pv). deamidation (Pis), biotinyiation OVX carbamylation or carbamoylation (Pao), carboxylation (Psi), decarboxylatior. (Piz)> disulfide bond formation (Pss), fatty acid acylation (P~), myristoylation (Pss), palmitoylation (Pse), stearoylation (Pa?), formylation (Pse), glycation (T39J. glycosylation (P4o). glycophosphatidylinositol anchor (P;), hydroxyiation (P), incorporation of selenocysieine (P), lipidation (P40, lipoic acid addition (P«). methyiation (P4&). N- or C-termina! blocking (P), N~ or C-terminal removal CP4g), nitration (P«j, oxidation of methionine (P50), phosphorylation (P51), proteolytic cleavage (P52), prenylation (P5j): famesylation (P5i), geranyi geranylation (P55), pyridoxal phosphate addition (P56).. siaiylation (P57), desialylation (PSK), sulfation (Pss), ubiquitinylation or ubiquitination (P), addition of ubiquitin-like molecules (Pei), primary structure (Fez), secondary structure (P), tertiary structure (P64), quaternary structure (Pes), chemical stability (P66), thermal stability (Pev). A list of these parameters is summarized in Table 2. In an embodiment, a TNF-a of the present invention is characterized by a profile of one or more of the following physiochemical parameters (Px) and pharmacological traits (Ty) comprising: an apparent molecular weight (Pi) of about 1 to 250, such as ], 2, 3, 4, 5, 6, 7, 8, 9, 10.. 11, 12, 13. 14, 15, 16, 17,18,19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 32, 32, 33.. 34: 35, 36, 37, 38, 39, 40.. 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57; 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70; 71, 72, 73, 74, 75, 76, 77, 78, 79,, 80, 81.. 82. 83, 84, 85, 86, 87.. 88, 89, 90, 91, 92.. 93, 94, 95, 96, 97, 98, 99, 100, 110, 120, 130, 140, 150, 160, 170,. 180,190, 200, 210, 220, 230, 240, 250 kDa and in one embodiment, 10-30 kDa; a pi (P2) range of about 2 to 14 such as 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14 and in one embodiment, 4-8.5; about 2 to 50 isoforms (P3), such as2; 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18,19. 20; 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 33, 32, 33, 34, 35, 36, 37, 385 39, 40, 41, 42, 43, 44, 45; 46, 47, 48, 49, 50 isoforms and in one embodiment, 10-40 isoforms; a percentage by weight carbohydrate (Ps) of about 1 to 99%, such as 1,2, 3, 4, 5, 6, 7,8,9, 10.. 11, 12, 13,. 14, 15, 16, 17, 18, 19,20,21,22,23,24,25,26,27,28, 29, 30, 3], 32, 33, 34, 35, 36, 37, 38, 39, 40, 41.. 42, 43, 44.. 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66,. 67, 68, 69, 70, 71., 72, 73, 74, 75, 76, 77. ?8, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93; 94, 95, 96, 97, 98, 99 and in one embodiment, 0-10%;an observed molecular weigh! of the mcule after the N-linked oligosaccharides are removed (T't) of about 8 to 30 kDa; an observed molecular weight of the molecule after the N-linked and O-linked oligosaccharides are removed (Pi') of about 8 to 25 kDa, and in one embodiment, 3 0 to 20 kDa; an imrnunoreactivity profile (In) that is distinct from that of a human TNF-a expressed ir, a non-human cell system, and in one embodiment, the protein concentration of the TNF-a of the present invention is underestimated when assayed using an EL1SA kit which contains a human TNF-a expressed in a non-human cell system. in an embodiment, a LT-a of the present invention is characterized by a profile of one or more of the following physiochemical parameters (Px) and pharmacological traits (Ty) comprising: an apparent molecular weight (Pi) of about 1 to 250, such as 1, 2, 3, 4, 5. 6, 7, 8, 9, 10,11, 12, !3. 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28., 29, 30, 31,32, 33, 34, 35, 36. 37. 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, SI, 82, 83, 84, 85, 86, 87, 88, 89, 90; 91, 92, 93, 94, 95, 96: 97, 98, 99, 100, 110, 120, 130,, 140, 150, 160, 370, 180, 190, 200, 210, 220, 230, 240, 250 kDa and in one embodiment. 15 to 32 kDa; a pi (P2) range of about 2 to 14 such as 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14 and in one embodiment 5 to 11; about 2 to 100 isoforms (P3); such as 2, 3, 4, 5, 6, 7, 8, 9, 10, 11,12, 13, 14, 15, 16, 17,18, 19, 20, 23, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 83, 82, 83, 84, 85: 86, 87. 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100 isoforms and in one embodiment 7-33 isoforms; a percentage by weight carbohydrate (P5) of about 0 to 99% such as 0, 1, 2, 3, 4, 5, 6, 7,8,9,10,31,12, 13,14, 15, 16,17, 18,19,20,21,22,23,24,25,26,27,28,29,30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 13 54, 55; 56, 51, 58, 59, 60, 61. 62, 63.. 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 7?.. 78, 79, 80, 81. 82, 83; 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99% and ir. one embodiment 0 to 42%: an observed molecular weighi of the molecule after the N-linked oligosaccharides are removed (?(,) of about 10 to 30 kDa and in one embodiment, 12 to 25 kDa; an observed molecular weight of the molecule after the N-linked and O-linked oligosaccharides are removed (P?) of about 10 to 25 kDa and in one embodiment, 12 to 23 kDa; an immunoreactivity profile (Tn) that is distinct from that of a human LT-a expressed ir. a non-human eel] system, and in one embodiment, the protein concentration of the LT-a of the present invention is underestimated when assayed using an ELISA kit which contains a human LT-a expressed in a non-human cell system. In an embodiment, a TNFRI-Fc of the present invention is characterized by a profile of one or more of the following physiochemica) parameters (Px) and pharmacological traits (Ty) comprising: an apparent molecular weight (Pi) of about 5 to 120 kD such as 5, 6, 7, 8. 9. 10, 11. 12, 13, 14, 15, 16, 17, 18, 19,20,21,22,23,24,25,26,27,28,29,30, 31,32,33, 34, 35, 36, 37, 38. 39, 40, 41, 42, 43, 44: 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58. 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82. 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105r 106, 107, 108, 109. 110, 113, 112, 113, 114, 115, 116, 117, 118, 119, 120 and in one embodiment, 45-75kDa; a pi (PV) range of about 2 to about 12 such as 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12 and in one embodiment. 5.5-9.5; about 2 to about 20 isoforms (P3) such as 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18. 19, 20 isoforms, and in one embodiment, 8-16 isoforms; a percentage by weight carbohydrate (Pj) of about 10-90%. such as 10, 11, 12, 13, 14, ]5: ]6, 17, 18. 19,20,21,22,23,24,25,26,27,28,29,30,31,32,33, 34, 35,36, 37, 38, 39; 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60; 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83. 84, 85, 86, 87, 88, 89, 90% and in one embodiment, 0-36%; an observed molecular weight of the molecule after the N-linked oligosaccharides are removed (T) of about 35 to 65 kDa and in one embodiment, 36 to 60 kDa; an observed molecular weight of the molecule after the N-linked and O-linked oligosaccharides are removed (P-?) of about 35 to 65 kDa and in one embodiment, 36 to 60 kDa: a percentage acidic monosaccharide content (Pg) of about 0-50%, such as 0,1, 2, 3, 4, 5,6,7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20,21,22, 23,24,25,26,27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, and in one embodiment, 0-10%; monosaccharide (Pg) and sialic acid (Pio) contents of, when normalized to GalNAc: 1 to 0.1-8 fucose, 1 to 7-27 GlcNAc, 1 to 1-14 galactose, 1 to 2-17 marmose and 1 to 0-3 NeuNAc, and in one embodiment, 1 to 1-4.5 fucose, 1 to 10-18 GlcNAc, 1 to 3-9 galactose. 1 to 4-11 mannose and 1 to 0.1-2 NeuNAc; when normalized to 3 times of mannose: 3 to 0.01-3 fucose, 3 to 0.01-3 GalNAc, 3 to 1-17 GlcNAc, 3 to 0.1-5 galactose and 3 to 0-3 NeuNAc, and in one embodiment, 3 to 0.1-1.5 fucose, 3 to 0.1- 1 GalNAc, 3 to 3-11 GlcNAc, 3 to 1-2.5 galactose and 3 to 0-2 NeuNAc; sulfate content (Pn) of, when normalized to GalNac: 1 to 0.1-21 sulfate and in one embodiment. 1 to 1.5-14 sulfate; when normalized to 3 times of mannose: 3 to 0.1-6 sulfate, and in one embodiment, 3 to 0.5-4 sulfate; sulfation (Pss) expressed as a percentage of the monosaccharide content of the molecule of 0-50%, such as 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26: 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41. 42, 43, 44,45, 46, 47, 48,49, 50, and in one embodiment, 10-16 %; a neutral percentage of N-linked oligosaccharides (P) of about 30 to 100% such as 30, 31, 32. 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55. 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76,77,78.79,80, 81,82,83,84, 85, 86, 87,88, 89,90,91,92,93,94,95, 96,97,98, 99, 100%, and in one embodiment, 80 to 100%, and a further embodiment, 94 to 97%: an acidic percentage of"N-linked oligosaccharides (Pm) of about 0 to 50% such as 0, ],2: 3, 4, 5, 6. 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 3D, 31, 32, 33, 34, 35, 36, 37, 38., 39, 40, 41, 42, 43, 445 45, 46, 47, 48, 49, 50%. and in one embodiment 0 to 20% , and a further embodiment, 3 to 6%; a neutral percentage of O-linked oligosaccharides (Pis) of about 24 to 67% such as 24, 25, 26, 27; 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 495 50, 51, 52, 53, 54, 55, 56, 57: 58, 59, 60, 61, 62, 63, 64, 65, 66, 67%, and in one embodiment, 29 to 62% , and a further embodiment, 34 to 57%; an acidic percentage of O-linked oligosaccharides (Pit) of about 10 to 80% such as 10, 13, 12, 13, 14, 15, 16, 17, 18, 19,20,21,22,23,24,25,26,27,28, 29., 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56. 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, ">9, 80% and in one embodiment, 38 and 71%, and a further embodiment, 43 to 66% £ site of N-glycosylation (Pzi) including N-299 (numbering from the start of the signal sequence) identified by PMF after PNGase treatment. In an embodiment, a TNFRII-Fc of the present invention is characterized by a profile of one or more of the following physio chemical parameters (Px) and pharmacological traits (Tyj comprising: an apparent molecular weight (P;) of about 10 to 150. such as 10, 11, 12. 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29,30, 33, 32, 33, 34, 35, 36, 37, 38, 39, 40: 43, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64; 65, 66, 67, 68, 69, 70, 73, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85,86,87,88,89,90,91,92,93,94,95,96,97,98,99,100, 110, 120,130, 340, 150, and in one embodiment, 46 to 118 kDa; a pi (P2) range of about 2 to 34, such as 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 34 and in one embodiment, 4 to 1 0; about 2 lo 52 isoforms (P3) such as 2, 3, 4, 5,6,7, 8,9, 30, 11, 12, 13, 34, 15, 36, 17, 38, 19, 20, 21, 22: 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 4), 42; 43, 44, 45.. 46, 47, 48.. 49, 50, 5 3, 52 and in one embodiment 10-40 isoforms; £ percentage by weight carbohydrate CP5) of about 0 to 99%, such as 0, 1, 2, 3, 4, 5, 6,7.8,9,10. 11,12,13, 14, 15,16,17, 18, 19, 20,21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34. 35: 36, 37, 38, 39,. 40: 41, 42.. 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53. 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64,. 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77. 78, 79, 80, 81, 82, 83, 84, 85. 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99% and in one embodiment, 0 to 56%; an observed molecular weight of the molecule after the N-linked oligosaccharides are removed (Ptj of about 40 to 100 kDa and in one embodiment, 46 to 87 kDa; an observed molecular weight of the molecule after the N-linked and O-linked oligosaccharides are removed (P?) of about 40 to 95 kDa and in one embodiment, 42 to 80 kDa; a percentage acidic rnonosaccharide content (Pg) of about 0 to 50%, such as 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32; 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, and in one embodiment, 1 to 10 %; monosacchande (P$) and sialic acid (Pjo) contents of, when normalized to GalNAc: 1 to 0.01-3 fucose, 1 to 0.1-5 GlcNAc, 1 to 0.1-3 galactose, 1 to 0.1-3 mannose and 1 to 0.01-3 NeuNAc; and in one embodiment, 3 to 0.01-2 fucose, 1 to 0.1-3 GlcNAc. 1 to 0.1-2 galactose, 1 to 0.1-2 mannose and 1 to 0.01-2 NeuNAc; when normalized to 3 times of mannose: 3 to 0.01-3 fucose, 3 to 1-17- GalNAc, 3 to 2-32 GlcNAc, 3 to 1-9 galactose and 3 to 0.1-3 NeuNAc and in one embodiment, 3 to 0.1-2 fucose, 3 to 3-11 GalNAc, 3 to 5-21 GlcNAc, 3 to 3-6 galactose and 3 to 0.1-2 NeuNAc; sulfate content (Pa) of, when normalized to GalNAc: 1 to 0.1-6 sulfate and in one embodiment, 1 to 1-4 sulfate; when normalized to 3 times of mannose: 3 to 4-29 sulfate and in one embodiment, 3 to 9-19 sulfate; sulfation (?5o) expressed as a percentage of the monosaccharide content of the molecule of 10 to 90%, such as 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26. 27, 28, 29, 30, 31, 32, 33, 34: 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49. 50, 51, 52, 53, 54; 55, 56, 57, 58, 59, 60, 61, 62, 63.. 64, 65: 66, 67, 68, 69, 70, 7K 72. 73, 74, "5, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90%, and in one embodiment 27 to 41%: a neutral percentage of N-linked oligosaccharides (P!3) of about 10 to 100%. such as 10,11,12,13,14. 15J6, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27., 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44: AS, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58. 59; 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74: 75, 76, 77, 78, 79, 80. 81.. 82. 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, and in one embodiment, 69 to 89% and a further embodiment, 74 to 84%; an acidic percentage of N-linked oligosaccharides (PM) of about 0 to 80%, such as 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 30, 1 1, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55. 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75. 76, 77, 78, 79, 80 and in one embodiment, 11 to 31% and a further embodiment, 1 6 to 26%; a neutra] percentage of 0-linked oligosaccharides (P) of about 5 to 90%, such as 5, 6,7,8,9, 10, 11. 12, 13, 14, 15, 16, 17, 18, 19,20,21,22,23, 24,25,26,27, 28,29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56: 57, 58, 59, 60, 61.. 62, 63.. 64, 65; 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78. 79, 80, 81., 82, 83, 84, 85, 86, 87, 88; 89, 90, and in one embodiment, 17 to 54% and a further embodiment 22 to 49%; an acidic percentage of 0-linked oligosaccharides (Pj of about 5 to 99%, such as 5, 6,7,8.9, 10. 13, 12, 13, 14, 15, 16, 17, 18,19,20,21,22,23,24,25,26,27,28,29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52; 53, 54. 55., 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73: 74, 75, 76, 77, 78. 79, 80, 81, 82, 83, 84, 85, 86, 87: 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, and in one embodiment, 46 to 83% and a further embodiment, 51 to 78%; one or more N-glycan structures as listed in Table 37(a) in the N-linked fraction (Pie); one or more 0-glycan structures as listed in Table 37(b) in the O-linked fraction a biological activity that is distinct from that of a human TNFRII-Fc expressed in a non-humajj cell system, and in one embodiment, the ability of TNFRII-Fc of the present invention to neutralise TNF-a induced cytotoxiciry (Tao) in L-929 cells is 8-1 8 fold more potent than a human TNFRII-Fc expressed in E. coll ceils. In an embodiment, an OX40-Fc of the present invention is characterized by a profile of one or more of the following physiochemical parameters (Px) and pharmacological traits (Ty) comprising: an apparent molecular weight (Pi) of about 1 to 250, such as 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12.13,14. 15,16,17,18, 19, 20, 21, 22, 23,24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56; 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77S 78, 79, 80, 81, 82, 83, 84: 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 110, 120, 130.. 140, 150, 160, 170, 180, 190, 200; 210, 220, 230, 240, 250 kDa and in one embodiment, 46 to 75 kDa; a pi (P2) range of about 2 to 14 such as 2, 3, 4, 5, 6, 75 8. 9, 1D, 11, 12, 13,14 and in one embodiment. 4 to 9; about 2 to 50 isoforms (P3), such as 2, 3; 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21. 22, 23, 24,25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41. 42, 43, 44, 45, 46, 47. 48, 49, 50 isoforms and in one embodiment 8-16 isoforms; a percentage by weight carbohydrate (P5) of about 0 to 99% such as 0, 1, 2, 3; 4, 5, 6, 7,8,9, 10, 1L 12, 13, 14, 15, 16, 17, 18, 19,20,21,22,23,24,25,26,27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56,57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73; 74, 75, 76, 77, 78, 79, 80, 8L 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99% and in one embodiment 0 tc 36%; an observed molecular weight of the molecule after the N-linked oligosaccharides are removed (?(,) of about 40 to 75 kDa, and in one embodiment, 44 to 72 kDa: an observed molecular weight of the molecule after the N-linked and O-linked oligosaccharides are removed (P7) of about 38 to 75 kDa, and in one embodiment, 41 to 70 kDa; an observed molecular weight of the molecule after the N-linked oligosaccharides are removed (Ptj of about 46 to 65 kDa: an observed molecular weight of the molecule after the N-linked and O-linked oligosaccharides are removed (P?) of about 46 to 65 kDa; monosacchande (P9) and sialic acid contents (Pio) of, when normalized to Gal'NAc: 1 tc 0.01-3 fucose, 1 to 1-4 GlcNAc, 1 to 0.1-3 galactose. 1 to 0.1-3 mannose and 1 to 0-3 NeuNAc, and in one embodiment, 1 to 0.1-1 fucose, 1 to 2-3 GlcNAc. 1 to 0.5-2 galactose, 1 to 0.5-1 mannose and 1 to 0-2 NeuNAc; when normalized to 3 times of mannose: 3 to 0.1-3 fucose, 3 to 1-7 GalNAc, 3 to 3-15 GlcNAc, 3 to 2-9 galactose and 3 to 0-3 NeuNAc, and in one embodiment, 3 to 0.5-2 fucose, 3 to 3-5 GalNAc, 3 to 6-10 GlcNAc, 3 to 4-5 galactose and 3 to 0-2 NeuNAc; a sialic acid content (Pjo) expressed as a percentage of the monosacchande content of the molecule of about 0 to 50%, such as 0, 1, 2, 3, 43 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40,41. 42, 43, 44, 45, 46, 47, 48, 49, 50% and in one embodiment 0-10%; a sulfate content (Pn) of, when normalized to GalNAc: is 1 to 0-3 sulfate and in one embodiment. 1 to 0.30-2 sulfate; when normalized to 3 times of mannose; 3 to 0.1-7 sulfate and m a further embodiment is 3 to 1-5 sulfate; sulfation (Psti) expressed as a percentage of the monosaccharide content of the molecule is 0-50% such as 0, 1,2. 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17,18, 19, 20, 21. 22, 23. 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44r 45; 46, 47; 48., 49, 50 and in one embodiment 9 to 15 %; a neutral percentage of N-linked oligosaccharides (Pi3) of about 69 to 100%, and in one embodiment, 74 to 100% and in a further embodiment, 79 to 95 %; an acidic percentage of N-linked oligosaccharides (P) of about 0 to 31%, and in one embodiment 0 to 26%. and a further embodiment, 5 to 21 %; a neutral percentage of O-linked oligosaccharides (Pis) of about 20 to 100%, hi one embodiment 40 to 90% and a further embodiment, 45 to 80%; an acidic percentage of 0-linlced oligosaccharides (Pie) of about 0 to 80%, in one embodiment 10 to 60% and a further embodiment, 20 to 55%; sites of N-glycosylation (Pii) including N-160 and N-298 (numbering from the start of the signal sequence) identified by PMF after PNGase treatment. In an embodiment, a BAFF of the present invention is characterized by a profile of one or more of the following physiochemical parameters (Px) and pharmacological traits (Ty) comprising: an apparent molecular weight (Pi) of about 1 to 250. such as ], 2, 3, 4. 5, 6, 7, S, 9, 10.11,12,13,34, 15, 16, 17, 18, 19,20,21,22,23,24,25,26,27,28,29,30,31,32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45. 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56., 57. 58. 59. 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79. 80, 81. 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 110. 120, 130, 140, 150, 160, 170, 180.. 190. 200, 210, 220, 230, 240, 250 kDa and in one embodiment 10 to 22 kDa; a pi (P;) range of about 2 to 14 such as 2. 3, 4, 5S 6, 7, 8, 9, 10, 11, 12, 13, 14 and in one embodiment 4 to 8; about 2 to 50 isoforms (P3)., such as 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 39, 20, 21, 22, 23, 24,25, 26, 27, 28, 29, 30, 31, 32, 335 34, 35, 36, 37, 38': 39, 40, 41, 42, 43. 44, 45, 46, 47, 48, 49, 50 isoforms and in one embodiment 5 to 10 isoforms; a percentage by weight carbohydrate (P;.) of about 0 to 99%, such as 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11. 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33. 34, 35, 36, 37, 38. 39, 40.. 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56. 57, 58, 59, 60, 61, 62, 63, 64: 65, 66, 67, 68, 695 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84: 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99% and in one embodiment 0 to 25%; ac observed molecular weight of the molecule after the N-linked oligosaccharides are removed (P61 of about 8 to 22 kDa, and in one embodiment, 10 to 22 kDa; an observed molecular weight of the molecule after the N-linked and O-linked oligosaccharides are removed (P?) of about 8 to 22 kDa, and in one embodiment, 10 to 22 kDa; E biological activity that is distinct from that of a human BAFF expressed in a non-human cell system, and in one embodiment, the ability of BAPF of the present invention to induce proliferation (Tii) in RPMI 8226 cells is 1.1-2.4 fold more potent than a human BAFF expressed in E. coll cells. In an embodimen;. a NGFR-Fc of the present invention is characterized by a profile of one or more of the following physiochemical parameters (Px) and pharmacological traits (Ty) comprising: an apparent molecular weight (Pi) of about ] to 250, such as I, 2, 3, 4, 5, 6, 7, S: 9, 10, 1L 12,13. 14,15, 16,17, 18, 19,20,21,22,23,24,25,26,27,28,29,30,31,32, 33. 34. 35, 36. 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59. 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 110, 120; 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230., 240, 250 kDa and in one embodiment 55 to 105 kDa; a pi (P2) range of about 2 to 14 such as 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, and in one embodiment, 3 to 6; about 2 to 50 (?3j, such as 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25., 26,27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45. 46, 47, 48, 49, 50 isoforms and in one embodiment 8 to 16 isoforms; a percentage by weight carbohydrate (Ps) of about 0 to 99% such as 0, 1, 2, 35 4, 5, 6, 7,8,9, 10, li.12, 13, 14,15,16,17, 18, 19,20,21,22,23,24,25,26,27,28,29,30, 31, 32, 33, 34: 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 5". 58. 59. 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 7g: 79r g(j, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99% and in one embodiment 11 to 53%; an observed molecular weight of the molecule following removal of N-linked oligosaccharides (Pe) of between 45 and 100 kDa, and in one embodiment, 48 to 90 kDa; an observed molecular weight of the molecule after the N-linked and 0-linked oligosaccharides are removed (P?) of about 45 to 95 kDa, and in one embodiment, 48 ic 85 kDa, In an embodiment, a Fas Ligand of the present invention is characterized by a profile of one or more of the following physiochemical parameters (Px) and pharmacological traits (Tj comprising: an apparent molecular weight (Pi) of about 1 to 250, such as 1. 2. 3, 4, 5, 6, 7, 8, 9, 10,11, 12. 13: 14, 15, 16, 17,. 18, 19,20,21,22,23,24,25,26,27,28,29,30,31,32, 33, 34, 35, 36. 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83. 84, 85., 86, 87, 88. 89, 90, 91, 92, 93, 94, 95, 96, 91, 98, 99, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, 200,210, 220, 230,240, 250 kDa and in one embodiment 15 to 35 kDa, a pi (P2) range of about 2 to 14 such as 2, 3,4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14; about 2 to 50 isoforms (P3), such as 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19: 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37; 38, 39, 40, 41, 42; 43, 44, 45, 46; 47, 48, 49, 50 isoforms; a percentage by weight carbohydrate (Ps) of about 0 to 99% such as 0. 1, 2, 3, 4, 5, 6, 7, 8,9. 10, :1, 12, 13,. 14, 15, 16, 17, 18, 19,20,21,22,23,24,25,26,27,28,29,30, 31,32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73; 74, 75, 76, 77, 78, 79, 80, 81, 82, 83: 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97; 983 99% and in one embodiment 0 to 51% an observed molecular weight of the molecule following removal of N-linked oligosaccharides (Pe) of between 10 and 28 kDa, and in one embodiment, 12 to 21 kDa: a site of N-glycosylation (Pai) including N-184 (numbering from the start of the signal sequence) identified by PMF after PNGase treatment. In a particular embodiment, the present invention contemplates an isolated form of protein or chimeric molecule thereof in or related to the TNF superfamily selected from the group comprising TNF-a, TNF-a-Fc, LT-a, LT-a-Fc, TNFRI, TNFRI-Fc, TNFRII, TNFRII-Fc, 0X40, OX40-P c, BAFF, BAFF-Fc, NGFR, NGFR-Fc; Fas Ligand, Fas Ligand-Fc. An isolated protein or chimeric molecule of the present invention comprises distinctive pharmacological traits selected from the group comprising or consisting of therapeutic efficiency (!]), effective therapeutic dose (TCIDso) (2), bioavailability (Ta), time between dosages tc maintain therapeutic levels (14), rate of absorption (T5). rate of excretion (T), specific activity fT-}5 thermal stability (Tj), lyophilization stability (T9); serum/plasma stability (Tic), serum half-life (Tn), solubility in blood stream (Tu), immunoreactivity profile (T-.3J, immunogenicity (Tn), inhibition by neutralizing antibodies (TKA). side effects (Tj;), receptor/ligand binding affinity (Tie), receptor/liganc activation (T), tissue or cell n-pe specificity (Tjs), ability to cross biological membranes or barriers (i.e. gut long, blood brain barriers, sicin etc) (Ti9)5 angiogenic ability (Ti9A), tissue uptake (T2o), stability to degradation (T2)j. stabilit}' to freeze-thaw (T2z), stability to proteases (723), stability to ubiquitination (T24), ease of administration (T2s)= mode of administration (T26), compatibility with other pharmaceutical excipients or carriers (Ta?). persistence in organism or environment fg), stability' in storage (Tg), toxicity in an organism or environment and the like In addition, the protein or chimeric molecule of the present invention may have altered biological effects on different cells types (Tai). including without being limited to human primary cells, such as lymphocytes, erythrocytes, retinal cells, hepatocytes, neurons. keratinocytes, endothelial cells, endodermal cells, ectodermal cells, mesodennal cells, epithelial cells, kidney cells, liver cells, bone cells, bone marrow cells, lymph node cells, dermal cells, fibroblasts. T-cells, B-cells, plasma cells, natural killer cells, macrophages, granulocytes, neutrophils, Langerhans cells, dendritic cells, eosinophils, basophils, mammary cells, lobule cells, prostate cells, lung cells, oesophageal cells, pancreatic cells, Beta cells (insulin secreting cells), hemangioblasts, muscle cells, oval cells (hepatocytes), mesenchymal cells, brain microvessel endothelial cells, astrocytes, glial cells, various stem cells including adult and embryonic stem cells, various progenitor cells; and other human immortal, transformed or cancer cell lines. The biological effects on the cells include effects on proliferation (Tss), differentiation (133), apoptosis (T3i), growth in cell size (T35). cytokine adhesion (T), cell adhesion (737), cell spreading (738), cell motiliry (T39), migration and invasion (740), chemotaxis (7i). eel! engulfinent (T«). signal transduction (743), recruitment of proteins to receptors/ligands (744), activation of the JAK/S7A7 pathway (7), activation of the Ras-erk pathway (746), actJ\'ation of the AK7 pathway (74?), activation of the PKC pathway (74s), activation of the PKA pathway (749), activation of src (Tso), activation of fas (75]), activation of 7NFR (752), activation of NFkB (TSi), activation of p38MAPK (T54), activation of ofos (75i). secretion (756), receptor internalization (77), receptor cross-taljc (7ji,0; up or down regulation of surface markers (759). alteration of FACS front/side scatter profiles (76e), alteration of subgroup ratios (TeO, differential gene expression (762), cell necrosis (7fc3), cell clumping (76); cell repulsion (765), binding to heparin sulfates (766),binding ic glycosyiatec structures (T67j, binding to chondroitin sulfates (Tfis), binding to extracellular matrix (such as collagen, fibronectin) (T69)> binding to artificial materials (.such as scaffolds) (T70), binding to carriers (T7]); binding to co-factors (Tn) the effect alone or in combination with other proteins on stem cell proliferation, differentiation and/or self-renewai (Tr) and the like. These are summarized in Table 3. The present invention further provides a chimeric molecule comprising an isolated protein or a fragment thereof, such as an extra-cellular domain of a membrane bound protein, linked to the constant (Fc) or framework region of a human immunogiobulin via one or more protein linker. Such a chimeric molecule is also referred to herein as protein-Fc. Examples of such protein-Fc contemplated by the present invention include TNF-a-Fc, LT-a-Fc, TNFRl-Fc: TNFRH-Fc, OX40-Fc, BAFF-Fc, NGFR-Fc, Fas Ligand-Fc. .Such protein-Fc has fc profile of measurable physiochemical parameters indicative of or associated with one or more distinctive pharmacological traits of the isolated protein-Fc. Other chimeric molecules contemplated by the present invention include the protein or protein-Fc or a fragment thereof, linked to a lipid moiety such as a polyunsaturated fatty acid molecule. Such lipid moieties may be linked to an amino acid residue in the backbone of the moiecule or to a side chain of such an amino acid residue. The present invention further provides a chimeric molecule comprising an isolated protein or a fragment thereof, such as an extra-cellular domain of a membrane bound protein, linked to the constant (Fc) or framework region of a mammalian immunogiobulin via one or more protein linker. In another aspect, the mammal Fc or framework region of the immunogiobulin is derived from a mammal selected from the group consisting of primates, including humans, marmosetSj orangutans and gorillas, livestock animals (e.g. cows, sheep, pigs, horses, donkeys), laboratory test animals (e.g. mice, rats, guinea pigs, hamsters, rabbits, companion animals (e.g. cats, dogs) and captured wild animals (e.g. rodents, foxes, deer, kangaroos). In another embodiment the Fc or framework region is a human immunogiobulin. In a particular embodiment the mammal is a human. Such a chimeric molecule is also referred to herein as protein-Fc. Other chimeric molecules contemplated by the present invention include the protein or protein-Fc or a fragment thereof linked ic a iipid moiety such as a polyunsaturated fatty acid molecule. Such lipidmoieties may be linked to an amino acid residue in the background of the molecule or to a side chain of such an amino acid residue. The chimeric molecules of the present invention, including TNF-a-Fc, LT-a-Fc, TNFRJ-Fc; TNFRII-Fc; OX40-Fc: BAFF-Fc, NGFR-Fc, Fas Ligand-Fc have a profile of measurable physiochemical parameters indicative of or associated with one or more distinctive pharmacological traits of the isolated protein-Fc. In particular, as used herein the terms "TNKRI-Fc" and "TNFRII-Fc" refer to the fusion of a fragment of the TNFR poiypeptide (e.g. TNFRI or TNFRII) comprising one or more extracellular domains of TNFRI or TNFRII. linked directly or via one or more protein linkers known in the an to a constant (Fc) or framework region of an imm-uno globulin or a fragment thereof to form a chimeric protein. The fragment of the TNFR (TNFRI or TNFRIT) poiypeptide may be selected from one or more of SEQ ID NOs: 64, 66, 68, 92, 94, 96. 98. The Fc region may be selected from the Fc region of the human isotypes of IgGi (for example, as substantial!)' set forth in SEQ ID N0;2, SEQ ID NO:4), IgG2 (for example, as substantially set forth in SEQ ID NO:6) IgG3 (for example, as substantially set forth in SEQ ID NO:S); lgG4 (for example, as substantially set forth in SEQ ID NO: 10), IgAl (for example, as substantially set forth in SEQ ID NO: 12), IgA2 (for example, as substantial!}1 set forth in SEQ ID NO: 14), IgM (for example, as substantially set forth in SEQ ID NO: 16), IgE (for example, as substantially set forth in SEQ ID NO: 18) or IgD (for example, as substantially set forth in SEQ ID NO: 20), In particular embodiment, the Fc receptor binding region or the complement activating region of the Fc region may be modified recombinantly. comprising one or more amino acid insertions, deletions or substitutions relative to the amino acid sequence of the Fc region. In addition, the receptor binding region or the complement activating region of the Fc region may be modified chemically by changes to its glycosylation pattern, the addition or removal of carbohydrate moieties, the addition of polyunsaturated fatty acid moieties or other lipid based moieties to the amino acid backbone or to any associated co- or post-translational entities. The Fc region may also be in a truncated form, resulting from the cleavage by an enzyme including papam, pepsin or any other site-specific proteases. The Fc region may promote the spontaneous formation by the chimeric protein of a dimer, trimer or higher order multimer that is better capable of binding a TNF-a molecule and preventing it from binding to cell-bound receptors than the equivalent monomer. Therefore, the "TNFRI-Fc Jypeptide'' and "TMFRIl-Fc poJypeptide" contemplated by the present invention are antagonists of TNF-a activity. As used herein, "TNF" includes reference to TNF-a. Accordingly, the present invention provides an isolated polypeptide encoded by a nucieotide sequence selected from the list consisting of SEQ ID NOs: 27, 29, 31, 33, 35, 37, 39, 43. 45, 47, 49, 51, 53, 55.. 59, 61, 63, 65: 61, 69, 71, 73, 75, 77, 79, 81, 83, 85, 89, 91, 93, 95,. 91, 99: 101, 103, 105, 107, 109, 311, 113, 115, 117, 119, 121, 327, 129, 131, 133, 135, 137. 139. 141, 143, 147, 149, 151, 153, 155, 157, 159, 163, 165, 167, 169, 171, 173, 175, i 77, 179. 183, 185, 187, 189, or a nucieotide sequence having at least about 65% identity to any one of the above-listed sequence or a nucieotide sequence capable of hybridizing to any one of the above sequences or their complementary forms under low stringency conditions. Another aspect of the present invention provides an isolated polypeptide encoded by a nucieotide sequence selected from the list consisting of SEQ ID NOs: 191, 192, 193 following splicing of their respective mRNA species by cellular processes. Yet another aspect of the present invention provides an isolated polypeptide comprising an amino acid sequence selected from the list consisting of SEQ ID NOs: 28, 30, 32, 34, 36, 38,, 40, 44, 46, 48, 50, 52, 54: 56, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 90, 92,94,96,98, 100, 102, 104, 106, 108, 110, 112, 114, 116, 118, 120, 122, 128, 330, 332, 134, 136, 13S, 140, 142, 344, 148, 350, 152, 154, 156, 158, 160, 164, 366, 168, 170, 172, 174, ]76, 378, 180, 184, 186, 188, 390. or an amino acid sequence having at least about 65% similarity to one or more of the above sequences, The present invention further contemplates a pharmaceutical composition comprising at least part of the protein or chimeric molecule thereof, together with a pharmaceutical]}' acceptable carrier, co-factor and/or diluent, ith respect to the primary structure, the present invention provides an isolated protein or chimeric molecule thereof, or a fragment thereof, encoded by a nucleotide sequence selected from the lisi consisting of SEQ ID NOs; 27, 29, 31, 33, 35, 37, 39, 43, 45, 47, 49, 51, 53, 55, 59, 61; 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107. IDS', ill, 113, 115, 117, 119, 121, 127, 129, 131, 133, 135, 137, 139, 141, 143, 147, 149, 15!, 153, 155, 157, 159, 163, 165, 167, 169, 171, 173, 175, 177, 179, 183, 185, 3 87, 189, or a nucleotide sequence having at least about 60% identity to any one of the above-listed sequence or. a nucleotide sequence capable of hybridizing to any one of the above sequences or their complementary forms under low stringency conditions. Still, another aspect of the present invention provides an isolated nucleic acid molecule encoding protein or chimeric molecule thereof or a functional part thereof comprising a sequence of nucleotides having at least 60% similarity selected from the list consisting of SEQ ID NOs: 27; 29.. 31, 33, 35, 37, 39, 43, 45, 47, 49, 51, 53, 55, 59, 61, 63, 65, 67, 69, 71, 73, 75, 7n, 79, 81, 83, 85, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107, 109, 111, 113, 115, 117.. 119, 121. 127, 129, 131, 133, 135, 137, 139, 141, 143, 147, 149, 151, 153, 155, 157. 159, 163, 165. 167, 369, 171, 173., 175, 177, 179, 183, 185, 187, 189 or after optimal alignment and/or being capable of hybridizing to one or more of SEQ ID NOs: 27, 29, 31, 33, 35, 37. 39, 43, 45. 47; 49, 51, 53, 55, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85,89,91,93.95,97,99, 101, 103, 105, 107, 109, 111, 113, 115,117, 119, 121, 127, 129, 131, 133, 135, 137, 139. 141, 143, 147, 149, 151, 153, 155, 157, 159, 163, 165, 167, 169, 171; 173, 175, 177, 179, 183, 185, 387, 189 or their complementary forms under low stringency conditions. In a particular embodiment, the present invention is directed to an isolated nucleic acid molecule comprising a sequence of nucleotides encoding a protein or chimeric molecule in or related to the TNF superfamily, selected from the group comprising TNF-a, TNF-a-Fc, LT-a, LT-a-Fc, TNFRI, TNFRI-Fc, TNFRJI, TNFRII-Fc, OX40, OX40-Fc, BAFF, BAFF-Fc, NGFR. NGFR-Fc, Fas Ligand, Fas Ligand-Fc, or a fragment thereof, an amino acid sequence substantially as set forth in one or more of SEQ ID NOs: 28, 30. 32, 34, 36, 38, 40, 44, 46, 48, 50. 52, 54, 56, 60. 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 90, 92, 94, 96, 98, 100. 102. 104, 106, 108, 110, 132, 114, 116, 118, 120, 122, 128, 130, 132, 134, . 138, 140. 142. 144, 148, 150, 152, 154., 156, 158, 160, 164, 166, 168, 370, 172, 174, i?6. 178, 180, 184; 186, 188, 190 or an amino acid sequence having at least about 60% similarity to one or more of SEQ ID NOs: 28, 30; 32, 34, 36: 38, 40, 44, 46; 48, 50, 52, 54, 56, 60, 62, 64, 66, 68., 70, 72, 74, 76, 78, 80, 82; 84, 86, 90, 92, 94, 96, 98, 100, 102, 104, 106, 108, 110, 312. i!4, 116, 118, 120, 122, 128, 130, 132, 134, 136, 138, 340, 142, 144, 148, 150, 152, 354; 356, 158, 160, 164, 166, 168, 170, 172, 174, 176, 178, 180, 184, 186, 188. 190 after alignment. In another aspect, the present invention provides an isolated nucleic acid molecule encoding a protein or chrmeric molecule in or related to the TNF superfamily, selected from the group comprising TNF-a-Fc, LT-a-Fc, TNFRI-Fc, TNFRII-Fc, OX40-Fc, BAFF-Fc, NGFR-Fc. Fas Ligand-Fc, or a fragment thereof, comprising a sequence of nucleotides selected from the group consisting of SEQ ID NOs: 31, 335 35, 45, 47, 49, 51, 63, 65, 67, 91, 93, 95, 97, 129. 131, 151, 153, 155, 165, 167, 185, 187, linked directly or via one or more nucleotide sequences encoding protein linkers known in the art to nucleotide sequences encoding the constant (Fc) or framework region of a human immunoglobulin, substantially as sei forth in one or more of SEQ ID NOs: 1, 3, 5, 7, 9, 11, 13, 15, 17 or 19 In £ particular embodiment, the nucleotide sequences encoding protein linker comprises nucleotide sequences selected from IP, GSSNT, TRA or VDGIQWIP. In another aspect, the present invention provides an isolated protein in or related to the TNF superfamily, selected from the group comprising TNF-a-Fc, LT-a-Fc, TNFPJ-Fc, TNFRII-Fc, OX40-Fc, BAFF-Fc, NGFR-Fc, Fas Ligand-Fc, or a fragment thereof, comprising an amino acid sequence selected from the group consisting of SEQ ID NOs: 32, 34, 36. 46, 48, 50, 52., 64, 66, 68, 92, 94, 96, 98, 130, 132, 152, 154, 156, 166, 168, 186, 188 linked directly or via one or more protein linkers known in the art, to the constant (Fc.) or framework region of a human immunoglobulin, substantially as set forth in one or more of SEQ ID NOs:2, 4, 6, 8, 10, 12, 14, 16, 18 or 20. The present invention further extends to uses of an isolated protein or chimeric molecule thereof thereof or nucleic acid molecules encoding same in diagnostic, prophylactic, therapeutic, nutritional and/or research applications. More particularly, the presentinvention extends To a method of treating or preventing a condition or ameliorating the symptoms of a condition in an animai subject, said method comprising administering to said animal subject an effective amount of an isolated protein or chimeric molecule thereof. In one embodiment, the present invention provides a method for treating an inflammatory disease state which is characterized, exacerbated or otherwise associated with an excess of TNF-a in the subject, said method comprising administering to said subject a therapeutical] v effective amount of a pharmaceutical composition comprising TNPRI and/or TNFRJI and/or a chimeric TNFRI or TNFRII molecule. In one embodiment, the disease state is selected from the list of: psoriasis, Behcet's disease, bullous dermatitis, eczema, fungal infection, leprosy, neutrophilic dermatitis, pityriasis maculara (or pityriasis rosea). pityriasis nigra (or tinea nigra), pityriasis rubra pilaris, systemic lupus erythematosus. systemic vascularitis and toxic epidermal necrolysis. In addition, the disease state may be caused by the use of medication, for instance, the Aldara cream, including but not limited to erythema, erosion, ulceration, flaking, scaling, dryness, scabbing, crusting, weeping or exudating of skin. In addition, the present invention extends tc uses of a protein or chimeric molecule thereof for screening small molecules, which may have a variety of diagnostic, prophylactic, therapeutic, nutritional and-'or research applications. The present invention further contemplates using an isolated protein or chimeric molecule thereof as immunogens to generate antibodies for therapeutic or diagnostic applications. The present invention further contemplates using an isolated protein or chimeric molecule thereof in culture mediums for stem cells used in stem cell or related therapy. The subject invention also provides a human derived protein or chimeric molecule thereof for use as a standard protein in an immunoassay and kits thereof, The subject invention also extends to a method for determining the level of human cell-expressed human protein or chimeric molecule thereof in a biological preparation. The subject invention also provides the use of a protein or chimeric molecule thereof in the manufacture of a formulation for diagnostic, prophylactic, therapeutic, nutritional and/orresearch applications. In particular, the subject invention provides for a formulation suitable for topical application comprising a TNFRI and/or TNFRII and/or a chimeric TNFR1 or TNF.RI1 molecule comprising TNFRI or TNFRII fused direct]}' or via one or more protein linkers to a Fc portion of an antibody or their functional homologs. In one embodiment, the topical application comprises one or more of TNFRI-Fc or TNFRII-Fc as described herein. TABLE 1 Sequence Identifier (Table Removed) (Table 2 Removed) (Table 3 Removed) (Table 4 Removed) abbreviations and atlernate names (Table 5 Removed) abbreviations for amino acids (Table 5a Removed)codes for non-conventional amino acids (Table 5b Removed)Amino acid polarity and charge groups (Table 6 Removed)stem cell list BRIEF DESCRIPTION OF THE FIGURES Figure 1 is a diagrammatic representation of the cloning process for inserting cDNA encoding a protein of the present invention into the pIRESbleoS or pIRESbleo3-Fc vector. Figure 2(a) shows a set of LC-MS chromatograms of N-glycans released from the TNFRII-Fc of the present invention. Top: Total Ion Chromatogram; Bottom: Base Peak Chromatogram, Figure 2(b) shows a set of MS/MS spectra of the N-glycans present in the TNFRII-Fc of the present invention. (1) [M-Ff]~ 1461, Rt 22.0min; (2) [M-2H]2' 811, Rt 23.9min; (3) [M-2H]2" 892, Rt 24.6min; (4) [M-2H]2' J037; Rt 27.2min. Figure 2(c) shows a set of LC-MS chromatograms of N-glycans released from TNFRII-Fc expressed in Chinese Hamster Ovary cells (Enbrel). Top: Total Ion Chromatogram; Bottom: Base Peak Chromatogram. Figure 2(d) shows a set of MS/MS spectra of the N-glycans present in TNFKII-Fc expressed in Chinese Hamster Ovary cells. (1) [M-H]" 1462, Rt 22.5min; (2) [M-2H]2' 893, Rt 23.6mm; (3) [M-2H]2" 1038, Rt 26.1min; (4) [M-2H]2' 1184; Rt 30-lmin; (5) [M-H]' 1598, Rt 39.1min: (6) [M-H]' ] 906, Rt 39.2min. Figure 2(e) shows a set of LC-MS chromatograms of O-glycans released from the TNFRI]-Fc of the present invention. Top: Total Ion Chromatogram; Bottom: Base Peak Chromatogram. Figure 2(f) shows a set of MS/MS spectra of the O-glycans present in the TNFRJI-Fc of the present invention. (1-A and 1-B) [M-H]" 676, Rt 21.3min; (2-A and 2-B) [M-HJ" 967, Rt 23.2min; (3) [M-H]" 749, Rt 24.3min; (4-A and 4-B) [M-H]" 1041, Rt 28.9min; (5-A and 5-B) [M-H]" ]332. Rt 33.4min. Figure 2(g) shows a set of LC-MS chromatograins of 0-glycans released from TNFRII-Fc expressed in Chinese Hamster Ovary cells (Enbrel). Top: Total Ion Chromatogram; Bottom: Base Peak Chromatogram. Figure 2(h) shows a set of MS/MS spectra of the 0-glycans present in TNFRII-Fc expressed in Chinese Hamster Ovary cells. (1-A and 1-B) [M-H]" 676, Rt 22.8min; (2-A and 2-B) [M-H]' 967, Rt 23.2min. Figure 3(a) is a photograph of a hand of a patient suffering from pityriasis rubria pilaris prior to treatment, Note the redded skin and open lesions. Figure 3(b) is a photograph of the same hand as shown in Figure 3(a) two weeks after application of 2mL of a topical composition of the TNFRII-Fc of the present invention (250 ug/ml TNFKJI-Fc; 20mg/ml thalidomide). Note the reduction of reddening and absence of lesions, Figure 4 is a graph showing cell death of WEHJ 164 cells treated with increasing concentrations of TNT-a of the present invention. Figure 5 is a graph showing cell death of WEHI 164 cells treated with increasing concentrations of LT-a of the present invention. Figure 6 is a graph showing the neutralizing ability of TNFRI-Fc of the present invention on the TNF-a mediated cytotoxicity of WEHI-164 cells. Figure 7 is a graph showing the neutralizing ability of TNFRII-Fc of the present invention on the TNF-a mediated cytotoxicity of WEH1-164 cells. Figure 8 is a graph comparing the inhibitor}' effect of TNFRII-Fc of the present invention (crosses) and TNFRIl-Fc expressed in non-human cells (diamonds) on the TNF-a mediated cvtotoxicitv of murine L-929 cells. Figure 9 is a graph comparing the proliferation of RPMI 8226 cells by BAFF of the present invention (filled circles) and human BAFF expressed using non-human cells (open circles). Figure 10 is a graph showing the neutralizing ability of NGFR-Fc of the present invention on the NGF-beta induced proliferation of TF-1 cells. Figure 11 represents the in vitro comparison of immunoreactivity profiles between TNF-a of the present invention (squares) and human TNF-a expressed in E. coli cells (horizontal lines, R&D Systems; triangles WHO). ELISA kit standard curve (circles). Figure 12 represents the in vitro comparison of immunoreactivity profiles between LT-a of the present invention (squares) and human LT-a expressed in E. coli cells (diamonds). Figure 13 is a graph showing the biodistribution of TNFRII-Fc in mice following transdermal application of TNFRII-Fc in a topical formulation of the present invention. DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENTS It is to be understood that unless otherwise indicated, the subject invention is not limited to specific formulations, manufacturing methods, diagnostic methods, assay protocols, nutritional protocols, or research protocols or the like as such may vary. It is also to be understood that the terminology used herein is for the purpose of describing particular embodiments only and is not intended to be limiting. It must be noted that, as used in the subject specification, the singular forms "a", "an" and "the" include plural aspects unless the context already dictates otherwise. Thus, for example, reference to "a protein", "a cytokine" or "a chimeric molecule" or "a receptor" includes a single protein, cytokine or receptor or chimeric molecule as well as two or more proteins, cytokines or receptors or chimeric molecules; a "physiochemical parameter" includes a single parameter as well as two or more parameters and so forth. The terms "compound", "active agent", "chemical agent", "pharmacologically active agent", "medicament", "active" and "drug" are used interchangeably herein to refer to a chemical compound and in particular a protein or chimeric molecule thereof that induces a desired pharmacological and/or physiological effect. The terms also encompass pharmaceutically acceptable and pharmacologically active ingredients of those active agents specifically mentioned herein including but not limited to salts, esters, amides, prodrugs, active metabolites, analogs and the like. When the terms "compound", "active agent", "chemical agent" "pharmacologically active agent", "medicament", "active" and "drug" are used, then it is to be understood that this includes the active agent per se as well as pharmaceutically acceptable, pharmacologically active salts, esters, amides, prodrugs, metabolites, analogs, etc. Reference to a "compound", "active agent", "chemical agent" "pharmacologically active agent", "medicament", "active" and "drug" includes combinations of two or more actives such as two or more cytokines. A "combination" also includes multi-part such as a two-part compositor] where the agents are provided separately and given or dispensed separately or admixed together prior to dispensation. For example, a multi-part pharmaceutical pack may have two or more proteins or chimeric molecules in or related to the TNF superfamily, selected from the group comprising TNF-a, TNF-a-Fc, LT-a, LT-a-Fc, TNFR1, TNFRl-Fc, TNFRII, TNFRII-Fc, OX40, OX40-Fc, BAPF, BAFF-Fc, NGFR, NGFR-Fc, Fas Ligand, Fas Ligand-Fc separately maintained. The terms "effective amount" and "therapeutically effective amount" of an agent as used herein mean a sufficient amount of the protein or chimeric molecule thereof, alone or in combination with other agents to provide the desired therapeutic or physiological effect or outcome. Undesirable effects, e.g. side effects, are sometimes manifested along with the desired therapeutic effect; hence, a practitioner balances the potential benefits against the potential risks in determining what is an appropriate "effective amount". The exact amount required will vary from subject to subject, depending on the species, age and general condition of the subject, mode of administration and the like. Thus, it may not be possible to specify an exact "effective amount". However, an appropriate "effective amount" in any individual case may be determined by one of ordinary skill in the art using only routine experimentation. By "pharmaceutically acceptable" carrier, excipient or diluent is meant a pharmaceutical vehicle comprised of a material that is not biologically or otherwise undesirable, i.e. the material may be administered to a subject along with the selected active agent without causing any or a substantial adverse reaction. Carriers may include excipients and other additives such as diluents, detergents, coloring agents, wetting or emulsifying agents, pH buffering agents, preservatives, and the like. Similarly, a "pharmacologically acceptable" salt, ester, amide, prodrug or derivative of a compound as provided herein is a salt, ester, amide, prodrug or derivative that this not biologically or otherwise undesirable. The terms "Treating" and "treatment" as used herein refer to reduction in severity and/or frequency of symptoms of the condition being treated, elimination of symptoms and/or underlying cause, prevention of the occurrence of symptoms of the condition and/or their underlying cause and improvement or remediation or amelioration of damage following a condition. "Treating" a subject may involve prevention of a condition or other adverse physiological event in a susceptible individual as well as treatment of a clinically symptomatic individual by ameliorating the symptoms of the condition. A "subject" as used herein refers to an animal, in a particular embodiment, a mammal and in a further embodiment human who can benefit from the pharmaceutical formulations and methods of the present invention. There is no limitation on the type of animal that could benefit from the presently described pharmaceutical formulations and methods. A subject regardless of whether a human or non-human animal may be referred to as an individual, patient, animal, host or recipient. The compounds and methods of the present invention have applications in human medicine, veterinary medicine as well as in general, domestic or wild animal husbandry. As indicated above, in a particular embodiment, the animals are humans or other primates such as orangutans, gorillas, marmosets, livestock animals, laboratory test animals, companion animals or captive wild animals, as well as avian species. Examples of laboratory test animals include mice, rats, rabbits, guinea pigs and hamsters. Rabbits and rodent animals, such as rats and mice, provide a convenient test system or animal model. Livestock animals include sheep, cows, pigs, goats, horses 'and donkeys. Non-mammalian animals such as avian species, fish, and amphibians including Xenopus spp prokaryotes and non-mammalian eukaryotes, The term "cytokine" is used in its most general sense and includes any of various proteins secreted by cells to regulate the immune system, modulate the functional activities of individual cells and/or tissues, and/or induce a range of physiological responses. As used herein the term "cytokine" should be understood to refer to a "complete" cytokine as well as fragments, derivatives or homologs or chimeras thereof comprising one or more aminoacid additions, deletions or substitutions, but which substantially retain the biological activity of the complete cytokine. A "cytokine receptor" is a cell membrane associated or soluble portion of the cytokine receptor involved m cytokine signalling or regulation. As used herein the term "cytokine receptor" should be understood to refer to a "complete" cytokine receptor as well as fragments, derivatives or homologs or chimeras thereof comprising one or more amino acid additions, deletions or substitutions, but which substantially retain the biological activity of the complete cytokine receptor. The term "protein" is used in its most general sense and includes cytokines and cytokine receptors. As used herein, the term "protein" should be understood to refer to a "complete" protein as well as fragments, derivatives or homologs or chimeras thereof comprising one or more amino acid additions, deletions or substitutions, but which substantially retain the biological activity of the complete protein. The term "polypeptide" refers to a polymer of amino acids and its equivalent but does not imply a limitation as to a specific length of the product, thus, peptides. oligopeptides, polypeptides and proteins are included within the definition of a "polypeptide". This term also includes all co- or post-translationally modified forms of a polypeptide. Also included within the definition are, for example, polypeptides containing one or more analogs of an amino acid including, for example, unnatural ammo acids such as those given in Table 5 (a) or polypeptides with substituted linkages. The present invention contemplates an isolated protein or chimeric molecule thereof having a profile of measurable physiochemical parameters (Px), wherein the profile is indicative of, associated with or forms the basis of one or more distinctive pharmacological traits (Ty), The isolated protein or chimeric molecule is a protein in or related to the TNF superfamily, selected from the group comprising TNF-a, TNF-a-Fc, LT-a, LT-a-Fc, TNFRJ, TNFRI-FC, TNFRIL TNFRIJ-FC, 0x40, ox4o-Fc, BAFF, BAFF-FC, NGFR, NGFR-Fc, Fas Ligand, Fas Ligand-Fc, As used herein, the terms TNF-a, TNF-a-Fc, LT-a, LT-a-Fc, TNFRI. TNFRJ-Fc, TNFRII, TNFRII-Fc, OX40, OX40-Fc, BAFF, BAFF-Fc,NGFR, NGFR-Fc, Fas Ligand, Fas Ligand-Fc includes reference to the whole polypeptide as well as fragments thereof. More particularly, the present invention provides an isolated protein or chimeric molecule thereof having a physiochemical profile comprising an array of measurable pbysiochemical parameters, {[Px]i, [Px]2,...[Px]rJ> wherein Px represents a measurable physiochemical parameter and "n" is an integer >1, wherein each of [Px]i to [Px]n is a different measurable physiochemical parameter, wherein the value of any one or more of the measurable physiochemical characteristics is indicative of, associated with, or forms the basis of, a distinctive pharmacological trait, Ty, or a number of distinctive pharmacological traits {[Ty]i, [Ty]2, ....[Ty]m} wherein Ty represents a distinctive pharmacological trait and in is an integer >1 and each of [Ty]i to [Ty]m is a different pharmacological trait. As used herein, the term "measurable physiochemical parameters" (Px) refers to one or more measurable characteristics of an isolated protein or chimeric molecule thereof. Exemplar)1 "distinctive measurable physiochemical parameters" include, but are not limited to apparent molecular weight (Pj), isoelectric point (pi) (Pz), number of isoforms (Ps), relative intensities of the different number of isoforms (P0, percentage by weight carbohydrate (P), observed molecular weight follcrwing N-linked oligosaccharide deglycosylation (Pg), observed molecular weight following N-linked and O-linked oligosaccharide deglycosylation (Pv), percentage acidic monosaccharide content (Pg), monosaccharide content (Pg), sialic acid content (Pio), sulfate and phosphate content (Pu), Ser/Thr:GalNAc ratio (P12), neutral percentage of N-linked oligosaccharide content (Pis), acidic percentage of N-linked oligosaccharide content (Pn), neutral percentage of O-linked oligosaccharide content (Pis), acidic percentage of O-linked oligosaccharide content (Pie), ratio of N-iinked oligosaccharides (Pn), ratio of O-linked oligosaccharides (Pig), structure of N-linked oligosaccharide fraction (Pi9), structure of O-linked oligosaccharide fraction (P2o)> position and make up of N-linked oligosaccharides Q?2i\ position and malceup of O-linked oligosaccharides (Pjj), co-translational modification (P2a), post-translational modification (p2i), acylation (Pis), acetylation (P26), amidation (?2i), deamidation (PIB), biotinylation (P2&), carbamylation or carbamoylation (P30), carboxylation (Psi),decarboxylation (P32): disulfide bond formation (P33); fatty acid acylation (P34), myristoylation (Pas), palmitoylation (P36), stearoylation (Py?), formylation (P38), glycation (?39), glycosylation (P4o), glycophosphatidylinositol anchor (P4i), hydroxylation (P42), incorporation of selenocysteine (P43), lipidation (P44), lipoic acid addition (P4s), methylation (P4;). N or C terminal blocking (P47), N or C terminal removal (P4g), nitration (P49), oxidation of methionine (P50), phosphorylation (P51), proteolytic cleavage (P52), prenylation (PJ3)S famesylation (Ps-0, geranyl geranylation (P55), pyridoxal phosphate addition (Pse), sialylation (Psv), desialylation (Pss), sulfation (Pss), ubiquitinylation or ubiquitiriation (Peo), addition of ubiquitin-like molecules (Pei), primary structure (Pez), secondary structure (Pes), tertiary structure (Pw), quaternary structure (Pes), chemical stability (P66), thermal stability (Pev)- A summary of these parameters is provided is Table The term "distinctive pharmacological traits" would be readily understood by one of skill in the art to include any pharmacological or clinically relevant property of the protein or chimeric molecule of the present invention. Exemplary "pharmacological traits" which in no way limit the invention include: therapeutic efficiency (Ti), effective therapeutic dose (TCIDso) (T:), bioavailability (T3). time between dosages to maintain therapeutic levels (T4), rate of absorption (Ts), rate of excretion (Te), specific activity (Ty), thermal stability (Tg), lyophilization stability (Tg), serum/plasma stability' (Tio), serum half-life (Tn), solubility in blood stream (Tn), immunoreactivity profile (Ti3), immunogenicity (Tj4), inhibition by neutralizing antibodies (Tu/Q, side effects (Tis), receptor/ligand binding affinity (Tjg), receptor./ligand activation (Tn)3 tissue or cell type specificity (Tis), ability' to cross biological membranes or barriers (i.e. gut, lung, blood brain barriers, skin etc) (Tip), angiogenic ability (T]9A), tissue uptake (Tzo), stability to degradation (Tji), stability to freeze-thaw (Tjj), stability to proteases (Tz3), stability to ubiquitination (Ta4), ease of administration (Tas), mode of administration (T26), compatibility with other pharmaceutical excipients or carriers OV), persistence in organism or environment Og), stability in storage (Tzy), toxicity in an organism or environment and the like (T3o). In addition, the protein or chimeric molecule of the present invention may have altered biological effects on different cells types (T3i). including but not limited to human primarycells, such as lymphocytes, erythrocytes, retinal cells, hepatocytes, neurons, keratinocytes, endothehal cells, endodermal cells, ectodermal cells, mesodermal cells, epithelial cells, kidney cells. liver cells, bone cells, bone marrow cells, lymph node cells, dermal cells, fibroblasts, T-cells. B-cells, plasma cells, natural killer cells, macrophages, neutrophils, granulocytes Langerhans cells, dendritic cells, eosinophils. basophils, mammary cells, lobule cells, prostate cells, lung cells, oesophageal cells, pancreatic cells, Beta cells (insulin secreting cells), hemangioblasts, muscle cells, oval cells (hepatocytes), mesenchymal cells, brain microvessel endothelial cells, astrocytes, glial cells, various stem cells including adult and embryonic stem cells, various progenitor cells; and other human immortal, transformed or cancer cell lines. The biological effects on the cells include effects on proliferation (Tsz), differentiation (133), apoptosis (134), growth in cell size (Tas), cytokine adhesion Hog), cell adhesion (Tsv). cell spreading (Tsg), cell motility (739), migration and invasion (T4o), chemotaxis (Tu), cell engulfment (T42), signal transduction (To), recruitment of proteins to receptors/ligands 44), activation of the JAK/STAT pathway (T), activation of the Ras-erk pathway O), activation of the AKT pathway (T47), activation of the PKC pathway (Ttg), activation of the PKA pathway (749), activation of src (Tso), activation of fas (Tsi), activation of TNFR (Tsz), activation ofNFkB (Tsa), activation of p38MAPK 54), activation of c-fos (Tjs), secretion (Tsg), receptor internalization (157). receptor cross-talk (Tsg), up or down regulation of surface markers (T59). alteration of FACS front/side scatter profiles (Teo), alteration of subgroup ratios (Tgi). differential gene expression (Tgz), cell necrosis (Tea), cell clumping (Tei): cell repulsion (Tes), binding to heparin sulfates (Tee), binding to glycosylated structures (Te?), binding to chondroitin sulfates (Tag), binding to extracellular matrix (such as collagen, fibronectin) (lei), binding to artificial materials (such as scaffolds) (Tvo), binding to carriers (Tvi). binding to co-factors (T/z), the effect alone or in combination with other proteins on stem cell proliferation, differentiation and/or self-renewal (Tya) and the like, A summary of these traits is provided in Table 3. As used herein the term "distinctive'' with regard to a pharmacological trait of a protein or a chimeric molecule of the present invention refers to one or more pharmacological traits of the protein or chimeric molecule thereof, which are distinctive for fee particular physiochemical profile. In a particular embodiment, one or more of the pharmacological traits of the isolated protein or chimeric molecule thereof is different from, or distinctive relative to a form of the same protein or chimeric molecule produced in a prokaryotic or lower eukaryotic cell or even a higher non-human eukaryotic cell. In a particular embodiment, the pharmacological traits of the subject isolated protein or chimeric molecule thereof are substantially similar to or functionally equivalent to a naturally occurring protein. As used herein the term "prokaryote" refers to any prokaryotic cell, which includes any bacterial cell (including actinobacterial cells) or archaeal cell. The meaning of the term "non-mammalian eukaryote", as used herein is self-evident. However, for clarity, this term specifically includes any non-mammalian eukaryote including: yeasts such as Saccharomyces spp. or Pichea spp.; other fungi; insects, including Drosophila spp. and insect cell cultures; fish, including Danio spp.; amphibians, including Xenopus spp.; plants and plant cell cultures. Reference to a "stem cell" includes embryonic or adult stem cells and includes those stem cells listed in Table 6. A protein or chimeric molecule of the present invention may be used alone or in a cocktail of proteins to induce one or more of stem cell proliferation, differentiation or self-renewal. Primary structure of a protein or chimeric molecule thereof may be measured as an amino acid sequence. Secondary structure may be measured as the number andVor relative position of one or more protein secondary structures such as a-helices, parallel |3-sheets, antiparallel [3-sheets or turns. Tertiary structure describes the folding of the polypeptide chain tc assemble the different secondary structure elements in a particular arrangement. As helices and sheets are units of secondary structure, so the domain is the unit of tertiary structure. In multi-domain proteins, tertiary structure includes the arrangement of domains relative to each other. Accordingly, tertiary structure may be measured as the presence, absence, number and/or relative position of one or more protein "domains". Exemplary domains which in no way limit the present invention include: lone helices, helix-turn-helix domains, four helix bundles, DNA binding domains, three helix bundles, Greek key helix bundles, helix-helix packing domains, p-sandwiches. aligned (3-sandwiches, orthogonal [3-sandwiches, p-barrels, up and down antiparallel p-sheets, Greek key topology domains, jellyroll topology domains, p-propellers, p-trefoils, p-Helices. Rossman folds, o/p horseshoes, a/P barrels, cn-p topologies, disulphide rich folds, serine proteinase inhibitor domains, sea anemone toxin domains, EGF-like domains, complement C-module domain, wheat plant toxin domains, Naja (Cobra) neurotoxin domains, green mamba anticholinesterase domains, Kringle domains, mucin like region, globular domains, spacer regions. Quaternary structure is described as the arrangement of different polypeptide chains within the protein structure, with each chain possessing individual primary, secondary and tertiary structure elements. Examples include either homo- or hetro-oh'gomeric multimerization (e.g. dimerization or trimerization). With respect to the primary structure, the present invention provides an isolated protein or chimeric molecule thereof, or a fragment thereof, encoded by a nucleotide sequence selected from the Hst consisting of SEQ ID NOs: 27, 29, 31, 33, 35, 37, 39, 43, 45, 47, 49, 51,53,55,59,61,63.65,67,69,71,73,75,77,79, 81,83,85, 89,91,93,95,97, 99, 101, 103. 105: 107. 109. Ill, 113, 115, 117, 119, 121, 127, 129, 131, 133, 135, 137, 139, 141, 143; 147, 149, 151, 153, 155, 157, 159, 163, 165, 167, 169, 171, 173, 175, 177, 179, 183, 185, 187. 189. or a nucleotide sequence having at least about 60% identity to any one of the above-listed sequence or a nucleotide sequence capable of hybridizing to any one of the above sequences or their complementary forms under low stringency conditions. Another aspect of the present invention provides an isolated polypeptide encoded by a nucleotide sequence selected from the list consisting of SEQ ID NOs; 191, 192, 193 following splicing of their respective mKNA species by cellular processes. Still, another aspect of the present invention provides an isolated nucleic acid molecule encoding protein or chimeric molecule thereof or a functional part thereof comprising a sequence of nucleotides having at least 60% similarity selected from the list consisting of SEQ ID NOs: 27, 29, 31,33, 35,37,39,43,45,47,49, 51, 53, 55, 59, 61, 63, 65, 67,69, 71, 73, 75. 77, 79, 81, 83, 85, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107, 109, 111, 113, 115, 117, 119: 121., 127, 129, 131, 133, 135, 137, 139, 141, 143, 147, 149, 151, 153, 155, 157, 159, 163. 165, 167, 169, 171, 173, 175, 177, 179, 183, 185, 187, 189 or after optimal alignment and/or being capable of hybridizing to one or more of SEQ ID NOs: 27, 29, 31. 33, 35, 37, 39, 43. 45, 47, 49, 51, 53, 55, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85,89,91,93,95,97,99, 101, 103, 105, 107, 109, 111,113,115, 117, 119, 121, 127, 129, 131, 133, 135, 137, 139, 141, 143, 147, 149, 151, 153, 155, 157, 159, 163, 165, 167, 169, 171, 173, 175, 177, 179, 183, 185, 187, 189 or their complementary forms under low stringency conditions. In a particular embodiment, the present invention is directed to an isolated nucleic acid molecule comprising a sequence of nucleotides encoding a protein or chimeric molecule thereof, or a fragment thereof, an amino acid sequence substantially as set forth in one or more of SEQ ID NOs; 28, 30, 32, 34, 36, 38, 40, 44, 46, 48, 50, 52, 54, 56, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 90, 92, 94, 96, 98, 100, 102, 104, 106, 108, 110, 112, 114, 116, 118, 120, 122, 128, 130, 132, 134, 136, 138, 140, 142, 144, 148, 150, 152, 154, 156, 158, 160,164, 166, 168, 170,172,174, 176,178,180, 184, 186, 188, 190 or an amino acid sequence having at least about 60% similarity to one or more of SEQ ID NOs: 28, 30, 32, 34, 36, 38, 40, 44, 46, 48, 50, 52, 54, 56, 60, 62, 64, 66, 68: 70, 72, 74, 76, 78, 80, 82, 84,86,90,92,94,96,98, 100, 102, 104, 106, 108, 110,112, 114, 116, 118, 120, 122, 128, 130, 132, 134, 136. 138, 140, 142, 144, 148, 150, 152, 154, 156, 158, 160, 164, 166, 168, 170, 172, 174,176, 178, 180,184,186,188,190 after optimal alignment. In another aspect, the present invention provides an isolated nucleic acid molecule encoding a protein molecule, or a fragment thereof, comprising a sequence of nucleotides selected from the group consisting of SEQ ID NOs: 31, 33, 35, 45, 47, 49, 51, 63, 65, 67, 91, 93., 95, 97, 129, 131, 151, 153, 155, 165, 167, 185, 187, linked directly or via one or more nucleotide sequences encoding protein linkers known in the art to nucleotide sequences encoding the constant (Fc) or framework region of a human immunoglobulin, substantially as set forth in one or more of SEQ ID NOs: 1, 3, 5, 7, 9, 11, 13, 15, 17 01 19. In a particular embodiment, the nucleotide sequences encoding protein linker comprises nucleotide sequences selected from IP, GSSNT, TRA or VDGIQWIP. In another aspect, the present invention provides an isolated protein molecule, or a fragment thereof, comprising an amino acid sequence selected from the group consisting of SEQ ID NOs: 32, 34. 36,46,48, 50,52,64,66,68,92,94,96,98, 130, 132, 152, 154, 156, 166, 168, 186, 188 linked directly or via one or more protein linkers known in the art, to the constant (Fc) or framework region of a human immunoglobulin, substantially as set forth in one or more of SEQ ID NOs: 2, 4, 6,8, 10,12,14, 16, 18 or 20. .Another aspect of the present invention provides an isolated protein or chimeric molecule thereof, or a fragment thereof, comprising an amino acid sequence selected from the list consisting of SEQ ID NOs: 28, 30, 32, 34, 36, 38, 40,44, 46, 48, 50, 52, 54, 56, 60, 62, 64, 66, 68, 70, 72; 74. 76, 78, 80, 82, 84, 86, 90, 92, 94, 96, 98, 100, 102, 104, 106, 108, 110, 112, 114, 116, 118, 120, 122, 128, 130, 132, 134, 136, 138, 140, 142, 144, 148, 150, 152, 154, 156, 158, 160, 164, 166, 168, 170, 172, 174, 176, 178, 180, 184, 186, 188, 190, or an amino acid sequence having at least about 65% similarity to one or more of the above sequences. In a particular embodiment, percentage amino acid similarity or nucleotide identity levels include at least about 61% or at least about 62% or at least about 63% or at least about 64% or at least about 65% or at least about 66% or at least about 67% or at least about 68% or at least about 69% or at least about 70% or at least about 71% or at least about 72% or at least about 73% or at least about 74% or at least about 75% or at least about 76% or at least about 77% or at least about 78% or at least about 79% or at least about 80%i or at least about 81% or at least about 82% or at least about 83% or at least about 84% or at least about 85% or at least about 86% or at least about 87% or at least about 88% or at least about 89% or at least about 90% or at least about 91% or at least about 92% or at least about 93% or at least about 94% or at least about 95% or at least about 96% or at least about 97% or at least about 98% or at least about 99% similarity or identity. A "derivative" of a polypeptide of the present invention also encompasses a portion or a pan of a full-length parent polypeptide, which retains partial transcriptional activity of the parent polypeptide and includes a variant. Such "biologically-active fragments" include deletion mutants and small peptides, for example, for at least 10, in a particular embodiment, at least 20 and in a further embodiment at least 30 contiguous amino acids. which exhibit the requisite activity. Peptides of this type may be obtained through theapplication of standard recombinant nucleic acid techniques or synthesized using conventional liquid or solid phase synthesis techniques. For example, reference may be made to solution synthesis or solid phase synthesis as described, for example, in Chapter 9 entitled "Peptide Synthesis" by Atherton and Shephard which is included in a publication entitled "Synthetic Vaccines" edited by Nicholson and published by Blackwell Scientific Publications. Alternatively, peptides can be produced by digestion of an amino acid sequence of the invention with proteinases such as endoLys-C, endoArg-C, endoGlu-C and staphylococcus V8-protease. The digested fragments can be purified by, for example, high performance liquid chromatographic (HPLC) techniques. Any such fragment, irrespective of its means of generation, is to be understood as being encompassed by the term "derivative" as used herein. The term "variant" refers, therefore, to nucleotide sequences displaying substantial sequence identity with reference nucleotide sequences or polynucleotides that hybridize with a reference sequence under stringency conditions that are defined hereinafter. The terms "nucleotide sequence", "polynucleotide" and "nucleic acid molecule" may be used herein interchangeably and encompass polynucleotides in which one or more nucleotides have been added or deleted, or replaced with different nucleotides. In this regard, it is well understood in the an that certain alterations inclusive of mutations, additions, deletions and substitutions can be made to a reference nucleotide sequence whereby the altered polynucleotide retains the biological function or activity of the reference polynucleotide or the encoded polypeptide. The term "variant" also includes naturally occurring allelic variants. The nucleic acid molecules of the present invention may be in the form of a vector or other nucleic acid construct. In one embodiment, the vector is DNA and may optionally comprise a selectable marker. Examples of selectable markers include genes conferring resistance to compounds such as antibiotics, genes conferring the ability to grow on selected substrates, genes encoding proteins that produce detectable signals such as luminescence. A wide variety of suchmarkers are known and available, including, for example, antibiotic resistance genes such as the neomycin resistance gene (neo) and the hygromycin resistance gene (hyg). Selectable markers also include genes conferring the ability to grown on certain media substrates such as the tk gene (thymidine kinase) or the hprt gene (hypoxanthine phosphoribosyltransl'erase) which confer the ability to grow on HAT medium (hypoxanthine, aminopterin and thymidine); and the bacterial gpt gene (guanine/xanthine phosphoribosyltransferase) which allows growth on MAX medium (mycophenolic acid, ademne and xanthine). Other selectable markers for use in mammalian cells and plasmids carrying a variety of selectable markers are described in Sambrook et al Molecular Cloning - A Laboratory Manual, Cold Spring Harbour, New York, USA, 1990. The selectable marker may depend on its own promoter for expression and the marker gene ma}' be derived from a very different organism than the organism being targeted (e.g. prokaryotic marker genes used in targeting mammalian cells). However, it is favorable to replace the original promoter with transcriptional machinery known to function in the recipient cells. A large number of transcriptional initiation regions are available for such purposes including, for example, metallothionein promoters, thymidine kinase promoters, p-actin promoters, immunoglobulin promoters, SV40 promoters and human cytomegalovirus promoters. A widely used example is the pSV2-rceo plasmid which has the bacterial neomycin phosphotransferase gene under control of the SV40 early promoter and confers in mammalian cells resistance to G418 (an antibiotic related to neomycin). A number of other variations may be employed to enhance expression of the selectable markers in animal cells, such as the addition of a poly(A) sequence and the addition of synthetic translation initiation sequences. Both constitutive and inducible promoters may be used. The genetic construct of the present invention may also comprise a 3' non-translated sequence. A 3' non-translated sequence refers to that portion of a gene comprising a DNA segment thai contains a polyadenylation signal and any other regulator)' signals capable of affecting mRNA processing or gene expression. The polyadenylation signal is characterized by affecting the addition of polyadenylic acid tracts to the 3' end of themKNA precursor. Polyadenylation signals are commonly recognized by the presence of homology to the canonical form 5' AATAAA-3' although variations are not uncommon. Accordingly, a genetic construct comprising a nucleic acid molecule of the present invention, operably linked to a promoter, may be cloned into a suitable vector for delivery to a cell or tissue in which regulation is faulty, malfunctioning or non-existent, in order to rectify and/or provide the appropriate regulation. Vectors comprising appropriate genetic constructs may be delivered into target eukaryotic cells by a number of different means well known to those skilled in the art of molecular biology. The term "similarity" as used herein includes exact identity between compared sequences at the nucleotide or amino acid level. Where there is non-identity at the nucleotide level, "similarity''' includes differences between sequences which result in different amino acids that are nevertheless related to each other at the structural, functional, biochemical and/or conformational levels. Where there is non-identity at the amino acid level, "similarity" includes amino acids that are nevertheless related to each other at the structural, functional, biochemical and/or conformational levels. This includes "conserved" amino acid residues which are equivalent on the basis of polarity' and/or charge. Table 5(b) displays the amino acids that are "equivalent" on the basis of polarity and/or charge. In a particular embodiment, nucleotide and sequence comparisons are made at the level of identity rather than similarity. Terms used to describe sequence relationships between two or more polynucleotides or polypeptides include "reference sequence", "comparison window", "sequence similarity", "sequence identity", "percentage of sequence similarity", "percentage of sequence identity", "substantially similar" and "substantial identity". A "reference sequence" is at least 12 but frequently 15 to 18 and often at least 25 or above, such as 30 monomer units, inclusive of nucleotides and amino acid residues, in length. Because two polynucleotides may each comprise (1) a sequence (i.e. only a portion of the complete polynucleotide sequence) that is similar between the two polynucleotides, and (2) a sequence that is divergent between the two polynucleotides, sequence comparisons between two (or more) polynucleotides are typically performed by comparing sequences of the two polynucleotides over a "comparison window" to identify and compare local regions of sequence similarity. A "comparison window" refers to a conceptual segment of typically 12 contiguous residues that is compared to a reference sequence. The comparison window may comprise additions or deletions (i.e. gaps) of about 20% or less as compared to the reference sequence (which does not comprise additions or deletions) for optimal alignment of the two sequences. Optimal alignment of sequences for aligning a comparison window may be conducted by computerized implementations of algorithms (GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package Release 7.0, Genetics Computer Group, 575 Science Drive Madison, WI, USA) or by inspection and the best alignment (i.e. resulting in the highest percentage hoinology over the comparison window) generated by any of the various methods selected. Reference also may be made to the BLAST family of programs as for example disclosed by Altschul et al. (Nucl Acids Res 25:389, 1997). A detailed discussion of sequence analysis can be found in Unit 19.3 of Ausubel et al. (In: Current Protocols in Molecular Biology, John Wiley & Sons Inc. 1994-1998). The terms ''sequence similarity" and "sequence identity" as used herein refers to the extent that sequences are identical or functionally or structurally similar on a nucleotide-by-nucleotide basis or an amino acid-by-amino acid basis over a window of comparison. Thus, a "percentage of sequence identity", for example, is calculated by comparing two optimally aligned sequences over the window of comparison, determining the number of positions at which the identical nucleic acid base (e.g. A, T, C, G, I) or the identical amino acid residue (e.g. Ala, Pro, Ser, Thr, Gly, Val, Leu, He, Phe, Tyr, Trp, Lys, Arg. His, Asp, Glu, Asn, Gin, Cys and Met) occurs in both sequences to yield the number of matched positions, dividing the number of matched positions by the total number of positions in the window of comparison (i.e., the window size), and multiplying the result by 100 to yield the percentage of sequence identity. For the purposes of the present invention, "sequence identity" will be understood to mean the "match percentage" calculated by the DNASIS computer program (Version 2.5 for windows; available from Hitachi Software Engineering Co.. Ltd., South San Francisco, California, USA) using standard defaults as used in the reference manual accompanying the software. Similar comments apply in relation to sequence similarity. Reference herein to a low stringency includes and encompasses from at least about 0 to at least about 15% v/v formamide and from at least about 1 M to at least about 2 M salt for hybridization, and at least about 1 M to at least about 2 M salt for washing conditions. Generally, low stringency is at from about 25-30°C to about 42°C, such as 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36,. 37, 38, 39, 40, 41 and 42°C. The temperature may be altered and higher temperatures used to replace formamide and/or to give alternative stringency conditions. Alternative stringency conditions may be applied where necessary, such as medium stringency, which includes and encompasses from at least about 16% v/v to at least about 30% v/v formamide, such as 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29 and 30% and from at least about 0.5 M to at least about 0.9 M salt, such as 0.5, 0.6, 0.7, 0.8 or 0.9 M for hybridization, and at least about 0.5 M to at least about 0.9 M salt, such as 0.5, 0.6, 0.7. 0.8 or 0.9 M for washing conditions, or high stringency, which includes and encompasses from at least about 31% v/v to at least about 50% v/v formamide, such as 31, 32, 33, 34, 35, 36, 37; 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49 and 50% and from at least about 0.01 M to at least about 0.15 M salt, such as 0.01, 0.02, 0.03, 0.04, 0.05, 0.06, 0.07, 0.08, 0,09, 0.10, 0.11, 0.12, 0.13, 0.14 and 0.15 M for hybridization, and at least about 0.01 M to at least about 0.15 M salt, such as 0.01, 0.02, 0.03, 0.04, 0.05, 0.06, 0.07, 0.08. 0.09, 0.10, 0.1 L 0.12, 0.13, 0.14 and 0.15 M for washing conditions. In general, washing is .carried out Tm = 69.3 + 0.41 (G+C)% (Marmur and Doty, J Mol Biol 5:109, 1962). However, the Tm of a duplex DNA decreases by 1°C with every increase of 1% in the number of mismatch base pairs (Bonner and Laskey, Eur J Biochem 46:83, 1974. Formamide is optional in these hybridization conditions. Accordingly, in a particular embodiment levels of stringency are defined as follows: low stringency is 6 x SSC buffer, 0.1% w/v SDS at 25-42°C; a moderate stringency is 2 x SSC buffer, 0.1% w/v SDS at a temperature in the range 20°C to 65°C; high stringency is 0.1 x SSC buffer, 0.1% w/v SDS at a temperature of at least 65°C. As used herein, the terms "co- or post-translational modifications" refer to covalent modifications occurred during or after translation of the peptide chain. Exemplary co- or post-translational modifications include but are not limited to acylation (including acetylation), amidation or deamidation, biotinylation, carbamylation (or carbamoylation)..carboxylation or decarboxylation, disulfide bond formation, fatty acid acylation (including myristoylation. palmitoylation and stearoylation), formylation, glycation, glycosylation, hydroxylation. incorporation of selenocysteine, lipidation, lipoic acid addition, methylation. N- or C-terminal blocking, N- or C-terminal removal, nitration, oxidation of methionine, phosphorylation. proteolytic cleavage, prenylation (including famesylation, geranyl geranylation), pyridoxal phosphate addition, sialylation or desialylation, sulfation, ubiquitinylation (or ubiquitination) or addition of ubiquitin-like proteins. Acylation involves the hydrolysis of the N-terrninus initiator methionine and the addition of an acetyl group to the new N-termino amino acid. Acetyl Co-A is the acetyl donor for acylation. Amidation is the covalent linkage of an amide group to the carboxy terminus of a peptide and is frequently required for biological activity and stability of a protein. Deamidation is the hydrolytic removal of an amide group. Deamidation of amide containing amino acid residues is a rare modification that is performed by the organism to re-arrange the 3D structure and alter the charge ratio/pi. Biotinylation is a technique whereby biotinyl groups are incorporated into molecules, either thai catalyzed by holocarboxylase synthetase during enzyme biosynthesis or that undertaken in vitro to visualise specific substrates by incubating them with biotin-labeled probes and avidin or streptavidin that has been linked to any of a variety of substances amenable to biochemical assay. Carbamylation for carbamoylation) is the transfer of the carbamoyl from a carbamoyl-containing molecule (e.g., carbamoyl phosphate) to an acceptor moiety such as an amino group, Carboxylation of glutamic acid residues is a vitamin K dependent reaction that results in the formation of a gamma carboxyglutamic acid (Gla residue). Gla residues within several proteins of the blood-clotting cascade are necessary for biological function of the proteins. Carboxylation can also occur to aspartic acid residues. Disulfide bonds are covalent linkages that form when the thiol groups of two cysteine residues are oxidized to a disulfide. Many mammalian proteins contain disulfide bonds, and these are crucial for the creation and maintenance of tertiary structure of the protein, and thus biological activity. Protein synthesis in bacteria involves formylation and deformylation of N-terminal methionines. This formylation/deformylation cycle does not occur in cytoplasm of eukaryotic cells and is a unique feature of bacterial cells. In addition to the hydroxylation that occurs on glycine residues as part of the amidation process, hydroxylation can also occur in proline and lysine residues catalysed by prolyl and lysyl hydroxylase (Kivirikko et al FASEB Journal 3:1609-1617, 1989). Glycation is the uncontrolled, non-enzymatic addition of glucose or other sugars to the amino acid backbone of protein. Giycosylation is the addition of sugar units to the polypeptide backbone and is further described hereinafter. Hydroxylation is a reaction which is dependent on vitamin C as a co-factor. Adding to the importance of hydroxylation as a post- translation modification is that hydroxy-lysine serves as an attachment site for glycosylation. Selenoproteins are proteins which contain selenium as a trace element by the incorporation of a unique amino acid, selenocystebe, during translation. The tRNA for selenocysteine is charged with serine and then enzymatically selenylated to produce the selenocysteinyl-tRNA. The anticodon of selenocysteinyl-tRNA interacts with a stop codon in mRNA (UGA) instead of a serine codon. An element in the 3' non-translated region (UTR) of selenoprotein mRNAs determines whether UGA is read as a stop codon or as a selenocvsteine codon, Lipidation is a generic term that encompasses the covalent attachment of lipids to proteins, this includes fatty acid acylation and prenylation. Fatty acid acylation involves the covalent attachment of fatty acids such as the 14 carbon Myristic acid (Myristoylation), the 16 carbon Palmitic acid (Palmitoylation) and the 18 carbon Stearic acid (Stearoylation). Fatty acids are linked to proteins in the pre-Golgi compartment and may regulate the targeting of proteins to membranes (Blenis and Resh Curr Opm Cell Biol 5(6):9%4-9, 1993). Fatty acid acylation is, therefore, important in the functional activity of a protein (Bernstein Methods Mol Biol 237:195-204, 2004). Prenylation involves the addition of prenyl groups, namely the 15 carbon famesyl or the 20 carbon geranyl-geranyl group to acceptor proteins. The isoprenoid compounds, including famesyl diphosphate or geranylgeranyl diphosphate, are derived from the cholesterol biosynthetic pathway. The isoprenoid groups are attached by a thioether link to cysteine residues within the consensus sequence CAAX, (where A is any aliphatic amino acid, except alanme) located at the carboxy terminus of proteins. Prenylation enhances proteins ability to associate with lipid membranes and all known GTP-binding and hydrolyzing proteins (G proteins) are modified in this way, making prenylation crucial for signal transduction. (Rando Biochim Biophys Acta J300(]):5-16, 1996; Gelb et al. Curr Opin ChemBio!2(J,rAQ-&, 1998). Lipoic acid is a vitamin-like antioxidant that acts as a free radical scavenger. Lipoyl-lysine is formed by attaching lipoic acid through an amide bond to lysine by lipoate protein ligase. Protein methvlation is a common modification that can regulate the activity of proteins or create new types of amino acids. Protein methyltransferases transfer a methyl group from S-adenosyl-L-methionine to nucleophilic oxygen, nitrogen, or sulfur atoms on the protein. The effects of methvlation fall into two general categories. In the first, the relative levels of methyltransferases and methylesterases can control the extent of methylation at a particular carboxyl group, which in turn regulates the activity of the protein. This type of methylation is reversible. The second group of protein methylation reactions involves the irreversible modification of sulfur or nitrogen atoms in the protein. These reactions generate new ammo acids with altered biochemical properties that alter the activity of the protein (Clarke Curr Opin Cell Biol .5:977 983, 1993). Protein nitration is a significant post-translational modification, which operates as a transducer of nitric oxide signalling. Nitration of proteins modulates catalytic activity, cell signalling and cytoskeletal organization. Phosphorylation refers to the addition of a phosphate group by protein kinases. Serine, threonme and tyrosine residues are the amino acids subject to phosphorylation. Phosphorylation is a critical mechanism, which regulates biological activity of a protein. A majority of proteins are also modified by proteolytic cleavage. This may simply involve the removal of the initiation methionine. Other proteins are synthesized as inactive precursors (proproteins) that are activated by limited or specific proteolysis. Proteins destined for secretion or association with membranes (preproteins) are synthesized with a signal sequence of 12-36 predominantly hydrophobic amino acids, which is cleaved following passage through the ER membrane. Pyridoxal phosphate is a co-enzyme derivative of vitamin B6 and participates in transaminations. decarboxylations, racemizations, and numerous modifications of amino acid side chains. All pyridoxal phosphate-requiring enzymes act via the formation of a Schiff base between the amino acid and coenzyme. Most enzymes responsible for attaching the pyridoxal-phosphate group to the lysine residue are self activating. Sialylation refers to the attachment of sialic acid to the terminating positions of a glycoprotein via various sialyltransferase enzymes; and desialylation refers the removal of sialic acids. Sialic acids include but are not limited to, N-acetyl neuraminic acid (NeuAc) and N-glycolyl neuraminic acid (NeuGc). Sialyl structures that result from the sialylation of glycoproteins include sialyl Lewis structures, for example, sialyl Lews a and sialyl Lewis x, and sialyl T structures, for example, Sialyl-TF and Sialyl Tn.Sulfation occurs at tyrosine residues and is catalyzed by the enzyme tyrosylprotein sulfotransferase which occurs in the fram'-Golgi network. It has been determined that 1 in 20 of the proteins secreted by HepG2 cells and 1 in 3 of those secreted by fibroblasts contain at least one tyrosine sulfate residue. Sulfation has been shown to influence biological activity of proteins. Of particular interest is that the CCR5, a major HIV co-receptor, was shown to be tyrosine-sulfated and that Sulfation of one or more tyrosine residues in the N-terminal extracellular domain of CCR5 are required for optimal binding of MIP-1 alpha/CCLB, MIP-1 beta/CCL4, and RANTES/CCL5 and for optimal HIV co-receptor function (Moore J Biol Chem 278(27):24243-24246, 2003). Sulfation can also occur on sugars. In addition, sulfation of a carbohydrate moiety of a glycoprotein can occur by the action of glycosulfotransferases such as GalNAc(pl-4)GlcNAc(pl-2)Mana4 sulfotransferase. Post-translationai modifications can encompass protein-protein linkages. Ubiquitin is a 76 amino acid protein which both self associates and covalently attaches to other proteins in mammalian cells. The attachment is via a peptide bond between the C-terminus of ubiquitin and the amino group of lysine residues in other proteins. Attachment of a chain of ubiquitin molecules to a protein targets it for proteolysis by the proteasome and is an important mechanism for regulating the steady state levels of regulatory proteins e.g. with respect to the cell cycle (Wilkinson Annu Rev Nutr 75:161-89, 1995). In contrast, mono-ubiquitination can play a role in direct regulation of protein function. Ubiquitin-like proteins that can also be attached covalently to proteins to influence their function and turnover include NEDD-8, SUMO-1 and Apgl2. Glycosylation is the addition of sugar residues in the polypeptide backbone. Sugar residues, such as monosaccharides, disaccharides and oligosaccharides include but are not limited to: fucose -(Fuc), galactose (Gal), glucose (Glc), galactosamine (GalNAc), glucosamine (GlcNAc), mannose (Man), N-acetyl-lactosamine (lacNAc) N,N'-diacetyllactosediamine (lacdiNAc). These sugar units can attach to the polypeptide back bones in at least seven ways, namely, (1) via an N-glycosidic bond to the R-group of an asparagine residue in the consensus sequence Asn-X-Ser; Asn-X-Thr; or Asn-X-Cys (N-glycosylation).via an 0-glycosidic bond to the R-group of serine, threonine. hydroxyproline, ryrosine or hydroxylysine (O-glycosylation). (2) via the R-group of tyrosine in C-linked mannose; (4) as a glycophosphatidylinositol anchor used to secure some proteins to cell membranes; (5) as a single monosaccharide attachment of GlcNAc to the R-group of serine or threonine. This linkage is often reversibly associated with attachment of inorganic phosphate (Ym-o-Yang); (6) attachment of a linear polysaccharide to serine. threonine or asparagine (proteoglycans); (7) via a S-glycosidic bond to the R-group of cysteine. The glycosylation structure can comprise one or more of the following carbohydrate antigenic determinants in Table 7. TABLE 7 List of carbohydrate antigenic determinants (Table Removed) The carbohydrates will also contain several antennary structures, including mono, bi, tri and tetra outer structures. Glycosylation may be measured by the presence, absence or pattern of N-linked glycosylation. 0-linked glycosylation, C-linked mannose structure, and glycophosphatidylinositol anchor; the percentage of carbohydrate by mass; Ser/Thr -GalNAc ratio; the proportion of mono, bi, tri and tetra sugar structures or by lectin or antibody binding. Sialylation of a protein may be measured by the irnmunoreactivity of the protein with an antibody directed against a particluar sialyl structure. For example, Lewis x specific antibodies react with CEACAM1 expressed from granulocytes but not with recombinant human CEACAM] expressed in 293 cells (Lucka et al. Glycobiology 7.5 fT): 87-100, 2005). Alternatively, the presence of sialylated structures on a protein may be detected by a combination of glycosidase treatment followed by a suitable measurement procedure such as mass spectroscopy (MS), high performance liquid chromatography (HPLC) or glyco mass fingerprinting (GMF). The apparent molecular weight of a protein includes all elements of a protein complex (cofactors and non-covalently bonded domains) and all co- or post-translational modifications (addition or removal of covalently bonded groups to and from peptide). Apparent molecular weight is often affected by co- or post-translational modifications. A protein's apparent molecular weight may be determined by SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis), which is also the second dimension on its two-dimensional counterpart, 2D-PAGE (two-dimensional polyacrylamide gel electrophoresis). It may be determined more accurately, however, by mass spectrometry (MS)- either by Matrix-Assisted Laser Desorption lonization - Time of Flight (MALDI-TOF) MS, which produces charged molecular ions or the more sensitive Electrospray lonization (ESI) MS, which produces multiple-charged peaks. The apparent molecular weights of the protein or chimeric molecule thereof may be within the range of 1 to 1000 kDa. Accordingly, the isolated protein or chimeric molecule of the present invention has a apparent molecular weight of 1,2. 3.4. 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20,21,22,23,24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52r 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112, 113, 114, 115, 116, 117, 118. 119. 120, 121, 122, 123, 124, 125, 126, 127, 128, 129, 130, 131, 132, 133, 134, 135, 136, 137. 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149, 150, 151, 152, 153, 154, 155, 156, 157, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168, 169, 170, 171, 172, 173, 174, 175, 176, 177, 178, 179, 180, 181, 182, 183, 184, 185, 186, 187, 188, 189, 190, 191, 192, 193, 194, 195, 196, 197, 198, 199,200,201,202,203,204,205, 206, 207, 208, 209, 210, 211, 212, 213, 214, 215, 216, 217, 218, 219, 220, 221, 222, 223, 224, 225, 226, 227, 228, 229, 230, 231, 232, 233, 234, 235, 236, 237, 238, 239, 240, 241, 242. 243, 244, 245.. 246, 247, 248, 249, 250, 251, 252, 253, 254, 255, 256, 257, 258, 259, 260. 261, 262, 263, 264, 265, 266, 267, 268, 269, 270, 271, 272, 273, 274, 275, 276, 277, 278, 279, 280. 281, 282, 283, 284, 285, 286, 287, 288, 289, 290, 291, 292, 293: 294, 295, 296, 297, 298, 299, 300, 301, 302, 303, 304, 305, 306, 307, 308, 309, 310, 311, 312, 313, 314, 315, 316, 317, 318, 319, 320, 321, 322, 323, 324, 325, 326, 327, 328, 329, 330, 331, 332, 333, 334, 335, 336, 337, 338, 339, 340, 341, 342, 343, 344, 345, 346, 347, 348, 349, 350, 351, 352, 353, 354, 355, 356, 357, 358, 359, 360, 361, 362, 363, 364, 365, 366, 367, 368, 369, 370, 371, 372, 373, 374, 375. 376, 377, 378, 379, 380, 381, 382, 383, 384, 385, 386, 387, 388, 389, 390, 391, 392, 393, 394, 395, 396, 397, 398, 399, 400, 401, 402, 403, 404, 405, 406, 407. 408, 409, 410, 411, 412, 413, 414, 415, 416, 417, 418, 419, 420, 421, 422, 423, 424, 425, 426, 427, 428, 429, 430, 431, 432, 433, 434, 435, 436, 437, 438, 439, 440, 441, 442, 443, 444, 445, 446, 447, 448, 449, 450, 451, 452, 453, 454, 455, 456, 457, 458, 459, 460, 461, 462, 463, 464, 465, 466, 467, 468, 469, 470, 471, 472, 473, 474, 475, 476, 477, 478, 479. 480, 481, 482, 483, 484, 485, 486, 487, 488, 489, 490, 491, 492, 493, 494, 495, 496, 497, 498, 499, 500, 501, 502, 503, 504, 505, 506, 507, 508, 509, 510, 511, 512, 513, 514, 515, 516, 517, 518, 519, 520, 521, 522, 523, 524, 525, 526, 527, 528, 529, 530, 531, 532.. 533, 534, 535, 536, 537, 538, 539, 540, 541, 542, 543, 544, 545, 546, 547, 548, 549, 550., 551, 552, 553, 554, 555, 556, 557, 558, 559, 560, 561, 562, 563, 564, 565, 566, 567, 568, 569, 570, 571, 572, 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587., 588, 589, 590, 591, 592, 593, 594, 595, 596, 597, 598, 599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 620, 621, 622, 623, 624, 625, 626, 627, 628, 629, 630, 631, 632, 633, 634, 635, 636, 637, 638, 639, 640, 641, 642, 643, 644, 645, 646, 647, 648, 649, 650, 651, 652, 653, 654, 655, 656, 657, 658, 659, 660, 661, 662, 663, 664, 665, 666, 667, 668, 669, 670, 671, 672, 673, 674, 675, 676, 677, 678, 679, 680, 681, 682, 683, 684, 685, 686, 687, 688, 689, 690, 691, 692, 693, 694, 695, 696, 697, 698, 699, 700, 701, 702, 703, 704, 705, 706, 707, 708, 709, 710, 711, 712, 713, 714, 715, 716, 717, 718, 719, 720, 721, 722, 723, 724, 725, 726, 727, 728, 729, 730, 731, 732, 733, 734, 735, 736, 737, 738, 739, 740, 741, 742, 743, 744, 745, 746, 747, 748, 749, 750, 751, 752, 753, 754, 755, 756, 757, 758, 759, 760, 761, 762, 763, 764, 765, 766, 767, 768, 769, 770, 771, 772, 773, 774, 775, 776, 777, 778, 779, 780, 781, 782, 783, 784, 785, 786, 787, 788, 789, 790, 791, 792, 793, 794, 795, 796, 797, 798, 799, 800, 801, 802, 803, 804, 805, 806, 807, 808, 809, 810, 811, 812, 813, 814, 815, 816, 817, 818, 819, 820, 821. 822, 823, 824, 825, 826, 827, 828, 829, 830, 831, 832, 833, 834, 835, 836, 837, 838, 839, 840, 841, 842, 843, 844, 845, 846, 847, 848, 849, 850, 851, 852, 853, 854, 855, 856, 857, 858, 859, 860, 861, 862, 863, 864, 865, 866, 867, 868, 869, 870, 871, 872, 873, 874, 875, 876, 877, 878, 879, 880, 881, 882, 883, 884, 885, 886, 887, 888, 889, 890, 891, 892, 893, 894, 895, 896, 897, 898, 899, 900, 901, 902, 903, 904, 905, 906, 907, 908, 909, 910, 911, 912, 913, 914, 915, 916, 917, 918, 919, 920, 921, 922, 923, 924, 925, 926, 927, 928, 929, 930, 931, 932, 933, 934, 935, 936, 937, 938, 939, 940, 941, 942, 943, 944, 945, 946, 947, 948, 949, 950, 951, 952, 953, 954, 955, 956, 957, 958, 959, 960, 961, 962, 963, 964, 965, 966, 967, 968, 969, 970, 971, 972, 973, 974, 975, 976, 977, 978, 979, 980, 981, 982, 983; 984, 985, 986, 987, 988, 989, 990, 991, 992, 993, 994, 995, 996, 997, 998, 999, 1000 kDa. The molecular weight or molecular mass of a protein may be determined by any convenient means such as electrophoresis, mass spectrometry, gradient ultracentrifugation, The isoelectric pomi (or pi) of a protein is the pH at which the protein carries no net charge. This attribute ma}' be determined by isoelectric focusing (IEF), which is also the first dimension of 2D-PAGE. Experimentally determined pi values are affected by a range of co- or posi-translational modifications and therefore the difference between an experimental pi and theoretical pi may be as high as 5 units. Accordingly, an isolated protein or chimeric molecule of the present invention may have a pi of 0, 1.0, 1.1, 1.2, 1.3, 1.4, 1.5, 1.6. I.-7, 1.8, 1.9, 2.0, 2.1, 2.2, 2.3, 2.4, 2.5, 2.6, 2.7, 2.8, 2.9, 3.0, 3.1, 3.2, 3.3, 3.4, 3.4, 3.6, 3.7. 3.8, ?.9, 4.0, 4,1, 4.2, 4.3, 4.4, 4.5, 4.6, 4.7, 4.8, 4.9, 5.0, 5.1, 5.2, 5.3, 5.4, 5.5, 5.4, 5.7, 5.8, 5.9. 6.0, 6.1, 6.2, 6.3, 6.4, 6.5, 6.6, 6.7, 6.8, 6.9, 7,0, 7.1, 7.2, 7.3, 7.4, 7.5, 7.6, 7.4, 7.8, 7.9, 8.0, 8.1, 8.2, 8.3, 8.4, 8.5, 8.6, 8.7, 8.8, 8.9, 9.0, 9.1, 9.2, 9.3, 9.4, 9.5, 9.6, 9.7, 9.4, 9.9, 10.0, 10.L 10.2, 10.3, 10.4, 10,5, 10.6, 10.7, 10.8, 10.9, 11.0, 11.1, 11.2, 11.3, 11.4, 11.5, 11.6, 11.7, 11.8, 11.9, 12.0, 12.1, 12.2, 12.3, 12.4, 12.5, 12.6, 12.7, 12.8, 12.9, 13.0, 13.1, 13.2, 13.3, 13.4, 13.5, 13.6, 13.7, 13.8, 13.9, or 14.0. As used herein, the term "isoform" means multiple molecular forms of a given protein, and includes proteins differing at the level of (1) primary structure (such as due to alternate RNA splicing, or polymorphisms); (2) secondary structure (such as due to different co- or post translational modifications); and/or (3) tertiary or quaternary structure (such as due to different sub-unit interactions, homo- or hetero- oligomeric multimerization). In particular, the term "isoforrrT includes glycoform, which encompasses a protein or chimeric molecule thereof having a constant primary structure but differing at the level of secondary or tertiary structure or co-or posi-translationa] modification such as different glycosylation forms. Chemical stability of a protein ma}' be measured as the "half-life" of the protein in a particular solvent or environment. Typically, proteins with a molecular weight of less than 50 kDa have a half-life of approximately 5 to 20 minutes. The proteins or chimeric molecules of the present invention are contemplated to have a half-life of 1, 2, 3, 4, 5, 6, 7, 8,9, 10, 11, 12, 13, 14.. 15, 16, 17, 18, 19,20,21,22,23,24,25,26,27,28,29,30,31,32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100 hours. Another particularly convenient measure of chemical stability is the resistance of a protein or chimeric molecule thereof to protease digestion, such as trypsin or chymotrypsin digestion. The binding affinity of a protein or chimeric molecule thereof to its ligand or receptor may be measured as the equilibrium dissociation constant (Kd) or functionally equivalent measure. The solubility of a protein may be measured as the amount of protein that is soluble in a given solvent and/or the rate at which the protein dissolves. Furthennore, the rate and or level of solubility of a protein or chimeric molecule thereof in solvents of differing properties such as polarity, pH, temperature and the like may also provide measurable physiochemical characteristics of the protein or chimeric molecule thereof. Any "measurable physiochemical parameters" may be determined, measured, quantified or qualified using an}' methods known to one of skill in the art. Described below is a range of methodologies which may be useful in determining, measuring, quantifying or qualifying one or more measurable physiochemical parameters of an isolated protein or chimeric molecule thereof. However, it should be understood that the present invention is in no way limited to the particular methods described, or to the measurable physiochemical parameters that are measurable using these methods. Glycoproieins can be said to have two basic components that interact with each other to create the molecule as a whole- the amino acid sequence and the carbohydrate or sugar side chains. The carbohydrate component of the molecule exists in the form of monosaccharide or oligosaccharide side chains attached to the amine side chain of Asn or the hydroxyl side chain of Ser/Thi residues of the amino acid backbone by N- or 0-linkages, respectively. A monosaccharide is the term given to the smallest unit of a carbohydrate that is regarded as a sugar, having the basic formula of (CHaO),, and most often forming a ring structure of 5 or 6 atoms (pentoses and hexoses respectively). Oligosaccharides are combinations of monosaccharides forming structures of varying complexities that ma}' be either linear or branched but which generally do not have long chains of tandem repeating units (such as is the case for polysaccharides). The level of branching that the oligosaccharide contains as well as the terminal and branching substitutions dramatically affect the properties of the glycoprotein as a whole, and play an important role in the biological function of the molecule. Oligosaccharides are manufactured and attached to the amino acid backbone in the endoplasmic reticulurn (ER) and Golgi apparatus of the cell. Different organisms and cell types have different ratios of glycotransferases and endoglycosidases and exoglycosidases and therefore produce different oligosaccharide structures. One of the fundamental defence mechanisms of the body is the detection and destruction of aberrant isoforms and as such it is important to have correct glycosylation of a biological therapeutic not only to increase effectiveness but also to decrease detection by neutralizing antibodies. Glycan chains are often expressed in a branched fashion, and even when they are linear, such chains are often subject to various modifications. Thus, the complete sequencing of Oligosaccharides is difficult to accomplish by a single method and therefore requires iterative combinations of physical and chemical approaches that eventually yield the details of the structure under study. Determination of the glycosylation pattern of a protein can be performed using a number of different systems, for example using SDS-PAGE. This technique relies on the fact that glycosylated proteins often migrate as diffuse bands by SDS-PAGE. Differentiation between different isoibrms are performed by treating a protein with a series of agents. For example, a marked decrease in band width and change in migration position after digestion with peptide-N4-(N-acetyl-(3-D-glucosaminyl) asparagine amidase (PNGase) is considered diagnostic of N-linked glycosylation. To determine the composition of N-linked glycosylation, N-linked oligosaccharides are removed from the protein with PNGase cloned from Flavobacterium meningosepticum and expressed in E. coli. The removed N-linked oligosaccharides may be recovered from Alltech Carbograph SPE Carbon columns (Deerfield, Illinois, USA) as described by Packer el al. Glycoconj J 5(8):731-47, 1998. The sample can then be taken for monosaccharide analysis, sialic acid analysis or sulfate analysis on a Dionex system with a GP50 pump ED50 pulsed Amperometric or conductivity detector arid a variety of pH anion exchange columns, The extent of 0-linked glycosylation may be determined by first removing O-linked oligosaccharides from the target protein by (3-elimination. The removed O-linked oligosaccharides may be recovered from Alltech Carbograph SPE Carbon columns (Deerfield. Illinois. USA) as described by Packer el al. (1998, supra). The sample can then be taken for monosaccharide analysis, sialic acid analysis or sulfate analysis on a Dionex system with a GP50 pump ED50 pulsed Amperometric or conductivity detector and a variety of pH anion exchange columns, Monosaccharide subunits of an oligosaccharide have variable sensitivities to acid and thus can be released from the target protein by mild trifluoro-acetic acid (TFA) conditions, moderate TFA conditions, and strong hydrochloric acid (HC1) conditions. The monosaccharide mixtures are then separated by high pH anion exchange chromatography (HPAEC) using a variety of column media, and detected using pulsed amperometric electrochemical detection (PAD). High-pH anion-exchange chromatography with pulsed amperometric detection (HPAJEC-PAD) has been extensive!)' used to determine monosaccharide composition. Fluorophore-based labeling methods have been introduced and many are available in kit form. Adistinct advantage of fluorescent methods is an increase in sensitivity (about 50-fold). One potential disadvantage is thai different monosaccharides may demonstrate different selectivity for the fluorophore during the coupling reaction, either in the hydrolyzate or in the external standard mixture. However, the increase in sensitivity and the ability • to identify which monosaccharides are present from a small portion of the total amount of available glycoprotein, as well as the potential for greater sensitivity using laser-induced fluorescence, makes this approach attractive. In addition a conductivity detector may be used to determine the sulfate and phosphate composition. By using standards, the peak areas can be calculated to total amounts of each monosaccharide present. These data can indicate the level of N- and O-linked glycosylation, the extent of sialylation, and in combination with amino acid composition, percent by weight glycosylation, percent by weight acidic glycoproteins. Monosaccharide composition analysis of small amounts of protein is best performed with PVDF (PSQ) membranes, after electroblotting, or, if smaller aliquots are to be analyzed, on dot blots. PVDF is an ideal matrix for carbohydrate analysis because neither monosaccharides nor oligosaccharides bind to the membrane, once released by acid or enzymatic hydrolysis. Determination of the oligosaccharide content of the target molecule is performed by a number of techniques. The sugars are first removed from the amino acid backbone by enzymatic (such as digestion with PNGase)) or chemical (such as beta elimination with hydroxide) means. The sugars may be stabilised by reduction or labeled with a fluorophore for ease of detection. The resultant free oligosaccharides are then separated either by high pH anion exchange chromatography with pulsed amperometric electrochemical detection (HPAEC-PAD), which can be used with known standards to determine the ratios of the various structures and levels of sialylation, or by fluorophore assisted carbohydrate electrophoresis (FACE) a process similar to SDS-PAGE separation of proteins. In this process the oligosaccharides are labeled with a fluorophore that imparts electrophoretic mobility. They are separated on high percentage polyacrylamide gels and the resultant band pattern provides a profile of the oligosaccharide content of the target molecule. By using standards it is possible to gain some information on the actual structures present orthe bands can be cut and analysed using mass spectrometry to determine each of their structures. Fluorophore assisted carbohydrate electrophoresis (FACE) is a polyacrylamide gel electrophoresis system designed to separate individual oligosaccharides that have been released from a glycoconjugate. Oligosaccharides are removed from the sample protein by either chemical or enzymatic means in such a way as to retain the reducing terminus. Oligosaccharides are then either digested into monosaccharides or left intact and labeled with a fluorophore (either charged or non charged), High percentage polyacrylamide gels and various buffer systems are used to migrate the oligosaccharides/monosaccharides which migrate relative to their size/composition in much the same way as proteins. Sugars are visualised by densitometry and relative amounts of sugars can be determined by fluorophore detection. This process is compatible with MALDI-TOF MS, hence the method can be used to elucidate actual structures. Quartz crystal microbalance and surface plasmon resonance (QCM and SPR, respectively) are two methods of obtaining biological information through the physiochemical properties of a molecule. Both measure protein-protein interactions indirectly through the change that the interaction causes in the physical characteristics of a prefabricated chip. In QCM a single crystal quartz wafer is treated with a receptor/antibody etc which interacts with the ligand of interest. This chip is oscillated by the microbalance and the frequency of the chip recorded. The protein of interest is allowed to pass over the chip and the interaction with the bound molecule causes the frequency of the wafer to change. By changing the conditions by which the ligand interacts with the chip, it is possible to determine the binding characteristics of the target molecule. Apparent molecular weight is also a physiochemical property which can be used to determine the similarities between the protein or chimeric molecule of the present invention and those produced using alternative means. As used herein, the term "molecular weight" is defined as the sum of atomic weights of the constituent atoms in a molecule, sometimes also referred to as "molecular mass" (Mr).Molecular weight can be determined theoretically by summing the atomic masses of the constituent atoms in a molecule, The term "apparent molecular weight" is defined as the molecular weight determined by one or more analytical techniques such as SDS page or ultra centrifugation and depends on the relationship between the molecule and the detection system. The apparent molecular weight of a protein or chimeric molecule thereof can be determined using any one of a range of experimental methods. Analytical methods for determining the molecular weight of a protein include, without being limited to, size-exclusion chromatography (SEC), gel electrophoresis, Rayleigh light scattering, analytical ultracentrifugation. and, to some extent, time-of-flight mass spectrometry. Gel electrophoresis is a process of determining some of the physiochemical properties (specifically apparent molecular weight and pi) of a protein and in the case of 2 dimensional eiectrophoresis to separate the molecule into isoforms, thereby providing information on the post-translational modifications of the protein product. Specifically, electrophoresis is the process of forcing a charged molecule (such as protein or DNA) to migrate through a gel matrix (most commonly polyacrylamide or agarose) by applying an electric potential through its body. The most common forms of electrophoresis used on proteins are isoelectric focussing, native, and SDS polyacrylamide gel electrophoresis. In isoelectric focussing a protein is placed into a polyacrylamide gel that has a pH gradient across its length. Tae protein will migrate to the point in the gel where it has a net charge of zero thereby giving its isoelectric point. Glyco mass fingerprinting (GMF) is the process by which the oligosaccharide profile of a protein or one of its isoforms is identified by electrophoresis followed by specific mass spectrometric techniques. Sample protein is purified either by ID SDS-PAGE for total profile determination or 2D gel electrophoresis for specific isoform characterization. The protein band/spot is excised from the gel and de-stained to remove contaminants. The sugars are releasec by chemical or enzymatic means and desalted/separated using a nanoflow LC system and a graphitised carbon column. The LC flow can be directly injected into an electrospray mass spectrometer that is used to determine the mass and subsequently the identity of the oligosaccharides present on the sample. This provides a profile or fingerprint of each isoform which can be combined with quantitative techniques such as Dionex analysis to determine the total composition of the molecule being tested. Primary structure can be evaluated in determining the physiochemical properties of the protein or chimeric molecule of the present invention. The primary structure of a protein or chimeric molecule thereof can be assayed using one or more of the following systems. Information on the primary structure of a protein or chimeric molecule thereof can be determined using a combination of mass spectrometry (MS), DNA sequencing, amino acid composition, protein sequencing and peptide mass fingerprinting. To determine the sequence of the amino acid backbone either N-terminal chemical sequencing, tandem mass spectrometn' sequencing, or a combination of both is used. N-terminal chemical sequencing utilises Edman chemistry (Edman P. "Sequence determination5' Mo! Biol Biochem Biophys 8:211-55, 1970), which states that the peptide bond between the N-terminal amino acid and the amino acid in position 2 of the protein is weaker than all other peptide bonds in the sequence. By using moderate acidic conditions the N-terminal amino acid is removed derivatised with a fluorophore (FTIC) and the retention time on a reversed-phase HPLC column determined, and compared to a standard to identify what the amino acid is. This method will determine the actual primary structure of the molecule but is not quantitative. Alternatively tandem mass spectrometry in conjunction with nanoflow liquid chromatography may be used (LC-MS/MS). In this process the protein is digested into peptides using specific endoproteases and the molecular weigh! of the peptides determined. High energy collision gases such as nitrogen or argon are then used to break the peptide bonds and the masses of the resultant peptides measured. By calculating the change in mass of the peptides it is possible to determine the sequence of each of the peptides (each amino acid has a unique mass). By using different proteases the peptides may then be overlapped to determine their order and thus the entire sequence of the protein.Clearly, the combination of enzymatic digestion, chemical derivatization. liquid chromatography (LC)MS and tandem MS provides an extremely powerful tool for AA sequence analysis. For example, the detailed structure of recombinant soluble CD4 receptor was characterized by a combination of methods, which confirmed over 95% of the primary sequence of this 369 AA glycoprotein arid showed the whole nature of both N-and C-termini, the positions of attachment of the glycans, the structures of the glycans and the correct assignment of the disulfide bridges (Carr et al. J Biol Chem 264(35):21286-21295, 1989). Mass spectrometry (MS) is the process of measuring the mass of a molecule through extrapolation of its behavior in a charged environment under a vacuum. MS is very useful in stability studies and quality control. The method first requires digestion of samples by proteolytic enzymes (trypsin, V8 protease, chymotrypsin, subtilisin, and clostripain) (Franks el al. Characterization of proteins, Humana Press, Clifton, NJ, 1988; Hearn et al. Methods in Erizymol 704:190-212, 1984) and then separation of digested samples by reverse phase chromatography (RPC). With tryptic digestion in conjunction with LC-MS, the peptide map can be used to monitor the genetic stability, the homogeneity of production lots, and protein stability during fermentation, purification, dosage form manufacture and storage. Before a mass analysis, several ways are used to interface a HPLC to a mass spectrometer: ]) direct liquid injection; 2) supercritical fluid; 3) moving belt system; 4) thermospray. The HPLC/MS interface used in Caprioli's work used a fused sib'ca capillary column to transport the eluate from the column to the tip of the sample probe in the ionization chamber of the mass spectrometer. The probe tip is continuously bombarded with energetic Xe atoms, causing sputtering of the sample solution as it emerges from the tip of the capillary. The mass is then analyzed by the instrument (Caprioli et al. Biochem Biophys Res Commun 146:29]-299, 1987). MS/MS and LC/MS interfaces expand the potential applications of MS. MS/MS allows direct identificatior; of partial to full sequence for peptides up to 25 AAs. sites of deamidation and isomerization (Carr el al. Anal Chem (55:2802-2824, 1991). Coupled with RPC or capillary electrophoresis (CE), MS can perform highly sensitive analysis of proteins (Figeys and Aebersold, Electrophoresis 72:885-892, 1998; Nguyen et al. J Chromatogr A 705:21-45, 1995). LC/MS allows LC methodology to separate peptides before entering the MS, such as the continuous flow FAB interfaced with microbore HPLC (Caprioli et al. 1987, supra). The latter "interface" allows the sequencing of individual peptides from complex mixtures: Fragmentation of the peptides selected by the first MS is followed by passing through a cloud of ions in a collision cell: CID (collision induced dissociation). The collision generates characteristic set of fragments, from which the sequence may be deduced, without knowing other information, such as the cDNA sequence. In a single MS experiment, an unfractionated mixture of peptides (e.g. from an enzyme digest) is injected and the masses of the major ions are compared with those predicted from the cDNA sequence. The sequence of the recombinant human interleukin-2 was verified by fast atom bombardment (FAB)-MS analysis of CNBr and pro.teolytic digests (Fukuharaer al. JBiol Chem 250:10487-10494, 1985). Electrospray ionization MS (ESI-MS) uses an aerosol of solution protein to introduce into a needle under a high voltage, generating a series of charged peaks of the same molecules with various charges. Because each peak generated from the differently charged species produces an estimation of the molecular weights, these estimations can be combined to increase the overall precision of the molecular weight estimation. Matrix Assisted Laser Desorption Ionization MS (MALDI-MS) uses a high concentration of a chromophore. A higher intensity laser pulse will be absorbed by the matrix and the energy absorbed evaporates part of the matrix and carries the protein sample with it into the vapor phase almost entirely, The resulting ions are then analyzed in a time of flight MS. The mild ionization may enhance the capacity of the method to provide quaternary structure information. MALDl-MS can be run rapidly in less than 15 minutes. It does not need to fragment the molecules and the result is easy to interpret as a densitometric scan of an SDS-PAGE gel, with a mass range up to over lOOkDa. Amino acid sequence can be predicted by sequencing DNA that encodes a protein or chimeric molecule thereof. However, occasionally the actual protein sequence may be different. Traditionally, DNA sequencing reactions are just like the PCR reactions for replicating DNA (DNA denaturation, replication). By DNA cloning technology, the gene is cloned, and the nucleotide sequence determined. The amino acid sequence of a protein or chimeric molecule thereof can be assayed using one or more of the following systems. Full sequence description of the protein or chimeric molecule thereof is usually required to describe the product. Amino acid sequencing includes: in gel tryptic digestion, fractionation of the digested peptides by RPC-HPLC, screening the peptide peaks that have the most symmetrical absorbance profile by MALDI-TOF MS, and the first peptide (N-terminal) by Edman degradation. Edman chemically derived primary sequence data is the classical method to identify proteins at the molecular level. MALDI-TOF MS can be used for N-tenninal sequence analysis. However, all enzymatic digests for HPLC and peptide sequencing are recommended to first be subjected to MS or MS/MS protein identification to decrease the time and cost. The internal amino acid sequences from SDS-PAGE-separated proteins are obtained by elution of the peptides with HPLC separation after an in situ tryptic or lysyl endopeptidase digestion in the gel matrix. Internal sequencing of the standard peptide is recommended to be run with the analyzed samples to maintain the instruments at the peak performance. More than 80% of higher eukaryotic proteins are reported to have blocked amino-termini that prevent direct amino acid sequencing. When a blocked eukaryotic protein is encountered, the presence of the sequence of the internal standard assures that the instrument is operating properly. Edman degradation can be used for direct N-tenninal sequencing with a chemical procedure, which derivatizes the N-tenninal amino acids to release the amino acids and expose the amino terminal of the next AAs. The Edman sequencing includes: 1). By microbore HPLC, N-terminal sequence analysis is repeated by Edman chemistry cycles. Every cycle of the Edman chemistry can identify one amino acid. 2). After in-gel or PVDF bound protein digestions followed by HPLC separation of the resulting peptides, internal protein sequence analysis is conducted by Edman degradation chemistry.Microbore HPLC arid capillary HPLC are used for analysis and purification of peptide mixtures using RPC-HPLC. In-gel samples and PVDF samples are purified using different columns. MALD1-TOF MS analysis can be used for N-terminal analysis after HPLC fractionation. The selection criteria are: 1) The apparent purity of the HPLC fraction. 2) The mass and thus the estimated length of the peptide. The peptide mass information is useful for confirming the Edman sequencing amino acid assignments, and also in the possible detection of co- or post-translational modifications. In-gel digests are suitable for purification on the higher sensitivity HPLC system. The internal protein sequence analysis is first enzymatically digested by SDS-PAGE. Proteins in an SDS-PAGE mini-gel can be reliably digested in-gel only with trypsin. The peptide fragments are purified by RPC-HPLC and then analyzed by MALDI-TOF MS, screening for peptides suitable for Edman sequence analysis. Proteins in a gel can only be analyzed by internal sequencing analysis, but very accurate peptides masses can be obtained, which provides additional information useful in both amino acid assignment and database searching. PVDF-bound proteins are suitable for both N-terminal and internal Edman sequencing analysis. PVDF-bound proteins are digested with the proper enzyme (trypsin, endoproteinase Lys-C, endoproteinase Glu-C, clostripain, endoproteinase Asp-N, thermolysin) and a non-ionic detergent such as hydrogenated Triton X-100. In PVDF bound proteins, the detergents used for releasing digested peptides from the membrane can interfere with MALDI-TOF MS analysis. Before the enzyme is added, Cys is reduced with DTT and alkylated with iodoacetamide to generate carboxyamidomethyl Cys, which can be identified during N-terminal sequence analysis. To determine the amino acid composition of a protein or chimeric molecule thereof, the sample is hydrolyzed using phenol catalyzed strong hydrochloric acid (HCI) acidic conditions in the gaseous phase. Once the hydrolysis is performed the liberated amino acids are denvatised with a fiuorophore compound that imparts a specific reversed phase characteristic on the combined molecule. The derivatized .amino acids are separated using reversed phase high performance liquid chromatography (RP-HPLC) and detected with a fluorescence detector. By using external and internal standards it is possible to calculate the amount of each amino acid present in the sample from the observed peak area. This information may be used to determine sample identity and to quantify the amount of protein present in the sample. For instance, discrepancies between theoretical and actual results can be used to initially identify the possibility of a de-amidation site. In combination with monosaccharide analysis it may determine the composition % by weight glycosylation and percent by weight acidic glycoproteins. This method is limited in the information that it can provide on the actual sequence of the backbone however as there is inherent variability due to environmental contaminants and occasional destruction of amino acids. For example, it is not possible for this method to detect point mutations in the sequence. Peptide mass fingerprinting (PMF) is another method by which the identity of a protein or chimeric molecule thereof may be determined. The procedure involves an initial separation of the sample by electophoretic means (either 1 or 2 dimensional), excision of the spot/band from the gel and digestion with a specific endoprotease (typically porcine trypsin). Peptides are eluted from the gel fragment and analysed by mass spectrometry to determine the peptide masses present. The resultant peptide masses are then compared to a database of theoretical mass fragments for all reported proteins (or in the case of constructs for the theoretical peptide masses of the designed sequence). The technique relies on the fact that the "fingerprint" of a protein (i.e. its combination of peptide masses) is unique. Identity can be confidently determined (greater than 90% accuracy) with as little as 4 peptides and 30% sequence coverage. Modifications such as lipid moieties and de-amidation can be identified during the PMF stage of analysis. Peaks that do not correspond to those of the identified protein are further analysed by tandem mass spectrometry (MS-MS), a technique that uses the energy created by the impact of a collision gas to break the weaker bond of the PTM. The newly freed molecule and the original peptide are then re-analysed for mass to identify the post-translational modification and the peptide fragment to which it was attached. HPLC is classified into different modes depending on the size, charge, hydrophobicity, function or specific content of the target biomolecules. Generally, two or morechromatographic methods are used to purify a protein. It is of paramount importance to consider both the characteristics of the protein and the sample solvent when the chromatographic modes are selected. Secondary structures of a protein or chimeric molecule of the present invention can also be evaluated in characterising their properties. The secondary structure of a protein or chimeric molecule thereof can be assayed using one or more of the following systems. To study the secondary structures of proteins, most commonly several spectroscopic methods should be applied and compared. Electromagnetic energy can be defined as a continuous waveform of radiation, depending on the size and shape of the wave. Different spectroscopic methods use different electromagnetic energy. The wavelength, is the extent of a single wave of radiation (the distance between two successive maxima of the waves). When the radiant energy increases, the wavelength becomes shorter. The relationship between frequency and wavenumber is: Wavenumber (cm" ) = Frequency (s" ) / The speed of light (cm/s). The absorption of electromagnetic radiation by molecules includes vibrational and rotational transitions, and electronic transitions. Infrared (IR) and Raman spectroscopy are most commonly used to measure the vibrational energies of molecules in order to determine secondary structure. However, they are different in their approach to determine molecular absorbance. The energy of the scattered radiation is less than the incident radiation for the Stokes line. The energy of the scattered radiation is more than the incident radiation for the anti-Stokes line. The energy increase or decrease from the excitation is related to the vibrational energy spacing in the ground electronic state of the molecule. Therefore, the wavenumber of the Stokes and anti-Stokes lines are a direct measure of the vibrational energies of the molecule. Only the Stokes shift is observed in a Raman spectrum, The Stokes lines are at smaller wavenurnbers (or higher wavelengths) than the exciting light. A high power excitation source, such as a laser, should be used to enhance the efficiency of Raman scattering. The excitation source should be monochromatic because we are interested in the energy (wavenumber) difference between the excitation and the Stokes lines. For a vibrational motion to be IR active, the dipole moment of the molecule must change. Therefore, the symmetric stretch in carbon dioxide is not IR active because there is no change in the dipole moment. The asymmetric stretch is IR active due to a change in dipole moment. For a vibration to be Raman active, the polarizability of the molecule must change with the vibrational motion. The symmetric stretch in carbon dioxide is Raman active because the polarizability of the molecule change. Thus, Raman spectroscopy complements IR spectroscopy (Herzberg el al, Infrared and Raman Spectra of Polyatomic Molecules, Van Nostrand Reinhold, New York, NY, 1945). For example. IR is not able to detect a homonuclear diatomic molecule due to the lack of dipole moments, but Raman spectroscopy can detect it because the molecular polarizability is changed by stretching and contraction of the bond, further, the interactions between electrons and nuclei are changed. For highly symmetric polyatomic molecules with a center of inversion (such as benzene), it is more likely that bands active in the IR spectrum are not active in the Raman spectrum or vice-versa. In molecules with little or no symmetry, modes are likely to be active in both infrared and Raman spectroscopy. IR spectroscopy measures the wavelength and intensity of the absorption of infrared light by a sample, Infrared light is so energetic that it can excite the molecular vibrations to higher energy levels. Both infrared and RAMAN spectroscopy measure the vibrations of bond lengths and angles. IR characterizes vibrations in molecules by measuring the absorption of light of certain energies corresponding to the vibrational excitation of the molecule from v = 0 to v = 1 (or higher) states. There are selection rules that govern the ability of a molecule to be detected by infrared spectroscopy - Not all of the normal modes of vibration can be excited by infrared radiation (Herzberg el al. 1945, supra], IR spectra can provide qualitative and quantitative information of the secondary structures of proteins, such as a helix, P sheet, (5 turn and disordered structure. The most informative IR bands for protein analysis are amide I (1620-1700 cm"1), amide II (1520-1580 cm'1) and amide III (1220-1350 cm"1). Amide I is the most intense absorption band in proteins. It consists of stretching vibration of the C=0 (70-85% and C-N groups (10-20%). The exact band position is dictated by the backbone conformation and the hydrogen bonding pattern. Amide II is more complex than Amide I. Amide II is governed by in-plane N-H bending (40-60%), C-N (18-40%) and C-C (10%) stretching vibrations. Amide III bands are not very useful (Krimrn and Bandekar, Adv Protein Chem 3S/181-364, 1986). Most of the (3-sheet structures of FTIR amide I band usually are located at about 1629 cm"1 with a minim urn of 1615 cm"1 and a maximum of 1637 cm"1; the minor component may show peaks around 1696 cm"1 (lowest value 1685 cm"1), a-helix is mainly found at 1652 cm"1. An absorption near 1680 cm"1 is now assigned to (3 turns. The principle of Raman scattering is different from that of infrared absorption. Raman spectroscopy measures the wavelength and intensity of inelastically scattered light from molecules. The Raman scattered light occurs at wavelengths that are shifted from the incident light by the energies of molecular vibrations. To be Raman active, for the vibration to be inelastically scattered, a change in polarizability during the vibration is essential. In the symmetric stretch, the strength of electron binding is different between the minimum and maximum internuclear distances. Therefore the polarizability changes during the vibration, and this vibrational mode scatters Raman light, the vibration is Raman active. In the asymmetric stretch the electrons are more easily polarized in the bond that expands but are less easily polarized in the bond that compresses. There is no overall change in polarizability and the asymmetric, stretch is Raman inactive (Herzberg et al. 1945, supra}. Circular dichroism can be used to detect any asymmetrical structures, such as proteins. Optically active, chromophores absorb different amount of right and left polarized light, this absorbance difference results in either a positive or negative absorption spectrum (Usually, the right polarized spectrum is subtracted from the left polarized spectrum). Commonly, the far UV or amide region (190-250nm) is mainly contributed from peptide bonds, providing information on the environment of the carbonyl group of the amide bond and consequently the secondary structure of the protein, a-helix usually displays two negative peaks at 208, 222 nm (Holzwarth el al. J Am Chem Soc 175:350, 1965), (3-sheet displays one negative peak at 218 nm, random coils has a negative peak at 196 nm. Near UV region peaks are (250-350 nm) contributed from the environment of the aromatic chromophores (The, Tyr, Trp). Disulfide bonds give rise to minor CD bands around 250 nm. Intense dichroism is commonly associated with the side-chain structures being held tightly in a highly folded, three-dimensional structure. Denaturation of the protein mostly releases the steric hindrance, a weaker CD spectrum is obtained along with an increasing degree of denaturation. For example, the side chain CD spectrum of hGH is quite sensitive to the partial denaturation by adding denaturants. Some reversible chemical alterations of the molecules, such as reduction of the disulfide bonds, or alkaline titrations will change the side-chain CD spectrum. For hGH, these spectral difference can be caused by entirely the removal of a chromophores, or by affecting changes in the particular chromophore's CD response, but not by the gross denaturation or conformational changes (Aloj et al. J Biol Chem 247:1146-1151, 1971). UV absorption spectroscopy is one of the most significant methods to determine protein properties. It can provide information about protein concentrations and the immediate environments of chromophoric groups. Proteins functional groups, such as amino, alcoholic (or phenolic) hydroxyl. carbonyl, carboxyl, or thiol can be transformed into strong chromophores. Visible and near UV spectroscopy are used to monitor two types of Bchromophores: metal loproteins (more than 400 nm) and proteins that contains Phe, Trp, Tyr residues (260-28Onm). The change in UV or fluorescence signal can be negative or positive, depending on the protein sequence and solution properties. Fluorescence measures the emission energy after the molecule has been irradiated into an excited state. Many proteins emitted fluorescence in the range of 300 to 400 nm when excited at 250 to 300 nm from their aromatic amino acids. Only proteins with Phe, Trp, Tyr residues can be measured with the order of intensity Trp» Tyr» Phe. Fluorescence spectra can reflect the microenvironments information that is affected by the folding of the proteins. For example, a buried Trp is usually in a hydrophobic environment and will fluoresce at maximum 325 to 330 nm range, but an exposed residue or free amino acids fluoresces at around 350 to 355 nm. An often used agent to probe protein unfolding is Bis-ANS. The fluorescence of Bis-ANS is pH-independent. Even though its signal is weak in water, it can be increased significantly by binding to unfolding-exposed hydrophobic sites in proteins (James and Bottomley Arch Biochem Biophy 35(5:296-300, 1998). Effective quenching of Tyr and Trp in the folded proteins causes significant signal increase upon unfolding. A simple solute may cause the change also. To maximize detection sensitivity', a signal ratio can be used. For example, In the study of rFXIII unfolding, a ratio of fluorescence intensity' at 350nm to that at 330nm was used (Kurochkin ei al. J Mol Biol 248:414-430, 1995), Conformational changes may be studied by means of excitation-energy transfer between a fluorescent donor and an absorbing acceptor, because the efficiency of transfer depends on the distance between the two chromophores (Honroe el al. Biochem J 255:199-204, 1989). Fluorescence was used to probe a-Antitrypsin conformation (Kwon and Yu, Biophim Biophys Acta 1335:265-272, 1997), to determine Tm of HSA (Farruggia e1 al. Int J Biol Macromol 20:43-51, 1997), and to detect MerP unfolding interactions (Aronsson et al FEES Lett. 477:359-364, 1997). At neutral pH, the intensity of the fluorescence emission spectrum is in the order of Trp> Tyr, At acidic pH. due to the conformational changes which disrupts the energy transfer, the fluorescence from Tyr dominates over Trp. Fluorescence studies also confirm the presence of intermediates in the guanidine-induced unfolding transition of the proteins.Tertiary and quaternary structures of the physiochemical forms of a protein or chimeric molecule of the present invention are also important in ascertaining their function. The tertiary and quaternary structures of a protein or chimeric molecule thereof can be assayed using one or more of the following systems. NMR and X-ray crystallography are the most often used techniques to study the 3D structure of proteins. Other less detailed methods to probe protein tertiary structure include CD in near UY region, second-derivative of UV spectroscopy (Ackland et al. J Chromatogr 540:187-198, 1991) and fluorescence. NMR is one of the main experimental methods for molecular structure and intermolecular interactions in structural biology. In addition to studying protein structures, NMR can also be utilised to study the carbohydrate structures of a protein or chimeric molecule of the present invention. NMR spectroscopy is routinely used by chemists to study chemical structure using simple one-dimensional techniques, The structure of more complicated molecules can also be determined by two-dimensional techniques. Time domain NMR are used to probe molecular dynamics in solutions. Solid state NMR is used to determine the molecular structure of solids. NMR can be used to study structural and dynamic properties of proteins, nucleic acids, a variety of low molecular weight compounds of biological, pharmacological and medical interests. However, not all nuclei possess the correct property in order to be read by NMR, i.e., not all nuclei posses spin, which is required for NMR. The spin causes the nucleus to produce an NMR signal, functioning as a small magnetic field. The crystal structure of a protein or chimeric molecule thereof can be assayed using one or more of the following systems. X-ray crystallography is an experimental technique that applies the fact that X-rays are diffracted by crystals. X-rays have the appropriate wavelength (in the Angstrom range, -10-8 cm) to be scattered by the electron cloud of an atom of comparable size. The electron density can be reconstructed based on the diffraction pattern obtained from X-ray scattering off the periodic assembly of molecules or atoms in the crystal. Additional phase information either from the diffraction data or from supplementing diffraction experiments should be obtained to complete the reconstruction. A model is then progressively built into the experimental electron density, refined against the data and the result is a very accurate molecular structure. X ray diffraction has been developed to study the structure of all states of matter with any beam, e.g., ions, electrons, neutrons, and protons, with a wavelength similar to the distance between the atomic or molecular structures of interest. Light scattering spectroscopy is based on the simple principle that larger particles scatter light more than the smaller particles. A slope base line in the 310-400nm region originates from light scattering when large particles, such as aggregates, present in the solution (Schmid el al Protein structure, a practical approach, Creighton Ed., IRI Press, Oxford. England, 1989) Light scattering spectroscopy can be used to estimate the molecular weight of a protein and is a simple tool to monitor protein quaternary structure or protein aggregation. The degree of protein aggregation can be indicated by simple turbidity measurement. Final product pharmaceutical solutions are subjected to inspection of clarity because most aggregated proteins are present as haze and opalescence. Quasielastic light scattering spectroscopy (QELSS), sometimes called photon correlation spectroscopy (PCS), or dynamic light scattering (DLS). is a noninvasive probe of diffusion in complex fluids for macromolecules (proteins, polysaccharides, synthetic polymers, micelles, colloidal particles and aggregations). In most cases, light scattering spectroscopy yields directly the mutual diffusion coefficient of the scattering species. When applied to dilute monodisperse solutions, the diffusion coefficient obtained by QELSS can estimate the size. With poly disperse system, it estimates the width of molecular weight distribution. For accurate measurement, 200-500 mW laser power is mandatory, conventional AH7Kr+ gas lasers are widely used (Phillies Anal Chem (52/1049A-1057A, 1990). Protein aggregation was detected by human relaxin (Li et al. Biochemistry 34:5162-5112, 1995).Stability of a protein or chimeric molecule thereof is also an important determinant of function. Methods for analysing such characteristics include DSC, TGA and freeze-dry cryostage microscopy, analysis of freeze-thaw resistance, and protease resistance. A protein or chimeric molecule of the present invention may be more stable for lyophilization (freeze drying). Lyophilization is used to enhance the stability and/or shelf life of the product as it is stored in powder rather than liquid form. The process involves an initial freezing of the sample, then removal of the liquid by evaporation under vacuum. The end result is a dessicated "cake" of protein and excipients (other substances used in the formulation), The consistency of the resulting cake is critical for successful reconstitution. The lyophilization process can result in changes to the protein, especially aggregate formation though crosslinking, but also deamidation and other modifications. These can reduce efficacy by either losses, reduced activity or by inducing immune reactions against aggregates, In order to test lyophilization stability, the protein can be formulated for lyophilization using standard stabilizers (e.g. mannitol, trehalose, Tween 80, human serum albumin and the like). After lyophilization. the amount of protein recovered can be assayed by ELISA. while its activity can be assayed by a suitable bioassay. Aggregates of the protein can be detected by HPLC or Western blot analysis. Prior to lyophilization, the Tg or Te (define Tg or Te) of the formulation should be determined to set the maximum allowable temperature of the product during primary drying. Also, information about the crystallinity or amorphousity of the formulation helps to design the lyophilization cycle in a more rationale manner. Product information on these thermal parameters can be obtained by using differential scanning calorimetry (DSC), thermogravimetric analysis (TGA) or freeze-dry cryostage microscope. Differentia] Scanning Calorimetry (DSC) is a physical thermo-analytical method to measure, characterize and analyze thermal properties of materials and determine the heat capacities, melting enthalpies and transition points accordingly. DSC scans through a temperature range at a linear rate, Individual heaters within the instrument provide heat to sample and reference pans separately, based on the "power compensated null balance"principle. During a physical transition, the absorption or evolution of the energy causes an imbalance in the amount of energy supplied to that of the sample holder, Depending on the varying thermal behavior of the sample, the energy will be taken or diffused from the sample, and the temperature difference will be sensed as an electrical signal to the computer. As a result, an automatic adjustment of the heaters makes the temperature of the sample holder identical to the reference holder. The electrical power needed for the compensation is equivalent to the calorimetric effect. The purity of an organic substance can be estimated by DSC based on the shape and temperature of the DSC melting endotherm. The power-compensated DSC provides very high resolution compared to a heat flux DSC under the identical conditions. More well-defined and more accurate partial areas of melting can be generated from power-compensated DSC because the partial areas of melting are not "smeared" over a narrow temperature interval, as for the lesser-resolved heat flux DSC. The power-compensated DSC produces inherently better partial melting areas and therefore better purity analysis. By the help of StepScan DSC, the power-compensated DSC can provide a direct heat capacity measurement using the traditional and time-proven means without the need for deconvolution or the extraction of sine wave amplitudes. Thermogravimetric Analysis (TGA) measures sample mass loss and the rate of weight loss as a function of temperature or time. As DSC, freeze-dry cryostage can reach a wide temperature range rapidly. Currently, as an preformulation and formulation study tool, simulating the lyophilization cycle in a freeze dry cryostage provides the best platform to study thermal parameters of the protein formulations on a miniature scale. Freeze dry microscope can predict the influence of formulations and process factors on freezing and drying. Only a 2-3mL sample is required for a cryostage study, which makes this technique a valuable tool to study scarce, difficult-to-obtain drugs. It is a good tool to study the effect of freezing, rate, drying rate, thawing rate on the lyophilization cycle. Annealing research may be advanced by the studies from freeze-dry cryostage microscope. Because of extensive applications of lyophilization technology, and larger demand to stabilize the extremely expensive drugs (such as proteins and gene therapy drugs), it is expected that an in-process microscopic monitor should be realized in the pharmaceutical industries soon. The freeze-thaw resistance of a protein or chimeric molecule thereof can be assayed using one or more of the following systems. Co- or post translational modification such as glycosylation may protect proteins from repeated freeze/thaw cycles. To determine this, a protein or chimeric molecule of the present invention can be compared to carrier-free E. co//-produced counterparts. A protein or chimeric molecule thereof are diluted into suitable medium (e.g. cell growth medium,, PBS or the like) then frozen by various methods, for instance, snap frozen in liquid nitrogen, slowly frozen by being placed at -70 degrees or rapidly frozen on dry ice. The samples are then thawed either rapidly at room temperature or slowly at 4 degrees. Some samples are then refrozen and the process are repeated for a number of cycles. The amount of protein present can be measured by ELISA, and the activity measured in a suitable bioassay chosen by a skilled artisan. The amount of activity/protein remaining is compared to the starting material to determine the resistance over man}' the freeze/thaw cycles. A protein or chimeric molecule of the present invention may have altered thermal stability in solution. The thermal stability of the present invention may be determined in vitro as follows. A protein or chimeric molecule of the present invention can be mixed into buffer e.g. phosphate buffered saline containing carrier protein e.g. human serum albumin and incubated at a particular temperature for a particular time (e.g. 37 degrees for 7 days), The amount of protein or chimeric molecule thereof remaining after this treatment can be determined by ELISA and compared to material stored at -70 degrees. The biological activity of the remaining protein or chimeric molecule thereof is determined by performing a suitable bioassay chosen by a person skilled in the relevant art. The protease resistance of a protein or chimeric molecule thereof can be assayed using one or more of the following systems. To compare protease resistance, solution containing a protein or chimeric molecule of the present invention and solution containing E. coli expressed counterparts can be incubated with a protease of choice (e.g. unpurified serum proteases, purified proteases, recombinant proteases) for different time periods. The amount of protein remaining is measured by an appropriate ELISA (e.g. one in which the epitopes recognized by the capture and detection antibodies are separated by the protease cleavage site), and the activity of the remaining protein or chimeric molecule thereof is determined by a suitable bioassay chosen by a skilled artisan. The bioavailability of a protein or chimeric molecule thereof can be assayed using one or more of the following systems. Bioavailability is the degree to which a drug or other substance becomes available to the target tissue after administration. Bioavailability may depend on half life of the drug or its ability to reach the target tissue. Compositions comprising a protein or chimeric molecule of the present invention is injected subcutaneously or intramuscularly. The levels of the protein or its chimeric molecule can then be measured in the blood by ELISA or radioactive counts. Alternatively, the blood samples can be assayed for activity of the proteinby a suitable bioassay chosen by a skilled artisan, for instance, stimulation of proliferation of a particular target cell population. As the sample will be from plasma or serum, there may be a number of other molecules that could be responsible for the output activity. This can be controlled by using a neutralizing antibody to the protein being tested. Hence, any remaining bioactivity is due to the other serum components. The stability or half-life of a protein or chimeric molecule thereof can be assayed using one or more of the following systems. A protein or chimeric molecule of the present invention may have altered half-life in serum or plasma. The half-life of the present invention may be determined in vitro as follows. Composition containing the protein or chimeric molecule of the present invention can be mixed into human serum/plasma and incubated at a particular temperature for a particular time (e.g. 37 degrees for 4 hours, 12 hours etc). The amount of protein or chimeric molecule thereoi remaining after this treatment can be determined by ELISA. The biological activity of the remaining protein or chimeric molecule thereof is determined by performing a suitable bioassay chosen by a person skilled in the relevant art. The serum chosen may be from a variety of human blood groups (e.g. A, B, AB, O etc,) The half-life of a protein or chimeric molecule thereof can also be determined in vivo. Composition containing a protein or chimeric molecule thereof, which may be labeled by a radioactive tracer or other means, can be injected intravenously, subcutaneously, retro-orbitally, tail vein, intramuscularly or intraperitoneally) into the species of choice for the study, for instance, mouse, rat, pig, primate, human. Blood samples are taken at time points after injection and assayed for the presence of the protein or chimeric molecule thereof (either by ELISA or by TCA-precipitable radioactive counts). A comparison composition consisting of E. coli or CHO-produced protein or chimeric molecule thereof can be run as a control, To determine the half-life of protein or chimeric molecule of the present invention, in vivo, male Wag/Rij rats, or other suitable animals can be injected intravenously with a protein or chimeric molecule thereof. Just before the administration of the substrate, 200u,l of EDTA blood is sampled as negative control. At various time points after the injection, 200u,l EDTA blood can be taken from the animals using the same technique. After the last blood sampling, the animals are sacrificed. The specimen is centrifuged for 15 min at RT within 30 min of collection, The plasma samples are tested in a specific ELISA to determine the concentration of protein or chimeric molecule of the present invention in each sample. A protein or chimeric molecule of the present invention may cross the blood brain barrier. An in vitro assay to determine if protein or chimeric molecule of the present invention binds human brain endothelial cells can be tested using the following assays. Radiolabeled protein or chimeric molecule of the present invention can be tested for its ability to bind to human brain capillary endothelial cells. An isolated protein or chimeric molecule of the present invention can be custom conjugated with radiolabel to a specific activity using a method known in the art, for instance, with 125I by the chloramine T method, or with 3H, Primary cultures of human brain endothelial cells can be grown in flat-bottom 96-well plates until five days post-confluency then lightly fixed using acetone. Cells are. lysed, transferred to glass fibre membranes. Radiolabeled protein or chimeric molecule of the present invention can be detected using a liquid scintillation counter. In vivo assays for the determination of protein or chimeric molecule of the present invention binding to human brain endothelial cells can be tested using the following assays. A human-specific protein or chimeric molecule of the present invention are tested for binding to human brain capillaries using sections of human brain tissue that are fresh frozen (without fixation), sectioned on a cryostat, placed on glass slides and fixed in acetone. Binding of 3H-protein or chimeric molecule of the present invention is examined on brain sections using quantitative autoradiography. In vivo assay can be used to measure tissue distribution and blood clearance of human-specific protein or chimeric molecule of the present invention in a primate system. A protein or chimeric molecule of the present invention is used to determine the tissue distribution and blood clearance of 14C -labeled protein or chimeric molecule of the present invention in 2 male cynomolgus monkeys or other suitable primates, protein or chimeric molecule of the present invention is administered concurrently with a 3H -labeled control protein to the animals with an intravenous catheter. During the course of the study, blood samples are collected to determine the clearance of the proteins from the circulation. At 24 hours post-injection, the animals are euthanized and selected organs and representative tissues collected for the determination of isotope distribution and clearance by combustion. In addition, capillary depletion experiments are performed to samples from different regions of the brain in accordance with Triguero, e1 al, J of Neurochemistry 54:1882-1888, 1990. This method removes greater than 90% of the vasculature from the brain homogenate (Triguero el al. cited supra). The time-dependent redistribution of the radiolabeled protein or chimeric molecule of the present invention from the capillary fraction to the parenchyma fraction is consistent with the tune dependent migration of a protein or chimeric molecule of the present invention across the blood-brain barrier. A protein or chimeric molecule of the ^present invention may promote or inhibit angiogenesis, The angiogenic potential of the protein or chimeric molecule of the present invention may be assessed methods known in the art. For example, the extent of angiogenesis may be measured by microvessel sprouting in a model of angiogenesis. In this assay, rat fat microvessel fragments (RFMFs) are isolated as described in Shepherd el al. Arterioscler Thromb Vase Biol 24-898-904, 2004. Epididymal fat pads are harvested from euthanized animals, minced and digested in collagenase. RFMFs and single cells are separated from lipids and adipocytes by centrifugation and suspended in 0.1% BSA in PBS. The RFMF suspension is sequentially filtered to remove tissue debris, single cells, and red blood cells from the fragments. RFMFs are suspended in cold, pH-neutralized rat-tail type 1 collagen at 15,000 RFMF/ml and plated into wells (for example, 0.25 ml/well) of 48-well plate for culture. After polymerization of the collagen, an equal volume of DMEM containing 10% FBS is added to each gel. After formation of the gels, vascular extensions characteristic of 'angiogenic sprouts appear by day 4 of culture. These sprouts are readily distinguished from the parent vessel fragment by the absence of the rough, smooth-muscle associated appearance. The RFMF 3-D cultures can be treated with the protein or chimeric molecule of the present invention and vessel sprout lengths can be measured at day 5 and 6 of culture. The angiogenic potential of the protein or chimeric molecule of the present invention may also be assessed by an in vivo angiogenesis assay described in Guedez ei al. Am J Pathol 762:1431-1439, 2003. This assay consists of subcutaneous implantation of semiclosed silicone cylinders (angioreactors) into nude mice. Angioreactors are filled with extracellular matrix premixed with or without the protein or chimeric molecule of the present invention. Vascularization within angioreactors is quantified by the intravenous injection of fluorescein isothiocyanate (FITC)-dextran before their recovery, followed by spectrofluorimetry, Angioreactors examined by immunofluorescence is able to show cells and invading angiogenic vessels at different developmental stages. A protein or chimeric molecule of the present invention may have a distinct immunoreactivity profile determined by immunoassay techniques, which involve the interaction of the molecule with one or more antibodies directed against the molecule. Examples of immunoassay techniques include enzyme-linked immunoabsorbant assays (ELISA), dot blots and immunochromatographic assays such as lateral flow tests or strip tests. The level of the protein or chimeric molecule thereof may be measured using an immunoassay procedure, for example, a commerically purchased ELISA kit. The protein or chimeric molecule of the present invention may have a different immunoreactivity profile to non-human cell expressed protein or chimeric molecule thereof due to the specificity of the antibodies provided in an immunoassay kit. For instance, the capture and/or detection antibodies of the immunoassay may be antibodies specifically directed against non-human cell expressed human protein or chimeric molecule thereof. In addition, incorrect folding of the non-human cell expressed human protein or chimeric molecule thereof may result in the exposure of antigenic epitopes which are not exposed on the correctly folded human cell expressed human protein or chimeric molecule thereof. Incorrect folding may arise through, for instance, overproduction of heterologous proteins in the cytoplasm of non-human cells, for example, E. coll (Baneyx Current Opinion in Biotechnology, 70:41]-421. 1999). Further, non-human cell expressed human protein or chimeric molecule thereof may have a different pattern of post-translational modifications to that of the protein or chimeric molecule of the present invention. For example, the non-human cell expressed human protein or chimeric molecule thereof may exhibit abnormal ies and/oi types of carbohydrate structures, phosphate, sulfate, lipid or other residues. This may result in the exposure of antigenic epitopes which are not exposed on the protein or chimeric molecule of the present invention. Conversely, an altered pattern of posi-translational modifications may result in an absence of antigenic epitopes on the protein or chimeric molecule of the present invention which are exposed on the non-human cell expressed human protein or chimeric molecule thereof. Any one of, or combination of, the above-mentioned factors may lead to inaccurate measurements of; (a) naturally occurring human protein in laboratory samples or human tissues, or (b) human cell expressed recombinant human protein or chimeric molecule thereof in laboratory samples, human tissues or in human embryonic stem cell (hES) culture media, The immunoreactivity profile of a human cell expressed human protein or chimeric molecule thereof, as determined by the use of a suitable immunoassay, may provide an indication of the protein's immunogenicity in the human, as described hereinafter. Most biologic products elicit a certain level of antibody response against them. The antibody response can, in some cases, lead to potentially serious side effects and/or loss of efficacy. For instance, some patients treated with recombinant protein or chimeric molecule thereof expressed from non-human cells may generate neutralizing antibodies particularly during long-term therapeutic use and thereby reducing the protein's efficacy and or contribute to side effects. The protein or chimeric protein molecule expressed from human cells is unlikely to generate neutralizing antibodies therefore increasing its therapeutic efficacy compared with non-human cell expressed protein or chimeric molecule thereof. The immunogenicity of protein or chimeric molecule thereof can be assayed using one or more of the following systems. Most biologic products elicit a certain level of antibody response against them. The antibody response can, in some cases, lead to potentially serious side effects and/or loss of efficacy. For instance, some patients treated with recombinant EPO will generate neutralizing antibodies that also cross-react with the patient's own EPO. In this case, they can develop pure red cell aplasia and be resistant to EPO treatment, resulting in a need for constant dialysis, Immunogenicity is the properly of being able to evoke an immune response within an organism. Immunogenicity depends partly upon the size of the substance in question and partly upon how unlike host molecules it is. A protein or chimeric molecule thereof may have altered immunogenicity due to its novel physiochemical characteristics. For instance, the glycosylation structure of a protein or chimeric molecule thereof may shield or obscure the epitope(s) recognized by the antibody and therefore preventing or reducing antibody binding to the protein or chimeric molecule thereof. Alternatively, some antibodies may recognize a glycopeptide epitope not present in the non-glycosylated version of the protein. The ability of patient samples to recognize a protein or chimeric molecule thereof with a distinctive physiochemical form can be determined by various immunoassays, as described herein. A properly designed imrounoassay involves considerations directing to appropriate detection, quantitation and characterization of antibody responses. A number of recommendations for the design and optimization of immunoassays are outlined in Mire-Sluis et al. J Immunol Methods 289(l-2):l-l6, 2004, which is incorporated by reference. The use of protein or chimeric molecule thereof on therapeutic implants can be assayed using one or more of the following systems. The present invention extends to the use of a protein or chimeric molecule thereof to manipulate stem cells. A major therapeutic use of stem cells is in regeneration of tissue, cartilage or bone. In one embodiment, the cells are likely to be introduced to the body in a biocompatible three-dimensional matrix. The implant will consist of a mixture of cells, the scaffold, growth factors and accessor}' components such as biodegradable polymers, proteoglycans and the like. Incorporation of a protein or chimeric molecule thereof into these matrices during their construction is proposed to regulate the behavior of the cells. Such implants may be used for the formation of bone, the growth of neurons from progenitor cells, chondrocyte implantation for cartilage replacement and other applications. Human cell-derived proteins may reduce the quantity and/or variety of xenogeneic proteins from stem cell culture conditions and thereby reduce the risks of infection by non-human pathogens. A protein or chimeric molecule of the present invention may interact differently with the matrix used for the formation of the implant, as well as regulating the cells incorporated within the implant. It is anticipated that the combination of a protein or chimeric molecule of the present invention with 'the implant components will result in one or more of the following pharmacological traits, such as higher proliferation, enhanced differentiation, maintenance in a desired state of differentiation, greater lineage specificity of differentiation, enhanced secretion of matrix components, better 3-dimensional structure formation, enhanced signaling, better structural performance, reduced toxicity, reduced side effects, reduced inflammation, reduced immune cell infiltrate, reduced rejection, longer duration of the implant, longer function of the implant, better stimulation of the cells surrounding the implant, better tissue regeneration, better organ function, or better tissue remodeling. The effects of protein or chimeric molecule thereof on differential gene expression can be assayed using one or more of the following systems. The differences in gene expression can be analyzed in cells exposed to a protein or chimeric molecule thereof. Microarray technology enables the simultaneous determination of the mRNA expression of almost all genes in an organism's genome. This method uses gene "chips" in which oligonucleotides corresponding to the sequences of different genes are attached to a solid support. Labeled cDNA derived from mRNA isolated from the cell or tissue of interest is incubated with the chips to allow hybridisation between cDNA and the attached complementary' sequence. A control is also used, and following hybridisation and washing the signal from both is compared. Specialised software is used to determine which genes are up or down regulated or which have unchanged expression. Many thousands of genes can be analysed on each chip. For example using Affymetrix technology, the Human Genome U133 (HG-U133) Set, consisting of two GeneChip (registered trade mark) arrays, contains almost 45,000 probe sets representing more than 39,000 transcripts derived from approximately 33,000 well-substantiated human genes. The GeneChip (registered trade mark) Mouse Genome 430 2.0 contains over 39,000 transcripts on a single array. This type of analysis reveals changes in the global mKNA expression pattern and therefore differences in the expression of genes not known to be controlled by a particular stimulus may be uncovered, This technology is hence suitable to analyze the induced gene expression associated with protein or chimeric molecule of the present invention. The definition of known and novel genes regulated by the particular stimulus will assist in the identification of the biochemical pathways that are important in the biological activity of the particular protein or chimeric molecule of the present invention. This information will be useful in the identification of novel therapeutic targets. The system could also be used to look at differences in gene expression induced by a protein or chimeric molecule of the present invention as compared to commercially available products. The effects of protein or chimeric molecule thereof on binding ability can be assayed using one or more of the following systems. The binding ability of a protein or chimeric molecule of the present invention to various substances, including extracellular matrix, artificial materials, heparin sulfates. carriers or co-factors can be investigated. The effects of a protein or chimeric molecule thereof on the ability of a particular protein to bind an extracellular matrix can be determined using the following assays. A surface is coated with extracellular matrix proteins, including but not limited to collagen, vitronectin, fibronectm, laminin, in an appropriate buffer. The unbound sites can be blocked by methods known in the art, for instance, by incubation with BSA solution. The surface is washed, for instance, with PBS solutions, then a solution containing the protein to be tested, for instance a protein or chimeric molecule of the present invention, is added to the surface. After coating, the surface is washed and incubated with an antibody that recognizes a protein or chimeric molecule thereof. Bound antibody is then detected, for instance, by an enzyme-linked secondary antibody that recognizes the primary antibody, The bound antibodies are visualized by incubating with the appropriate substrate and observing a colour change reaction. Glycosylated proteins may adhere more strongly to the extracellular matrix proteins than unglycosylated proteins. Alternatively, an equivalent amount (specified by ELISA concentration or bioassay activity units) of a protein or chimeric molecule of the present invention, or a counterpart protein or chimeric molecule thereof expressed by non-human cells, are incubated with matrix coated wells, then following washing of the wells the amount bound is determined by ELISA, The amount bound can be indirectly measured by a drop in ELISA reactivity following incubation of the sample with the coated surface. The ability of protein or chimeric molecule thereof to bind artificial materials can be assayed using one or more of the following systems. In order to determine the binding ability of a protein or chimeric molecule thereof to artificial materials, a surface is coated with artificial material, including but not limited to metals, scaffolds, in an appropriate buffer. The surface is washed, for instance, with PBS solutions, then a solution containing the protein to be tested, for instance a protein or chimeric molecule of the present invention, is added to the surface, After coating, the surface is washed and incubated with an antibody that recognizes a protein or chimeric molecule thereof. Bound antibody is then detected, for instance, by a enzyme-linked secondary antibody that recognizes the primary antibody, The bound antibodies are visualized by incubating with the appropriate substrate and observing a color change reaction. Alternatively, an equivalent amount (specified by ELISA concentration or bioassay activity units) of a protein or chimeric molecule of the present invention, and a counterpart protein or chimeric molecule thereof expressed by non-human cells, are incubated with wells coated by artificial materials, the wells are then washed and the amount bound is determined by ELISA. The amount bound can be indirectly measured by a drop in ELISA reactivity following incubation of the sample with the coated surface. Ability to bind to artificial surfaces may have biological consequences, for instance, in stem coating. Alternatively, a scaffold coated with a protein or chimeric molecule of the present invention is used to seed cells on. The cell growth and differentiation is then monitored and compared to uncoated or differentially coated scaffolds. The ability of protein or chimeric molecule thereof to bind to heparin sulfates can be assayed using one or more of the following systems. A protein or chimeric molecule of the present invention is expected to interact differentially with heparin sulfates due to their physiochemical form. These differences axe expected to be evident in experimental models of cell proliferation, differentiation, migration and the like. The combination of a protein or chimeric molecule thereof with heparin sulfates is expected to have distinctive pharmacological traits for a given treatment. This may be an increase in serum half-life, bioavailability, reduced immune-related clearance, greater efficacy, reduced dosage fewer side effects and related advantages. The ability of protein or chimeric molecule thereof to bind to carriers or co-factors can be assayed using one or more of the following systems. Proteins or chimeric molecules thereof will be bound to other molecules when they are present in plasma. These molecules may be termed "carriers" or "co-factors" and will influence such factors as bioavailability or serum half life. Incubating purified versions of the proteins in plasma and analyzing the resulting solution by size exclusion chromatography can determine the interaction of a protein or chimeric molecule of the present invention with their binding partners, If the protein or chimeric molecule thereof binds a co-factor, the resulting complex will have a larger molecular weight, resulting in an altered elution tune. The complex can be compared for biological activity, in vitro or in vivo half-life and bioavailability. The effects of protein or chimeric molecule thereof on bioassays can be assayed using one or more of the following systems. Various bioassays can be performed to test the activity of a protein or chimeric molecule of the present invention, including assays on cell proliferation, cell differentiation, cell apoptosis, cell size, cytokine/cytokine receptor adhesion, cell adhesion, cell spreading, cell motility, migration and invasion, chemotaxis, ligand-receptor binding, receptor activation, signal transduction, and alteration of subgroup ratios. The effects of protein or chimeric molecule thereof on cell proliferation can be assayed using one or more of the following systems. Cells, in a particular embodiment, exponentially growing cells, are incubated in a growth medium in the presence of a protein or chimeric molecule of the present invention. This can be performed in flasks or 96 well plates. The cells are grown for a period of time and then the number of cells is determined by either a direct (e.g. cell counting) or an indirect (MTT, MTS. tritiated thymidine) method. The increase or decrease in proliferation is determined by comparison with a medium only control assay. Different concentrations of protein or chimeric molecule thereof can be used in parallel series of experiments to get a dose response profile. This can be used to determine the ED50 and EDI00 (the dose required to generate the half maximal and maximal response effectively). The effects of protein or chimeric molecule thereof on cell differentiation or maintenance of cells in an undifferentiated state can be assayed using one or more of the following systems. Cells are incubated in a growth medium in the presence of a protein or chimeric molecule of the presem invention. After a suitable period of time, the cells are assayed for indicators of differentiation. This may be the expression of particular markers on the cell surface, cytoplasmic markers, an alteration in the cell dimensions, shape or cytoplasmic characteristics. The markers may include proteins, sugar structures (e.g. glycosaminocglycans such as heparin sulfates, chondioitin sulfates etc.) lipids (glycosphingolipids or lipid bilayer components). These changes can be assayed by a number of techniques including microscopy, western blot, FACS staining or forward/side scatter profiles. The effects of protein or chimeric molecule thereof on cell apoptosis can be assayed using one or more of the following systems. Apoptosis is defined as programmed cell death, and is distinct from other methods of cell death such as necrosis, It is characterized by defined changes in the cells, such as activation of signaling pathways (e.g. Fas, TNFR) resulting in the activation of a subset of proteases know as caspases. Initiator caspase activation leads to the activation of the executioner caspases which cleave a variety of cellular proteins resulting in nuclear fragmentation, cleavage of nuclear lamins, blebbing of the cytoplasm and destruction of the cell. Apoptosis can be induced by protein ligands such as FasL, TNFa and lymphotoxin or by signals such as UV light and substances causing DNA damage. Cells are incubated in a growth medium in the presence of protein or chimeric molecule thereof and or other agents as suitable for the assay. For instance, the presence of agents able to block transcription (actinomycin D) or translation (cycloheximide) may be required. Following incubation for an appropriate period, the number of cells is determined by a suitable method. A decrease in cell number may indicate apoptosis. Other indications of apoptosis may be obtained by staining of the cells, for instance, for annexins or obsen'ing characteristic laddering patterns of DMA. Further evidence for the confirmation of apoptosis may be achieved by preventing the expression of apoptotic markers by incubating with cell permeable caspases inhibitors (e.g. z-VAD FMK), then assaying for apoptotic markers. A protein or chimenc molecule of the present invention may prevent apoptosis by providing a survival signal through cellular survival pathways such as the Bcl2 or Akt pathways. Activation of these pathways can be confirmed by western blotting for an increase in cellular Bcl2 expression, or for an increase in the activated (phosphorylated) form of Akt using a phospho-specific antibody directed against Akt. For this assay, cells are incubated in the presence or absence of the survival factor (e.g. IL-3 and certain immune cells). A proportion of cells incubated in the absence of the survival factor will die by apoptosis upon extended culture, whereas cells incubated in sufficient quantities of survival factor will survive or proliferate. Activation of the cellular pathways responsible for these effects can be determined by western blotting, immunocytochemistry and FACS analysis. The effects of a protein or chimeric molecule thereof on the inhibition of apoptosis can be assayed using one or more of the following systems. A protein or chimeric molecule of the present invention is tested for in vitro activity to protect rat-, mouse-and human cortical neural cells from cell death under hypoxic conditions and with glucose deprivation. For this, neural cell cultures are prepared from rat embryos. To evaluate the effects of the protein or chimeric molecule of the present invention, the cells are maintained in modular incubator chambers in a water-jacketed incubator for up to 48 hours at 37° C, in serum-free medium with 30 mM glucose and humidified 95% air/5%CC>2 (normoxia) or in serum-free medium without glucose and humidified 95% N2/5% CC>2 (hypoxia and glucose deprivation), in the absence or presence of the protein or chimeric molecule of the present invention. The cell cultures are exposed to hypoxia and glucose deprivation for less than 24 hour and thereafter returned to normoxic conditions for the remainder of 24 hour. The cytotoxicity is analyzed by the fluorescence of Alamar blue, which reports cell viability as a function of metabolic activity. In another method, the neural cell cultures are exposed for 24 hours to 1 mM L-glutamate or a-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) under normoxic conditions, in the absence or presence of various concentrations of the protein or chimeric molecule of the present invention. The cytotoxicity is analyzed by the fluorescence of Alamai blue, which reports cell-viability as a function of metabolic activity. A protein or its chimeric molecule may affect the growth, apoptosis, development, or differentiation of a variety of cells. These changes can be reflected by, among other measurable parameters, changes in the cell size and changes in cytoplasmic complexity, which are due to intracellular organelle development. For instance, keratinocytes induced to differentiate by suspension culture exhibit downregulation of surface markers such as pi integrins, an increase in cell size and cytoplasmic complexity. The effects of a protein or chimeric molecule thereof on cell size, or cytoplasmic complexity can be assayed using one or more of the following systems. FACS measures the amount of light scattered off by a cell when a beam of laser is incident on it. An argon laser providing light with a wavelength of 488nm is frequently used. The larger the size of the cell, the greater the disruption of the beam of light in the forward direction, hence the level of forward scatter corresponds to the size of the cell. In order to measure changes in cell size, cells treated with a protein or chimeric molecule of the present invention are diluted in sheath fluid and injected into the flow cytometer (FACSVantage SE, Becton Dickinson). Untreated cells act as a control. The cells pass through a beam of light and the amount of forward scattering of the light corresponds to the size of the cells, Changes in intracellular organelle growth and development (cytoplasmic complexity) can also be measured by FACS. The intracellular organelles of the cell scatter light sideways. Hence, change 111 cytoplasmic complexity-' can be measured by the amount of side scattering of light by the cells by the above method, and the level of complexity of intracellular organelles and the level of granularity of the cell can be estimated by measuring the level of side scatter of light given off by the cells. The effect of a protein or chimeric molecule thereof on cell size or cytoplasmic complexity can be assessed by using FACS to compare the profiles given off by, for instance, 20,000 treated cells with the signals emitted by identical number of untreated cells. By comparing the signals from the different treated populations of cells, the relative changes in cell size and cytoplasimc complexity can be determined. The effects of a protein or chimeric molecule thereof on cell growth, apoptosis, development, or differentiation can be assayed using one or more of the following systems. Protein-induced apoptosis and changes in cell growth or cycles can be assessed by labeling the DNA of treated cells with dyes such as propidium iodine which has an excitation wavelength in the range of 488 nm and emission at 620 nm. Cells undergoing apoptosis has condensed DNA as well as different size and granularity. These factors give specific forward and size scatter profiles as well as fluorescence signal, and hence the population of cells undergoing apoptosis can be differentiated from normal cells. The amount of DNA in a cell also reflects which state of the cell cycle the cell is in. For instance, a cell in G2 stage will have twice the amount of DNA as a cell in Go state. This will be reflected by a doubling of the fluorescence signal given off by a cell in G2 phase. The effect of a protein or chimeric molecule thereof can be assessed by using FACS to compare the fluorescence signals given off by for instance, 20,000 treated cells with the signals emitted by identical number of untreated cells. • • The protein or its chimeric molecule of the present invention may also alter the expression of various proteins. The effects of the protein or chimeric molecule thereof on protein expression by cells can be assayed using one or more of the following systems. To assess the increase and decrease in expression of a protein in an entire cell, the cells can be fixed and permeabilised, then incubated with fluorescence conjugated antibody targeting the epitope of the protein of interest. A large variety of fluorescent labels can be used with an Argon laser system. Fluorescent molecules such as FITC, Alexa Fluor 488, Cyanine 2. Cyanine 3 are commonly used for this experiment. This method can also be used to estimate the changes in expression of surface markers and proteins by labeling non-permeabilised cells where only the epitope exposed on the cell surface can be labeled with antibodies. The effect of a protein or chimeric molecule thereof can be assessed by using FACS to compare the fluorescence signals given off by, for instance, 20,000 treated cells with the signals emitted by identical number of .untreated cells. The effects of a protein or its chimeric molecule on ligand/receptor adhesion can be assayed using one or more of the following systems. A protein or chimeric molecule of the present may be more or less adhesive to substrates compared to those of a previously known physiochemical form. The interaction may be with protein receptors for sugar structures (e.g. selectins, such as L-selectin and P-selectin), with extracellular matrix components such as fibronectin, collagens, vitronectins, and laminins. or with non-protein components such as sugar molecules (heparin sulfates, other glycosammoglycans). A protein or chimenc molecule thereof may also interact differently with non-biological origin materials stich as tissue culture plastics, medical device components (e.g. stents or other implants) or dental materials. In the case of medical devices this may alter the engraftment rates, the interaction of the implant with particular classes of cell type or the type of linkage formed with the body. An}' suitable assays for protein adhesion can be employed. For instance, a solution containing a protein or chimeric molecule of the present invention is incubated with a binding partner, in a particular embodiment, on an immobilised surface. Following incubation, the amount of the protein or the chimeric molecule present in the solution is assayed by ELISA and the difference between the amount remaining and the starting material is what has bound to the binding partner. For instance, the interaction between the protein or the chimeric molecule and an extracellular matrix protein could be determined by first coating wells of a 96 well plate with the ECM protein (e.g. fibronectin). Nonspecific binding is then blocked by incubation with a BSA solution. Following washing, a known concentration of a protein or its chimeric molecule solution is added for a defined period. The solution is then removed and assayed for the amount of protein or its chimeric molecule remaining in solution. The amount bound to the ECM protein can be determined by incubating the wells with an antibody to a protein or its chimeric molecule, then detecting with an appropriate system (either a labeled secondary antibody or by biotin-avidin enzyme complexes such as those used for ELISA). Methods for determining the amount bound to other surfaces may involve hydrolyzing a protein or its chimeric molecule from the inert implant surface, then measuring the amino acids present in the solution. The effects of a protein or a chimeric molecule thereof on cell adhesion can be assayed using one or more of the following systems. Cell adhesion to matrix (e.g. extracellular matrix components such as fibronectin, vitronectin, collagen, laminin etc.) is mediated at least in part by the integrin molecules. Integrin molecules consist of alpha and beta subunits, and the particular combinations of alpha and beta subunit give rise to the binding specificity to a particular ligand (e.g. a2bl integrin binds collagen, aSbl binds fibronectin etc). The integrins subunits have large extracellular domains responsible for binding ligand, and shorter cytoplasmic domains responsible for interaction with the cvtoskeleton. In the presence of ligand, the cytoplasmic domains are responsible for the induction of signal transduction events ("outside in signaling"). The affinity of integrins for their ligands can be modulated by extracellular signaling events that in turn lead to changes in the cytoplasmic tails of the integrins ("inside out signaling"). Incubation with a protein or chimeric molecule of the present invention can potentially alter cell adhesion in a number of ways. First, it can alter qualitatively the expression of particular integrin subsets, leading to changes in binding ability. Secondly, the amount of a particular integrin expressed may alter, leading to altered cell binding to its target matrix. Thirdly, the affinity of a particular integrin may be altered without changing its surface expression (inside-out signaling). All these changes may alter the binding of cells to either a spectrum of ligands, or alter the binding to a particular ligand. A protein or chimeric molecule of the present invention can be tested in Cell-ECM adhesion assays which are generally performed in 96 well plate. Wells are coated with matrix, then unbound sites within the wells are blocked with BSA. A defined number of cells are incubated with the coated wells, then unbound cells are washed away and the bound cells incubated in the presence or absence of the protein or the chimeric molecule thereof, The number of cells is determined by an indirect method such as MTT/MTS. Alternatively, the cells are labeled with a radioactive label (e.g. 51Cr) and a known amount of radioactivity (i.e. cells) is added to each well. The amount of bound radioactivity is determined and calculated as a percentage of the amount loaded. Cells also adhere to other cells, for instance, adhesion of one population of cells to a monolayer of another type of cells. To assay for this, the suspension cells added to the monolayer cells would be labeled with radioactivity. The cells are then incubated in the presence or absence of a protein or chimeric molecule thereof. The unbound cells would be washed away and the remaining mixed population of cells can be lysed and assayed for the amount of radioactivity present. The effects of a protein or chimeric molecule thereof on cell spreading can be assayed using one or more of the following systems. A protein or chimeric molecule of the present invention may have altered effects on cell spreading. Initiation of cell spreading is a key step in cell motility and invasive behavior. Cells spreading can be initiated in vitro in a number of ways. Plating a suspension of cells onto ECM components will result in attachment and ligand binding by integrin receptors. This initiates signal transduction events resulting in the activation of a family of the Cdc42, Rac and Rho small GTPases. Activation of these proteins results in actin polymerization and an extension of a lamellipodium, resulting hi gradual flattening of the cells and contact of more integrins with their receptors. Eventually the cells have flattened totally and formed focal adhesions (large structures containing integrins and signaling proteins). Cell spreading can also be initiated by stimulation of adherent cells with growth factors, again resulting in activation of the Cdc42/Rac/Rho proteins and lamellipodium formation. Cell spreading can be quantitated by examining a large number of cells at different time points following stimulation with a protein or chimeric molecule thereof. The area of each cell can be determined using image analysis programs and the percentage of cells spread as well as the degree of cell spreading can be compared with time. More rapid spreading may be initiated by a higher activation of the Cdc42/Rac/Kho pathways, alternatively, temporal, qualitative and quantitative differences in their activation may be observed with a protein or chimeric molecule of the present invention. This in turn may reflect differences in the signaling events induced by the protein or chimeric molecule of the present invention. The effects of a protein or a chimeric molecule thereof on cell motility, migration and invasion can be assayed using one or more of the following systems. Cells adherent to a tissue culture dish do not remain statically anchored to one spot, but rather constantly extend and retract portions of their cell body. When viewed under time-lapse photography, the cells can be observed to move around the dish, either as isolated single cells or as a cell colony. This motion may be either "random walk" (i.e. not directed in a particular direction), or directional. Both types of motion can be increased by the addition of growth factors. Time-lapse photography can be used to quantitate the overall distance covered by the cells in a given time period, as well as the overall directionality. In the case of directional migration, cells will move towards a source of chemoattractant by sensing the chemical gradient and orienting their migration machinery towards it. In many instances, the chemoattractant is a growth factor. Directional migration can be quantitated by providing a source of chemoattractant (e.g. via a thin pipette) then imaging the cells migrating towards it with time-lapse photography. An alternative system for determining directed migration is the Boyden chamber assay. In this assay, cells are placed in an upper chamber that is connected to a lower chamber via small holes in the partitioning membrane. Growth medium is put in both chambers, but chemoattractant is added only to the lower chamber, resulting in a diffusion gradient between the two chambers. The cells are attracted to the growth factor source and migrate through the holes in the separation membrane and on to the lower side of the membrane. After a number of hours, the membrane is removed and the number of cells that has migrated onto the bottom of the membrane is determined. The process of cellular invasion utilises many of the same components as migration. Cell invasion can be modeled using layers of extracellular matrix through which the cells invade. For instance, Matrigel is a mixture of basement membrane components (ECM components, growth factors etc.) that is liquid at 4 degrees but rapidly sets at 37 degrees to form a gel. This can be used to coat the upper surface of a Boyden chamber, and the chemoattractant added to the lower layer. For cells to pass onto the lower surface of the membrane, they must degrade the matrigel using enzymes such as collagenases and matrix metalloproteinases (MMPs) as well as migrating directionally towards the chemoattractant. This assay mimics the various processes required for cellular invasion. The effects of a protein or a chimeric molecule thereof on chemotaxis can be assayed using one or more of the following systems. The migration of cells toward the chemoattractant can be measured in vitro in a Boyden chamber, A protein or chimeric molecule of the present in invention is placed in the lower chamber and an appropriate target cell population is placed in the upper chamber. To mimic the in viiro process of immune cells migrating from the blood to sites of inflammation, migration through a layer of cells may be measured. Coating the upper surface of the well of the Boyden chamber with a confluent sheet of cells, for instance, epithelial, endothelial or fibroblastic cells, will prevent direct migration of immune cells through the holes in the well. Instead, the cells will need to adhere to the monolayer and migrate through it towards the protein to be tested. The presence of cells on the under surface of the Boyden chamber or in the medium in the lower well in only those wells treated with the protein or chimeric molecule thereof is indicative of the chemotactic ability of the protein or the chimeric molecule. To show that the effect is specific to a protein or chimeric molecule thereof, a neutralising antibody can be incubated with the protein in the lower chamber. Alternatively, to test the ability of a substance (chemical, protein, sugar) to prevent chemotaxis. the substance is included in the lower chamber of the Boyden chamber along with a solution containing known chemotactic ability (this may be a specific chemokine, conditioned medium from a cell source or cells secreting a range of chemokines). A susceptible target cell population is then added to the upper chamber and the assay performed as described above. The effects of a protein or chimeric molecule thereof on ligand-receptor binding can be assayed using one or more of the following systems. A protein or chimeric molecule of the present invention may have different ligand-receptor binding abilities, Ligand-receptor binding can be measured by various parameters, for instance, the dissociation constant (Kd), dissociation rate constant (off rate) (k~), association rate constant (on rate) (k4). Differences in ligand-receptor binding may correlate with different timing and activation of signaling, leading to different biological outcomes. Ligand-receptor binding can be measured and analysed by either Scatchard plot or by other means such as Biacore. For Scatchard analysis, a protein or its chimeric molecule, labeled with, for instance. radioactively labeled (eg, 125I), is incubated in the presence of differing amounts of cold competitor of a protein or its chimeric molecule, with cells, or extracts thereof, expressing the corresponding ligand or receptor. The amount of specifically bound labeled protein or its chimeric molecule is determined and the binding parameters calculated. For the Biacore. the corresponding recombinant ligand or receptor of the protein or its chimeric molecule is coupled to the detection unit. Solutions containing a protein or chimeric molecule thereof of choice are then passed over the detection cell and binding is determined by a change in the properties of the detection unit. On rates can be determined by passing solutions containing the protein or the chimeric molecule over the detection cell until a fixed reading is recorded (when the available sites are all occupied). A solution not containing the protein or the chimeric molecule is then passed over the cell and the protein dissociates from the corresponding ligand or receptor, giving the off rate. The effects of a protein or chimeric molecule thereof on receptor activation can be assayed using one or more of the following systems. Interaction with a protein or a chimeric molecule thereof and its corresponding ligand or receptor may be paralleled by differences in the signaling events induced from the cell's endogenous protein. The timing of interaction may be characteristic of a protein or chimeric molecule thereof as definitely on/off rates or dissociation constants. Activated receptors are often internalized by the cells. The receptor/ligand complex can then be dissociated (e.g., be lowering the pH within cellular vesicles, resulting in detachment of the ligand) and the receptor recycled to the cell surface. Alternatively, the complex may be targeted for destruction. In this case the receptors are effectively down-regulated and unable to generate more signal, whereas when they are recycled they are able to repeat the signaling process. Differential receptor binding or activation may result in the receptor being switched from a destruction to a recycling pathway, resulting in a stronger biological response. The effects of a protein or a chimeric molecule thereof on signal transduction can be assayed using one, or more of the following systems. Binding of ligands or receptors to the protein or its chimeric molecule thereof may initiate signaling, which may include reverse signaling, through a variety of cytoplasmic proteins. Reverse signaling occurs when a membrane-bound form of a ligand transduces a signal following binding by a soluble or membrane bound version of its receptor. Reverse signaling can also occur after binding of the membrane bound ligand by an antibody. These signaling events (including reverse signaling events) lead to changes in gene and protein expression. Hence, a protein or chimeric molecule of the present invention can induce or inhibit different signal transductions in various pathways or other signal transduction events, such as the activation of JAK/STAT pathway, Ras-erk pathway, AKT pathway, the activation of PKC, PKA, Src, Fas, TNFR, NFkB, p38MAPK, c-Fos, recruitment of proteins to receptors, receptor phosphorylation, receptor internalization, receptor cross-talk or secretion. The ligands or receptors recruited to the protein or chimeric molecule thereof may be unique to the protein or chimeric molecule of the present invention, due to different conformations of the ligand or receptors being induced. One way of assaying for these differences is to immunoprecipitate the ligand or receptor using an antibody crosslinked to sepahrose beads. Following immunoprecipitation and washing, the proteins are loaded on a 2D gel and the comparative spot patterns are analysed. Different spots can be cut out and identified by mass spectrometry. The effects of a protein or chimeric molecule thereof on up regulation and down regulation of surface markers can be assayed using one or more of the following systems. Cells may have a variety of responses to the protein or chimeric molecule of the present invention. There are a range of proteins on cell surfaces responsible for communication between the cells and the extracellular environment. Through regulated processes of endocytosis and exocytosis, various proteins are transported to and from the cell surface. Typical proteins found on the cells surface includes receptors, binding proteins, regulatory proteins and signaling molecules. Changes in expression and degradation rate of the proteins also changes the level of the proteins on the cell surface. Some proteins are also stored in intracellular reservoirs where specific signals can induce trafficking of proteins between this storage and the cellular membrane. Cells are incubated for an appropriate amount of time in medium containing a protein or chimeric molecule of the present invention, and their responses can be compared with cells exposed to the same medium without the protein or chimeric molecule of the present invention. The proteins on the cell membrane can be solubilised and separated from the cells by centrifugation. The level of expression of a specific protein can be measured by Western blotting. Cells can also be labeled with fluorescence conjugated antibodies, and visualized under confocal microscopy system or counted by fluorescence activated cell sorting (FACS). This will detect any changes in expression and distribution of proteins on the cells. By using multiple antibodies, changes in protein interaction can also be studied by confocal microscopy and immune-precipitation. Similarly, these experiments can be extended to in vivo animal models, Cells from specific part of animals treated with the protein or chimenc molecule of the present invention may be extracted and examined with identical methodologies. Cells induced to differentiate in vitro or in vivo by the addition of the protein or chimeric molecule of the present invention will express differentiation markers that distinguish them from the untreated cells. Some cells, for instance, progenitor or stem cells, can differentiate into many subpopulations, distinguishable by their surface markers. A protein or chimeric molecule of the present invention may stimulate the progenitor cells to differentiate into subgroups in a particular ratio. The protein of the present invention and its chimeric molecule may have effects upon cell repulsion. The effects of the protein or its chimeric molecule on the modulation of the growth and guidance of cells and neurons is a convenient assay for cell repulsion. Disrupting the interactions between subunits and other components of a protein leads to a way to inhibit the biological effects of the protein or its chimeric molecule. Compounds inhibiting such biological effects are identified by a number of ways. High throughput screening programs use a library of small chemical entities (chemicals or peptides) to generate lead compounds for clinical development. A number of assays can be used to screen a library compounds for their ability to affect a biologically relevant endpomt. Each potential compound in a library is tested with a particular assay in a single well, and the ability of the compound to affect the assay determined. Some examples of the assays are provided below: For this assay, cells are plated into a microtitre plate (96 plate, 384 plate or the like). The cells will have a readout mechanism for activation of a protein or chimeric molecule thereof. This may involve assaying for cell growth, assaying for stimulation of a particular pathway (e.g.. FRET based techniques), assaying for induction of a reporter gene (e.g., CAT, beta-galactosidase, fluorescent proteins), assaying for apoptosis and assaying for differentiation. Cells are then exposed to the protein or chimeric molecule of the present invention in the presence or absence of a particular small molecule. The drug can be added before, after or during the addition of the protein or chimeric molecule thereof. After an appropriate period of time, the individual wells are read using an appropriate method (eg, Fluorescence for FRET or induction of fluorescent proteins, cell number by MTT, beta-galactosidase activity etc). Control wells without addition of any drug or cytokine serve as comparisons. Any molecule able to inhibit the receptor/cytokine complex will give a different readout to the control wells, Further experiments will be required to show specificity of the inhibition. Alternatively, the drug could affect the detection method by a non-cytokine, non-receptor mechanism (a false positive). A ligand or receptor of the protein or chimeric molecule thereof is immobilised on a solid surface. A protein or its chimeric molecule and the compound to be tested are then added. This can be performed by adding a protein or its chimeric molecule first, then the compound; the compound first, then a protein or its chimeric molecule; or the compound and the protein or its chimeric molecule can be added together. Bound protein or the chimeric molecule is then detected by an appropriate detection antibody. The detection antibody can be labeled with an enzyme (e.g.. alkaline phosphatase or Horse-radish peroxidase for coiorimetric detection) or a fluorescent tag for fluorescence detection. Alternatively, a protein or its chimeric molecule can be labeled (e.g.. Biotin, radioactive labeling) and be detected with an appropriate technique (e.g., for Biotin labeling, streptavidin linked to a coiorimetric detection system, for radiolabeling the complex is solubilised and counted). Inhibition of protein binding is measured by a drop in the reading compared to the control wells. Soluble ligands or receptors of the protein or chimeric molecules thereof are bound to beads. This binding reaction can be either an adsorption process or involve chemically linking them to the plate. The beads are incubated with the protein or the chimeric molecules and a candidate compound in an appropriate well. This can be performed as the protein or the chimeric molecules first, then compound: compound first then the protein or the chimeric molecules; or compound and the protein or the chimeric molecules together. A fluorescently labeled detection antibody that recognizes a protein or chimeric molecule thereof is then added. The unbound antibody is removed and the beads are passed through FACS. The amount of fluorescence detected will decrease if a compound inhibits the interaction of a protein or chimeric molecule thereof with its receptor, To enable screening of multiple interactions between protein and its corresponding ligand/receptor against one inhibitor},' compound, the ability of the FACS machine to analyse scatter profiles is used. A bead with a larger diameter will have a different scatter profile to that of a smaller bead, and this can be separated out for analysis ("gating"). A number of different proteins, one of which is the protein or chimeric molecule of the present invention, are each linked to beads of a particular diameter. A mixture of ligands/receptors to the above-mentioned proteins are then added to the bead mixture in the presence of one candidate compound. The bound ligands/receptors are then detected using a specific secondary antibodies that is fluorescently labeled. The antibodies can be all labeled with the same detection fluorophore. The ability of the compound to prevent binding of a protein to its ligand/receptor is then determined by running the sample though a FACS machine and gating for each known bead size. The individual binding results are then analysed separately. The major benefit of this method of analysis is that the screening each compound can be tested in parallel with a number of proteins to decrease the time taken for screening proportionally. A protein or chimeric molecule thereof may also be characterised by its crystal structure. The physiochemical form of a protein or its chimeric molecule may provide a unique 3D crystal structure. In addition, the crystal structure of the protein-ligand/receptor complex may also be generated using a protein or chimeric molecule of the present invention. Since the present invention provides a protein or a chimeric molecule thereof which is substantially similar to a human naturally occurring form, the complex is likely to be a more reflective representation of the in vivo structure of the naturally occurring protein-ligand/receptor complex. Once a crystal structure has been obtained, interactions between a protein or its chimeric molecule and potential compounds inhibiting such interactions can be identified. Once potential compounds are identified by high throughput screening or from the crystal structure of the protein-ligand/receptor complex, a process of rational drug design can begin. There are several steps commonly taken in the design, of a mimetic from a compound having a given desired property. First, the particular parts of the compound that are critical and/or important in determining the desired property are determined. In the case of a peptide, this can be done by systematically varying the amino acid residues in the peptide, e.g. by substituting each residue in turn. Alanine scans of peptides are commonly used to refine such peptide motifs. These parts or residues constituting the active region of the compound are known as its "pharmacophore". Once the pharmacophore has been found, its structure is modeled according to its physical properties, e.g. stereochemistry, bonding, size and/or charge, using data from a range of sources, e.g. spectroscopic techniques, x-ray diffraction data and NMR. Computational analysis, similarity mapping (which models the charge and/or volume of a pharmacophore, rather than the bonding between atoms) and other techniques can be used in this modeling process. In a variant of this approach, the three-dimensional structure of the ligand and its binding partner are modeled. This can be especially useful where the ligand and/or binding partner change conformation on binding, allowing the model to take account of this in the design of the mimetic. Modeling can be used to generate inhibitors which interact with the linear sequence or a three-dimensional configuration. A template molecule is then selected onto which chemical groups which mimic the pharmacophore can be grafted, The template molecule and the chemical groups grafted onto it can conveniently be selected so that the mimetic is easy to synthesize, is likely to be pharmacologically acceptable, and does not degrade in vivo, while retaining the biological activity of the lead compound. Alternatively, where the mimetic is peptide-based, further stability can be achieved by cyclizing the peptide, increasing its rigidity. The mimetic or mimetics found by this approach can then be screened to see whether they have the target property, or to what extent they exhibit it. Further optimization or modification can then be earned out to arrive at one or more final mimetics for in vivo or clinical testing. The goal of rational drug design is to produce structural analogs of biologically active polypeptides of interest or of small molecules with which they interact (e.g. agonists., antagonists, inhibitors or enhancers) in order to fashion drugs which are, for example, more active or stable forms of the polypeptide, or which, e.g. enhance or interfere with the function of a polypeptide in vivo. See, e.g. Hodgson (Bio/Technology 9:19-21, 1991). In one approach, one first determines the three-dimensional structure of a protein of interest by x-ray crystallography, by computer modeling or most typically, by a combination of approaches. Usefu information regarding the structure of a polypeptide may also be gained by modeling based on the structure of homologous proteins. An example of rational drug design is the development of HIV protease inhibitors (Erickson et al. Science 249:521-533, 1990). In addition, target molecules may be analyzed by an alanine scan (Wells, Methods Enzymol 202:2699-2105, 1991), In this technique, an amino acid residue is replaced by Ala and its effect on the peptide Js activity is determined. Each of the amino acid residues of the peptide is analyzed in this manner to determine the important regions of the peptide. It is also possible to isolate a target-specific antibody, selected by a functional assay and then to solve its crystal structure. In principle, this approach yields a pharmacore upon which subsequent drug design can be based. It is possible to bypass protein crystallography altogether by generating ant'-idiotypic antibodies (anti-ids) to a functional pharmacologically active antibody. As a mirror image of a mirror images the binding site of the anti-ids would be expected to be an analog of the original receptor. The anti-id could then be used to identify and isolate peptides from banks of chemically or biologically produced banks of peptides. Selected peptides would then act as the pharmacore. In one aspect, the protein or chimeric molecule of the present invention is used as an immunogen to generate antibodies. The physiochemical form of a protein or chimeric molecule of the present invention may raise antibodies to the protein or the chimeric molecule; glycopeptides specific to the protein or chimeric molecule of the present invention: or antibodies directed to another co- or post-translationally modified peptide within the protein or chimeric molecule thereof. The protein of the present invention or its chimeric molecule may present epitopes not normally accessible (but possibly present) in vivo. For instance, there may be regions within a receptor domain that are normally in contact with another component of a heteromeric receptor. These epitopes may be used to generate monoclonal antibodies that cross react with the endogenous receptor. Such antibodies may block interaction of one receptor component with another and therefore prevent signal transduction. This may be therapeutically useful in the case of overexpression of a cytokine or receptor. The antibodies may also be therapeutically useful in diseases where the receptor is overexpressed and signals without needing the ligand. The antibodies are also useful to detect the levels of the protein or chimeric molecule thereof during the treatment of the disease (e.g.. serum levels for half-life determination). In addition, the antibodies are useful as diagnostic for determining the presence of a protein or chimeric molecule of the present invention in a particular sample. Reference to an "antibody" or "antibodies" includes reference to all the various forms of antibodies, including but not limited to: full antibodies (e.g. having an intact Fc region), including, for example, monoclonal antibodies; antigen-binding antibody fragments, including, for example, Fv, Fab, Fab' and F(ab')2 fragments; humanized antibodies; human antibodies (e.g., produced in transgenic animals or through phage display); and immunoglobulin-derived polypeptides produced through genetic engineering techniques. Unless otherwise specified, the terms "antibody" or "antibodies" and as used herein encompasses both full antibodies and antigen-binding fragments thereof. Unless stated otherwise, specificity in respect of an antibody of the present invention is intended to mean that the antibody binds substantially only to its target antigen with no appreciable binding to unrelated proteins. However, it is possible that an antibody will be designed or selected to bind to two or more related proteins. A related protein includes different splice variants or fragments of the same protein or homologous proteins from different species. Such antibodies are still considered to have specificity for those proteins and are encompassed by the present invention. The term "substantially" means in this context thai there is no detectable binding to a non-target antigen above basal, i.e. nonspecific, levels. The antibodies of the present invention may be prepared by well-known procedures. See, for example, Monoclonal Antibodies, Hybridomas: A New Dimension in Biological Analyses, Kennel et al. (eds.), Plenum Press, New York (1980); and Antibodies: A Laboratory Manual Harlow and Lane (eds.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, (1988). One method for producing an antibody of the present invention comprises immunizing a non-human animal, such as a mouse or a transgenic mouse, with a protein or chimeric molecule of the present invention, or immunogenic parts thereof, such as, for example, a peptide containing the receptor binding domain, whereby antibodies directed against the polypeptide of a protein or its chimeric molecule, or immunogenic parts thereof, are generated in the animal. Various means of increasing the antigenicity of a particular protein or its chimeric molecule, such as administering adjuvants or conjugated antigens, comprising the antigen against which an antibody response is desired and another component, are well known to those in the art and may be utilized. Immunizations typically involve an initial immunization followed by a series of booster immunizations. Animals may be bled and the serum assayed for antibody titer. Animals may be boosted until the titer plateaus. Conjugates may be made in recombinant cell culture as protein fusions. Also, aggregating agents such as alum are suitably used to enhance the immune response. Both polyclonal and monoclonal antibodies can be produced by this method. The methods for obtaining both types of antibodies are well known in the art. Polyclonal antibodies are less favored but are relatively easily prepared by injection of a suitable animal with an effective amount of a protein or chimeric molecule of the present invention, or immunogenic parts thereof, collecting serum from the animal and isolating specific antibodies to a protein or chimeric molecule thereof by any of the knownimmunoadsorbenl techniques. Antibodies produced by this technique are generally less favoured, because of the potential for heterogeneity of the product. The use of monoclonal antibodies is particularly favored because of the ability to produce them in large quantities and the homogeneity of the product. Monoclonal antibodies may be produced by conventional procedures. The term "monoclonal antibody" as used herein refers to an antibody obtained from a population of substantially homogeneous antibodies, i.e.. the individual antibodies comprising the population are identical except for possible naturally occurring mutations that may be present in minor amounts. Monoclonal antibodies are highly specific, being directed against a single antigenic site. Furthermore, in contrast to polyclonal antibody preparations which typically include different antibodies directed against different determinants (epitopes). each monoclonal antibody is directed against a single determinant on the antigen. The modifier "monoclonal" indicates the character of the antibody as being obtained from a substantially homogeneous population of antibodies, and is' not to be construed as requiring production of the antibody by any particular method. For example, the monoclonal antibodies to be used in accordance with the present invention may be made by the hybridoma method first described by Kohler ei al. Nature 256:495 (1975), or may be made by recombinant DMA methods (see, e.g., U.S. Pat. No. 4,816,567). The "monoclonal antibodies" may also be isolated from phage antibody libraries using for example, the techniques described in Clackson et al. Nature 352:624-628. 1991 and Marks era/. JMolBiol222:581-597, 1991. The present invention contemplates a method for producing a hybridoma cell line which comprises immunizing a non-human animal such as a mouse or a transgenic mouse, with a protein or chimeric molecule of the present invention; harvesting spleen cells from the immunized animal, fusing the harvested spleen cells to a myeloma cell line to generate hybridoma cells; and identifying a hybridoma cell line that produces a monoclonal antibody that binds a protein or chimeric molecule thereof.Such hybridoma cell lines and the monoclonal antibodies produced by them are encompassed by the present invention. Monoclonal antibodies secreted by the hybridoma cell lines are purified by conventional techniques. Hybridomas or the monoclonal antibodies produced by them may be screened further to identify monoclonal antibodies with particularly desirable properties, such as the ability to inhibit cytokine-signaling through its receptor. A protein or chimeric molecule thereof or immunogenic part thereof that may be used to immunize animals in the initial stages of the production of the antibodies of the present invention should be from a human-expressed source. Antigen-binding fragments of antibodies of the present invention may be produced by conventional techniques. Examples of such fragments include, but are not limited to. Fab, Fab'. F(ab')2 and Fv fragments, including single chain Fv fragments (termed sFv or scFv). Antibody fragments and derivatives produced by genetic engineering techniques, such as disulfide stabilized Fv fragments (dsFv), single chain variable region domain (Abs) molecules, minibodies and diabodies are also contemplated for use in accordance with the present invention Such fragments and derivatives of monoclonal antibodies directed against a protein or chimeric molecule thereof may be prepared and screened for desired properties, by known techniques, including the assays herein described. The assays provide the means to identify fragments and derivatives of the antibodies of the present invention that bind to a protein or chimeric molecule thereof, as well as identify those fragments and derivatives that also retain the activity of inhibiting signaling by a protein or chimeric molecule thereof. Certain of the techniques involve isolating DNA encoding a polypeptide chain (or a portion thereof) of a mAb of interest, and manipulating the DNA through recombinant DNA technology. The DNA may be fused to another DNA of interest, or altered (e.g. by mutagenesis or other conventional techniques) to add, delete, or substitute one or more amino acid residues, DNA encoding antibody polypeptides (e.g. heavy or light chain, variable region only or full length) may be isolated from B-cells of mice that have been immunized with a protein or chimeric molecule of the present invention. The DNA may be isolated using conventional procedures. Phage display is another example of a known technique whereby derivatives of antibodies may be prepared. In one approach, polypeptides that are components of an antibody of interest are expressed in any suitable recombinant expression system, and the expressed polypeptides are allowed to assemble to form antibody molecules. Single chain antibodies may be formed by linking heavy and light chain variable region (Fv region) fragments via an amino acid bridge (short peptide linker), resulting in a single polypeptide chain. Such single-chain Fvs (scFvs) have been prepared by fusing DNA encoding a peptide linker between DNAs encoding the two variable region polypeptides (VL and VH), The resulting antibody fragments can form dimers or trimers, depending on the length of a flexible linker between the two variable domains (Kortt et al. Protein Engineering 10:423, 1997). Techniques developed for the production of single chain antibodies include those described in U.S. Patent No. 4,946,778; Bird (Science 242:423, 1988), Huston er al, (Proc Natl Acad Sd USA 55:5879, 1988) and Ward et al. (Nature 334:544. 1989). Single chain antibodies derived from antibodies provided herein are encompassed by the present invention. In one embodiment, the present invention provides antibody fragments or chimeric, recombinant or synthetic forms of the antibodies that bind to the protein or chimeric molecule of the present invention and inhibit signaling by the protein or its chimeric molecule. Techniques are known for deriving an antibody of a different subclass or isotype from an antibody of interest, i.e., subclass switching. Thus. IgGl or IgG4 monoclonal antibodies may be derivec from an IgM monoclonal antibody, for example, and vice versa. Such techniques allow the preparation of new antibodies that possess the antigen-binding properties of a given antibody (the parent antibody), but also exhibit biological properties associated with an antibody isotype or subclass different from that of the parent antibody.Recombinant DNA techniques may be employed. Cloned DNA encoding particular antibody polypeptides may be employed in such procedures, e.g. DNA encoding the constant region of an antibody of the desired isotype. The monoclonal production process described above may be used in animals, for example mice, to produce monoclonal antibodies. Conventional antibodies derived from such animals, for example murine antibodies, are known to be generally unsuitable for administration to humans as they may cause an immune response. Therefore, such antibodies may need to be modified in order to provide antibodies suitable for administration to humans. Processes for preparing chimeric and/or humanized antibodies are well known in the art and are described in further detail below. The monoclonal antibodies herein specifically include "chimeric" antibodies in which the variable domain of the heavy and/or light chain is identical with or homologous to corresponding sequences in antibodies derived from a non-human species (e.g., murine), while the remainder of the chain(s) is identical with or homologous to corresponding sequences in antibodies derived from humans, as well as fragments of such antibodies, so long as they exhibit the desired biological activity (U.S. Pat. Mo. 4,816,567; and Morrison etal. Proc Nat! Acad Sci USA 57:6851-6855, 1984). "Humanized" forms of non-human (e.g., murine) antibodies are chimeric antibodies which contain minimal sequence derived from the non-human immunoglobulin. For the most part, humanized antibodies are human immunoglobulins (recipient antibody) in which the complementarity determining regions (CDRs) of the recipient are replaced by the corresponding CDRs from a non-human species (donor antibody) such as mouse, rat, rabbit or nonhuman primate having the desired properties, for example specificity, and affinity. In some instances, framework region residues of the human immunoglobulin are replaced by corresponding non-human residues. Furthermore, humanized antibodies may comprise residues which are not found in the recipient antibody or in the donor antibody. These modifications are made to further refine antibody performance. In general, the humanized antibody will comprise substantially all of at least one, and typically two. variable domains, in which all or substantially all of the complementarity determining regions correspond to those of a non-human immunoglobulin and all or substantially all of the framework region residues are those of a human immunoglobulin sequence. The humanized antibody optionally also will comprise at least a portion of an immunoglobulin constant region (Fc). typically that of a human immunoglobulin. For further details, see Jones el al. Nature 327:522-525, 1986; Reichmann et al. Nature 532:323-329, 1988; Presta: Curr Op Struct Biol 2:593-596, 1992; Liu el al Proc Nat! Acad Sci USA §4:3439, 1987: Larrick et al. Bio/Technology 7:934, 1989; and Winter and Harris, TIPS J4:139, 1993. In a further embodiment, the present invention provides an immunoassay kit with the ability to assay the level of human protein expressed from human cells present in a biological preparation, including a biological preparation comprising the naturally occurring human protein. A biological preparation which can be assayed using the immunoassay kit of the present invention includes but is not limited to laboratory samples, cells, tissues, blood, serum, plasma, urine, stool, saliva and sputum. The immunoassay kit of the present invention comprises a solid phase support matrix, not limited to but including a membrane, dipstick, bead, gel. tube or a multi-well, flat-bottomed, round-bottomed or v-bottomed microplate, for example, a 96-well microplate; a preparation of antibody directed against the human protein of interest (the capture antibody); a preparation of blocking solution (for example, BSA or casein); a preparation of secondary antibody (the detection antibody), also directed against the human protein of interest and conjugated to a suitable detection molecule (for example, alkaline phosphatase); a solution of chromagenic substrate (for example, nitro blue tetrazolium); a solution of additional substrate (for example, 5-bromo-4-chloro-3-indolyl phosphate): a stock solution of substrate buffer (for example, 0.1M Tris-HCL (pH 7.5) and 0.1M NaCl, 50mM MgCl2j; a preparation of the protein or chimeric molecule of the present invention with known concentration (the standard); and instructions for use. A suitable detection molecule may be chosen from the list consisting an enzyme, a dye, a fluorescent molecule, a chemiluminescent. an isotope or such agents as colloidal gold conjugated to molecules including, but not limited to, such molecules as staphylococcal protein A or streptococcal protein G. In a particular embodiment, the capture and detection antibodies are monoclonal antibodies, the production of which comprises immunizing a non-human animal, such as a mouse or a transgenic mouse, with a protein or chimeric molecule of the present invention, followed by standard methods, as hereinbefore described. Monoclonal antibodies may alternatively be produced by recombinant methods, as hereinbefore described and may comprise human or chimeric antibody portions or domains. In another embodiment, the capture and detection antibodies are polyclonal antibodies, the production of which comprises immunizing a non-human animal, such as a mouse, rabbit, goat or horse, with a protein or chimeric molecule of the present invention, followed by standard methods, as hereinbefore described. The components of the immunoassay kit are provided in predetermined ratios, with the relative amounts of the various reagents suitably varied to provide for concentrations in solution of the reagents that substantially maximize the sensitivity of the assay. Particularly, the reagents may be provided as dry powders, usually lyophilized, including excipients. which on dissolution provide for each reagent solution having the appropriate concentration for combining with the biological preparation to be tested. The instructions for use may detail the method for using the immunoassay kit of the present invention. For example, the instructions for use may describe the method for coating the solid phase support matrix with a prepared solution of capture antibody under suitable conditions, for example, overnight at 4°C. The instructions for use may further detail blocking non-specific protein binding sites with the prepared blocking solution; adding and incubating serially diluted sample containing the protein or chimeric protein of the present invention under suitable conditions, for example, 1 hour at 37°C or 2 hours at room temperature, followed by a series of washes using a suitable buffer known in the art, for example, a solution of 0.05% Tween 20 in 0.1M PBS (pH 7.2). In addition, the instructions ma)' provide that a preparation of detection antibody is applied followed by incubation under suitable conditions, for example, 1 hour at 37°C or 2 hours at room temperature, followed by a further series of washes. A working solution of detection buffer is prepared from the supplied detection substrate(s) and substrate buffer, then added to each well under a suitable conditions ranging from 5 minutes at room temperature to 1 hour at 37°C, The chromatogenic reaction may be halted with the addition of IN NaOH or 2N H2S-pe 3A 3B and 3C, Dubin Johnson Syndrome, Dubowitz Syndrome, Duchenne, Duchenne Muscular Dystrophy, Duchenne's Paralysis, Duhring's Disease, Duncan Disease, Duncan's Disease, Duodenal Atresia, Duodenal Stenosis, Duodenitis, Duplication 4p Syndrome, Duplication 6q Partial, Dupuy's Syndrome, Dupuytren's Contracture, Dutch-Kennedy Syndrome, Dwarfism, Dwarfism Campomelic, Dwarfism Cortical Thickening of the Tubular Bones & Transient Hypocalcemia, Dwarfism Levi's Type, Dwarfism Metatropic, Dwarfism-Onychodysp'lasia, Dwarfism-Pericarditis, Dwarfism with Renal Atrophy and Deafness, Dwarfism with Rickets, DWM, Dyggve Melchior Clausen Syndrome, Dysautonomia Familial, Dysbetalipoproteinemia Familial, Dyschondrodysplasia with Hemangiomas, Dyschondrosteosis, Dyschromatosis Universalis Hereditaria, Dysencephalia Splanchnocystica, Dyskeratosis Congenita, Dyskeratosis Congenita Autosomal Recessive, Dyskeratosis Congenita Scoggins Type, Dyskeratosis Congenita Syndrome, Dyskeratosis Follicularis Vegetans, Dyslexia, Dysmyelogenic Leukodystrophy, Dysmyelogenic Leukodystrophy-Megalobare, Dysphonia Spastica, Dysplasia Epiphysialis Punctata, Dysplasia Epiphyseal Hemimelica, Dysplasia of Nails With Hypodontia, Dysplasia Cleidocranial, Dysplasia Fibrous, Dysplasia Gigantism SyndromeX-Linked, Dysplasia Osteodental, Dysplastic Nevus Syndrome, Dysplastic Nevus Type, Dyssynergia Cerebellaris Myoclonica, Dyssynergia Esophagus. Dystonia, Dystopia Canthorum, Dystrophia Adiposogenitalis, Dystrophia Endothelialis Cornea, Dystrophia Mesodermalis, Dystrophic Epidermoiysis Bullosa, Dystrophy, Asphyxiating Thoracic, Dystrophy Myotonic, E-D Syndrome, Eagle-Barrett Syndrome, Eales Retinopathy, Eales Disease, Ear Anomalies-Contractures-Dysplasia of Bone with Kyphoscoliosis, Ear Patella Short Stature Syndrome, Early Constraint Defects, Early Hypercalcemia Syndrome with Elfin Facie, Early-onset Dystonia, Eaton Lambert Syndrome, EB, Ebstein's anomaly, EBV Susceptibility (EBVS), EBVS, BCD, ECPSG, Ectodermal Dysplasias, Ectodermal Dysplasia Anhidrotic with Cleft Lip and Cleft Palate, Ectodermal Dysplasia-Exocrine Pancreatic Insufficiency, Ectodermal Dysplasia Rapp-Hodgkin type, Ectodermal and Mesodermal Dysplasia Congenital, Ectodermal and Mesodermal Dvspiasia with Osseous Involvement, Ectodermosis Erosiva Pluriorificialis, Ectopia Lentis, Ectopia Vesicae, Ectopic ACTH Syndrome, Ectopic Adrenocorticotropic Hormone Syndrome. Ectopic Anus. Ectrodactilia of the Hand, Ectrodactyly, Ectrodactyly-Ectodermal Dysplasia-Clefting Syndrome, Ectrodactyly Ectodermal Dysplasias Clefcing Syndrome, Ectrodactyly Ectoderma] Dysplasia Cleft Lip/Cleft Palate, Eczema, Eczema-Thrombocytopenia-Immunodeficiency Syndrome, EDA, EDMD, EDS, EDS Arterial- Ecchymotic Type, EDS Arthrochalasia, EDS Classic Severe Form, EDS Dysfibronectinemic, EDS Gravis Type, EDS Hypermobility, EDS Kyphoscoliotic, EDS Kyphoscoliosis, EDS Mitis Type, EDS Ocular-Scoliotic, EDS Progeroid, EDS Periodontosis, EDS Vascular, EEC Syndrome, EFE, EHBA, EHK, Ehlers Danlos Syndrome, Ehlers-Danlos syndrome, Ehlers Danlos IX, Eisenmenger Complex, Eisenmenger's complex, Eisenmenger Disease, Eisenmenger Reaction, Eisenmenger Syndrome, Ekbom Syndrome, Ekman-Lobstein Disease, Ektrodactyly of the Hand. EKV, Elastin fiber disorders, Elastorrhexis Generalized, Elastosis Dystrophica Syndrome, Elective Mutism (obsolete), Elective Mutism, Electrocardiogram (ECG or EKG), Electron Transfer Flavoprotein (ETF) Dehydrogenase Deficiency: (GAII & MAJDD), Electrophysiologic study (EPS), Elephant Nails From Birth, Elephantiasis Congenita Angiomatosa, Hemangiectatic Hypertrophy, Elfin Facies with Hypercalcemia, Ellis-van Creveld Syndrome, Ellis Van Creveld Syndrome, Embryoma Kidney, Embryonal Adenomyosarcoma Kidney, Embryonal Carcinosarcoma Kidney, Embryonal Mixed Tumor Kidney. EMC. Emery Dreyfus Muscular Dystrophy, Emery-Dreifuss Muscular Dystrophy, Emery-Dreifuss Syndrome, EMF, EMG Syndrome, Empty Sella Syndrome, Encephalitis Periaxialis Diffusa, Encephalitis Periaxialis Concentrica, Encephalocele, Encephalofacia) Angiomatosis, Encephalopathy. Bncephalotrigeminal Angiomatosis, Enchondromatosis with Multiple Cavernous Hemangiomas, Endemic Polyneuritis, Endocardial Cushion Defect, Endocardial Cushion Defects, Endocardial Dysplasia, Endocardial Fibroelastosis (EFE), Endogenous Hypertriglyceridemia, Endolymphatic Hydrops, Endometrial Growths, Endometriosis, Endomyocardial Fibrosis, Endothelial Cornea! Dystrophy Congenital, Endothelial Epithelial Cornea! Dystrophy, Endothelium, Engelmann Disease, Enlarged Tongue, Entero colitis, Enterocyte Cobalamin Malabsorption, Eosinophia Syndrome, Eosinophilic Cdlulitis, Eosinophilic Fasciitis, Eosinophilic Granuloma, Eosinophilic Syndrome, Epidermal Nevus Syndrome, Epideraiolysis Bullosa, Epidermolysis Bullosa Acquisita, Epidermolysis Bullosa Hereditaria, Epidermolysis Bullosa Letalias, Epidermolysis Hereditaria Tarda, Epidermolytic Hyperkeratosis. Epidermolytic Hyperkeratosis (Bullous CJE), Epilepsia Procursiva, Epilepsy, Epinephrine. Epiphyseal Changes and High Myopia, Epiphyseai Osteochondroma Benign, Epiphysealis Hemimelica Dysplasia, Episodic-Abnormal Eye Movement, Epithelial Basement Membrane Cornea! Dystrophy, Epithelial Cornea! Dystrophy of Meesmarin Juvenile, Epitheliomatosis Multiplex with Nevus, Epithelium, Epival, EPS. Epstein-Barr Virus-Induced Lymphoproliferative Disease in Males, Erb-Goldflam syndrome, Erdheim Chester Disease, Erythema Multiforme Exudativum, Erythema Polymorphe Stevens Johnson Type, Erythroblastophthisis, Erythroblastosis Fetalis, Erythroblastosis Neonatorum, Erythroblastotic Anemia of Childhood, Erythrocyte Phosphoglycerate Kinase Deficiency. Erythrogenesis Imperfecta, Erythrokeratodermia Progressive Symmetrica, Erythrokeratodermia Progressive Symmetrica Ichthyosis, Erythrokeratodermia Variabilis, Erythrokeratodermia Variabilis Type, Erythrokeratolysis Hiemalis, Erythropoietic Porphyrias, Erythropoietic Porphyria, Escobar Syndrome, Esophagea) Atresia, Esophageal Aperistalsis, Esophagitis-Peptic Ulcer, Esophagus Atresia and/or Tracheoesophageal Fistula. Essential Familial Hyperlipemia, Essential Fructosuria, Essential Hematuria, Essential Hemorrhagic Thrombocythemia, Essential Mixed Cryoglobulinemia. Essential Moschowitz Disease, Essential Thrombocythemia, Essential Thrombocytopenia, Essential Thrombocytosis, Essential Tremor, Esterase Inhibitor Deficiency, Estren-Dameshek variant of Fanconi Anemia, Estrogen-related Cholestasis, ET, ETF, Ethylmalonic Adipicaeiduria, Eulenburg Disease, pc, EVCS, Exaggerated Startle Reaction, Exencephaly, Exogenous Hypertriglyceridemia, Ex omphalos-Macro glossia-Gigantism Syndrom, Exophthalmic Goiter, Expanded Rubella Syndrome, Exstrophy of the Bladder, EXT, External Chondromatosis Syndrome, Extrahepatic Biliary Atresia, Extramedullary Plasmacytoma, Exudative Retinitis, Eye Retraction Syndrome, FA1, FAA, Fabry Disease, FAC, FACE, FACD, FACE, FACF, FACG, FACH, Facial Nerve Palsy, Facial Paralysis, Facial Ectodermal Dysplasias, Facial Ectodermal Dysplasia, Facio-Scapulo-Humeral Dystrophy, Facio-Auriculo-Vertebral Spectrum, Facio-cardio-cutaneous syndrome, Facio-Fronto-Nasa] Dysplasia, Faciocutaneoskeletal Syndrome, Faciodigitogenital syndrome, Faciogenital dysplasia, Faciogenitopopliteal Syndrome, Faciopalatoosseous Syndrome, Faciopalatoosseous Syndrome Type n, Facioscapulohumeral muscular dystrophy, Factitious Hypoglycemia, Factor VIII Deficiency, Factor IX Deficiency, Factor XI Deficiency, Factor XH deficiency, Factor XIII Deficiency, Fahr Disease, Fahr's Disease, Failure of Secretion Gastric Intrinsic Factor, Fairbank Disease, Pallet's Tetralogy, Familial Acrogeria, Familial Acromicria, Familial Adenomatous Colon Polyposis, Familial Adenomatous Polyposis with Extraintestinal Manifestations, Familial Alobai Holoprosencephaly, Familial Alpha-Lipoprotein Deficiency, Familial Amyotrophic Chorea with Acanthocytosis, Familial Arrhythmic Myoclonus, Familial Articular Chondrocalcinosis, Familial Atypical Mole-Malignant Melanoma Syndrome, Familial Broad Beta Disease, Familial Calcium Gout, Familial Calcium Pyrophosphate Arthropathy, Familial Chronic Obstructive Lung Disease, Familial Continuous Skin Peeling, Familial Cutaneous Amyloidosis, Familial Dysproteinemia, Familial Emphysema, Familial Enteropathy Microvillus, Familial Foveal Retinoschisis, Familial Hibernation Syndrome, Familial High Cholesterol, Familial Hemochromatosis, Familial High Blood Cholesterol, Familial High-Density Lipoprotein Deficiency, Familial High Serum Cholesterol. Familial Hyperlipidema, Familial Hypoproteinemia with Lymphangietatic Enteropathy, Familial Jaundice, Familial Juvenile Nephronophtisis-Associated Ocular Anomaly. Familial Lichen Amyloidosis (Type IX), Familial Lumbar Stenosis, Familial Lymphedema Praecox, Familial Mediterranean Fever, Familial Multiple Polyposis, Familial Nuchal Bleb, Familial Paroxysmal Polyserositis, Familial Polyposis Coli, Familial Primary Pulmonary Hypertension, Familial Renal Glycosuria, Familial Splenic Anemia, Familial Startle Disease, Familial Visceral Amyloidosis (Type VET), FAMMM, FANCA; FANCB, FANCC, FANCD, FANCE, Fanconi Panmyelopathy, Fanconi Pancytopenia. Fanconi II, Fanconi's Anemia, Fancoci's Anemia Type I, Fanconi's Anemia Complementation Group, Fanconi's Anemia Complementation Group A, Fanconi's Anemia Complementation Group B, Fanconi's Anemia Complementation Group C, Fanconi's Anemia Complementation Group D, Fanconi's Anemia Complementation Group E, Fanconi's Anemia Complementation Group G, Fanconi's Anemia Complementation Group H, Fanconi's Anemia Estren-Dameshek Variant, FANF, FANG, FANH, FAP, FAPG, Farber's Disease, Farber's Lipogranulomatosis, FAS, Fasting Hypoglycemia, Fat-Induced Hyperlipemia, Fatal Granulomatous Disease of Childhood, Fatty Oxidation Disorders, Fatty Liver with Encephalopathy, FAV, FCH, FCMD, PCS Syndrome, FD, FDH, Febrile Mucocutaneous Syndrome Stevens Johnson Type, Febrile Neutrophilic Dermatosis Acute, Febrile Seizures, Feinberg's syndrome, Feissinger-Leroy-Reiter Syndrome, Female Pseudo-Turner Syndrome, Femoral Dysgenesis Bilateral-Robin Anomaly, Femora] Dysgenesis Bilateral, Femoral Facial Syndrome, Femoral Hypoplasia-Unusual Facies Syndrome, Fetal Alcohol Syndrome, Fetal Anti-Convulsant Syndrome, Fetal Cystic Hygroraa. Fetal Effects of Alcohol, Fetal Effects of Chickenpox, Fetal Effects of Thalidomide, Fetal Effects of Varicella Zoster Virus, Fetal Endomyocardial Fibrosis, Fetal Face Syndrome, Fetai Iritis Syndrome, Fetal Transfusion Syndrome, Fetal Valproate Syndrome, Fetai Valproic Acid Exposure Syndrome, Fetal Varicella Infection,, Fetal Varicella Zoster Syndrome, FFDD Type II, FG Syndrome, FGDY, FHS, Fibrin Stabilizing Factor Deficiency, Fibrinase Deficiency, Fibrinoid Degeneration of Astrocytes, Fibrinoid Leukodystrophy, Fibrinoligase Deficiency, Fibroblastoma Perineural, Fibrocystic -Disease of Pancreas, Fibrodysplasia Ossificans Progressiva. Fibroelastic Endocarditis, Fibromyalgia, Fibromyalgia-Fibromyositis, Fibromyositis, Fibrosing Cholangitis, Fibrositis, Fibrous Ankylosis of Multiple Joints, Fibrous Cavernositis, Fibrous Dysplasia, Fibrous Plaques of the Penis, Fibrous Sclerosis of the Penis, Fickler-Winkler Type, Fiedler Disease, Fifth Digit Syndrome, Filippi Syndrome, Finnish Type Amyloidosis (Type V), First Degree Congenital Heart Block. First and Second Branchial Arch Syndrome, Fischer's Syndrome, Fish Odor Syndrome, Fissured Tongue, Flat Adenoma Syndrome, Flatau-Schilder Disease, Flavin Containing Monooxygenase 2, Floating Beta Disease, Floating-Harbor Syndrome, Floating Spleen, Floppy Infant Syndrome, Floppy Valve Syndrome, Fluent aphasia, FMD, FMF, FMO Adult Liver Form, FM02, FND, Focal Brain Ischemia, Focal Dermal Dysplasia Syndrome, Focal Dermal Hypoplasia, Focal Dermato-Phalangeal Dysplasia, Focal Dystonia, Focal Epilepsy, Focal Facial Dermal Dysplasia Type II, Focal Neuromyotonia, FODH, Foiling Syndrome, Fong Disease, FOP, Forbes Disease, Forbes-Albright Syndrome, Forestier's Disease, Forsius-Eriksson Syndrome (X-Linked). Fothergill Disease, Fountain Syndrome, Foveal Dystrophy Progressive, FPO Syndrome Type II, FPO, Fraccaro Type Achondrogenesis (Type IB), Fragile X syndrome, Franceschetti-Zwalen-KJein Syndrome, Francois Dyscephaly Syndrome, Francois-Neetens Speckled Dystrophy, Flecked Corneal Dystrophy, Fraser Syndrome, FRAXA, FRDA, Fredrickson Type 1 Hyperlipoproteinemia, Freeman-Sheldon Syndrome, Freire-Maia Syndrome, Prey's Syndrome, Friedreich's Ataxia, Friedreich's Disease, Friedreich's Tabes. FRNS, Froelich's Syndrome, Frommel-Chiari Syndrome, Frommel-Chiari Syndrome Lactation-Uterus Atrophy, Frontodigital Syndrome, Frontofacionasal Dysostosis, Fromofacionasal Dysplasia, Frontonasal Dysplasia, Frontonasal Dysplasia with Corona] Craniosynostosis, Fructose-1-Phosphate Aldolase Deficiency, Fructosemia, Fructosuria, Fryns Syndrome, FSH, FSHD, FSS, Fuchs Dystrophy, Fucosidosis Type 1, Fucosidosis Type 2, Fucosidosis Type 3, Fukuhara Syndrome, Fukuyama Disease, Fukuyama Type Muscular Dystrophy, Fumarylacetoacetase deficiency, Furrowed Tongue, G Syndrome, G6PD Deficiency, G6PD, GA 1, GA IIB, GA IIA, GA II, GAD & MADD, Galactorrhea-Amenorrhea Syndrome Nonpuerperal, Galactorrhea-Amenorrhea without Pregnancy, Galactosamine-6-Sulfatase Deficiency, Galactose-] -Phosphate Uridyl Transferase Deficiency, Galactosemia, GALB Deficiency, Galloway-Mowat Syndrome, Galloway Syndrome, GAIT Deficiency, Gammaglobulin Deficiency, GAN, Ganglioside Neuraminidase Deficiency, Ganglioside Sialidase Deficiency, Gangliosidosis GM1 Type 1, Gangliosidosis GM2 Type 2, Gangliosidosis Beta Hexosaminidase B Defeciency, Gardner Syndrome, Gargoylism, Garies-Mason Syndrome, Gasser Syndrome, Gastric Intrinsic Factor Failure of Secretion, Enterocyte Cobalamin, Gastrinoma, Gastritis, Gastroesophageal Laceration-Hemorrhage. Gastrointestinal Polyposis and Ectodermal Changes, Gastrointestinal ulcers, Gastroschisis, Gaucher Disease, Gaucher-Schlagenhaufen Gayet-Wemicke Syndrome, GBS, GCA, GCM Syndrome, GCPS, Gee-Herter Disease, Gee-Thaysen Disease, Gehrig's Disease, Gelineau's Syndrome, Genee-Wiedemann Syndrome, Generalized Dystonia, Generalized Familial Neuromyotonia, Generalized Fibromatosis, Generalized Flexion Epilepsy, Generalized Glycogenosis, Generalized Hyperhidrosis, Generalized Lipofuscinosis, Generalized Myasthenia Gravis, Generalized Mvotonia, Generalized Sporadic Neuromytonia, Genetic Disorders, Genital Defects, Genital and Urinary Tract Defects, Gerstmann Syndrome, Gerstmann Tetrad, GHBP, GHD. GHR, Giant Axonal Disease. Giant Axonal Neuropathy, Giant Benign Lymphoma, Giant Cell Glioblastoma Astrocytoma, Giant Cell Arteritis, Giant Cell Disease of the Liver, Giant Ceil Hepatitis, Giant Cell of Newborns Cirrhosis, Giant Cyst of the Retina, Giant Lymph Node Hyperplasia, Giant Platelet Syndrome Hereditary, Giant Tongue, gic MacuJar Dystrophy, Gilbert's Disease, Gilbert Syndrome, Gilbert-Dreyfus Syndrome, Gilbert-Lereboullet Syndrome, Gilford Syndrome, Gilles de la Tourette's syndrome, Gillespie Syndrome, Gingival Fibromatosis-Abnormal Fingers Nails Nose Ear Splenomegaly, GLA Deficiency, GLA, GLB1, Glaucoma, Glioma Retina, Global aphasia, Globoid Leukodystrophy, Glossoptosis Micrognathia and Cleft Palate, Glucocerebrosidase deficiency, Glucocerebrosidosis, Glucose-6-Phosphate Dehydrogenase Deficiency, G!ucose-6-Phosphate Tranpon Defect, Glucose-6-Phospate Translocase Deficiency, Glucose-G-Phosphatase Deficiency, Glucose-Galactose Malabsorption, Glucosyl Ceramide Lipidosis, Glutaric Aciduria I. Glutaric Acidemia I, Glutaric Acidemia II, Glutaric Aciduria II. Glutaric Aciduria Type II, Glutaric Aciduria Type III, Glutaricacidemia I, Glutaricacidemia II. Glutaricaeiduria I, Glutaricaciduria II, Glutaricaciduria Type IIA, Glutaricaciduria Type IIB, Glutaryl-CoA Dehydrogenase Deficiency, Glutaurate-Aspartate Transport Defect, Gluten-Sensitive Enteropathy, Glycogen Disease of Muscle Type VII, Glycogen Storage Disease I, Glycogen Storage Disease III, Glycogen Storage Disease TV7, Glycogen Storage Disease Type V, Glycogen Storage Disease VI. Glycogen Storage Disease VE, Glycogen Storage Disease VIII, Glycogen Storage Disease Type H, Glycogen Storage Disease-Type II, Glycogenosis, Glycogenosis Type I, Glycogenosis Type IA, Glycogenosis Type IB, Glycogenosis Type II, Glycogenosis Type II, Glycogenosis Type III, Glycogenosis Type IV, Glycogenosis Type V. Glycogenosis Type VI, Glycogenosis Type VII, Glycogenosis Type VIII, Glycolic Aciduria, Glycolipid Lipidosis, GM2 Gangliosidosis Type 1, GM2 Gangliosidosis Type 1, GNPTA, Goitrous Autoimmune Thyroiditis, Goldenhar Syndrome, Goldenhar-Gorlin Syndrome, Goldscheider's Disease, Goltz Syndrome, Goltz-Gorlin Syndrome, Gonadal Dysgenesis 45 X, Gonadal Dysgenesis XO, Goniodysgenesis-Hypodontia, Goodman Syndrome. Goodman, Goodpastare Syndrome, Gordon Syndrome, Gorlin's Syndrome, Gorlin-Chaudhry-Moss Syndrome, Gottron Erythrokeratodermia Congenitalis Progressiva Symmetrica, Gottron's Syndrome, Gougerot-Carteaud Syndrome, Grand Mai Epilepsy, Granular Type Corneal Dystrophy, Granulomatous Arteritis, Granulomatous Colitis, Granulomatous Dermatitis with Eosinophilia, Granulomatous Ileitis, Graves Disease, Graves' Hyperthyroidism, Graves' Disease, Greig Cephalopolysyndactyiy Syndrome, Groenouw Type I Comeal Dystrophy, Groenouw Type II Corneal Dystrophy, Gronblad-Strandberg Syndrome, Grotton Syndrome, Growth Hormone Receptor Deficiency, Growth Hormone Binding Protein Deficiency, Growth Hormone Deficiency, Growth-Mental Deficiency Syndrome of Myhre, Growth Retardation-Rieger Anomaly, GRS, Gruber Syndrome, GS, GSD6, GSD8, GTS, Guanosine Triphosphate-Cyclohydrolase Deficiency, Guanosine Triphosphate-Cyclohydrolase Deficiency, Guenther Porphyria, Guerin-Stern Syndrome, Guillain-Barre, Guillain-Barre Syndrome, Gunther Disease, H Disease, H, Gottron's Syndrome, Habit Spasms, HAE, Hageman Factor Deficiency. Hageman factor, Haim-Munk Syndrome, Hajdu-Cheney Syndrome. Hajdu Cheney, HAL Deficiency, Hall-Pallister Syndrome, Hallermarm-Streiff-Francois syndrome. Hallermann-Streiff Syndrome, Hallervorden-Spatz Disease, Hallervorden-Spatz Syndrome. Hallopeau-Siemens Disease, Hallux Duplication Postaxial Polydactyly and Absence of Corpus Callosum, Halushi-Behcet's Syndrome, Hamartoma of the Lymphatics, Hand-Schueller-Christian Syndrome, HANE, Hanhart Syndrome, Happy Puppet Syndrome, Harada Syndrome, HARD +/-E Syndrome, HARD Syndrome, Hare Lip, Harlequin Fetus, Harlequin Type DOC 6, Harlequin Type Ichthyosis, Harley Syndrome, Harrington Syndrome, Hart Syndrome, Hartnup Disease, Hartnup Disorder, Hartnup Syndrome, Hashimoto's Disease, Hashimoto-Pritzker Syndrome, Hashimoto's Syndrome, Hashimoto's Thyroiditis, Hashimoto-Pritzker Syndrome, Hay Well's Syndrome, Hay-Wells Syndrome of Ectodermal Dysplasia, HCMM, HCP, HCTD, HD, Heart-Hand Syndrome (Holt-Oram Type). Heart Disease, Hecht Syndrome, HED, Heerferdt-Waldenstrorn and Lofgren's Syndromes., Hegglin's Disease, Heinrichsbauer Syndrome, Hemangiomas, Hemangioma Familial, Hemangioma-Thrombocytopenia Syndrome, Hemangiomatosis Chondrodystrophica, Hemangiomatous Bronchial Clefts-Lip Pseudocleft Syndrome, Hemifacial Microsomia, Hemimegalencephaly, Hemip-aresis of Cerebral Palsy, Hemipiegia of Cerebral Palsy, Hemisection of the Spinal Cord, Hemochromatosis, Hemochromatosis Syndrome, Hemodialysis-Related Amyloidosis, Hemoglobin Lepore Syndromes, Hemolytic Anemia of Newborn, Hemolytic Cold Antibody Anemia, Hemolytic Disease of Newborn, Hemoiytic-Uremic Syndrome, Hemophilia, Hemophilia A, Hemophilia B, Hemophilia B Factor DC, Hemophilia C, Hemorrhagic Dystrophic Thrombocytopenia, Hemorrhagica Aleukia, Hemosiderosis, Hepatic Fructokinase Deficiency, Hepatic Phosphorylase Kinase Deficiency, Hepatic Porphyria, Hepatic Porphyrias, Hepatic Veno-Occlusive Diseas, Hepatitis C, Hepato-Renal Syndrome, Hepatolenticular Degeneration, Hepatophosphorylase Deficiency, Hepatorenal Glycogenosis, Hepatorenal Syndrome, Hepatorenal Tyrosinemia, Hereditary Acromelalgia, Hereditary Alkaptonuria, Hereditary Amyloidosis, Hereditary Angioedema, Hereditary Areflexic Dystasia, Heredopathia Atactica Polyneuritiformis, Hereditary Ataxia, Hereditary Ataxia Friedrich's Type, Hereditary Benign Acanthosis Nigricans, Hereditary Cerebellar Ataxia, Hereditary Chorea, Hereditary Chronic Progressive Chorea, Hereditary1 Connective Tissue Disorders, Hereditary Coproporphyria, Hereditary Coproporphyria Porphyria, Hereditary Cutaneous Malignant Melanoma, Hereditary Deafness-Retinitis Pigmemosa, Heritable Disorder of Zinc Deficiency, Hereditary DNS, Hereditary Dystopic Lipidosis, Hereditary Emphysema, Hereditary Fructose Intolerance, Hereditary Hemorrhagic Telangiectasia, Hereditary Hemorrhagic Telangiectasia Type I, Hereditary Hemorrhagic Telangiectasia Type II, Hereditary Hemorrhagic Telangiectasia Type III, Hereditary Hyperuricemia and Choreoathetosis Syndrome, Hereditary Leptocytosis Major, Hereditary Leptocytosis Minor, Hereditary' Lymphedema, Hereditary Lymphedema Tarda, Hereditan,' Lymphedema Type I, Hereditary Lymphedema Type II, Hereditary Motor Sensor}' Neuropathy, Hereditary Motor Sensory Neuropathy I, Hereditary Motor Sensory Neuropathy Type III, Hereditary Nephritis, Hereditary Nephritis and Nerve Deafness, Hereditan' Nephropathic Amyloidosis, Hereditary Nephropathy and Deafness, Hereditary Nonpolyposis Colorectal Cancer, Hereditary Nonpolyposis Colorectal Carcinoma, Hereditan,' Nonspherocytic Hemolytic Anemia, Hereditary Onychoosteodysplasia, Hereditary Optic Neuroretinopathy, Hereditary Polyposis Coli, Hereditary Sensory and Autonomic Neuropathy Type I, Hereditary Sensory and Autonomic Neuropathy Type II, Hereditary Sensory and Autonomic Neuropathy Type III, Hereditary Sensor,' Motor Neuropathy, Hereditary Sensory Neuropathy type I, Hereditary Sensory Neuropathy Type I, Hereditary Sensory Neuropathy Type II, Hereditary Sensory Neuropathy Type HI, Hereditary Sensory Radicular Neuropathy Type I, Hereditary Sensor)' Radicular Neuropathy Type I, Hereditary Sensory Radicular Neuropathy Type EL, Hereditary Site Specific Cancer, Hereditary Spherocytic Hemolytic Anemia, Hereditary Spherocytosis, Hereditary Tyrosinemia Type 1, Heritable Connective Tissue Disorders, Herlitz Syndrome. Hermans-Herzberg Phakomatosis, Hermansky-Pudlak Syndrome, Hermaphroditism, Herpes Zoster, Herpes Iris Stevens-Johnson Type, Hers Disease, Heterozygous Beta Thalassemia, Hexoaminidase Alpha-Subunit Deficiency (Variant B), Hexoaminidase Alpha-Subunit Deficiency (Variant B), HFA, HFM, HGPS, HH, HHHO, HHRH, HHT. Hiatal Hernia-Microcephaly-Nephrosis Galloway Type, Hidradenitis Suppurativa, Hidrosadenitis Axillaris, Hidrosadenitis Suppurativa, Hidrotic Ectodermal Dysplasias, HIE Syndrome, High Imperfbrate Anus, High Potassium, High Scapula, HIM, Hirschsprung's Disease, Hirschsprung's Disease Acquired, Hirschsprung Disease Polydactyly of Ulnar & Big Toe and VSD, Hirschsprung Disease with Type D Brachydactyly, Hirsutism, HIS Deficiency, Histidine Ammonia-Lyase (HAL) Deficiency, Histidase Deficiency, Histidinemia, Histiocytosis. Histiocytosis X, HLHS, HLP Type II, HMG, HMI, HMSN I, HNHA, HOCM, Hodgkin Disease, Hodgkin's Disease, Hodgkin's Lymphoma, Hollaender-Simons Disease, Holmes-Adie Syndrome, Holocarboxylase Synthetase Deficiency, Holoprosencephaly, Holoprosencephaly Malformation Complex, Holoprosencephaiy Sequence, Holt-Oram Syndrome, Holt-Oram Type Heart-Hand Syndrome, Homocystinemia, Homocystinuria, Homogentisic Acid Oxidase Deficiency, Homogentisic Acidura, Homozygous Alpha-]-Antitrypsin Deficiency, HOOD, Homer Syndrome, Horton's disease, HOS, HOS], Houston-Hams Type Achrondrogenesis (Type 1A), HPS, HRS, HS, HSAN Type I, HSAN Type II, HSAN-H1, HSMN, HSMN Type HI, HSN 1, HSN-III, Huebner-Herter Disease, Hunner's Patch, Hunner's Ulcer, Hunter Syndrome, Hunter-Thompson Type Acromesomelic Dysplasia, Huntington's Chorea, Huntington's Disease, Hurler Disease, Hurler Syndrome, HurJer-Scheie Syndrome, HUS, Hutchinson-Gilford Progeria Syndrome, Hutchinson-Gilford Syndrome, Hutchinson-Weber-Peutz Syndrome, Hutterite Syndrome Bowen-Conradi Type, Hyaline Parmeuropathy. Hydranencephaly, Hydrocephalus, Hydrocephalus Agyria and Retinal Dysplasia, Hydrocephalus Internal Dandy-Walker Type, Hydrocephalus Noncommunicating Dandy-Walker Type. Hydrocephaiy, Hydronephrosis With Peculiar Facial Expression. Hydroxylase Deficiency, Hygroma Colli, Hyper-IgE Syndrome, Hyper-IgM Syndrome, Hyperaidosteronism, Hyperaidosteronism With Hypokalemic Alkatosis, Hyperaidosteronism Without Hypertension, Hyperammonemia, Hyperammonemia Due to Carbamylphosphate Synthetase Deficiency, Hyperammonemia Due to Ornithine Transcarbamylase Deficiency, Hyperammonemia Type II, Hyper-Beta Camosinemia, Hyperbilirubinemia I. Hyperbilirubinemia II, Hypercalcemia Familial with Nephrocalcinosis and Indicanuria, Hypercalcemia-Supravalvar Aortic Stenosis, Hypercalciurie Rickets, Hypercapnic acidosis, Hypercatabolic Protein-Losing Enteropathy, Hyperchloremic acidosis, Hypercholesterolemia, Hypercholesterolemia Type IV, Hyperchylomicronemia, Hypercystinuria, Hyperekplexia, Hyperextensible joints, Hyperglobulinemic Purpura, Hyperglychiemia with Ketoacidosis and Lactic Acidosis Propionic Type, Hyperglycinemia Nonketotic, Hypergonadotropic Hypogonadism, Hyperimmunoglobulin E Syndrome, Hyperimmunoglobulin E-Recurrent Infection Syndrome, HvperimmunogJobulinemia E-Staphylococcal, Hyperkalemia, Hyperkinetic Syndrome, Hyperlipemic Retinitis, Hyperlipidemia I, Hyperlipidernia IV, Hyperlipoproteinemia Type I. Hyperlipoprotememia Type IE, Hyperllpoproteinemia Type IV, Hyperoxaluria, Hyperphalang)'-Clinodactyly of Index Finger with Pierre Robin Syndrome, Hyperphenylalanemia, Hyperplastic Epidermolysis Bullosa, Hyperpnea, Hyperpotassemia, Hyperprebeta-Lipoproteinemia, Hj'perprolinemia Type I, Hyperprolinemia Type II, Hypersplenism, Hypertelorism with Esophagea] Abnormalities and Hypospadias, Hypertelorism-Hypospadias Syndrome, Hypertrophic Cardio myopathy, Hypertrophic Interstitial Neuropathy, Hypertrophic Interstitial Neuritis, Hypertrophic Interstitial Radiculoneuropathy, Hypertrophic Neuropathy of Refsum, Hypertrophic Obstructive Cardio rnyopathy, Hyperuricemia Choreoathetosis Self-multilation Syndrome, Hyperuricemia-OIigophrenia, Hypervalinemia, Hypocalcified (Hypomineralized) Type, Hypochondrogenesis, Hypochrondroplasia, Hypogamrnaglobulinemia, Hypogammaglobulinemia Transient of Infancy, Hypogenital Dystrophy with Diabetic Tendency, Hypoglossia-Hypodactylia Syndrome, Hypoglycemia, Exogenous HypogJycemia, Hypoglycemia with Macroglossia, Hypoglycosylation Syndrome Type la, Hypoglycosylation Syndrome Type la, Hypogonadism with Anosmia, Hypogonadotropic Hypogonadism and Anosmia, Hypohidrotic Ectodermal Dysplasia, Hypohidrotic Ectodermal Dyspiasia Autosomal Dominant type, Hypohidrotic Ectodermal Dysplasias Autorecessive, Hypokalemia, Hypokalemic Alkalosis with Hypercalciuria, Hypokalemic Syndrome, Hypolactasia, Hypomaturation Type (Snow-Capped Teeth), Hypomelanosis of Ito, Hypomelia-Hypotrichosis-Facial Hemangioma Syndrome, Hypomyelination Neuropath}1, Hypoparathyroidism, Hypophosphatasia, Hypophosphatemic Rickets with Hypercalcemia, Hypopigmentation, Hypopigmented macular lesion, Hypoplasia of the Depressor Anguli Oris Muscle with Cardiac Defects, Hypoplastic Anemia, Hypoplastic Congenita] Anemia, Hypoplastic Chondrodystrophy, Hypoplastic Enamel-Onycholysis-Hypohidrosis. Hypoplastic (Hypoplastic-Explastic) Type, Hypoplastic Left Heart Syndrome. Hypoplastic-Triphalangeal Thumbs, Hypopotassemia Syndrome, Hypospadias-Dysphagia Syndrome, Hyposmia, Hypothalamic Hamartoblastoma Hypopituitarism Imperforate Anus Polydactyly, Hypothalamic Infantilism-Obesity, Hypothyroidism, Hypotonia-Hypomentia-Hypogonadism-Obesity Syndrome, Hypoxanthine-Guanine Phosphoribosyltranferase Defect (Complete Absense of), I-Cell Disease, latrogenic Hypoglycemia., IBGC, IBIDS Syndrome, IBM, IBS, 1C, I-Cell Disease, ICD, ICE Syndrome Cogan-Reese Type, Icelandic Type Amyloidosis (Type VI), I-Cell Disease, Ichthyosiform Erythroderma Corneal Involvement and Deafness, Ichthyosiform Erythroderma Hair Abnormality Growth and Men, Ichthyosiform Erythroderma with Leukocyte Vacuolation, Ichthyosis, Ichthyosis Congenita, Ichthyosis Congenital with Trichothiodystrophy., Ichthyosis Hystrix, Ichthyosis Hystrix Gravior, Ichthyosis Linearis Circumflexa, Ichthyosis Simplex, Ichthyosis Tay Syndrome, Ichthyosis Vulgaris, Ichthyotic Neutral Lipid Storage Disease, Icteric Leptospirosis, Icterohemorrhagic Leptospirosis. Icterus (Chronic Familial), Icterus Gravis Neonatorum, Icterus Intermittens Juvenalis, Idiopathic Alveolar Hypoventilation, Idiopathic Amyloidosis, Idiopathic Arteritis of Takayasu, Idiopathic Basal Ganglia Calcification (IBGC), Idiopathic Brachial Plexus Neuropathy, Idiopathic Cervical Dystonia, Idiopathic Dilatation of the Pulmonary Artery. Idiopathic Facial Palsy, Idiopathic Familial Hyperlipemia, Idiopathic Hypertrophic Sub-aortic Stenosis, Idiopathic Hypoproteinemia, Idiopathic Immunoglobulin Deficiency, Idiopathic Neonatal Hepatitis, Idiopathic Non-Specific Ulcerative Colitis, Idiopathic Peripheral Periphlebitis, Idiopathic Pulmonary Fibrosis, Idiopathic Refractory Sideroblastic Anemia, Idiopathic Renal Hematuria, Idiopathic Steatorrhea, Idiopathic Thrombocythemia. Idiopathic Thrombocytopenic Purpura, Idiopathic Thrombocytopenia Purpura (ITP), IDPA, IgA Nephropathy, IHSS, Deitis, Ileocolitis, Illinois Type Amyloidosis, ILS. M, IMD2, IMD5, Immune Defect due to Absence of Thymus, Immune Hemolytic Anemia Paroxysmal Cold, Immunodeficiency with Ataxia Telangiectasia, Immunodeficiency Cellular with Abnormal Immunoglobulin Synthesis, Immunodeficiency Common Variable Unclassiflable, Immunodeficiency with Hyper-IgM, Immunodeficiency with Leukopenia, lmmunodeficiency-2, Immunodeficiency-5 (MD5), Immunoglobulin Deficiency. Imperforate Anus, Imperforate Anus with Hand Foot and Ear Anomalies, Imperforate Nasolacrimal Duct and Premature Aging Syndrome, Impotent Neutrophil Syndrome, Inability To Open Mouth Completely And Short Finger-Flexor. IN AD, Inborn Error of Urea Synthesis Arginase Type, Inborn Error of Urea Synthesis Arginino Succinic Type, Inborn Errors of Urea Synthesis Carbamyl Phosphate Type, Inborn Error of Urea Synthesis Citrullinemia Type, Inborn Errors of Urea Synthesis Glutamate Synthetase Type. INCL, Inclusion body myositis, Incomplete Atrioventricular Septal Defect, Incomplete Testicular Feminization, Incontinentia Pigmenti, Incontinenti Pigmenti Achromians, Index Finger Anomaly with Pierre Robin Syndrome, Indiana Type Amyloidosis (Type II), Indolent systemic mastocytosis, Infantile Acquired Aphasia, Infantile Autosomal Recessive Polycystic Kidney Disease, Infantile Beriberi, Infantile Cerebral Ganglioside, Infantile Cerebral Paralysis, Infantile Cystinosis, Infantile Epileptic, Infantile Fanconi Syndrome with Cystinosis, Infantile Finnish Type Neuronal Ceroid Lipofuscinosis, Infantile Gauche: Disease. Infantile Hypoglycemia, Infantile Hypophasphatasia, Infantile Lobar Emphysema, Infantile Myoclonic Encephalopathy, Infantile Myoclonic Encephalopatliy and Polymyoclonia, Infantile Myofibromatosis, Infantile Necrotizing Encephalopathy, Infantile Neuronal Ceroid Lipofuscinosis, Infantile Neuroaxonal Dystrophy, Infantile Onset Schindler Disease, Infantile Phytanic Acid Storage Disease, Infantile Refsum Disease (IRD), Infantile Sipoidosis GM-2 Gangliosideosis (Type S), Infantile Sleep Apnea. Infantile Spasms, Infantile Spinal Muscular Atrophy (all types), Infantile Spinal Muscular Atrophy ALS, Infantile Spinal Muscular Atrophy Type I, Infantile Type Neuronai Ceroid Lipofuscinosis, Infectious Jaundice, Inflammatory Bowel Disease, Inflammatory Breast Cancer. Inflammatory Linear Nevus Sebaceous Syndrome, Iniencephaly, Insulin Resistant Acanthosis Nigricans, Insulin Lipodystrophy, Insulin dependent Diabetes, Intention Myoclonus, Intermediate Cystinosis, Intermediate Maple Syrup Urine Disease, Intermittent Ataxia with Pyruvate Dehydrogenase Deficiency, Intermittent Maple Syrup Urine Disease, Internal Hydrocephalus, Interstitial Cystitis, Interstitial Deletion of 4q Included. Intestinal Lipodystrophy, Intestinal Lipophagic Granulomatosis, Intestinal Lymphangiectasia, Intestinal Polyposis I, Intestinal Polyposis II, Intestinal Polyposis III, Intestinal Polyposis-Cutaneous Pigmentation Syndrome, Intestinal Pseudoobstruction with External Ophthalmoplegia, Intracranial Neoplasm, Intracranial Tumors. Intracranial Vascular Malformations, Intrauterine Dwarfism. Intrauterine Synechiae, Inverted Smile And Occult Neuropathic Bladder, Iowa Type Amyloidosis (Type IV), IP, IPA, Iridocorneal Endothelial Syndrome, Iridocorneal Endothelial (ICE) Syndrome Cogan-Resse Type, Iridogoniodysgenesis With Somatic Anomalies, Iris Atrophy with Corneal Edema and Glaucoma, Iris Nevus Syndrome, Iron Overload Anemia, Iron Overload Disease, Irritable Bowel Syndrome, Irritable Colon Syndrome, Isaacs Syndrome, Isaacs-Merten Syndrome, Ischemic Cardio myopathy, Isolated Lissencephaly Sequence, Isoleucine 33 Amyloidosis, Isovaleric Acid Co A Dehydrogenase Deficiency, Isovaleric Acidaemia, Isovalericacidemia, Isovaleryl CoA Carboxylase Deficiency, ITO Hypomelanosis, ITO, ITP, IVA, Ivemark Syndrome, Iwanoff Cysts. Jackknife Convulsion, Jackson-Weiss Craniosynostosis. Jackson-Weiss Syndrome, Jacksonian Epilepsy, Jacobsen Syndrome, Jadassohn-Lewandowsky Syndrome, Jaffe-Lichenstein Disease, Jakob's Disease, Jakob-Creutzfeldt Disease, Janeway I, Janeway Dysgammaglobulinemia. Jansen Metaphyseal Dysostosis, Jansen Type Metaphyseal Chondrodysplasia, Jarcho-Levin Syndrome, Jaw-Winking, JBS, JDMS, Jegher's Syndrome, Jejunal Atresia, Jejunitis, Jejunoileitis, Jervell and Lange-Nielsen Syndrome, Jeune Syndrome.. JMS, Job Syndrome, Job-Buckley Syndrome, Johanson-Blizzard Syndrome, John Dalton, Johnson-Stevens Disease, Jonston's Alopecia, Joseph's Disease, Joseph's Disease Type I, Joseph's Disease Type II, Joseph's Disease Type III, Joubert Syndrome, Joubert-Bolthauser Syndrome, JRA, Juberg Hayward Syndrome, Juberg-Marsidi Syndrome, Juberg-Marsidi Mental Retardation Syndrome, Jumping Frenchmen, Jumping Frenchmen of Maine, Juvenile Arthritis, Juvenile Autosomal Recessive Polycystic Kidney Disease, Juvenile Cystinosis, Juvenile (Childhood) Dermatomyositis (JDMS), Juvenile Diabetes, Juvenile Gaucher Disease, Juvenile Gout Choreoathetosis and Mental Retardation Syndrome, Juvenile Intestinal Malabsorption of Vit B12, Juvenile Intestinal Malabsorption of Vitamin B12, Juvenile Macular Degeneration, Juvenile Pernicious Anemia, Juvenile Retinoschisis, Juvenile Rheumatoid Arthritis, Juvenile Spinal Muscular Atrophy Included, Juvenile Spinal Muscular Atrophy ALS Included, Juvenile Spinal Muscular Atrophy Type III, Juxta-Articular Adiposis Dolorosa, Juxtaglomerular Hyperplasia, Kabuki Make-Up Syndrome, Kahler Disease, Kallrnann Syndrome, Kanner Syndrome, Kanzaki Disease, Kaposi Disease (not Kaposi Sarcoma), Kappa Light Chain Deficiency, Karsch-Neugebauer Syndrome, Kartagener Syndrome-Chronic Sinobronchial Disease and Dextrocardia, Kartagener Triad, Kasabach-Merritt Syndrome, Kast Syndrome, Kawasaki Disease, Kawasaki Syndrome, KBG Syndrome, KD, Keams-Sayre Disease, Kearns-Sayre Syndrome, Kennedy Disease, Kennedy Syndrome, Kennedy Type Spinal and Bulbar Muscular Atrophy, Kennedy-Stefanis Disease, Kenny Disease, Kenny Syndrome, Kenny Type Tubular Stenosis, Kenny-Caffe Syndrome, Kera. Palmoplant. Con. Pes Planus Ony. Periodon. Arach., Keratitis Ichthyosis Deafness Syndrome, Keratoconus, Keratoconus Posticus Circumscriptus, Keratolysis, Keratolysis Exfoliativa Congenita, Keratolytic Winter Erythema, Keratomalacia., Keratosis Follicularis, Keratosis Follicularis Spinulosa Decalvans, Keratosis Follicularis Spinulosa Decalvans Ichthyosis, Keratosis Nigricans, Keratosis Palmoplantaris with Periodontopathia and Onychogryposis, Keratosis Palmoplantaris Congenital Pes Planus Onychogryposis Periodontosis Arachnodactyly, Keratosis Palmoplantaris Congenital, Pes Planus, Onychogryphosis, Periodontosis, Arachnodactyly, Acroosteolysis, Keratosis Rubra Figurata, Keratosis Seborrheica, Ketoacid Decarboxylase Deficiency, Ketoaciduria, Ketotic Glycinemia, KFS, KID Syndrome, Kidney Agenesis, Kidneys Cystic-Retinal Aplasia Joubert Syndrome, Killian Syndrome, Killian/Teschler-Nicola Syndrome, Kiloh-Nevin syndrome III, Kinky Hair Disease, Kinsbourne Syndrome, Kleeblattschadel Deformity, Kleine-Levin Syndrome, Kleine-Levin Hibernation Syndrome, Klinefelter, Klippel-Feil Syndrome, Klippel-Feil Syndrome Type 1, Klippel-Feil Syndrome Type I13 Klippel-Feil Syndrome Type III, Klippel Trenaunay Syndrome, Klippel-Trenaunay-Weber Syndrome, Kluver-Bucy Syndrome, KMS. Kniest Dyspiasia, Kniest Syndrome, Kobner's Disease, Koebberling-Dunnigan Syndrome, Kohlmeier-Degos Disease, Kok Disease. Korsakoff Psychosis, Korsakoff s Syndrome, Kiabbe's Disease Included, Krabbe's Leukodystrophy, Kramer Syndrome, KSS, KTS, KTW Syndrome, Kufs Disease, Kugelberg-Welander Disease, Kugelberg-Welander Syndrome, Kussmaul-Landry Paralysis, KWS, L-3-Hydroxy-Acyl-CoA Dehydrogenase (LCHAD) Deficiency, Laband Syndrome, Labhart-Willi Syndrome, Labyrinthine Syndrome. Labyrinthine Hydrops, Lacrimo-Auriculo-Dento-Digital Syndrome, Lactase Isolated Intolerance, Lactase Deficiency, Lactation-Uterus Atrophy, Lactic Acidosis Leber Hereditary Optic Neuropathy, Lactic and Pyruvate Acidemia with Carbohydrate Sensitivity, Lactic and Pyruvate Acidemia with Episodic Ataxia and Weakness, Lactic and Pyruvate, Lactic acidosis, Lactose Intolerance of Adulthood, Lactose Intolerance, Lactose Intolerance of Childhood, LADD Syndrome, LADD, Lafora Disease Included, Lafora Body Disease, Laki-Lorand Factor Deficiency, LAM, Lambert Type Ichthyosis, Lambert-Eaton Syndrome, Lambert-Eaton Myasthenic Syndrome, Lamellar Recessive Ichthyosis, Lamellar Ichthyosis, Lancereaux-Mathieu-Weil Spirochetosis. Landau-Kleffeer Syndrome, Landouzy Dejerine Muscular Dystrophy, Lanciry Ascending Paralysis, Langer-Salidino Type Achondrogensis (Type II), Langer Giedion Syndrome, Langerhans-Cell Granulornatosis, Langerhans-Cell Histiocytosis (LCH), Large Atrial and Ventricular Defect, Laron Dwarfism, Laron Type Pituitary Dwarfism, Larsen Syndrome, Laryngeal Dystonia, Latah (Observed in Malaysia), Late Infantile Neuroaxonal Dystrophy, Late Infantile NeuroaxonaJ Dystrophy, Late Onset Cockayne Syndrome Type III (Type C), Late-Onset Dystonia, Late-Onset Immunoglobulin Deficiency, Late Onset Pelizaeus-Merzbacher Brain Sclerosis, Lattice Corneal Dystrophy, Lattice Dystrophy, Launois-Bensaude, Launois-Cleret Syndrome, Laurence Syndrome, Laurence-Moon Syndrome, Laurence-Moon/Bardet-Biedl, Lawrence-Seip Syndrome, LCA, LCAD Deficiency, LCAD, LC.AD, LCADH Deficiency, LCH, LCHAD, LCPD, Le Jeune Syndrome, Leband Syndrome, Leber's Amaurosis, Leber's Congenital Amaurosis,Congenital Absence of the Rods and Cones, Leber's Congenital Tapetoretinal Degeneration, Leber's Congenital Tapetoretinal Dysplasia, Leber's Disease, Leber's Optic Atrophy, Leber's Optic Neuropathy, Left Ventricular Fibrosis, Leg Ulcer, Legg-Calve-Perthes Disease, Leigh's Disease, Leigh's Syndrome, Leigh's Syndrome (Subacute Necrotizing Encephalomyelopathy), Leigh Necrotizing Encephalopathy, Lennox-Gastaut Syndrome, Lentigio-Polypose-Digestive Syndrome, Lenz Dysmorphogenetic Syndrome, Lenz Dysplasia, Lenz Microphthalmia Syndrome, Lenz Syndrome, LEOPARD Syndrome, Leprechaunism, Leptomeningeal Angiomatosis, Leptospiral Jaundice, Leri-Weill Disease, Leri-Weil Dyschondrosteosis, Leri-Weil Syndrome, Lermoyez Syndrome, Leroy Disease, Lesch Nyhan Syndrome, Lethal Infantile Cardio myopathy, Lethal Neonatal Dwarfism, Lethal Osteochondrodysplasia, Letterer-Siwe Disease, Leukocytic Anomaly Albinism, Leukocytic Inclusions with Platelet Abnormality, Leukodystrophy, Leukodystrophy with Rosenthal Fibers, Leukoencephalitis Periaxialis Concentric, Levine-Critchley Syndrome, Levulosuria, Levy-Holiister Syndrome, LGMD, LGS, LHON, LIC, Lichen Ruber Acuminatus, Lichen Acuminatus, Lichen Amyloidosis, Lichen Planus, Lichen Psoriasis, Lignac-Debre-Fancord Syndrome, Lignac-Fanconi Syndrome, Ligneous Conjunctivitis, Limb-Girdle Muscular Dystrophy, Limb Malformations-Dento-Digital Syndrome, Limit Dextrinosis, Linear Nevoid Hypermelanosis, Linear Nevus Sebacous Syndrome, Linear Scleroderma, Linear Sebaceous Nevus Sequence, Linear Sebaceous Nevus Syndrome, Lingua Fissurata. Lingua Plicata, Lingua Scrotalis, Linguofacial Dyskinesia, Lip Pseudocleft-hemangiomatous Branchial Cyst Syndrome, Lipid Granulomatosis, Lipid Histiocytosis, Lipid Kerasin Type, Lipid Storage Disease, Lipid-Storage myopathy Associated with SCAD Deficiency. Lipidosis Ganglioside Infantile, Lipoatrophic Diabetes Mellitus, Lipodystrophy, Lipoid Corneal Dystrophy, Lipoid Hyperplasia-Male Pseudohermaphroditism, Lipomatosis of Pancreas Congenital, Lipomucopolysaccharidosis Type I, Lipomyelomeningocele, Lipoprotein Lipase Deficiency Familial, LIS, LIS1, Lissencephaly 1, Lissencephaly Type I, Lissencephaly variants with agenesis of the corpus callosum cerebellar hypoplasia or other anomalies, Little Disease, Liver Phosphorylase Deficiency, LKS, LM Syndrome, Lobar Atrophy, Lobar Atrophy of the Brain, Lobar Holoprosencephaly, Lobar Tension Emphysema in Infancy, Lobstein Disease (Type I), Lobster Claw Deformity, Localized Epidermolysis Bullosa, Localized Lipodystrophy, Localized Neuritis of the Shoulder Girdle, Loeffier's Disease, Loeffler Endomyocardial Fibrosis with Eosinophilia, Loeffler Fibroplastic Parietal Endocarditis, Loken Syndrome, Loken-Senior Syndrome, Long-Chain 3-hydroxyacyl-CoA Dehydrogenase (LCHAD), Long Chain Acyl CoA Dehydrogenase Deficiency, Long-Chain Acyl-CoA Dehydrogenase (ACADL), Long-Chain Acyl-CoA Dehydrogenase Deficiency, Long QT Syndrome without Deafness, Lou Gehrig's Disease, Lou Gehrig's Disease Included, Louis-Bar Syndrome, Lew Blood Sugar, Low-Density Beta Lipoprotein Deficiency, Low Imperforate Anus, Low Potassium Syndrome, Lowe syndrome, Lowe's Syndrome, Lowe-Bickel Syndrome, Lowe-Terry-MacLachlan Syndrome, Lower Back Pain, LS, LTD, Lubs Syndrome, Luft Disease, Lumbar Canal Stenosis, Lumbar Spinal Stenosis, Lumbosacral Spinal Stenosis. Lundborg-Unverricht Disease, Lundborg-Unverricht Disease Included, Lupus, Lupus, Lupus Erythematosus, Luschka-Magendde Foramina Atresia, Lyell Syndrome, Lyelles Syndrome, Lymphadenoid Goiter, Lymphangiectatic Protein-Losing Enteropathy, Lymphangioleiomatosis, Lymphangioleimyomatosis, Lymphangiomas, Lymphatic Malformations, Lynch Syndromes, Lynch Syndrome I, Lynch Syndrome n, Lysosomal Alpha-N-Acetylgalactosaminidase Deficiency Schindler Type, Lysosomal Glycoaminoacid Storage Disease-Angiokeratoma Corporis Diffusum, Lysosomal Glucosidase Deficiency, MAA, Machado Disease, Machado-Joseph Disease, Macrencephaly, Macrocephaly, Macrocephaly Hemihypertrophy, Macrocephaly with Multiple Lipomas and Hernangiomata, Macrocephaly with Pseudopapilledema and Multiple Hemangiomata. Macroglobulinemia, Macroglossia, Macroglossia-Omphalocele-Visceromegaly Syndrome, Macrostomia Ablepheron Syndrome, Macrothrombocytopenia Familial Bernard-Soulier Type, Macula Lutea degeneration, Macuiar Amyloidosis, Macular Degeneration, Macuiar Degeneration Disciform, Macuiar Degeneration Senile, Macuiar Dystrophy, Maculai Type Corneal Dystrophy, MAD, Madelung's Disease, Maffucci Syndrome, Major Epilepsy, Malabsorption, Malabsorption-Ectodermal Dysplasia-Nasal Alar Hypoplasia, Maladie de Roger, Maladie de Tics, Malaria, Male Malformation of Limbs and Kidneys, Male Turner Syndrome, Malignant Acanthosis, Malignant Acanthosis Nigricans, Malignant Astrocytoma, Malignant Atrophic Papulosis, Malignant Fever, Malignant Hyperphenylalaninemia, Malignant Hyperpyrexia, Malignant Hyperthermia, Malignant Melanoma, Malignant Tumors of the Central Nervous System, Mallory-Weiss Laceration, Mallory-Weiss Tear, Mallory-Weiss Syndrome, Mammary Paget's Disease, Mandibular Ameloblastoma, Mandibulofacial Dysostosis, Mannosidosis. Map-Doi-Fingerpnnt Type Cornea! Dystrophy, Maple Syrup Urine Disease. Marble Bones, Marchiafava-Micheli Syndrome, Marcus Gunn Jaw-Winking Syndrome, Marcus Gunn Phenomenon, Marcus Gunn Ptosis with jaw-winking, Marcus Gunn Syndrome, Marcus Gunn (Jaw-Winking) Syndrome. Marcus Gunn Ptosis (with jaw-winking), Maiden-Walker Syndrome, Maiden-Walker Type Connective Tissue Disorder, Marfan's Abiotrophy, Marfan-Achard syndrome, Marfan Syndrome, Marfan's Syndrome I, Marfan's Variant, Marfanoid Hypermobility Syndrome, Marginal Corneal Dystrophy, Marie's Ataxia, Marie Disease, Marie-Sainton Disease, Marie Strumpell Disease, Marie-Strumpell Spondylitis, Marinesco-Sjogren Syndrome, Marinesco-Sjogren-Gorland Syndrome, Marker X Syndrome, Maroteaux Lamy Syndrome, Maroteaux Type Acrornesomelic Dysplasia, Marshall's Ectodermal Dysplasias With Ocular and Hearing Defects, Marshall-Smith Syndrome, Marshall Syndrome, Marshall Type Deafness-Myopia-Cataract-Saddle Nose, Martin-Albright Syndrome, Martin-Bell Syndrome, Martorell Syndrome, MASA Syndrome, Massive Myoclonia, Mast Cell Leukemia, Mastocytosis, Mastocytosis With an Associated Hematologic Disorder, Maumenee Cornea] Dystrophy, Maxillary Ameloblastoma, Maxillofecial Dysostosis, Maxillonasal Dysplasia, Maxillonasal Dysplasia Binder Type, Maxillopalpebral Synkinesis, May-Hegglin Anomaly, MCAD Deficiency. MCAD, McArdle Disease, McCune-Albright, MCD, McKusick Type Metaphyseal Chondrodysplasia, MCR, MCTD, Meckel Syndrome, Meckel-Gruber Syndrome, Median Cleft Face Syndrome, Mediterranean Anemia, Medium-Cham Acyl-CoA dehydrogenase (ACADM), Medium Chain Acyl-CoA Dehydrogenase fMCAD) Deficiency, Medium-Chain Acyl-CoA Dehydrogenase Deficiency, Medullary Cystic Disease, Medullary Sponge Kidney, MEF, Megaesophagus, Megalencephaly, Megalencephaly with Hyaline Inclusion, Megalencephaly with Hyaline Panneuropathy, Megaloblastic Anemia, Megaloblastic Anemia of Pregnancy, Megalocomea-Mental Retardation Syndrome, Meier-Gorlin Syndrome, Meige's Lymphedema, Meige's Syndrome, Melanodermic Leukodystrophy, Melanoplakia-Intestinal Polyposis, Melanoplakia-Intestinal Polyposis, MELAS Syndrome, MELAS, Melkersson Syndrome, Melnick-Fraser Syndrome, Melnick-Needles Osteodysplasty. Melm'ck-Meedles Syndrome, Membranous Lipodystrophy, Mendes Da Costa Syndrome. Merdere Disease, Meniere's Disease, Meningeal Capillary Angiomatosis, Menkes Disease, Menke's Syndrome I, Mental Retardation Aphasia Shuffling Gait Adducted Thumbs (MASA)., Mental Retardation-Deafness-Skeleta] Abnormalities-Coarse Face with Full Lips, Mental Retardation with Hypopiastic 5th Fingernails and Toenails, Mental Retardation with Osteocartilaginous Abnormalities, Mental Retradation-X-linked with Growth Delay-Deafness-Microgenitalism, Menzel Type OPCA, Mermaid Syndrome, MERRF, MERRF Syndrome, Merten-Singleton Syndrome, MES, Mesangial IGA Nephropathy, Mesenteric Lipodystrophy, Mesiodens-Cataract Syndrome, Mesodermal Dysmorphodystrophy, Mesomelic Dwarfism-Madelung Deformity, Metabolic Acidosis, Metachromatic Leukodystrophy, Metatarsus Varus, Metatropic Dwarfism Syndrome, Metatropic Dysplasia, Metatropic Dysplasia I, Metatropic Dysplasia II, Methylmaionic Acidemia, Methylmaionic Aciduria, Meulengracht's Disease, MFD1, MG, MH, MHA, Micrencephaly, Microcephalic Primordial Dwarfism I, Microcephaly, Microcephaly-Hiatal Hernia-Nephrosis Galloway Type, Microcephaly-Hiatal Hemia-Nephrotic Syndrome, Microcystic Cornea! Dystrophy, Microcythemia, Microlissencephaly, Microphthalmia, Microphthalmia or Anophthalmos with Associated Anomalies, Micropolygyria With Muscular Dystrophy, Microtia Absent Patellae Micrognathia Syndrome, Microvillus Inclusion Disease, MID, Midsystolic-click-late systolic murmur syndrome, Miescher's Type I Syndrome, Mikulicz Syndrome, Mikulicz-Radecki Syndrome, Mikulicz-Sjogren Syndrome, Mild Autosomal Recessive, Mild Intermediate Maple Syrup Urine Disease, Mild Maple Syrup Urine Disease, Miller Syndrome, Miller-Dieker Syndrome, Miller-Fisher Syndrome, Milroy Disease, Minkowski-Chauffard Syndrome, Minor Epilepsy, Minot-Von Willebrand Disease, Mirror-Image Dextrocardia, Mitochondrial Beta-Oxidation Disorders, Mitrochondrial and Cytosolic, Mitochondrial Cytopathy, Mitochondrial Cytopathy, Keam-Sayre Type. Mitochondrial Encephalopathy, Mitochondrial Encephalo myopathy Lactic Acidosis and Strokelike Episodes, Mitochondrial myopathy, Mitochondria! myopathy Encephalopathy Lactic Acidosis Stroke-Like Episode, Mitochondrial PEPCK Deficiency, Mitral-valve prolapse. Mixed Apnea, Mixed Connective Tissue Disease, Mixed Hepatic Porphyria, Mixed Non-Fluent Aphasia, Mixed Sleep Apnea, Mixed Tonic and Clonjc Torticollis, MJD. MKS, ML I, ML IL ML III, ML IV, ML Disorder Type I, ML Disorder Type II, ML. Disorder Type HI, ML Disorder Type IV, MLNS, MMR Syndrome, MND, MNGIE, MNS, Mobitz I, Mobitz II, Mobius Syndrome, Moebius Syndrome, Moersch-Woltmann Syndrome, Mohr Syndrome, Monilethrix, Monomodal Visual Amnesia. Mononeuritis Multiplex., Mononeuriris Peripheral, Mononeuropathy Peripheral, Monosomy 3p2, Monosomy 9p Partial, Monosomy IIq Partial, Monosomy 13q Partial, Monosomy 18q Syndrome, Monosomy X, Monostotic Fibrous Dysplasia, Morgagni-Turner-Albright Syndrome, Morphea, Morquio Disease, Morquio Syndrome, Morquio Syndrome A, Morquio Syndrome B, Morquio-Brailsford Syndrome, Morvan Disease, Mosaic Tetrasomy 9p, Motor Neuron Disease, Motor Neuron Syndrome, Motor Neurone Disease, Motoneuron Disease, Motoneurone Disease, Motor System Disease (Focal and Slow), Moya-moya Disease, Moyamoya Disease, MPS, MPS I, MPS 1 H, MPS 1 H/S Hurler/Scheie Syndrome, MPS 1 S Scheie Syndrome, MPS II, MPS I1A, MPS IB, MPS II-AR Autosomal Recessive Hunter Syndrome, MPS II-XR, MPS H-XR Severe Autosomal Recessive, MPS in, MPS III A B C and D Sanfiloppo A, MPS IV, MPS IV A and B Morquio A, MPS V, MPS VI, MPS VI Severe Intermediate Mild Maroteaux-Lamy, MPS VH, MPS VII Sly Syndrome, MPS VIII, MPS Disorder, MPS Disorder I, MPS Disorder II, MPS Disorder HI, MPS Disorder VI, MPS Disorder Type VII, MRS, MS, MSA, MSD, MSL, MSS, MSUD, MSUD, MSUD Type Ib, MSUD Type II, Mucocutaneous Lymph Node Syndrome, Mucolipidosis I, Mucolipidosis II, Mucolipidosis in, Mucolipidosis IV, Mucopolysaccharidosis, Mucopolysaccharidosis I-H. Mucopolysaccharidosis I-S, Mucopolysaccharidosis II, Mucopolysaccharidosis III, Mucopolysaccharidosis IV, Mucopolysaccharidosis VI, Mucopolysaccharidosis VH, Mucopolysaccharidosis Type I, Mucopolysaccharidosis Type II, Mucopolysaccharidosis Type III, Mucopolysaccharidosis Type VII, Mucosis, Mucosulfatidosis, Mucous Colitis, Mucoviscidosis, Mulibrey Dwarfism, Mulibrey Nanism Syndrome, Mullenan Duct Aplasia-Renal Aplasia-Cervicothoracic Somite Dysplasia, Mullerian Duct-Renal-Cervicothoracic-Upper Limb Defects, Mullerian Duct and Renal Agenesis with Upper Limb and Rib Anomalies, Mullerian-Renal-Cervicothoracic Somite Abnormalities, Multi-Infarct Dementia Binswanger's Type, Multicentric Castleman's Disease. Multifocal Eosinophilic Granuloma, Multiple Acyl-CoA Dehydrogenase Deficiency, Multiple Acyl-CoA Dehydrogenase Deficiency / Glutaric Aciduria Type II, Multiple Angiomas and Endochondromas, Multiple Carboxylase Deficiency, Multiple Cartilaginous Enchondroses, Multiple Cartilaginous Exostoses, Multiple Enchondromatosis, Multiple Endocrine Deficiency Syndrome Type II, Multiple Epiphyseal Dysplasia, Multiple Exostoses, Multiple Exostoses Syndrome, Multiple Familial Poiyposis, Multiple Lentigines Syndrome, Multiple Myeloma, Multiple Neuritis of the Shoulder Girdle.. Multiple Osteochondromatosis, Multiple Peripheral Neuritis, Multiple Polyposis of the Colon, Multiple Pterygium Syndrome, Multiple Sclerosis, Multiple Sulfatase Deficiency, Multiple Symmetric Lipomatosis, Multiple System Atrophy. Multisyncstotic Osteodysgenesis, Multisynostotic Osteodysgenesis with Long Bone Fractures, Mulvihill-Smith Syndrome, MURCS Association, Murk Jansen Type Metaphyseal Chondrodysplasia, Muscle Carnitine Deficiency, Muscle Core Disease, Muscle Phosphofructokinase Deficiency, Muscular Central Core Disease, Muscular Dystrophy, Muscular Dystrophy Classic X-linked Recessive, Muscular Dystrophy Congenital With Central Nervous System Involvement, Muscular Dystrophy Congenital Progressive with Mental Retardation, Muscular Dystrophy Facioscapulohumeral, Muscular Rheumatism, Muscular Rigidity - Progressive Spasm, Musculoskeletal Pain Syndrome, Mutilating Acropathy. Mutism, mvp, MVP, MWS, Myasthenia Gravis, Myasthenia Gravis Pseudoparalytica, Myasthenic Syndrome of Lambert-Eaton, Myelinoclastic Diffuse Sclerosis, Myelomatosis, Myhre Syndrome, Myoclonic Astatic Petit Mai Epilepsy, Myoclonic Dystonia, Myoclonic Encephalopathy of Infants, Myoclonic Epilepsy, Myoclonic Epilepsy Hartung Type, Myoclonus Epilepsy Associated with Ragged Red Fibers, Myoclonic Epilepsy and Ragged-Red Fiber Disease, Myoclonic Progressive Familial Epilepsy, Myoclonic Progressive Familial Epilepsy, Myoclonic Seizure, Myoclonus. Myoclonus Epilepsy, Myoencephalopathy Ragged-Red Fiber Disease, Myofibromatosis, Myofibromatosis Congenital, Myogenic Facio-Scapulo-Peroneal Syndrome, MyoneurogastointestinaJ Disorder and Encephalopathy, Myopathic Arthrogryposis Multiplex Congenita, Myopathic Carnitine Deficiency, Myopathy Central Fibrillar, myopathy Congenital Nonprogressive, myopathy Congenital Nonprogressive with Central Axis, myopathy with Deficiency of Carnitine Palmitoyltransferase, myopathy-Marinesco-Sjogren Syndrome, myopathy-Metabolic Carnitine Palmitoyltransderase Deficiency, myopathy Mitochondrial-Encephalopathy-Lactic Acidosis-Stroke, myopathy with Sarcoplasmic Bodies and Intermediate Filaments, Myophosphorylase Deficiency, Myositis Ossificans Progressiv, Myotonia Atrophica, Myotonia Congenita, Myotonia Congenita Intermittens, Myotonic Dystrophy, Myotonic myopathy Dwarfism Chondrodystrophy Ocular and Facial Anomalies, Myotubular myopathy, Myotubular myopathy X-linked, Myproic Acid, Myriachit (Observed in Siberia), Myxedema. N-Acetylglucosamine-1-Phosphotransferase Deficiency, N-Acetyl Glutaraate Synthetase Deficiency, NADH-CoQ reductase deficiency, Naegeli Ectodermal Dysplasias, Nager Syndrome, Nager Acrofacial Dysostosis Syndrome, Nager Syndrome, NAGS Deficiency, Nail Dystrophy-Deafness Syndrome, Nail Dysgenesis and Hypodontia, Nail-Patella Syndrome, Nance-Horan Syndrome, Nanocephalic Dwarfism, Nanocephaly, Nanophthalmia, Narcolepsy, Narcoleptic syndrome, NARP, Nasal-fronto-faciodysplasia, Nasal Alar Hypoplasia Hypothyroidism Pancreatic Achylia Congenital Deafness, Nasomaxillary Hypoplasia, Nasu Lipodystrophy, NBIA1, ND, NDI, NDP, Necrotizing Encephalomyelopathy of Leigh's, Necrotizing Respiratory Granulomatosis, Neill-Dingwali Syndrome, Nelson Syndrome, Nemaline myopathy, Neonatal Adrenoleukodystrophy, Neonatal Adrenoleukodystrophy (NALD), Neonatal Adrenoleulcodystrophy (ALD), Neonatal Autosomal Recessive Polycystic Kidney Disease, Neonatal Dwarfism, Neonatal Hepatitis, Neonatal Hypoglycemia, Neonatal Lactose Intolerance, Neonatal Lymphedema due to Exudative Enteropathy, Neonatal Necrotizing Enterocolitis, Neonatal Progeroid Syndrome, Neonatal Pseudo-Hydrocephalic Progeroid Syndrome of Wiedemann-Rautenstrauch, Neoplastk Arachnoiditis, Nephroblastom, Nephrogenic Diabetes Insipidus. Nephronophthesis Familial Juvenile, Nephropathic Cystinosis, Nephropathy-Pseudohennaphroditism-Wilms Tumor, Nephrosis-Microcephaly Syndrome, Nephrosis-Neuronal Dysmigration Syndrome, Nephrotic-Glycosuric-Dwarfism-Rickets-Hypophosphatemic Syndrome, Netherton Disease, Netherton Syndrome. Netherton Syndrome Ichthyosis, Nettleship Falls Syndrome (X-Linked), Neu-Laxova Syndrome, Neuhauser Syndrome, Neural-tube defects, Neuralgic Amyotrophy, Neuraminidase Deficiency, Neuraocutaneous melanosis, Neurinoma of the Acoustic Nerve, Neurinoma, Neuroacanthocytosis, Neuroaxonal Dystrophy Schindler Type, Neurodegeneration with brain iron accumulation type 1 (NBIA1), Neurofibroma of the Acoustic Nerve, Neurogenic Arthrogryposis Multiplex Congenita, Neuromyelitis Optica, Neuromyotonia, Neuromyotonia, Focal, Neuromyotonia, Generalized. Familial, Neuromyotonia, Generalized, Sporadic, Neuronal Axonal Dystrophy Schindler Type, Neuronal Ceroid Lipofuscinosis Adult Type. Neuronal Ceroid Lipofuscinosis Juvenile Type, Neuronal Ceroid Lipofuscinosis Type 1. Neuronopathic Acute. Gaucher Disease, Neuropathic Amyioidosis, Neuropathic Beriberi, Neuropathy Ataxia and Retinitis Pigmentosa, Neuropathy of Brachialpelxus' Syndrome, Neuropathy Hereditary Sensory Type I. Neuropathy Hereditary Sensory Type II, Neuropsychiatric Porphyria. Neutral Lipid Storage Disease, Nevii, Nevoid Basal Cell Carcinoma Syndrome, Nevus, Nevus Cavernosus, Nevus Comedonicus, Nevus Depigmentosus, Nevus Sebaceous of Jadassohn, Nezelofs Syndrome, Nezelofs Thymic Aplasia, Nezelof Type Severe Combined immunodeficiency. NF, NF1, NF2, NF-1, NF-2, NHS, Niemann Pick Disease, Nieman Pick disease Type A (acute neuronopathic form), Nieman Pick disease Type B, Nieman Pick Disease Type C (chronic neuronopathic form), Nieman Pick disease Type D (Nova Scotia variant), Nieman Pick disease Type E, Nieman Pick disease Type F (sea-blue histiocyte disease), Night Blindness, Nigrospinodentatal Degeneration, Niikawakuroki Syndrome, NLS, NM, Noack Syndrome Type 1, Nocturnal Myoclonus Hereditary Essential Myoclonus, Nodular Cornea Degeneration, Non-Bullous CIE, Non-Bullous Congenital Ichthyosiform Erythroderma, Non-Communicating Hydrocephalus, Non-Deletion Type Aipha-Thalassemia / Mental Retardation syndrome, Non-Ketonic Hyperglycinemia Type l (NKHT), Non-Ketotic Hyperglycinemia, Non-Lipid Reticuloendotheliosis, Non-Neuronopathic Chronic Adult Gaucher Disease, Non-Scarring Epiderrnolysis Bullosa, Nonarteriosclerotic Cerebral Calcifications, Nonarticular Rheumatism, Noncerebral,Juvenile Gaucher Disease, Nondiabetic Glycosuria, Nonischemic Cardio myopathy, Nonketob'c Hypoglycemia and Camitine Deficiency due to MCAD Deficiency, Nonketotic Hypoglycemia Caused by Deficiency of Acyl-CoA Dehydrogenase, Nonketotic Glycinemia, Nonne's Syndrome, Nonne-Milroy-Meige Syndrome. Nonopalescent Opalescent Dentine, Nonpuerperal Galactorrhea-Amenorrhea, Nonsecretory Myeloma, Nonspherocytic Hemolytic Anemia, Nontropical Sprue, Noonan Syndrome, Norepinephrine, Normal Pressure Hydrocephalus, Norman-Roberts Syndrome, Norrbortnian Gaucher Disease, Nome Disease, Norwegian Type Hereditary Cholestasis, NPD. NPS, NS, NSA, Nuchal Dystonia Dementia Syndrome, Nutritional Neuropathy, Nyhan Syndrome, OAV Spectrum, Obstructive Apnea, Obstructive Hydrocephalus, Obstructive Sleep Apnea, OCC Syndrome. Occlusive Thromboaortopathy, OCCS, Occult IntracraniaJ Vascular Malformations. Occult Spinal Dysraphism Sequence, Ochoa Syndrome, Ochronosis, Ochronotic Arthritis, OCR, OCRL, Octocephaly, Ocular Albinism, Ocular Herpes, Ocular Myasthenia Gravis, Oculo-Auriculo-Vertebral Dysplasia, Oculo-Auriculo-Vertebral Spectrum, Oculo-Bucco-Genital Syndrome, Oculocerebral Syndrome with Hypopigrnentation, Oculocerebrocutaneous Syndrome, Oculo-Cerebro-Renal, Oculocerebrorenal Dystrophy, Oculocerebrorenal Syndrome, Oculocraniosomatic Syndrome (obsolete), Oculocutaneous Albinism, Oculo cutaneous Albinism Chediak-Higashi Type, Oculo-Dento-Digital Dysplasia, Oculodentodigital Syndrome, Oculo-Dento-Osseous Dysplasia, Oculo Gastrointestina] Muscular Dystrophy, Oculo Gastrointestinal Muscular Dystrophy, Oculomandibulodyscephaly with hypotrichosis, Ocuiomandibulofacial Syndrome, Oculomotor with Congenital Contractures and Muscle Atrophy, Oculosympathetic Palsy, ODD Syndrome, ODOD, Odontogenic Tumor, Odontotrichomelic Syndrome, OFD, OFD Syndrome, Ohio Type Amyloidosis (Type VII), 01, OI Congenita, 01 Tarda, Oldfield Syndrome, Oligohydrarnnios Sequence, Oligophrenia Microphthalmos, Oligophrenic Polydystrophy, Olivopontocerebellar Atrophy, Olivopontocerebellar Atrophy with Dementia and Extrapyramidal Signs, Olivopontocerebellar Atrophy with Retinal Degeneration, Olivopontocerebellar Atrophy I, Olivopontocerebellar Atrophy II, Olivopontocerebellar Atrophy HI, Olivopontocerebellar Atrophy TV, Olivopontocerebellar Atrophy V. Oilier Disease, Oilier Osteochondromatosis, Omphalocele-Visceromegaly-Macroglossia Syndrome, Ondine's Curse, Onion-Bulb Neuropathy, Onion Bulb Polyneuropathy, Onychoosteodysplasia, Onychotrichodysplasia with Neutroperua. OPCA, OPCA I, OPCA II, OPCA in, OPCA IV, OPCA V, OPD Syndrome, OPD Syndrome Type I, OPD Syndrome Type E, OPD I Syndrome, OPD II Syndrome, Ophthahnoarthropathy, Ophthalmoplegia-Intestinal Pseudoobstruction, Ophthalmoplegia. Pigmentary Degeneration of the Retina and Cadio myopathy, Ophthaimoplegia Plus Syndrome, Ophthalmoplegia Syndrome, Opitz BBB SyBdrome, Opitz BBB/G Compound Syndrome, Opitz BBBG Syndrome, Opitz-Frias Syndrome, Opitz G Syndrome, Opitz G/BBB Syndrome, Opitz Hypertelorism-Hypospadias Syndrome, Opitz-Kaveggia Syndrome, Opitz Oculogenitolaryngeal Syndrome, Opitz Trigonocephaly Syndrome, Opitz Syndrome, Opsoclonus, Opsoclonus-Myoclonus, Opthalmoneuromyelitis, Optic Atrophy Polyneuropathy and Deafness, Optic Neuroencephalomyelopatby, Optic Neuromyelitis, Opticornyelitis, Optochiasmatic Arachnoiditis, Oral-Facial Clefts, Oral-facial Dyskinesia, Oral Facial Dystonia, Oral-Facial-Digital Syndrome, Oral-Facial-Digital Syndrome Type I, Oral-Facial-Digital Syndrome I. Oral-Facial-Digital Syndrome II, Oral-Facial-Digital Syndrome III, Oral-Facial-Digital Syndrome IV, Orbital Cyst with Cerebral and Focal Dermal Malformations, Omithine Carbamyl Transferase Deficiency, Ornithine Transcarbamylase Deficiency, Orocraniodigital Syndrome, Orofaciodigital Syndrome, Oromandibular Dystonia, Orthostatic Hypotension, Osler-Weber-Rendu disease, Osseous-Oculo-Dento Dysplasia, Osseous-Oculo-Dento Dysplasia, Osteitis deformans, Osteochondrodystrophy Deformans, Osteochondroplasia, Osteodysplasty of Melnick and Needles, Osteogenesis Imperfect, Osteogenesis Imperfecta, Osteogenesis Imperfecta Congenita, Osteogenesis Imperfecta Tarda, Osteohypertrophic Nevus Flammeus, Osteopathia Hyperostotica Scleroticans Multiplex Infantalis. Osteopathia Hyperostotica Scleroticans Multiplex Infantalis, Osteopathyrosis, Osteopetrosis, Osteopetrosis Autosomal Dominant Adult Type, Osteopetrosis Autosomal Recessive Malignant Infantile Type, Osteopetrosis Mild Autosomal Recessive Intermediate Typ, Osteosclerosis Fragilis Generaiisata, Osteosclerotic Myeloma, Ostium Primum Defect (endocardia! cushion defects included), Ostium Secundum Defect, OTC Deficiency, Oto Palato Digital Syndrome, Oto-Palato-Digita] Syndrome Type I, Oto-Palatal-Digital Syndrome Type II, Otodental Dysplasia, Otopalatodigital Syndrome, Otopalataidigital Syndrome Type II, Oudtshoom Skin, Ovarian Dwarfism Turner Type, Ovary Aplasia Turner Type, OWR, Oxalosis, Oxidase deficiency, Oxycephaly, Oxycephaly-Acrocephaly, P-V, PA, PAC, Pachyonychia Ichtyosiforme. Pachyonychia Congerdta with Natal Teeth. Pachyonychia Congenita, Pachyonychia Congenita Keratosis Disseminata Circumscripta (follicularis), Pachyonychia Congenita Jadassohn-Lewandowsky Type, PAF with MSA, Paget's Disease, Paget's Disease of Bone, Paget's Disease of the Breast, Paget's Disease of the Nipple, Paget's Disease of the Nipple and Areola, Pagon Syndrome, Painful Ophthalmoplegia, PAIS, Palatal Myoclonus, Palato-Oto-Digital Syndrome., Palatal-Oto-Digital Syndrome Type I, Palatal-Oto-Digital Syndrome Type II, Pallister Syndrome, Pallister-Hall Syndrome, Pallister-Killian Mosaic Syndrome, Pallister Mosaic Aneuploidy, Pallister Mosaic Syndrome, Pallister Mosaic Syndrome Tetrasomy 12p, Pallister- W Syndrome, Palmoplantar Hyperkeratosis and Alopecia, Palsy, Pancreatic Fibrosis, Pancreatic Insufficiency and Bone Marrow Dysfunction, Pancreatic Ulcerogenic Tumor Syndrome, Panmyelophthisis, Panmyelopathy, Pantothenate kinase associated neurodegeneration (PKAN). Papillon-Lefevre Syndrome, Papillotonic Psuedotabes, Paralysis Periodica Paramyotonica. Paralytic Beriberi, Paralytic Brachial Neuritis, Paramedian Lower Lip Pits-Poplitea! Pyen'gium Syndrome, Paramedian Diencephalic Syndrome, Paramyeloidosis, Paramyoclonus Multiple, Paramyotonia Congenita, Paramyotonia Congenita of Von Eulenburg, Parkinson's disease, Paroxysmal Atrial Tachycardia, Paroxysmal Cold HemogJobinuria, Paroxysmal Dystorua, Paroxysmal Dystonia Choreathetosis, Paroxysmal Kinesigenic Dystonia, Paroxysmal Nocturnal Hemoglobinuria, Paroxysmal Normal Hemoglobinuria, Paroxysmal Sleep, Parrot Syndrome, Parry Disease, Parry-Romberg Syndrome, Parsonage-Turner Syndrome, Partial Androgen Insensitivity Syndrome, Partial Deletion of the Short Ann of Chromosome 4, Partial Deletion of the Short Arm of Chromosome 5, Partial Deletion of Short Arm of Chromosome 9, Partial Duplication 3q Syndrome, Partial Duplication 15q Syndrome, Partial Facial Palsy With Urinary Abnormalities, Partial, Gigantism of Hands and Feet- Nevi-Hemihypertrophy-Macrocephaly, Partial Lipodystrophy, Partial Monosomy of Long Arm of Chromosome II, Partial Monosomy of the Long Arm of Chromosome 13, Partial Spinal Sensory Syndrome, Partial Trisomy IIq, Partington Syndrome, PAT, Patent Ductus Arteriosus, Pathological Myocionus, Pauciarticular-Onset Juvenile Arthritis, Paulitis, PBC, PBS, PC Deficiency, PC Deficiency Group A, PC Deficiency Group B, PC, Eulenburg Disease, PCC Deficiency, PCH, PCLD, PCT, PD, PDA, PDH Deficiency, Pearson Syndrome Pyruvate Carboxylase Deficiency, Pediatric Obstructive Sleep Apnea, Peeling Skin Syndrome, Pelizaeus-Merzbacher Disease, Pelizaeus-Merzbacher Brain Sclerosis, Pellagra-Cerebellar Ataxia-Renaj Aminoaciduria Syndrome, Pelvic Pain Syndrome, Pemphigus Vulgaris, Pena Shokeir II Syndrome. Pena Shokeir Syndrome Type II, Penile Fibromatosis, Penile Fibrosis, Penile Induration, Penta X Syndrome, Pentalogy of Cantrell, Pentalogy Syndrome, Pentasomy X, PEPCK Deficiency, Pepper Syndrome, Perheentupa Syndrome, Periarticular Fibrositis, Pericardial Constriction with Growth Failure, Pericollagen Amyloidosis, Perinatal Polycystic Kidney Diseases, Perineal Anus, Periodic Amyloid Syndrome. Periodic Peritonitis Syndrome, Periodic Somnolence and Morbid Hunger, Periodic Syndrome, Peripheral Cystoid Degeneration of the Retina, Peripheral Dysostosis-Nasal Hypoplasia-Mental Retardation, Peripheral Neuritis, Peripheral Neuropathy, Peritoneopericardial Diaphragmatic Hernia, Pernicious Anemia, Peromelia with Micrognathia. Peroneal Muscular Atrophy, Peroneal Nerve Palsy, Peroutka Sneeze, Peroxisomal Acyl-CoA Oxidase. Peroxisomal Beta-Oxidation Disorders, Peroxisomal Bifunctional Enzyme, Peroxisomal Thiolase, Peroxisomal Thiolase Deficiency, Persistent Truncus Arteriosus, Perthes Disease, Petit Mai Epilepsy, Petit Mai Variant, Peutz-Jeghers Syndrome, Peutz-Touraine Syndrome, Peyronie Disease, Pfeiffer, Pfeiffer Syndrome Type I, PGA I, PGA II PGA III, PGK, PH Type I, PH Type I, Pharyngeal Pouch Syndrome, PHD Short-Chain Acyl-CoA Dehydrogenase Deficiency, Phenylalanine Hydroxylase Deficiency, Phenylalaninemia, Phenylketonuria, Phenylpyruvic Oligophrenia, Phocornelia, Phocomelia Syndrome, Phosphoenolpyruvate Carboxykinase Deficiency, Phosphofructokmase Deficiency, Phosphogly cerate Kinase Deficiency, Phosphoglycerokinase, Phosphorylase 6 Kinase Deficiency, Phosphorylase Deficiency Glycogen Storage Disease, Phosphorylase Kinase Deficiency of Liver, Photic Sneeze Reflex, Photic Sneezing, Phototherapeutic keratectomy, PHS, Physicist John Dalton, Phytanic Acid Storage Disease, Pi Phenorype ZZ, PI, Pick Disease of the Brain, Pick's Disease, Pickwickian Syndrome, Pierre Robin Anomalad, Pierre Robin Complex, Pierre Robin Sequence, Pierre Robin Syndrome, Pierre Robin Syndrome with Hyperphalangy and Clinodactyly, Pierre-Marie's Disease, Pigmentary Degeneration of Globus Pallidus Substantia Nigra Red Nucleus, Pili Torti and Nerve Deaftiess, Pili Torti-Sensorineural Hearing Loss, Pituitary Dwarfism n, Pituitary Tumor after Adrenal ectomy, Pityriasis Pilaris, Pityriasis Rubra Pilaris, PJS, PKAN, PKD, PKD1, PKD25 PKD3, PKU, PKU1, Plagiocephaly, Plasma Cell Myeloma, Plasma Cell Leukemia, Plasma Thromboplastin Component Deficiency, Plasma Transglutaminase Deficiency, Plastic Induration Corpora Cavernosa, Plastic Induration of the Penis, PLD, Plicated Tongue, PLS, PMD, Pneumorenal Syndrome, PNH, PNM, PNP Deficiency, POD, POH, Poikiloderma Atrophicans and Cataract, Poikiloderma Congenitale, Poland Anomaly, Poland Sequence, Poland Syndactyly. Poland Syndrome, Poliodystrophia Cerebri Progressiva, Polyarthritis Enterica, Polyarteritis Nodosa, Polyanicular-Onset Juvenile Arthritis Type I, Poly articular-Onset Juvenile Arthritis Type II, Polyarticular-Onset Juvenile Arthritis Types I and n, Polychondritis, Polycystic Kidney Disease, Polycystic Kidney Disease Medullary Type, Polycystic Liver Disease, Polycystic Ovary Disease, Polycystic Renal Diseases, Polydactyly-Joubert Syndrome, Polydysplastic Epidermolysis Bullosa, Polydystrophia Oligophrenia, Polydystrophic Dwarfism, Polyglandular Autoimmune Syndrome Type III, Polyglandular Autoimmune Syndrome Type II, Polyglandular Autoimmune Syndrome Type 1, Polyglandular Autoimmune Syndrome Type II, Polyglandular Deficiency Syndrome Type II, Polyglandular Syndromes, Polymorphic Macula Lutea Degeneration, Polymorphic Macular Degeneration, Polymorphism of Platelet Glycoprotien Ib, Polymorphous Comeal Dystrophy Hereditary, Polymyalgia Rheumatica, Polymyositis and Dermatomyositis, Primary Agammaglobulinemia, Polyneuritis Peripheral, Polyneuropathy-Deafhess-Optic Atrophy. Polyneuropalhy Peripheral, Polyneuropathy and Polyradiculoneuropathy, Polyostotic Fibrous Dysplasia, Polyostotic Sclerosing Histiocytosis, Polyposis Familial, Polyposis Gardner Type, Polyposis Hamartomatous Intestinal, Polyposis-Osteomatosis-Epidermoid Cyst Syndrome, Polyposis Skin Pigmentation Alopecia and Fingernail Changes, Polyps and Spots Syndrome, Polyserositis Recurrent. Polysemy Y, Polysyndactyly with Peculiar Skull Shape, Polysyndactyly-Dysmorphic Craniofacies Greig Type, Pompe Disease, Pompe Disease, Popliteal Pterygium Syndrome, Porcupine Man, Porencephaly, Porencephaly, Porphobilinogen deaminase (PBG-D), Porphyria, Porphyria Acute Intermittent, Porphyria ALA-D, Porphyria Cutanea Tarda, Porphyria Cutanea Tarda Hereditaria, Porphyria Cutanea Tarda Symptomatica, Porphyria Hepatica Variegate, Porphyria Swedish Type, Porphyria Variegate, Porphyriam Acute Intermittent, Porphyrins, Porrigo Decalvans, Port Wine Stains, Portuguese Type Amyloidosis, Post-Infective Polyneuritis, Postanoxic Intention Myoclonus, Postaxial Acrofacial Dysostosis, Postaxial Polydactyly, Postencephalitic Intention Myoclonus, Posterior Cornea! Dystrophy Hereditary, Posterior Thalamic Syndrome, Postmyelographic Arachnoiditis, Postnatal Cerebral Palsy, Postoperative Cholestasis, Postpartum Galactorrhea-Amenorrhea Syndrome, Postpartum Hypopiruitarism, Postpartum Panhypopituitary Syndrome, Postpartum Panhypopituitarism, Postpartum Pituitary Necrosis, Postural Hypotension, Potassium-Losing Nephritis, Potassium Loss Syndrome. Potter Type I Infantile Polycystic Kidney Diseases, Potter Type III Poiycystic Kidney Disease, PPH, PPS, Prader-Willi Syndrome, Prader-Labhart-Willi Fancone Syndrome, Prealbumin Tyr-77 Amyloidosis, Preexcitation Syndrome, Pregnenolone Deficiency, Premature Atrial Contractions, Premature Senility Syndrome, Premature Supra ventricular Contractions, Premature Ventricular Complexes, Prenatal or Connatal Neuroaxonal Dystrophy, Presenile Dementia, Presenile Macula Lutea Retinae Degeneration, Primary Adrenal Insufficiency, Primary Agammaglobulinemias, Primary Aldosteronism, Primary Alveolar Hypoventilation. Primary Amyloidosis, Primary Anemia, Primary Beriberi, Primary Biliary, Primary Biliary Cirrhosis. Primary Brown Syndrome, Primary Camitine Deficiency, Primary Central Hypoventilation Syndrome, Primary Ciliary Dyskinesia Kartagener Type, Primary Cutaneous Amyloidosis, Primary Dystonia, Primary Failure Adrenocortical Insufficiency, Primary Familial Hypoplasia of the Maxilla, Primary Hemochromatosis, Primary Hyperhidrosis. Primary Hyperoxaluria [Type I], Primary Hyperoxaluria Type 1 (PHI), Primary Hyperoxaluria Type 1, Primary Hyperoxaluria Type II, Primary Hyperoxaluria Type III, Primary Hypogonadism, Primary' Intestinal Lymphangiectasia, Primary Lateral Sclerosis, Primary Nonhereditary Amyloidosis, Primary Obliterative Pulmonary Vascular Disease, Primary Progressive Multiple Sclerosis, Primary Pulmonary Hypertension, Primary Reading Disability, Primary Renal Glycosuria, Primary Sclerosing Cholangitis, Primary Thrombocythemia, Primary Tumors of Central Nervous System, Primary Visual Agnosia, Proctocolitis Idiopathic, Proctocolitis Idiopathic, Progeria of Adulthood, Progeria of Childhood, Progeroid Nanism, Progeriod Short Stature with Pigmented Nevi, Progeroid Syndrome of De Barsy, Progressive Autonomic Failure with Multiple System Atrophy, Progressive Bulbar Palsy, Progressive Bulbar Palsy Included, Progressive Cardiomyopathic Lentiginosis, Progressive Cerebellar Ataxia Familial, Progressive Cerebral Poliodystrophy, Progressive Choroidal Atrophy, Progressive Diaphyseal Dysplasia, Progressive Facial Hemiatrophy, Progressive Familial Myoclonic Epilepsy, Progressive Hemifacial Atrophy, Progressive Hypoerythemia, Progressive Infantile Poliodystrophy, Progressive Lenticular Degeneration, Progressive Lipodystrophy, Progressive Muscular Dystrophy of Childhood, Progressive Myoclonic Epilepsy, Progressive Osseous Heteroplasia, Progressive Pallid Degeneration Syndrome, Progressive Spinobulbar Muscular Atrophy, Progressive Supranuclear Palsy, Progressive Systemic Sclerosis, Progressive Tapetochoroidal Dystrophy, Proiine Oxidase Deficiency, Propionic Acidemia, Propionic Acidemia Type I (PCCA Deficiency), Propionic Acidemia Type II (PCCB Deficiency), Propionyl CoA Carboxylase Deficiency, Protanomaly, Protanopia, Protein-Losing Enteropathy Secondary to Congestive Heart Failure, Proteus Syndrome, Proximal Deletion of 4q Included, PRP, PRS, Prune Belly Syndrome, PS, Pseudo-Hurler Polydystrophy, Pseudo-Polydystrophy, Pseudoacanthosis Nigricans, Pseudoachondroplasia, Pseudocholinesterase Deficiency, Pseudogout Familial, Pseudohemophilia, Pseudohermaphroditism, Pseudohermaphroditism-Nephron Disorder-Wilm's Tumor, Pseudohypertrophic Muscular Dystrophy, Pseiidohypoparathyroidism, Pseudohypophosphatasia, Pseudopolydystrophy, Pseudothalidomide Syndrome, Pseudoxanthoma Elasticum, Psoriasis, Psorospermosis Follicularis, PSP, PSS, Psychomotor Convulsion, Psychomotor Epilepsy, Psychomotor Equivalent Epilepsy, PTC Deficiency, Pterygium, Pterygium Colli Syndrome, Pterygium Universale, Pterygolymphangiectasia, Pulmonary Atresia, Pulmonary Lymphangiomyomatosis, Pulmonary Stenosis, Pulmonic Stenosis-Ventricular Septal Defect, Pulp Stones, Pulpa! Dysplasia, Pulseless Disease, Pure Alymphocytosis, Pure Cutaneous Histiocytosis, Purine Nucleoside Phosphorylase Deficiency, Purpura Hemorrhagica, Purtilo Syndrome, PXE, PXE Dominant Type, PXE Recessive Type, Pycnodysostosis, Pyknodysostosis, Pyknoepilepsy, Pyroglutamic Aciduria, Pyroglutamicaciduria, Pyrroline Carboxylate Dehydrogenase Deficiency, Pyruvate Carboxylase Deficiency, Pyruvate Carboxylase Deficiency Group Ab Pyruvate Carboxylase Deficiency Group B; Pyruvate Dehydrogenase Deficiency, Pyruvate Kinase Deficiency, q25-qter, q26 or q27-qter, q31 or 32-qter, QT Prolongation with Extracellular Hypohypocalcinemia, QT Prolongation without Congenital Deafness, QT Prolonged with Congenital Deafness, Quadriparesis of Cerebral Palsy, Quadriplegia of Cerebral Palsy, Quanta! Squander, Quantal Squander, r4, r6, r!4, r 18, r.21, r22, Rachischisis Posterior, Radial Aplasia-Amegakaryocytic Thrombocytopenia, Radial Aplasia-Thrombocytopenia Syndrome, Radial Nerve Palsy, Radicular Neuropathy Sensory, Radicular Neuropathy Sensory Recessive, Radicular Dentin Dysplasia, Rapid-onset Dystonia-parkinsonism, Rapp-Hodgkin Syndrome, Rapp-Hodgkin (hypohidrotic) Ectodermal Dysplasia syndrome, Rapp-Hodgkin Hypohidrotic Ectodermal Dysplasias, Rare hereditary ataxia with polyneuritic changes and deafness caused by a defect in the enzyme phytanic acid hydroxylase, Rautenstrauch-Wiedemann Syndrome, Rautenstrauch-Wiedemann Type Neonatal Progeria. Raynaud's Phenomenon, RDP. Reactive Functional Hypoglycemia, Reactive Hypoglycemia Secondary to Mild Diabetes, Recessive Type Kenny-Caffe Syndrome, Recklin Recessive Type Myotonia Congenita, Recklinghausen Disease, Rectoperineal Fistula, Recurrent Vomiting, Reflex Neurovascular Dystrophy, Reflex Sympathetic Dystrophy Syndrome, Refractive Errors, Refractor}' Anemia, Refrigeration Palsy, Refsum Disease, Refsum's Disease, Regional Enteritis, Reid-Barlow's syndrome, Reifenstein Syndrome, Reiger Anomaly-Growth Retardation, Reiger Syndrome, Reimann Periodic Disease, Reimann's Syndrome, Reis-Bucklers Cornea! Dystrophy, Reiter's Syndrome, Relapsing Guillain-Barre Syndrome, Relapsing-Remitting Multiple Sclerosis, Renal Agenesis, Renal Dysplasia-Blindness Hereditary, Renal Dysplasia-Retmal Aplasia Loken-Senior Type. Renal Glycosuria, Renal Glycosuria Type A, Renal Glycosuria Type B, Renal Glycosuria Type 0, Renal-Oculocerebrodystrophy, Renal-Retinal Dysplasia with Medullary Cystic Disease, Renal-Retinal Dystrophy Familial, Renal-Retinal Syndrome, Rendu-Osler-Weber Syndrome, Respirator)' Acidosis, Respiratory Chain Disorders, Respiratory Myoclonus, Restless Legs Syndrome, Restrictive Cardio myopathy, Retention Hyperlipemia, Rethore Syndrome (obsolete), Reticular Dysgenesis, Retinal Aplastic-Cystic Kidneys-Joubert Syndrome, Retinal Cone Degeneration, Retinal Cone Dystrophy, Retinal Cone-Rod Dystrophy, Retinitis Pigmentosa, Retinitis Pigmentosa and Congenital Deafness, Retinoblastoma, Retinol Deficiency, Retinoschisis, Retinoschisis Juvenile, Retraction Syndrome, Retrobulbar Neuropathy. Retrolenticular Syndrome, Rett Syndrome, Reverse Coarction, Reye Syndrome, Reye's Syndrome, RGS, Rh Blood Factors, Rh Disease, Rh Factor Incompatibility, Rh Incompatibility, Rhesus Incompatibility, Rheumatic Fever. Rheumatoid Arthritis, Rheumatoid Myositis, Rhinosinusogenic Cerebral Arachnoiditis, Rhizomelic Chondrodysplasia Punctata (RCDP),Acatalasemia,Classical Refsum disease, RHS, Rhythmical Myoclonus, Rib Gap Defects with Micrognathia, Ribbing Disease (obsolete), Ribbing Disease, Richner-Hanhart Syndrome, Rieger Syndrome, Rietefs Syndrome, Right Ventricular Fibrosis. Riley-Day Syndrome, Riley-Smith syndrome, Ring Chromosome 14, Ring Chromosome 18, Ring 4, Ring 4 Chromosome, Ring 6, Ring 6 Chromosome, Ring 9, Ring 9 Chromosome R9, Ring 14, Ring 15, Ring 15 Chromosome (mosaic pattern), Ring 18, Ring Chromosome 18, Ring 21, Ring 21 Chromosome, Ring 22, Ring 22 Chromosome, Ritter Disease, Ritter-Lyell Syndrome, RLS, RMSS, Roberts SC-Phocomelia Syndrome, Roberts Syndrome, Roberts Tetraphocomelia Syndrome, Robertson's Ectodermal Dyspiasias, Robin Anomalad, Robin Sequence. Robin Syndrome, Robinow Dwarfism, Robinow Syndrome, Robinow Syndrome Dominant Form, Robinow Syndrome Recessive Form, Rod myopafhy, Roger Disease, Rokitansky's Disease, Romano-Ward Syndrome, Romberg Syndrome, Rootless Teeth, Rosenberg-Chutorian Syndrome, Rosewater Syndrome, Rosselli-Gulienatti Syndrome, Rothmund-Thornson Syndrome, Roussy-Levy Syndrome, RP, RS X-Linked, RS, RSDS, RSH Syndrome, RSS, RSTS, RTS, Rubella Congenital, Rubinstein Syndrome, Rubinstein-Taybi Syndrome, Rubinstein Taybi Broad Thumb-Hallux syndrome, Rufous Albinism, Ruhr's Syndrome. Russell's Diencephalic Cachexia, Russell's Syndrome, Russell Syndrome, Russell-Silver Dwarfism, Russell-Silver Syndrome, Russell-Silver Syndrome X-iinked, Ruvalcaba-Myhre-Smith syndrome (RMSS), Ruvalcaba Syndrome, Ruvalcaba Type Osseous Dysplasia with Mental Retardation, Sacral Regression, Sacral Agenesis Congenital, SAE, Saethre-Chotzen Syndrome, Sakati, Sakati Syndrome, Sakati- Nyhan Syndrome, Salaam Spasms, Salivosudoriparous Syndrome, Salzman Nodular Comeal Dystrophy, Sandhoff Disease, Sanfilippo Syndrome, Sanfilippo Type A, Sanfilippo Type B, Santavuori Disease, Santavuori-Haltia Disease, Sarcoid of Boeck, Sarcoidosis, Sathre-chotzen, Saturday Night Palsy, SBMA, SC Phocomelia Syndrome, SC Syndrome, SCA 3, SCAD Deficiency, SCAD Deficiency Adult-Onset Localized, SCAD Deficiency Congenital Generalized, SCAD, SCADH Deficiency, Scalded Skin Syndrome, Scalp Defect Congenital, Scaphocephaly, Scapula Elevata, Scapuloperoneal myopathy, Scapuloperoneal Muscular Dystrophy, Scapuloperoneal Syndrome Myopathic Type, Scarring Bullosa, SCHAD, Schaumarm's Disease, Scheie Syndrome, Schereshevkii-Turner Syndrome, Schilder Disease, Schilder Encephalitis, Schilder's Disease, Schindler Disease Type I (Infantile Onset), Schindler Disease Infantile Onset, Schindler Disease, Schindler Disease Type II (Adult Onset), Schinzel Syndrome, Schinzel-Giedion Syndrome, Schinzel Acrocallosal Syndrome, Schinzel-Giedion Midface-Retraction Syndrome, Schizencephaly, Schizophrenia, Schmid Type Metaphyseal Chondrodysplasia, Schmid Metaphyseal Dysostosis, Schmid-Fraccaro Syndrome, Schmidt Syndrome, Schopf-Schultz-Passarge Syndrome, Schueller-Christian Disease, Schut-Haymaker Type, Schwartz-Jampel-Aberfeld Syndrome, Schwartz-Jampel Syndrome Types 1A and IB, Schwartz-Jampel Syndrome, Schwartz-Jampel Syndrome Type 2, SCID, Scleroderma, Sclerosis Familial Progressive Systemic, Sclerosis Diffuse Familial Brain, Sciatic Nerve Crush, Scott Craniodigital Syndrome With Mental Retardation, Scrota! Tongue, SCS, SD, SDS, SDYS, Seasonal Conjunctivitis, Sebaceous Nevus Syndrome, Sebaceous nevus, Seborrheic Keratosis, Seborrheic Warts, Seckel Syndrome, Seckel Type Dwarfism, Second Degree Congenital Heart Block, Secondary Amyloidosis, Secondary Blepharospasm, Secondary Non-tropical Sprue, Secondary Brown Syndrome, Secondary Beriberi, Secondary Generalized Amyloidosis, Secondary Dystonia, Secretory Component Deficiency, Secretory IgA Deficiency, SED Tarda, SED Congenital, SEDC, Segmental linear achromic nevus, Segmentai Dystonia, Segmental Myoclonus, Seip Syndrome, Seitelberger Disease, Seizures, Selective Deficiency of IgG Subclasses, Selective Mutism, Selective Deficiency of IgG Subclass, Selective IgM Deficiency, Selective Mutism, Selective IgA Deficiency, Self-Healing Histiocytosis, Semilobar Holoprosencephaly, Seminiferous Tubule Dysgenesis, Senile Retinoschisis, Senile Warts, Senior-Loken Syndrome, Sensory Neuropathy Hereditary Type 1, Sensory Neuropathy Hereditary Type II, Sensory Neuropathy Hereditary Type I, Sensory Radicular Neuropathy, Sensory Radicular Neuropathy Recessive, Septic Progressive Granulomatosis, Septo-Optic Dysplasia, Serous Circumscribed Meningitis, Serum Protease Inhibitor Deficiency, Serum Carnosinase Deficiency, Setleis Syndrome, Severe Combined Immunodeficiency, Severe Combined Immunodeficiency with Adenosine Deaminase Deficiency, Severe Combined Immunodeficiency (SCDD), Sex Reversal, Sexual Infantilism, SGB Syndrome, Sheehan Syndrome, Shields Type Dentinogenesis Imperfecta, Shingles,varicella-zoster virus, Ship Beriberi, SHORT Syndrome, Short Arm 18 Deletion Syndrome, Short Chain Acyl CoA Dehydrogenase Deficiency, Short Chain Acyl-CoA Dehydrogenase (SCAD) Deficiency, Short Stature and Facial Telangiectasis, Short Stature Facial/Skeletal Anomalies-Retardation-Macrodontia, Short Stature-Hyperextensibility-Rieger Anomaly-Teething Delay, Short Stature-Onychodysplasia, Short Stature Telangiectatic Erythema of the Face, SHORT Syndrome, Shoshin Beriberi, Shoulder girdle syndrome, Shprintzen-Goldberg Syndrome, Shulman Syndrome, Shwachman-Bodian Syndrome, Shwachman-Diamond Syndrome, Shwachman Syndrome, Shwachman-Diamond-Oski Syndrome, Shwachmann Syndrome, Shy Drager Syndrome, Shy-Magee Syndrome. SI Deficiency, Sialidase Deficiency, Sialidosis Type I Juvenile, Sialidosis Type II Infantile, Sialidosis, Sialolipidosis, Sick Sinus Syndrome. Sickle Cell Anemia, Sickle Cell Disease, Sickle Cell-Hemoglobin C Disease, Sickle Cell-Hemoglobin D Disease, Sickle Cell-Thalassemia Disease, Sickle Cell Trait, Sideroblastic Anemias, Sideroblastic Anemia, Sideroblastosis, SIDS, Siegel-Cattan-Mamou Syndrome, Siemens-Bloch type Pigmented Dermatosis, Siemens Syndrome, Siewerling-Creutzfeldt Disease, Siewert Syndrome, Silver Syndrome, Silver-Russell Dwarfism, Silver-Russell Syndrome, Simmond's Disease, Simons Syndrome, Simplex Epidermolysis Bullosa, Simpson Dysmorphia Syndrome, Simpson-Golabi-Behmel Syndrome, Sinding-Larsen-Johanssoc Disease, Singleton-Merten Syndrome, Sinus Arrhythmia, Sinus Venosus, Sinus tachycardia, Sirenomelia Sequence, Sirenomelus, Situs Inversus Bronchiectasis and Sinusitis, SJA Syndrome, Sjogren Larsson Syndrome Ichthyosis, Sjogren Syndrome. Sjogren's Syndrome, SJS, Skeletal dysplasia, Skeletal Dysplasia Weismarm Netter Stuhl Type, Skin Peeling Syndrome, Skin Neoplasms, Skull Asymmetry and Mild Retardation, Skull Asymmetry and Mild Syndactyly, SLE, Sleep Epilepsy, Sleep Apnea. SLO, Sly Syndrome, SMA, SMA Infantile Acute Form, SMA I, SMA III, SMA type L SMA type H, SMA type III, SMA3, SMAXl, SMCR, Smith Lernli Opitz Syndrome, Smith Magenis Syndrome, Smith-Magenis Chromosome Region, Smith-McCort Dwarflsm, Smith-Opitz-Inborn Syndrome, Smith Disease, Smoldering Myeloma, SMS, SNE, Sneezing From Light Exposure, Sodium valproate, Solitary Plasmacytoma of Bone, Sorsby Disease, Sotos Syndrome, Souques-Charcot Syndrome, South African Genetic Porphyria, Spasmodic Dysphonia, Spasmodic Torticollis, Spasmodic Wryneck, Spastic Cerebral Palsy, Spastic Colon, Spastic Dysphonia, Spastic Paraplegia, SPD Calcinosis, Specific Antibody Deficiency with Normal Immunoglobulins, Specific Reading Disability, SPH2, Spherocytic Anemia, Spherocytosis, Spherophakia-Brachymorphia Syndrome, Sphingomyelin Lipidosis, Sphingomyelinase Deficiency, Spider fingers, Spielmeyer-Vogt Disease, Spielmeyer-Vogt-Batten Syndrome, Spina Bifida, Spina Bifida Aperta, Spinal Arachnoiditis, Spinal Arteriovenous Malformation, Spinal Alaxia Hereditofamilial, Spinal and Bulbar Muscular Atrophy, Spinal Cord Crush, Spinal Diffuse Idiopathic Skeletal Hyperostosis, Spina] DISH, Spinal Muscular Atrophy, Spinal Muscular Atrophy All Types, Spinal Muscular Atrophy Type ALS, Spinal Muscular Atrophy-Hypertrophy of the Calves, Spinal Muscular Atrophy Type I, Spinal Muscular Atrophy Type HI, Spinal Muscular Atrophy type 3, Spinal Muscular Atrophy-Hypertrophy of the Calves, Spinal Ossifying Arachnoiditis, Spinal Stenosis, Spino Cerebellar Ataxia, Spinocerebellar Atrophy Type I, Spinocerebellar Ataxia Type I (SCA1), Spinocerebellar Ataxia Type D (SCAITj, Spinocerebellar Ataxia Type III (SCAIII), Spinocerebellar Ataxia Type III (SCA 3), Spinocerebellar Ataxia Type TV (SCAIV), Spinocerebellar Ataxia Type V (SCAV), Spinocerebellar Ataxia Type VI (SCAVI), Spinocerebellar Ataxia Type VII (SCAVII), Spirochetal Jaundice, Splenic Agenesis Syndrome, Splenic Ptosis, Splenoptosis, Split Hand Deformity-Mandibulofacial Dysostosis, Split Hand Deformity, Spondyloarthritis, Spondylocostal Dysplasia - Type I, Spondyloepiphyseal Dysplasia Tarda, Spondylothoracic Dysplasia, Spondylotic Caudal Radiculopathy, Sponge Kidney, Spongioblastoma Multiforme, Spontaneous Hypoglycemia, Sprengel Deformity, Spring Ophthalmia, SRS, ST, Stale Fish Syndrome, Staphyloccal Scalded Skin Syndrome, Stargardt's Disease, Startle Disease, Status Epilepticus, Steele-Richardson-Olszewski Syndrome, Steely Hair Disease, Stein-Leventhal Syndrome, Steinert Disease, Stengel's Syndrome, Stengel-Batten-Mayou-Spielmeyer-Vogt-Stock Disease, Stenosing Cholangitis, Stenosis of the Lumbar Vertebral Canal, Stenosis, Steroid Sulfatase Deficiency, Stevanovic's Ectodermal Dysplasias, Stevens Johnson Syndrome, STGD, Stickler Syndrome, Stiff-Man Syndrome, Stiff Person Syndrome, Still's Disease, Stilling-Turk-Duane Syndrome, Stillis Disease, Stimulus-Sensitive Myoclonus, Stone Man Syndrome, Stone Man, Streeter Anomaly, Striatonigral Degeneration Autosomal Dominant Type, Striopallidodentate Calcinosis, Stroma. Descemet's Membrane, Stromal Corneal Dystrophy, Strums Lymphomatosa, Sturge-Kalischer-Weber Syndrome, Sturge Weber Syndrome, Sturge-Weber Phakomatosis, Subacute Necrotizing Encephalomyelopathy, Subacute Spongiform Encephalopathy, Subacute Necrotizing Encephalopathy, Subacute Sarcoidosis, Subacute Neuronopathic, Subaortic Stenosis, Subcortical Arteriosclerotic Encephalopathy, Subendocardial Sclerosis, Succinylcholine Sensitivity, Sucrase-Isomaltase Deficiency Congenital, Sucrose-Isomaltose Malabsorption Congenital, Sucrose Intolerance Congenital, Sudanophilic Leukodystrophy ADL, Sudanophilic Leukodystrophy Pelizaeus-Merzbacher Type, Sudanophilic Leukodystrophy Included, Sudden Infant Death Syndrome, Sudeck's Atrophy, Sugio-Kajii Syndrome, Summerskill Syndrome, Sumrnil Acrocephalosyndactyly, Summitt's Acrocephalosyndactyly, Summitt Syndrome, Superior Oblique Tendon Sheath Syndrome, Suprarenal glands, Supravalvular Aortic Stenosis, Supraventricular tachycardia, Surdicardiac Syndrome, Surdocardiac Syndrome, SVT, Sweat Gland Abscess, Sweating Gustatory Syndrome, Sweet Syndrome, Swiss Cheese Cartilage Syndrome, Syndactylic Oxycephaly, Syndactyly Type I with Microcephaly and Mental Retardation, Syndromatic Hepatic Ductular Hypoplasia, Syringomyelia, Systemic. Aleukemic Reticuloendotheliosis, Systemic Amyloidosis, Systemic Carnitine Deficiency, Systemic Elastorrhexis, Systemic Lupus Erythematosus, Systemic Mast Cell Disease, Systemic Mastocytosis, Systemic-Onset Juvenile Arthritis, Systemic Sclerosis, Systopic Spleen, T-Lymphocyte Deficiency, Tachyalimentation Hypoglycemia, Tachycardia, Takahara syndrome, Takayasu Disease, Takayasu Arteritis, Talipes Calcaneus, Talipes Equinovarus, Talipes Equinus, Talipes Varus, Talipes Valgus, Tandem Spinal Stenosis, Tangier Disease, Tapetoretinal Degeneration, TAR Syndrome, Tardive Dystonia, Tardive Muscular Dystrophy, Tardive Dysldnesia, Tardive Oral Dyskinesia, Tardive Dystonia, Tardy Ulnar Palsy, Target Cell Anemia, Tarsomegaly, Tarui Disease, TAS Midline Defects Included, TAS Midline Defect, Tay Sachs Sphingolipidosis, Tay Sachs Disease, Tay Syndrome Ichthyosis, Tay Sachs Sphingolipidosis, Tay Syndrome Ichthyosis, Taybi Syndrome Type I, Taybi Syndrome, TCD, TCOF1, TCS, TD, TDO Syndrome, TDO-I, TDO-II. TDO-II1, Telangiectasis, Telecanthus with Associated Abnormalities, Telecanthus-Hypospadias Syndrome, Temporal Lobe Epilepsy, Temporal Arteritis/Giant Cell Arteritis, Temporal Arteritis, TEN, Tendon Sheath Adherence Superior Obliqu, Tension Myalgia, Terminal Deletion of 4q Included, Terrian Corneal Dystrophy, Teschler-Nicola/Killian Syndrome, Tethered Spinal Cord Syndrome, Tethered Cord Malformation Sequence, Tethered Cord Syndrome, Tethered Cervical Spinal Cord Syndrome. Tetrahydrobiopterin Deficiencies, Tetrahydrobiopterin Deficiencies, Tetralogy of Fallot, Tetraphocomelia-Thrombocytopenia Syndrome, Tetrasomy Short Arm of Chromosome 9, Tetrasomy 9p, Tetrasomy Short Arm of Chromosome 18, Thalamic Syndrome, Thalamic Pain Syndrome, Thalamic Hyperesthetic Anesthesia, Thalassemia Intermedia. Thalassemia Minor, Thalassemia Major, Thiamine Deficiency, Thiamine-Responsive Maple Syrup Urine Disease, Thin-Basement-Membrane Nephropathy, Thiolase deficiency,RCDP,Acyl-CoA dihydroxyacetonephosphate acyltransferase, Third and Fourth Pharyngeai Pouch Syndrome, Third Degree Congenital (Complete) Heart Block, Thomsen Disease, Thoracic-Pelvic-Phalangeal Dystrophy, Thoracic Spinal Canal, Thoracoabdominal Syndrome, Thoraeoabdominal Ectopia Cordis Syndrome, Three M Syndrome, Three-M Slender-Boned Nanism, Thrombasthenia of Glanzmann and Naegeli, Tnrombocythemia Essential, Thrombocytopenia-Absent Radius Syndrome, Thrombocytopenia-HemangiomE Syndrome, Thrombocytopenia-Absent Radii Syndrome, Thrombophilia Hereditary Due to AT III, Thrombotic Thrombocytopenic Purpura, Thromboulcerative Colitis, Thymic Dysplasia with Normal Immunoglobulins, Thymic Agenesis,Thymic Aplasia DiGeorge Type, Thymic Hypoplasia Agammaglobulinemias Primary Included, Thymic Hypoplasia DiGeorge Type, Thymus Congenital Aplasia, Tic Douloureux, Tics. Tinel's syndrome, Tolosa Hunt Syndrome. Tonic Spasmodic Torticollis, Tonic Pupil Syndrome, Tooth and Nail Syndrome, Torch Infection, TORCH Syndrome, Torsion Dystonia. Torticollis, Total Lipodystrophy, Total anomalous pulmonary venous connection. Touraine's Aphthosis, Tourette Syndrome, Tourette's disorder, Townes-Brocks Syndrome, Townes Syndrome, Toxic Paralytic Anemia, Toxic Epidermal Necrolysis, Toxopachyosteose Diaphysaire Tibio-Peroniere, Toxopachyosteose, Toxoplasmosis Other Agents Rubella Cytomegalovirus Herpes Simplex, Tracheoesophageal Fistula with or without Esophageal Atresia, Tracheoesophageal Fistula, Transient neonatal myasthenia gravis. Transitional Atrioventricular Septal Defect, Transposition of the great arteries, Transtelephonic Monitoring, Transthyretin Methionine- 30 Amyloidosis (Type I), Trapezoidocephaly-Multiple Synostosis Syndrome, Treacher Collins Syndrome, Treacher Collins-Franceschetti Syndrome 1, Trevor Disease, Triatrial Heart, Tricho-Dento-Osseous Syndrome, Trichodento Osseous Syndrome, Trichopoliodystrophy, Trichorhinophalangeal Syndrome, Trichorhinophalangeal Syndrome, Tricuspid atresia, Trifunctional Protein Deficiency, Trigeminal Neuralgia, Triglyceride Storage Disease Impaired Long-Chain Fatty Acid Oxidation, Trigonitis, Trigonocephaly, Trigonocephaly Syndrome, Trigonocephaly "C" Syndrome, Trimethylaminuria, Triphalangeal Thumbs-Hypoplastic Distal Phalanges-Onychodystrophy, Triphalangeal Thumb Syndrome, Triple Symptom Complex of Behcet, Triple X Syndrome, Triple X Syndrome, Triploid Syndrome, Triploidy, Triploidy Syndrome, Trismus-Pseudocamptodactyly Syndrome, Trisomy, Trisomy G Syndrome, Trisomy X, Trisomy 6q Partial, Trisomy 6q Syndrome Partial, Trisomy 9 Mosaic, Trisomy 9P Syndrome (Partial) Included, Trisomy llq Partial, Trisomy 14 Mosaic, Trisomy 14 Mosaicism Syndrome, Trisomy 21 Syndrome, Trisomy 22 Mosaic, Trisomy 22 Mosaicism Syndrome, TRPS; TRPS1, TRPS2, TRPS3, True Hermaphroditism, Truncus arteriosus, Tryptophan Malabsorption, Tryptophan Pyrrolase Deficiency, TS, TTP, TTTS, Tuberous Sclerosis, Tubular Ectasia, Turcot Syndrome, Turner Syndrome, Turner-Kieser Syndrome, Turner Phenotype with Normal Chromosomes (Karyotype), Turner-Vamy Syndrome, Turricephaly. Twin-Twin Transfusion Syndrome, Twin-to-Twin Transfusion Syndrome, Type A, Type B, Type AB, Type 0, Type I Diabetes, Type I Familial Incomplete Male, Type I Familial Incomplete Male Pseudohermaphroditism, Type I Gaucher Disease, Type I (PCCA Deficiency), Type I Tyrosinemia, Type II Gaucher Disease, Type li Histiocytosis, Type II (PCCB Deficiency), Type II Tyrosinnemia, Type IIA Distal Arthrogryposis Multiplex Congenita, Type III Gaucher Disease, Type III Tyrosinemia, Type III Dentinogenesis Imperfecta, Typical Retinoschisis, Tyrosinase Negative Albinism (Type I), Tyrosinase Positive Albinism (Type II), Tyrosinemia type 1 acute form, Tyroshiemia type 1 chronic form, Tyrosinosis, UCE, Ulcerative Colitis. Ulcerative Colitis Chronic Non-Specific, Ulnar-Mammary Syndrome, Ulnar-Mammary Syndrome of Pallister, Ulnar Nerve Palsy. UMS, Unclassified FODs, Unconjugated Benign Bilirubinemiav, Underactivity of Parathyroid, Unilateral Ichthyosiform Erythroderma with Ipsilateral Malformations Limb, Unilateral Chondromatosis, Unilateral Defect of Pectoralis Muscle and Syndactyly of the Hand, Unilateral Hemidysplasia Type, Unilateral Megalencephaly, Unilateral Partial Lipodystrophy, Unilateral Renal Agenesis, Unstable Colon, Unverricht Disease, Unverricht-Lundborg Disease, Unverricht-Lundborg-Laf Disease, Unverricht Syndrome, Upper Limb - Cardiovascular Syndrome (Holt-Gram), Upper Motor Neuron Disease, Upper Airway Apnea, Urea Cycle Defects or Disorders, Urea Cycle Disorder Arginase Type, Urea Cycle Disorder Arginino Succinase Type, Urea Cycle Disorders Carbamyl Phosphate Synthetase Type, Urea Cycle Disorder Citrullinemia Type, Urea Cycle Disorders N-Acrtyl Qlutamate Synthetase Typ, Urea Cycle Disorder OTC Type, Urethral Syndrome, Urethro-Oculo-Articular Syndrome, Uridine Diphosphate Glucuronosyltransferase Severe Def. Type I, Urinary Tract Defects, Urofacial Syndrome, Uroporphyrinogen III cosynthase, Urticaria pigmentosa, Usher Syndrome, Usher Type I, Usher Type II, Usher Type III, Usher Type IV, Uterine Synechiae, Uoporphyrinogen I-synthase, Uveitis, Uveomeningitis Syndrome, V-CJD, VACTEL Association, VACTERL Association, VACTERL Syndrome, Valgus Calcaneus, Valine Transaminase Deficiency, Valinemia, Valproic Acid, Valproate acid exposure, Valproic acid exposure, Valproic acid, Van Buren's Disease, Van der Hoeve-Habertsma-Waardenburg-Gauldi Syndrome, Variable Onset Immunoglobulin Deficiency Dysgammaglobulinemia, Variant Creutzfeldt-Jakob Disease (V-CJD), Varicella Embryopathy, Variegate Porphyria, Vascular Birthmarks, Vascular Dementia Binswanger's Type, Vascular Erectile Tumor, Vascular Hemophilia, Vascular Malformations, Vascular Malformations of the Brain, Vasculitis, Vasomotor Ataxia, Vasopressin-Resistant Diabetes Insipidus, Vasopressin-Sensitive Diabetes Insipidus, VATER Association, Vcf syndrome, Vcfs, Velocardiofacial Syndrome, VeloCardioFacial Syndrome, Venereal Arthritis, Venous Malformations, Ventricular Fibrillation, Ventricular Septal Defects, Congenital Ventricular Defects, Ventricular Septal Defect, Ventricular Tachycardia, Venual Malformations, VEOHD, Vermis Aplasia, Vermis Cerebellar Agenesis, Vernal Keratoconjunctivitis, Verruca, Vertebral Anal Tracheoesophageal Esophageal Radial, Vertebral Ankylosing Hyperostosis, Very Early Onset Huntington's Disease, Very Long Chain Acyl-CoA Dehydrogenase (VLCAD) Deficiency, Vestibular Schwannoma, Vestibular Schwannoma Neurofibromatosis, Vestibulocerebeliar. Virchow's Oxycephaly, Visceral Xanthogranulomatosis, Visceral Xantho-Granulornatosis, Visceral myopathy-External Ophthalmoplegia, Visceromegaly-Umbilical Hernia-Macroglossia Syndrome, Visual Amnesia, Vitamin A Deficiency, Vitamin B-l Deficiency, Vitelline Macular Dystrophy, Vitiligo, Vitiligo Capitis, Vitreoretinal Dystrophy, VKC, VKH Syndrome, VLCAD, Vogt Syndrome, Vogt Cephalosyndactyly, Vogt Koyanagi Harada Syndrome, Von Bechterew-Strumpell Syndrome, Von Eulenburg Paramyotonia Congenita, Von Prey's Syndrome, Von Gierke Disease, Von Hippei-Lindau Syndrome, Von Milculicz Syndrome, Von Recklinghausen Disease, Von Willebrandt Disease, VP, Vrolik Disease (Type II), VSD, Vulgaris Type Disorder of Cornification, Vulgaris Type Ichthyosis, W Syndrome, Waardenburg Syndrome, Waardenburg-Klein Syndrome, Waardenburg Syndrome Type I (WS1), Waardenburg Syndrome Type E (WS2), Waardenburg Syndrome Type IIA (WS2A), Waardenburg Syndrome Type IB (WS2B), Waardenburg Syndrome Type III (WS3), Waardenburg Syndrome Type IV (WS4), Waelsch's Syndrome, WAGR Complex, WAGR Syndrome, Waldenstroem's Macroglobulinemia, Waldenstrom's Purpura, Waldenstrom's Syndrome, Waldmann Disease, Walker-Warburg Syndrome, Wandering Spleen, Warburg Syndrome, Warm Antibody Hemolytic Anemia, Warm Reacting Antibody Disease, Wartenberg Syndrome, WAS, Water on the Brain, Watson Syndrome, Watson-Alagille Syndrome, Waterhouse-Friderichsen syndrome, Waxy Disease, WBS, Weaver Syndrome, Weaver-Smith Syndrome, Weber-Cockayne Disease, Wegener's Grarmlomatosis, Weil Disease, Weil Syndrome, Weill-Marchesani, Weill-Marchesani Syndrome, Weill-Reyes Syndrome, Weismann-Netter-Stuhl Syndrome, Weissenbacher-Zweymuller Syndrome, Wells Syndrome. Wenckebach, Werdnig-Hoffman Disease, Werdnig-Hoffinan Paralysis, Werlhofs Disease, Werner Syndrome, Wernicke's (C) I Syndrome, Wernicke's aphasia, Weraicke-Korsakoff Syndrome, West Syndrome, Wet Beriberi, WHCR, Whipple's Disease, Whipple Disease, Whistling face syndrome, Whistling Face-Windmill Vane Hand Syndrome, White-Darier Disease, Whitnall-Norman Syndrome, Whorled nevoid hypermelanosis, WHS, Wieacker Syndrome, Wieacher Syndrome, Wieacker-Wolff Syndrome, Wiedmann-Beckwith Syndrome, Wiedemann-Rautenstrauch Syndrome, Wildervanck Syndrome, Willebrand-Juergens Disease, Willi-Prader Syndrome, Williams Syndrome, Williams-Beuren Syndrome, Wilms' Tumor, Wilms' Tumor-Aniridia-Gonadoblastoma-Mental Retardation Syndrome, Wilms Tumor Aniridia Gonadoblastoma Mentai Retardation, Wilms' Tumor-Aniridia-Genitourinary Anomalies-Mental Retardation Syndrome, Wilms Tumor-Pseudohermaphroditism-Nephropathy, Wilms Tumor and Pseudohermaphroditism, Wilms Tumor-Pseuodohermaphroditism-Gloroerulopathy, Wilson's Disease, Winchester Syndrome, Winchester-Grossman Syndrome, Wiskott- Aldrich Syndrome, Wiskott-Aldrich Type Immunodeficiency, Witkop Ectodermal Dyspiasias, Witkop Tooth-Nail Syndrome, Wittmaack-Ekbom Syndrome, WM Syndrome, WMS, WNS, Wohlfart-Disease, Wohlfart-Kugelberg-Welander Disease, Wolf Syndrome, Wolf-Hirschhorn Chromosome Region (WHCR), Wolf-Hirschhom Syndrome, Wolff-Parkinson-White Syndrome, Wolfram Syndrome, Wolman Disease (Lysomal Acid Lypase Deficiency), Woody Guthrie's Disease, WPW Syndrome, Writer's Cramp, WS, WSS, WWS, Wyburn-Mason Syndrome, X-Linked Addison's Disease, X-linked Adrenoleukodystrophy (X-ALD), X-linked Adult Onset Spinobulbar Muscular Atrophy, X-linked Adult Spinal Muscular Atrophy, X-Linked Agammaglobulinemia with Growth Hormone Deficiency, X-Linked Agammaglobulinemia, Lymphopro lifer ate X-Linked Syndrome, X-linked Cardio myopathy and Neutropenia, X-Linked Centronuclear myopathy, X-linked Copper Deficiency, X-linked Copper Malabsorption, X-Linked Dominant Conradi-Hunermann Syndrome, X-Linked Dominant Inheritance Agenesis of Corpus Callosum, X-Linked Dystonia-parkinsonism, X Linked Ichthyosis, X-Linked Infantile Agammaglobulinemia., X-Linked Infantile Nectrotizing Encephalopathy, X-linked Juvenile Retinoschisis. X-linked Lissencephaly, X-linked Lymphoproliferative Syndrome, X-linked Mental Retardation-Clasped Thumb Syndrome, X-Linked Mental Retardation with Hypotonia, X-linked Mental Retardation and Macroorchidism, X-Linked Progressive Combined Variable Immunodeficiency, X-Linked Recessive Conradi-Hunermann Syndrome, X-Linked Recessive Severe Combined Immunodeficiency, X-Linked Retinoschisis. X-linked Spondyloepiphyseal Dysplasia, Xanthine Oxidase Deficiency (Xanthinuria Deficiency, Hereditary), Xanthinuria Deficiency, Hereditary (Xanthine Oxidase Deficiency), Xanthogranulomatosis Generalized, Xanthoma Tuberosum, Xeroderma Pigmentosum, Xeroderma Pigmentosum Dominant Type, Xeroderma Pigmentosum Type A I XPA Classical Form, Xeroderma Pigmentosum Type B II XPB, Xeroderma Pigme,ntosum Type E V XPE, Xeroderma Pigmentosum Type C III XPC, Xeroderma Pigmentosum Type D IV XPD, Xeroderma Pigmentosum Type F VI XPF, Xeroderma Pigmentosum Type G VII XPG, Xeroderma Pigmentosum Variant Type XP-V, Xeroderma-Talipes-and Enamel Defect, Xerodermic Idiocy. Xerophthalmia, Xerotic Keratitis, XL?, XO Syndrome, XP, XX Male Syndrome,Sex Reversal, XXXXX Syndrome, XXY Syndrome, XYY Syndrome, XYY Chromosome Pattern, Yellow Mutant Albinism. Yellow Nail Syndrome, YKL, Young Female Arteritis, Yunis-Varon Syndrome, YY Syndrome, Z-E Syndrome, Z- and -Protease Inhibitor Deficiency, Zellweger Syndrome, Zeliweger cerebro-hepato-renai syndrome, ZES, Ziehen-Oppenheim Disease (Torsion Dystonia), Zirnmermann-Laband Syndrome, Zinc Deficiency Congenital, Zinsser-Cole-Engman Syndrome, ZLS, Zollinger-Ellison Syndrome. In one embodiment, the pharmaceutical composition comprising an isolated TNF-a or chimeric molecule thereof can be used, alone or in conjunction with other biologies, drugs or therapies, for the treatment of diseases or conditions such as numerous solid tumors (especially by targeted tumor delivery) including endocrine cancers, gastrointestinal cancer, head and neck cancer, kidney and genitourinary cancer, malignant melanoma, esophageal cancer, colorectal cancer, adenocarcinoma of the pancreas, breast cancer, soft tissue sarcomas e.g. of the arm and leg, liver cancer, prostate cancer, glioma, astrocytoma, cholangiocarcinoma; infectious diseases such as HIV infections, and associated disease states such as, Kaposi's sarcoma, the treatment of malaria, Mycobacterium tuberculosis, Mycobacterium avium, Listeria monocytogenes, Salmonella typhimurium, Leishrnaniasis major, Trypanosoma cruzi, Toxoplasma gondii, Plasmodium chaubaudi, Plasmodium falciparum, Hepatitis C, SARS coronavirus infection and Legionella pneumophila pneumonia; sleeping disorders, such as sleep apnea; obesity (for adipose tissue ablation) and numerous pathologies (for general tissue ablation). In another embodiment, the pharmaceutical composition comprising an isolated LT-a or chimeric molecule thereof can be used, alone or in conjunction with other biologies, drugs or therapies in the treatment of diseases associated with tumor growth and metastasis, including adult solid tumors; endocrine cancer; gastrointestinal cancer; head and neck cancer; kidney and urologica! cancer, malignant melanoma, sarcoma, esophageal cancer, colorectal cancer, adenocarcinoma of the pancreas, gliomas, breast cancer and resulting bone metastasis; damaging effect to cells mediated by radiation or cytotoxic anticancer drugs; infectious diseases such as HIV infections, and associated disease states such as Kaposi's sarcoma, the treatment of malaria, Mycobacterium tuberculosis, Mycobacterium avium, Listeria monocytogenes, Salmonella typhimurium, Leishrnaniasis major, Trypanosoma cruzi, Toxoplasma gondii, hepatitis C, SARS, coronavirus infection and Legionella pneumophila pneumonia; nerve regeneration e.g. motor function recovery of crushed nerve injury; septicemia; and cachexia; autoimmune diseases such as rheumatoid arthritis, inflammatory bowel diseases, such as Crohn's disease; multiple sclerosis; and diabetes. In another embodiment, the pharmaceutical composition comprising an isolated TNFRJ or chimeric molecule thereof, such as TNFRI-Fc, can be used, alone or in conjunction with other biologies, drugs or therapies in the treatment of infectious diseases such as HIV; hepatitis C; HTV-1-associated tuberculosis; SARS; coronavirus infection; severe sepsis; septic shock, gram negative and gram positive bacteremia; endotoxic shock; arthritis including rheumatoid arthritis, polyarticular juvenile rheumatoid arthritis (JRA), spondyloarthropathy, psoriatic arthritis, severe gouty arthritis, ankylosing spondylitis, juvenile idiopathic arthritis, chronic polyarthritis, systemic lupus; pain such as in rheumatoid arthritis, pain and swelling after oral surgery, temporomandibular disorders, chronic back and/or neck disc-related pain, acute, severe sciatica, pain due to bone metastasis, sciatica due to herniated nucleus pulposus, complex regional pain syndrome -Type 1 (CRPS ]); psoriasis; asthma; allergic and non-allergic inflammatory responses in the airways; Wegener's granulomatosis; dermatomyositis; polymyositis; uveitis; non-infectious scleritis; myelodysplastic syndrome; Graves' ophthalmopathy; iritis in patients with ankylosing spondylitis; vasculitis; small vessel vasculitis; relapsing panniculitis; tumor necrosis factor receptor associated periodic syndrome (TRAPS); Weber-Christian disease (WCD); Behcet's disease; Churg-Strauss vasculitis; Churg-Strauss-Syndrome; polyarteritis nodosa; giant cell arteritis; sarcoidosis; polymyositis/dermatomyositis; Sjogren's syndrome; sleepiness in patients with sleep apnea e.g. due to obstructive sleep apnea in obesity; multicentric reticulohistiocytosis; pyoderma gangrenosum; Takayasu arteritis; cardiac mitochondria! dysfunction, oxidative stress, and apoptosis in heart failure; Adult-onset Stills disease (AOSD); Crohn's disease; alcoholic hepatitis; myositis; giant cell arteritis; spontaneous endometriosis; chronic infantile neurological cutaneous articular (CINCA) syndrome; Guillain-Barre syndrome; sarcoidosis; aphthous stomatitis; peri-prosthetic osteolysis e.g. following total hip replacement; primary amyloidosis; hyperimmunoglobulinemia and periodic fever syndrome; male and female infertility; inner ear inflammation; Langerhans-cell histiocytosis; immune thrombocytopenic purpura; chronic inflammatory demyelinating polyneuropathy; multicentric reticulohistiocytosis; autoimmune dacryoadenitis; peripheral neuropathy e.g. in celiac disease; polychondritis; pneumatosis cystoides intestinalis; neurosarcoidosis; pigmented villonodular synovitis; necrotizing vasculitis; acute childhood ulcerative colitis; inflammatory bowel disease; Kawasaki disease; myopathy e.g. in Duchenne muscular dystrophy (DMD); ocular inflammation in Adamantiades-Behcet disease; acrodermatitis continua of Hallopeau; hidradenitis suppurativa; renal amyloidosis; indeterminate colitis; post-transplant obliterative bronchiolitis; pyostomatitis vegetans; SAPHO syndrome; necrobiosis lipoidica; Red man syndrome; cancer e.g. breast cancer including in combinations with chemotherapy or other biological therapies; cancer-related cachexia; cutaneous T-cell lymphomas; graft rejection phenomena such as graft-versus host disease (GVHD) (e.g. acute non-infectious lung injury (idiopathic pneumonia syndrome, IPS) and subacute pulmonary dysfunction after allogeneic stem cell transplantation); lung graft ischemia-reperfusion injury; severe steroid-refractory acute GVHD; in hematopoietic stem cell transplants; in organ transplants eg chronic graft injury e.g. in renal allografts. In yet another embodiment, for treatment of rheumatoid arthritis, the pharmaceutical composition comprising TNFRJ molecule or a chimeric molecule such as, TNFRI-Fc can also be administered in combination with methotrexate. In another embodiment, the present invention is administered in combination with other biologically active molecules, such as Leflunomide, Azathioprin, cyclosporine A or sulfasalazine or other monoclonal antibodies (e.g. anti-TNF antibodies, antibodies to Mac I or LFA I) or other receptor associated with TNT production including IL-1 or IL-2 receptors. In another embodiment, the pharmaceutical composition comprising an isolated TNFRU or chimeric molecule thereof can be used, alone or in conjunction with other biologies, drugs or therapies in the treatment of infectious diseases such as HIV; hepatitis C; HIV-1-associated tuberculosis; SARS; coronavirus infection; severe sepsis; septic shock, gram negative and gram positive bacteremia; endotoxic shock; arthritis including rheumatoid arthritis, polyarticular juvenile rheumatoid arthritis (JRA), spondyloarthropathy, psoriatic arthritis, severe gouty arthritis, ankylosing spondylitis, juvenile idiopathic arthritis, chronic polyarthritis, systemic lupus; pain such as in rheumatoid arthritis, pain and swelling after oral surgery, temporomandibular disorders, chronic back and/or neck disc-related pain, acute, severe sciatica, pain due to bone metastasis, sciatica due to herniated nucleus pulposus. complex regional pain syndrome - Type 1 (CRPS 1); psoriasis; asthma; allergic and non-allergic inflammatory responses in the airways; Wegener's granulomatosis; dermatomyositis; polymyositis; uveitis; non-infectious scleritis; myelodysplastic syndrome; Graves' ophthalmopathy; iritis in patients with ankylosing spondylitis; vasculitis; small vessel vasculitis; relapsing panniculitis; tumor necrosis factor receptor associated periodic syndrome (TRAPS); Weber-Christian disease (WCD); Behcet's disease; Churg-Strauss vasculitis; Churg-Strauss-Syndrome; polyarteritis nodosa; giant cell arteritis; sarcoidosis; polymyositis/dermatomyositis; Sjogren's syndrome; sleepiness in patients with sleep apnea e.g. due to obstructive sleep apnea in obesity; multicentric reticuloliistiocytosis; pyoderma gangrenosum; Takayasu arteritis; cardiac mitochondrial dysfunction, oxidative stress, and apoptosis in heart failure; Adult-onset Stills disease (AOSD); Crohn's disease; alcoholic hepatitis; myositis; giant cell arteritis; spontaneous endometriosis; chronic infantile neurological cutaneous articular (CINCA) syndrome; Guillain-Barre syndrome; sarcoidosis; aphthous stomatitis; peri-prosthetic osteolysis e.g. following total hip replacement; primary amyloidosis; hyperimmunoglobulinemia and periodic fever syndrome; male and female infertility; inner ear inflammation; Langerhans-cell histiocytosis; immune throrabocytopenic purpura; chronic inflammatory demyelinating polyneuropathy; multicentric reticulohistiocytosis; autoimmune dacryoadenitis; peripheral neuropathy e.g. in celiac disease; polychondritis; pneumatosis cystoides intestinalis; neurosarcoidosis; pigmented villonodular synovitis; necrotizing vasculitis; acute childhood ulcerative colitis; inflammatory bowel disease; Kawasaki disease; myopathy e.g. in Duchenne muscular dystrophy (DMD); ocular inflammation in Adamantiades-Behcet disease; acrodermatitis continue of Hallopeau; hidradenitis suppurativa; renal amyloidosis; indeterminate colitis; post-transplant obliterative bronchiolitis; pyoslomatitis vegetans; SAPHO syndrome; necrobiosis lipoidica; Red man syndrome; cancer e.g. breast cancer including in combinations with chemotherapy or other biological therapies; cancer-related cachexia; cutaneous T-cell lymphomas; graft rejection phenomena such as graft-versus host disease (GVHD) (e.g. acute non-infectious lung injury (idiopathic pneumonia syndrome, PS) and subacute pulmonary dysfunction after allogeneic stem cell transplantation); iung graft ischemia-reperfusion injury; severe steroid-refractory acute GVHD; in hematopoietic stem cell transplants; in organ transplants eg chronic graft injury e.g. in renal allografts. For treatment of rheumatoid arthritis, the pharmaceutical composition comprising TNFRII or chimeric TNFRII molecule can also be administered in combination with methotrexate. In yet another embodiment, the present invention is administered in combination with other biologically active molecules, such as Leflunomide, Azathioprin, cyclosporine A or sulfasalazine or other monoclonal antibodies (e.g, anti-TNF antibodies, antibodies to Mac I or LFA I) or other receptor associated with TNF production including IL-1 or IL-2 receptors. Ir. another embodiment, the pharmaceutical composition comprising an isolated OX40 or chimeric molecule thereof can be used, alone or in conjunction with other biologies, drugs or therapies in the treatment of diseases including but not limited to T-cell mediated diseases such as allergic, inflammatory and autoimmune diseases such as transplant rejection, autoimmune disease and inflammation, graft-versus-host disease (GVHD), acute GVHD following allogeneic bone marrow transplant, rheumatoid arthritis (RA), inflammatory bowei disease, experimental allergic encephalomyelitis (EAE), multiple sclerosis, cancer, lupus nephritis, inflammatory' bowel disease, asthma, multiple sclerosis; Crohn's Disease; ulcerative colitis; polymyositis; breast cancer, colorectal cancer, autoimmuine encephalitis, inflammatory lung damage e.g. in asthma and pneumonia induced by influenza, and autoimmune diabetes. In another embodiment, the pharmaceutical composition comprising an isolated BAFF or chimeric molecule thereof can be used, alone or in conjunction with other biologies, drugs or therapies for regulating biological processes mediated by B cells, T cells, dendritic cells, macrophages, neutrophils, and activating the BAFFR e.g. to increase B-lymphocyte proliferation, activation and survivial; for treatment for immune deficiency (e.g. patients who have inadequate B lymphocyte proliferation, activation or survival, or who have Common Variable Immune Deficiency (CVED), or lgA deficiency); for enhancement of antibody production in vaccination procedures; for treatment of B cell malignancies such as chronic lymphocytic leukemia (B-CLL), non-Hodgkin's lymphoma (NHL), and multiple myeloma (MM). In yet another embodiment, BAFF linked to radionuclides, toxins or chemotherapeutic agents car. be used as therapy for targetting and killing B-cell malignancies. Examples of suitable radionuclides include Iodine-123, Iodine-131, Technetium-99 and Yttrium-90. Examples of suitable toxins include vanous toxin and truncated pseudomonas exotoxin. In still another embodiment, amino acid sequence variants of BAFF (and chimeric molecules containing BAFF) that have BAFF antagonist activity can be utilised in the treatment of diseases associated with de-regulated BAFF 3 expression, such as B cell lymphomas and autoimmune diseases. In another embodiment, the pharmaceutical composition comprising an isolated NGFR or chimeric molecule thereof can be used, alone or in conjunction with other biologies, drugs or therapies to inhibit breast cancer growth and other tumors for which NGF and other NGFR ligands are mitogens; to inhibit neurogenic inflammation contributing to the pathogenesis of cutaneous and systemic inflammatory diseases such as psoriasis, atopic dermatitis, urticaria,, rheumatoid arthritis, ulcerative colitis and bronchial asthma; to eliminate HIV infected macrophages from HIV-infected patients; and to block the development of autonomic dysreflexia after spinal cord injury e.g. bladder hyperreflexia. In another embodiment, the pharmaceutical composition comprising an isolated Fas Ligand or chimeric molecule thereof can be used, alone or in conjunction with other biologies, drugs or therapies for treatment of rheumatoid arthritis, osteoarthritis, graft verus host disease, toxic epidermal necrolysis, autoimmune lymphoproliferative syndrome, immune deficiency, liver failure, Alzheimer's disease, multiple sclerosis, nerve re-inneration after spinal cord injury and stroke. In yet another embodiment, the pharmaceutical composition comprising an isolated Fas Ligand or chimeric molecule thereof can be used, alone or in conjunction with other drugs or therapies, for the promotion of transplant allograft survival, and to prevent the onset of autoimmune diseases including multiple sclerosis and diabetes. In still another embodiment, the pharmaceutical composition comprising an isolated Fas Ligand or chimenc molecule thereof can be used, alone or in conjunction with other drugs or therapies, to induce apoptosis in a number of different malignant diseases including leukemias, glioma, breast cancer and other solid tumors that express Fas. However, the pharmaceutical composition of the present invention has higher pharmaceutical efficacy, increased thermal stability, increased serum half-life or higher solubility in the bloodstream when compared with the protein or chimeric molecule thereof expressed in non-human cell lines. The present invention also shows reduced risks for immune-related clearance or related side effects. Because of these improved properties, the composition of the present invention can be administered at a lower frequency than a protein or chimeric molecule expressed in non-human cell lines. Decreased frequency of administration is anticipated to enhance patient compliance resulting in improved treatment outcomes. The quality of life of the patient is also elevated. Accordingly, in one embodiment, the pharmaceutical composition of the present invention can be administered in a therapeutically effective amount to patients in the same way a protein or chimeric molecule expressed hi non-human cell lines is administered. The therapeutic amount is that amount of the composition necessary for the desired in vivo activity, The exact amount of composition administered is a matter of preference subject to such factors as the exact type of condition being treated, the condition of the patient being treated and the other ingredients in the composition. The pharmaceutical compositions containing the isoforms of the protein or chimeric molecule of the present invention may be formulated at a strength effective for administration by various means to a human patient experiencing one or more of the above disease conditions. Average therapeutically effective amounts of the composition may vary. Effective doses are anticipated to range from 0.1 ng/kg body weight to 20µg/kg body weight; or based upon the recommendations and prescription of a qualified physician. In a particular embodiment, compositions or preparations according to the present invention are prepared for topical application and comprise between from about 0.1 u.g and 20 g active agent (e.g. TNFRI and/or TNFRII and/or TNFRI-Fc and/or TNFRII-Fc) per course of treatment, Administration may be per hour, day, week, month or year. The topical composition of the present invention may be prepared by mixing TNFRI-Fc or a variant, homolog or analog thereof or TNFRI polypeptide or a variant, homolog or analog thereof and/or a TNFRII polypeptide or variant, homolog or analog thereof and/or TNFRII-Fc or a variant, homolog or analog thereof, with the pharmaceutical acceptable carrier or diluent as hereindescribed. In one embodiment, the pharmaceutical acceptable carrier or diluent is a cream, wherein the cream is selected from Cetaphil Moisturising Cream (Galderina Laboratories, L.P.). QV Cream (Lision Hong), Sorbolene or the like In another embodiment, the topical administration is prepared by mixing TNFRI polypeptide or E variant, homolog or analog thereof and/or a TNFRII polypeptide or variant, homolog or analog thereof and/or TNFRI-Fc or a variant, homolog or analog thereof or TKFRII-Fc or a variant, homolog or analog thereof with thalidomide and a pharmaceutical acceptable carrier or diluent. The final concentration of TNFRI polypeptide or a variant, homolog or analog thereof and/or a TNFRII polypeptide or variant, homolog or analog thereof and/or TNFRI-Fc or a variant, homolog or analog thereof or TNFRII-Fc or a variant, homolog or analog thereof in the topical preparation should be equal to or less than about 50 mg/ml. Reference herein to "equal to or less than 50 mg/ml includes without being limited to concentrations of 0.001, 0.002, 0.003, 0.004, 0,005, 0.006, 0.007, 0.008. 0.009, 0.01, 0.02, 0.03, 0.04, 0.05, 0.06, 0.07, 0,08, 0.09, 0.10, 0.11, 0.12, 0.13, 0.14, 0.15, 0.16, 0.17, 0,18, 0.19, 0.20, 0.21, 0.22, 0.23, 0.24, 0.25, 0.26, 0.27, 0.28, 0.29, 0.30, 0.31, 0.32, 0.33, 0.34r 0,35, 0.36, 0.37, 0.38, 0.39, 0.40, 0.41, 0.42, 0.43, 0.44, 0.45, 0.46, 0.47; 0.48, 0.49, 0.50,1.0, 1.5, 2.0, 2.5, 3.0, 3.5, 4.0, 4.5, 5.0, 5.5, 6.0, 6.5, 7.0, 7.5, 8.0, 8.5, 9.0, 9.5, 10,0, 10.5, 11.O, 11.5, 12.0, 12.5, 13.0, 13.5, 14.0, 14.5, 15.0, 15.5, 16,0, 16.5, 17.0, 17.5, 18.0, 18.5, 19.0, 19.5, 20.0, 20.5, 21.0, 21.5, 22.0, 22.5, 23.0, 23,5, 24.0, 24.5, 25.0, 25.5, 26,0, 26.5. 27.0, 27.5, 28.0, 28.5, 29.0, 29.5, 30.0, 30.5, 31.0, 31.5, 32.0, 32.5, 33.0, 33.5, 34.0, 34.5, 35,0, 35.5, 36.0, 36.5, 37.0, 37.5, 38.5, 39.0, 39.5, 40.0, 40.5, 41.0, 41.5, 42.0, 42.5, 43.0: 43.5, 44.0, 44.5, 46.0, 46.5, 47.0, 47.5, 48.0, 48.5, 49.0, 49.5 and 50.0 mg/ml, In one embodiment, the final concentration of TNFRl-Fc or a variant, homolog or analog thereof or TNFRII-Fc or a variant, homolog or analog thereof in the topical preparation is about 0.25 mg/ml. The topical composition comprising TNFRI-Fc and/or TNFRJI-Fc, may further comprise thalidomide or its variants, homologs or analogs, especially non-teratogeneic analogs. This embodiment counters TNF alpha at two levels, namely, by inhibiting the biosynthetic pathway for TNF alpha and by neutralizing excess TNF alpha. Thalidomide, or alpha- (N-phthalimido) glutarimide, is a glutamic acid derivative. It has a two-ringed structure with an asymmetric carbon in the glutarimide ring. It exists as an equal mixture of S(-) and R(+) enantiomers that convert rapidly under physiologic conditions. Thalidomide is an knmunomodulatory molecule, exhibiting anti-inflammatory and immunosuppressive properties, although its mechanisms of action are not fully understood. Thalidomide exhibits the ability to suppress TNF alpha production and to modify the -expression of TNF alpha induced adhesion molecules on endothelial cells and on human leukocytes, Thalidomide selectively inhibits the production of TNF-alpha in a number of LPS stimulated cell types including human monocytes, (Sampaio el al, J Exp Med 173(3):699-703,1991) and alveoli cells. (Tavares et al. Respir Meet P/(l):31-9, 1997) and this results from the enhanced degradation of TNF-alpha mRNA (Moreira et al. J Exp Med 777(6): 1675-80, 1993). The final concentration of thalidomide in the topical preparation should be equal to or less than 100 mg/ml. Reference herein to "equal to or less than 100 mg/ml includes concentrations of 0.01, 0.02: 0.03, 0.04, 0.05, 0.06, 0.07, 0.08, 0.09, 0.1, 0.2, 0.3, 0.4, 0.5, 0,6,0.7,0.8,0,9, 3,2,3,4,5, 6,7,8,9, 10, 11,12, ]3, 14, 15, 16, 17, 18, 19,20,21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68; 69, 70, 71,72,73,74,75,76,77,78,79, 80, 81, 82, 83, 84, 85, 86,87,88, 89,90,91,92,93,94, 95, 96,97,98, 99 and 100mg/ml. In a particular embodiment, the final concentration of thalidomide in the topical composition is 10 to 30 mg/ml, more preferably, the concentration of thalidomide in the topical composition is about 20 mg/ml. The present invention further extends to uses of the isolated protein or the chimeric molecule comprising at least part of the protein or chimeric molecule thereof and a composition comprising same in a variety of therapeutic and/or diagnostic applications. More particularly, the present invention extends to a method of treating or preventing a condition in a mammalian subject, wherein the condition can be ameliorated by increasing the amount or activity of the protein or chimeric molecule of the present invention, the method comprising administering to said mammalian subject an effective amount of an isolated protein, a chimeric molecule comprising the protein, a fragment or an extracellular domain thereof or a composition comprising the isolated protein or the chimeric molecule. In a particular aspect, the present invention provides a method for treating an inflammatory disease state which is characterized by an excess level of TNF-a or a disease condition which is associated or exacerbated by TNF-a in the subject, said method comprising administering to said subject a therapeutically effective amount of the topical composition comprising TNFRI-Fc and/or TNFRIl-Fc hereinbefore described. A condition associated by TNF-a is conveniently defined by a condition treatable by a TNF-a inhibitor, An excess of TNF-a is implicated in a range of autoimmune diseases such as rheumatoid arthritis, Crohn's Disease and a number of inflammatory skin conditions hereindescribed. An "excess" of TNF-a may be broadly defined as a greater amount of TNF-a in the blood or serum of the subject than can be bound by the subject's natural soluble TNF-a receptors. Typically, the result of excess TNF-a is an inflammatory response. In a particular embodiment, the "disease state" is a disease state comprising one or more symptoms which manifest themselves on or in the skin of said subject and the method comprises administering the topical composition comprising THFRI-Fc and/or TNFRII-Fc, as hereinbefore described, to the affected skin of the subject. More preferably the disease state is selected from the list consisting of: psoriasis, Behcet's disease, bullous dermatitis, eczema, fungal infection, leprosy, neutrophilic dermatitis, pityriasis maculara (or pityriasis rosea), pityriasis nigra (or tinea nigra), pityriasis rubra pilaris, systemic lupus erythematosus, systemic vascularitis and toxic epidermal necrolysis; or a disease state caused by the use of medication, such as Aldara cream, including erythema, erosion, ulceration, flaking, scaling, dryness, scabbing, crusting, weeping or exudating of skin. However, the present invention should not be considered in any way limited to the treatment of these diseases only. As used herein the term "a disease state characterized by an excess level of TNF-a in the subject" should be understood to include disease states which are characterized by a detectable excess of TNF mRNA in tissue or TNF-a in the serum of the subject as well as diseases which are amenable to treatment using any agent which reduces the amount or activity of TNF-a in the subject regardless of whether the subject has a detectable excess of serum TNF-a. In a particular embodiment the present invention contemplates a method for treating psoriasis, said method comprising administering to said subject a therapeutically effective amount of the pharmaceutical composition comprising TNFRI-Fc and / or TNFRIl-Fc hereinbefore described, Accordingly, as used herein, the term "psoriasis" is to be understood to cover all variants of the disease, including plague psoriasis, guttate psoriasis, inverse psoriasis, seborrheic psoriasis, nail psoriaisi, generalized erythrodermic psoriasis, pustular psoriasis, palmar-plantar pustulosis, Von Zumbusch psoriasis and psoriatic arthritis. The method of the present invention comprises administration of the pharmaceutical composition to the subject. Administration of the composition may be per hour, per day, per week, per month or per year, Furthermore, administration may include multiple administrations per unit of time, for example administration may include 1, 2, 3, 4 or 5 administrations of the pharmaceutical composition per hour, day, week, month or year. dministration may also include a single administration per multiple units of time, for example, administration may include one administration per 1, 2, 3, 4 or 5 hours, days, weeks, months or years. As indicated above, administration is preferably by topical application to a biological surface or to a synthetic surface that is then applied to a biological surface. For example, the composition may be applied to gauze or a patch which is then placed on an area to be treated. Furthermore, the amount of pharmaceutical composition administered at each administration may include from O.lml to 10ml per 100 cm2 of affected area. This includes amounts of 0,1, 0.2, 0.3, 0,4, 0.5, 0.6, 0.7, 0.8, 0.9, 1.0, 1.1, 1.2, 1,3, 1.4, 1.5, 1.6, 1.7, 1.8, 1.9, 2.0, 2.1, 2.2, 2,3, 2.4, 2.5, 2,6, 2.7, 2.8,2:9, 3.0, 3.1, 3.2, 3.3, 3.4, 3.5, 3.6, 3.7, 3.8, 3.9, 4.0, 4.1, 4.2, 4.3, 4,4, 4.5, 4.6, 4.7, 4.8, 4.9, 5.0; 5.1, 5.2, 5.3, 5.4, 5.5, 5.6, 5.7, 5.8, 5.9, 6.0, 6.0, 6.2, 6.3, 6.4, 6.5, 6.6, 6.7, 6.8, 6.9, 7.0, 7.1, 7.2, 7.3, 7.4, 7.5, 7.6, 7.7, 7.8, 7.9, 8.0, 8.1, 8.0, 8,3, 8,4, 8,5, £.6, 8,7, 8.8, 8.9, 9.0, 9.1, 9.2, 9.3, 9.4, 9.5, 9.6, 9.7, 9.8, 9.9, 10.0 ml per 100 cm2 of area to be treated. In one embodiment, the area of skin manifesting one or more symptoms of the disease state is treated once per day, by applying about 0.5ml of a topical composition comprising: TNFRI (0,25 mg/ml) and thalidomide (20 rag/ml), per about 100 cm2 of affected area once per day. In some embodiments up to about 2ml of a topical composition comprising TNFRI (0.25 mg/mi) and thalidomide (20 mg/ml), per about 100 cm2 of effected area. In another embodiment, the inflammation area is treated once per day. by applying 0.5ml of topical composition preparation (TNFRI (0.25 mg/ml); thalidomide (20 mg/ml)) per 100 cm2 of inflammatory area once per day. In some embodiments up to about 2ml of topical composition (TNFRI1 (0.25 mg/ml); thalidomide (20 mg/ml)) is applied on about 100cm2 of affected area once per day, In another embodiment, the inflammation area is treated once every two days, by applying 0.5ml of topical composition (TNFRI (0.25 mg/ml); thalidomide (20 mg/ml)) per approximately 100 square centimeter of inflammatory area. In some embodiments up to 2ml of topical composition (TNFRI (0.25 mg/ml); thalidomide (20 mg/ml)) is applied on approximately 100 cm2 of affected area once every two days, In a particular embodiment, the inflammation area is treated once every two days, by applying 0.5ml of topical composition (TNFRII (0.25 mg/ml); thalidomide (20 mg/ml)) per 100 square centimeter of inflammatory area. In some embodiments up to 2ml of topical preparation (TNFRII (0.25 mg/ml); thalidomide (20 mg/ml)) is applied on 100 cm2 of affected area once every two days. in one embodiment, the area of skin manifesting one or more symptoms of the disease state is treated once per day, by applying about 0.5ml of a topical composition comprising: TNFRI-Fc (0.25 mg/ml) and thalidomide (20 mg/ml), per about 100 cm2 of affected area once per day. In some embodiments up to about 2ml of a topical composition comprising: TNFRI-Fc (0.25 mg/ml) and thalidomide (20 mg/ml), per about 100 cm2 of affected area. In another embodiment, the inflammation area is treated once per day, by applying 0.5ml of topical composition (TNFRII-Fc (0.25 mg/ml); thalidomide (20 mg/ml)) per 100 cm2 of inflammatory area once per day. In some embodiments up to about 2ml of topical composition (TNFRII-Fc (0.25 mg/ml): thalidomide (20 mg/ml)) is applied on about 100 cm" of affected area once per day. In another embodiment, the inflammation area is treated once every two days, by applying 0,5ml of topical composition (TNFRI-Fc (0.25 mg/ml); thalidomide (20 mg/ml)) per approximately 100 square centimeter of inflammatory area. In some embodiments up to 2ml of topical composition (TNFRI-Fc (0.25 mg/ml); thalidomide (20 mg/ml)) is applied on approximately 100 cm2 of affected area once every two days. In one embodiment, the inflammation area is treated once every two days, by applying 0.5ml of topical composition (TNFRII-Fc (0.25 mg/ml); thalidomide (20 mg/ml)) per 100 square centimeter of inflammatory area. In some embodiments up to 2ml of topical preparation (TNFRII-Fc (0.25 mg/ml); thalidomide (20 mg/ml)) is applied on 100 cm2 of affected area once every two days, The present invention further contemplates a method comprising co-administration of the pharmaceutical composition of the present invention in combination with another therapeutic agent or treatment protocol. One or more other therapeutic agents may be co-administered with TNFRJ and/or TNFRII and/or TNFRI-Fc and/or TNFRII-Fc, By "co-administered" is meant simultaneous administration in the same formulation or in two different formulations via the same or different routes or sequential administration by the same or different routes. By "sequential" administration is meant a time difference of from seconds, minutes, hours or days between the administration of the two agents or treatment protocols. The sequentially administered agents or treatment protocols may be administered in any order. When another therapeutic agent is co-administered, it may be provided systemically or topically. Accordingly, the present invention provides a multi-part pharmaceutical pack comprising a first part containing TNFRI and/or TNFRII and/or TNFRI-Fc and/or TNFRII-Fc in a form suitable for topical administration and a second or subsequent part containing another active agent in a form suitable for topical or systemic application said first part further comprising a pharmaceutically acceptable topical carrier. ID one embodiment, therefore, the present invention contemplates a method for treating psoriasis or a related skin disorder in a subject, said method comprising topically administering to the subject an effective amount of a pharmaceutical composition comprising TNFRJ and/or TNFRII and/or TNFRI-Fc and/or TNFRII-Fc together with another active agent. Other active agents which may be co-administered with the pharmaceutical composition of the present invention include: (i) Tar: Coal tar is known to assist in psoriasis treatment and it is available as crude coal tar coal, tar lotion, and in refined forms incorporated into ready made creams, lotions and shampoos, A chemical similar to those found in tar may be used on its own - known as Dithranol or Anthralin. (ii) (ii) UV light: Conveniently applied via an artificial light source. (iii) Cortisone: External cortisone in various different bases can help psoriasis, but this helps usually only 1-2 days at the most. There are certain areas such as ears and the backs of hands where tar treatments are not very helpful, and in these areas cortisone applications are usually best. Internal cortisone tablets are best avoided in psoriasis unless every other treatment has not helped. The main problem with these tablets is that they may help, but when they are stopped psoriasis can suddenly flare it and become worse than it originally was, known as the rebound effect. (iv) Calcipotriol: Calcipotriol is a synthetic form of vitamin D. Vitamin D has been recognised for many years to improve some of the important abnormalities present in psoriasis skin, but ingestion of even only slightly above the daily recommended amount of Vitamin D can lead to problems with calcium metabolism in the body (possible kidney stones and irregular heart beats). Calcipotriol has been found to also have the ability to improve psoriasis, but with minimum effects on internal calcium metabolism. There is a risk of facial dermatitis if the ointment is used on the face or neck, so application is only recommended for the trunk and limbs, and it is important that the hands are thoroughly washed after application to avoid inadvertent transfer to the skin of the face, (v) PUVA phototherapy: PUVA is the name given to treatment comprising the use of psoralen, which sensitises the skin to the effect of artificial ultraviolet radiation in the A range (UVA), in conjunction with UVA. The combination of the two has a powerful effect on the plaques of psoriasis, slowing down the rapid division of cells that is recognised to occur in active psoriasis. The dose of UVA exposure is carefully increased as burning of the skin can occur if the treatment id introduced too rapidly. A variation on PUVA phototherapy recently developed a technique known as bath PUVA. Rather than ingesting psoralen by mouth, a bath is taken for ten minutes just before UVA exposure containing the psoralen chemical. Sun protection with all forms of PUVA therapy is vita] on the days of the treatment. PUVA is not first line treatment of psoriasis. (vi) Methotrexate: Methotrexate has been used in psoriasis treatment. This active agent is also used in higher doses to treat some cancers and leukaemias. (vii) Tigason: Tigason is a "retinoid" (a synthetic derivative of Vitamin A) and may be used in the management of very severe cases of psoriasis, and with the pustular forms of psoriasis. (viii) Cyclosporin: Cyclosporin is known to suppress the inflammation that occurs during psoriasis in the skin. (ix) Anthralin: Anthralin is derived from Goa powder, which is from the bark of the araroba tree and has been used to treat psoriasis for more than 100 years. (x) Salicyclic Acid: Salicylic acid is a chemical that helps removing scale. (xi) Melatonin: A lipophilic powerful antioxidant that may prove to dampen down the inflammatory milieu. Additional active agents also include other cytokine inhibitors such as molecules in which inhibit IGF-1 or 1GF-1R, as well as molecules which inhibit IGF binding proteins such as IGFBP-l,2,3or4. Reference to inhibition of cytokines includes inhibiting the expression of genetic material encoding the cytokines. Such inhibitors include antisense nucleic acid molecules, sense nucleic acid molecules, dsRNA (DNA-derived or synthetic RNA) and ribozymes. The present invention is further described by the following non-limiting examples. EXAMPLE 1 Production of a Vector-Fc Construct (a) pIRESbleo3-Fc The DNA sequence encoding the Fc domain of human IgGl was amplified from EST cDNA library (Clone ID 6277773, Invitrogen) by Polymerase Chain Reaction (PCR), using forward primer (SEQ ID N0:21) and reverse primer (SEQ ID N0:22) incorporating restriction enzyme sites BamHl and BstXl respectively. This amplicon was cloned into the corresponding enzyme sites of pIRESbleo3 (Cat. No. 6989-1, BD Biosciences) to produce the construct pIRESbleo3-Fc. Digestion of pIRESbleo3-Fc with BamHl and BstXl released an expected size insert of 780 bp as determined by gel electrophoresis. (b) Production of a DNA construct expressing a Protein or a Protein-Fc The DNA sequence encoding the protein or the extra cellular domain thereof was amplified from an EST cDNA library' by PCR, using forward primer and reverse primers that incorporated restriction enzyme sites according to Table 8. After amplification, the amplicon was digested with suitable restriction enzymes and cloned into an expression vector as per Table 8, to produce the vector-Protein or vector-Protein-Fc constructs. Where a construct encoding a Protein-Fc was produced, the DNA sequence encoding the protein was cloned upstream of the Fc nucleotide sequence, such that the two sequences were fused in-frame so that when the protein was expressed it was fused directly or by a linker to the Fc domain. Preparation of the TNFRII-Fc-pCEP-4 involved amplification of the TNFRIl-Fc sequence and cloning into pCEP-4 using the enzyme sites given in Table 8. Suitable restriction enzymes were used to digest the vector containing the DNA sequence encoding the Protein or the Protein-Fc to release the expected siz.e fragments as shown in Table 8. Vector-Protein or vector-Protein-Fc constructs were sequenced to confirm the integrity of the cloning procedures as herein described. TABLE 8 Protein-Fc and relevant cloning information (Table Removed) (c) Production of a DNA construct expressing OX40-Fc The DNA sequence encoding the extra cellular domain (BCD) of OX40 was ligated upstream of the IgGI Fc sequence in a two-step cloning procedure. Step one involved the amplification of the first 292bp of the 0X40 ECD sequence using forward primer (SEQ ID NO: 123) and reverse primer (SEQ ID NO: 124) and an EST cDNA library (5180287, Invitrogen) as a template. The primers incorporated restriction sites EcoRV and BamHI respectively. The purified amplicon was cloned into corresponding restriction enzyme sites of the pIRESbleo3-Fc expression vector, upstream of the human IgGI Fc sequence. Step two involved amplification of the remaining 355bp of the 0X40 ECD sequence using forward primer (SEQ ID NO: 125) and reverse primer (SEQ ID NO: 126) using a previously amplified 0X40 sequence as a template. The primers incorporated the restriction site BaroHl at both ends of the amplicon. The purified amplicon was ligated into the BamHI site downstream of the first 0X40 sequence and upstream of the Fc sequence. Hpall digestion confirmed the correct orientation of the second 0X40 sequence. The introduction of an artificial Bam HI site within the 0X40 sequence does not result in a frameshift affecting the amino acid sequence of the translated protein. Alternatively, the nucleotide sequence encoding the Protein that was cloned into the vector (such as pIRESbleoS or pCEP4) can be amplified with primers that incorporate restriction sites allowing the cloning of the DNA sequence encoding the Protein upstream of the Fc nucleotide sequence in a vector-Fc (such as pIRESbleo3-Fc or pCEP4-Fc), such that the Protein and the Fc nucleotide sequences are fused in-frame directly or by a linker. (d) Preparation of Megaprep vector-Protein or vector-Protein-Fc 750ml of sterile LB broth containing ampicillin (100µgAnl) was inoculated with 750pl of overnight culture of E. Coli transformed with vector-Protein or vector-Protein-Fc. The culture was incubated at 37°C with shaking for 16 hours. Plasmid was prepared in accordance with a Qiagen Endofree Plasmid Mega Kit (Qiagen Mega Prep Kit #12381). EXAMPLE 2 (a) Production, Isolation and Purification of TNF-a of the Present Invention (i) Production of TNF-a of the Present Invention At day 0, five 500 cm2 tissue culture dishes (Corning) were seeded with 3 x 107 cells of a transformed embryonal human kidney cell line, for example HEK 293, HEK 293 c!8, HEK 293T, 293 CEN4, HEK 293F, HEK 293E, HEK 293FT, AD-293 (Stratagene), or 293A (Invitrogen). Cells were seeded in 90 ml per plate of Dulbecco's Modified Eagle's Medium/Ham's Nutrient Mixture F12 (DMEM/F12) (JRH Biosciences), the medium being supplemented with 10% (v/v) heat-inactivated fetal calf serum (PCS, JRH Biosciences), 4 mM L-glutamine (Amresco), 10 mM HEPES (Sigma), and 1% (v/v) Penicillin-Streptomycin (Penicillin G 5000 U/ml, Streptomycin Sulfate 5 mg/ml) (JRH Biosciences). The plates were incubated at 37 °C and 5% CO; overnight. At day 1, transfection was performed using calcium phosphate. Before transfection, the medium in each plate was replaced with 120 ml of fresh DMEM/F12 supplemented with 10% (v/v) heat-inactivated PCS or DCS, 4 mM L-glutamine, 10 mM HEPES, and 1% (v/v) Penicillin-Streptomycin. Calcium phosphate / DNA precipitate was prepared by adding 1200 p,g of pIRESbleoB (Invitrogen) plasmid DNA harboring the gene for human TNF-a and 3720 µl of 2 M calcium chloride solution (BD Biosciences) in sterile H2O to a final volume of 30 ml (solution A), Alternatively, the same amount of plasmid DNA was added to 3000 µl of 2.5 M CaCl2 in sterile IxTE was to a final volume of 30 ml (solution A). Solution A was added drop-wise to 30 ml of 2 x HEPES Buffered Saline (HBS) (solution B) (BD Biosciences) with a 10 ml pipette. During the course of addition, bubbles were gently blown through solution B. The mixture was incubated at 25 °C for 20 minutes and vortexed. 12 ml of the mixture was added drop-wise to each plate. The plates were incubated at 37 °C and 5% CO2 overnight. Alternatively, after 4 hours incubation the medium containing the transfection mixture was removed and 100 ml of DMEMYF12 supplemented with 10% (v/v) DCS, 4 mM L-glutamine, 1% (v/v) Penicillin-Streptomycin, and a final concentration of 3.5-4.0 mM HC1, with the medium having a final pH of 7, was added to each plate. The plates were incubated at 37°C and 5% CO2 overnight. At day 2. the cell culture supernatant was discarded. The contents in the plates were washed twice with 50 ml of DMEM/F12 medium per plate and 100 ml of fresh serum-free DMEM/F12 medium, supplemented with 40 mM N-acetyl-D-mannosamine (New Zealand Pharmaceuticals)., 7 or 10 mM L-Glutamine, 15 mM HEPES, 0.5 or 4.1 g/L Mannose (Sigma), 1% (v/v) Penicillin-Streptomycin, and ITS solution (5 mg/L bovine insulin, 5 mg/L partially iron saturated human transferrin and 5 µg/ml selenium) (Sigma) (alternatively, without ITS solution) was added to each plate. The plates were incubated at 37 °C and 5% CO2 overnight. At day 3, the cell culture supernatant was collected and 100 ml fresh serum-free DMEM/F12 medium, supplemented with 40 mM N-acetyl-D-mannosamine, 7 or 10 mM L-Glutamine, 15 mM HEPES (alternatively, without HEPES), 0.5 or 4.1 g/L Mannose, 1% (v/v) Penicillin-Streptomycin, and ITS solution (alternatively, without ITS solution) was added to each plate. The plates were incubated at 37 °C and 5% CO2 overnight, 100 mM PMSF (1% (v/v)) and 500 mM EDTA (1% (v/v)) were added to the collected cell culture supernatant and the mixture was stored at 4 °C. At day 4, the cell culture supernatant was collected. 100 mM PMSF (1% (v/v)) arid 500 mM EDTA (1% (v/v)) was added to the collected cell culture supernatant and combined with the day 3 collection. (Particulate material removed using a 0.45 micron low-protein binding filter (Durapore, Millipore). The combined collections were adjusted to pH 6 by the addition of a one tenth volume of 200 mM MES/ 50 mM MgC^ pH6 before particulate removal using a 0.45 micron low-protein binding filter (Durapore, Millipore). The mixture was either stored at -70 °C or used immediately. (ii) Isolation and Purification of TNF-a 950 ml of filtered cell culture supernatant was concentrated aproximately 20 fold using a tangential flow filtration (TFF) device (Pelicon XL, Ultracell, Millipore), The sample was pumped at 150 ml/min across 150 cm2 of regenerated cellulose membrane, with a nominal molecular weight cut-off of 5 KDa until the sample had concentrated down to a volume of 30 ml. The concentrated sample was diafiltered by the addition of 70 ml of 50 mM HEPES pH 8.5 followed by another concentration down to 30 ml. This diafiltration step was repeated twice with a final concentration to 50 ml. The concentrated diafiltered sample was then filtered through a 0.45 micron low-protein binding filter (Durapore, Millipore). Purification of TNF-a was achieved by passing the concentrated cell culture supernatant from the TFF over an Ion Exchange column (Bio-Rad Laboratories, MacroPrep HS) pre-equilibrated with 50 mM HEPES pH 8.5. The bound TNF-a was then eluted from the column with a gradient from 50 mM HEPES pH 8.5 to 100 % 50 mM HEPES pH 8.5 containing 1M NaCl. The resulting fractions were analysed for apparent molecular weight md level of punty by ID SDS PAGE using 4-20 % gradient Tris-Glycine gels Invitrogen) and quantitated by anti-TNF-a ELISA (R & D Systems). Fractions containing FNF-a were combined and concentrated to less than 1 ml for size exclusion uhromatography using a centrifugal filter device (Amicon Ultra, Millipore). Size exclusion chromatography was performed on the combined anion exchange fractions using a Superdex 75 prep grade 16/70 column (Pharmacia, Uppsala, Sweden). An isocratic buffer of 1% ammonium bicarbonate was used at a flow rate of 1 ml/min. Total run time was 120 min with peaks eluting between 20 and 100 minutes. The eluted fractions were assayed by silver stained 4 - 20 % gradient Tris-Glycine gels (Invitrogen) and by TNF-a ELISA. The peak eluting at approximately 50 minutes was found to contain TNF-a. Fractions containing TNF-a were combined and concentrated to less than 2 ml using a centrifugal filter device (Amicon Ultra, Millipore). The purified TNF-a was found to have an apparent MW of around 17 kDa and to be at least 95 % pure as assessed by silver stained SDS PAGE. The final concentration of the TNF-a was found to be 157 µg/ml as determined by absorption at 280 nm using a molar extinction co-efficient of 21555 M-1 cm-1. (b) Production, Isolation and Purification of LT-a of the Present Invention (i) Production of LT-a of tbe Present Invention At day 0. five 500 cm2 tissue culture dishes (Corning) were seeded with 3 x 107 cells of a transformed embryonal human kidney cell line, for example HEK 293, HEK 293 c!8, HEK 293T, 293 CEN4, HEK 293F, HEK 293E, HEK 293FT, AD-293 (Stratagene), or 293A (Invitrogen). Cells were seeded in 90 ml per plate of Dulbecco's Modified Eagle's Medium/Hare's Nutrient Mixture F12 (DMEM/F12) (JRH Biosciences), the medium being supplemented with 10% (v/v) heat-inactivated fetal calf serum (PCS, JRH Biosciences), 4 mM L-glutamine (Amresco),. 10 mM HEPES (Sigma), and 1% (v/v) Penicillin-Streptomycin (Penicillin G 5000 U/ml. Streptomycin Sulphate 5 mg/ml) (JRH Biosciences). The plates were incubated at 37 °C and 5% C02 overnight. At day 1. transfection was performed using calcium phosphate. Before transfection, the medium in each plate was replaced with 120 ml of fresh DMEM/F12 supplemented with 10% (v/v) heat-inactivated PCS, 4 mM L-glutamine, 10 mM HEPES, and 1% (v/v) Penicillin-Streptomycin. Calcium phosphate / DNA precipitate was prepared by adding 1200 µg of pIRESb)eo3 (Invitrogen) plasmid DNA harboring the gene for human LT-a and 3720 µl of 2 M calcium solution (BD Biosciences) in sterile H2O (BD Biosciences) to a final volume of 30 mi (solution A). Solution A was added drop-wise to 30 ml of 2 x HEPES Buffered Saline (HBS) (solution B) (BD Biosciences) with a 10 ml pipette. During the course of addition, bubbles were gently blown through solution B, The mixture was incubated at 25 °C for 20 minutes and vortexed. 12 ml of the mixture was added drop-wise to each plate. The plates were incubated at 37 °C and 5% CO2 overnight. At day 2. the eel] culture supernatant was discarded. The contents in the plates were washed twice with 50 m! of DMEM/F12 medium per plate and 100 ml of fresh serum-free DMEM/F12 medium supplemented with 40 mM N-acetyl-D-mannosamine (New Zealand Pharmaceuticals),7 mM L-Glutamine (Amresco), 0.5 g/L Mannose (Sigma) and 1% (v/v) Penicillin-Streptomycin was added to each plate. The plates were incubated at 37 °C and 5% CO2 overnight. At day 3, the cell culture supernatant was collected and 100 ml fresh serum-free DMEM/F12 medium supplemented with 40 mM N-acetyl-D-mannosamine, 7 mM L-Glutamine, 0.5 g/L Mannose. and 1% (v/v) Penicillin-Streptomycin was added to each plate. The plates were incubated at 37 °C and 5% CO2 overnight. 100 mM PMSF (1% (v/v)) and 500 mM EDTA (1 % (v/v)) were added to the collected cell culture supernatant and the mixture wat stored at 4 °C. At day 4. the cell culture supernatant was collected. 100 mM PMSF (1% (v/v)) and 500 mM EDTA (1% (v'v)) was added to the collected cell culture supernatant and combined with the day 3 collection The combined collections were adjusted to pH 6 by the addition of a one tenth volume of 200 mM MES/ 50 mM MgCk pH 6 before particulate removal using a 0.45 micron iow-protein binding filter (Durapore, Millipore). The mixture was either stored at A°C or used immediately. For long-term storage, the supernatant was kept at -70°C. (ii) Isolation and Purification of LT-a of the Present Invention The process of Dye-hgand chromatography (DLC) was used as the primary step in the purification of LT-a. A library of immobilised reactive dye was used to screen LT-a for efficient binding and release in a batch purification microtitre format. Suitable dye-protein combinations were then tested in £ small scale column format. In small scale purification 5 ml samples of thawed cell culture supernatant were passed through 0.5 mi dye-iigand columns at a pH of either 6 or 7.3. In this optimisation step optimal reactive dye-cytokine and pH combinations were selected for maximal recovery in fractions for up scaling in bulk DLC. For bulk scale DLC reactive dye number 18 High (Zymatrix) was selected as the reactive dye with the best binding and elution properties for LT-a. The filtered cell culture supernatant was passed under gravity flow over 4,0 ml or 8.0 ml column bodies (Alltech. Extract Clean Filter columns) with 3 ml or 6 ml respectively of DLC resin pre-equilibrated to pH 6 with 50 mM MES/5 mM MgCl2. The column was washed with Buffer A (20 mM MES/5 mM MgCl2 pH 6) until fractions were free of protein as monitored by colounnetric protein assay ('Biorad protein assay). LT-a was eluted using three Elution Buffers in the following order: Elute 1; Buffer C (50 mM Tris-Cl/10 mM EDTA pH 8) Elute 2: ENl .0 (50 mM Tris-Cl/10 mM EDTA/1.0 M NaCl pH 8) Elute 3: EN2.0 (50 mM Tris-Cl/10 mM EDTA/2.0 M NaCJ pH 8) The eluted fractions were assayed by silver stained SDS PAGE using 4-20 % Tris-Glycine gels (bvitrogen) and by ami- LT-a ELISA (R & D Systems). LT-a was found to bind to reactive dye 18 High and was found to elute in Buffer C and Buffer ENl .0. It was estimated by SDS PAGE analysis that 70% of the contaminating proteins were removed in this primary purification step. DLC Fractions containing LT-a were pooled and concentrated to approximately 5 ml using a centrifugal filter device (Amicon Ultra, Millipore), The concentrated sample was then diluted ten fold before it was passed over a cation exchange column (Bio-Rad Laboratories, Uno SI) pre-equilibrated to pH 6.5 with 50 mM MES pH 6.5 (Sigma). The bound LT-a was then eluted from the column with a linear gradient from 50 mM MES pH 6.5 to 50 mM MES pH 6.5 containing 1 M NaCl. The resulting fractions were analysed for apparent molecular weight and level of purity by silver stained ID SDS PAGE using 4 - 20 % Tris-Glycine gels (Invitrogen). Fractions containing LT-a were pooled and concentrated to less than 1 ml for size exclusion chromatography using a centrifugal filter device (Amicon Ultra, Millipore). Size exclusion chromatography was performed on the concentrated sample using Superdex 75 prep grade 16/70 (Pharmacia, Uppsala, Sweden) column. An isocratic flow of 1% Ammonium Bicarbonate was used at a flow rate of Iml/min. Total run tune was 120 min with peaks eluting between 20 and 100 minutes. The eluted fractions were assayed by silver stained SDS PAGE using 4-20 % Tris-Glycine gels (Invitrogen). The peak eluting at approximately 45 minutes was found to contain LT-a. Fractions containint LT-a were pooled and concentrated to less than 2 ml using a centrifugal filter device (Amicon Ultra, Millipore). The purified LT-a was found to have an apparent MW of around 20-38 kDa and to be at least 95 % pure as assessed by silver stained SDS PAGE using 4-20 % Tris-Glycine gels (Invitrogen). The final concentration of the LT-a was found to be 78 µg as determined by absorption at 280 run using a molar extinction co-efficient of 21430 M-1 cm-1. (c) Production, Isolation and Purification of TNFRI-Fc of the Present Invention (i) Production of TNFRl-Fe of the Present Invention At day 0, five 500 cm2 tissue culture dishes (Corning) were seeded with 3 x 107 cells of a transformed embryonal human kidney cell line, for example HER 293, HEK 293 c!8, HEK 293T, 293 CEN4, HEK 293F, HEK 293E, HEK 293FT, AD-293 (Stratagene), or 293A (Invitrogen). Cells were seeded in 90 ml per plate of Dulbecco's Modified Eagle's Medium/Ham's Nutrient Mixture F12 (DMEM/F12) (JRH Biosciences), the medium being supplemented with 30% (v/v) heat-inactivated fetal calf serum (PCS, JRH Biosciences), 4 mM L-glutamine (Amresco), 10 mM HEPES (Sigma), and 1% (v/v) Penicillin-Streptomycin (Perucillin G 5000 U/ml, Streptomycin Sulfate 5 mg/ml) (JRH Biosciences). The plates were incubated at 37 °C and 5% CC>2 overnight. At day 1, transfection was performed using calcium phosphate. Before transfection, the medium in each plate was replaced with 120 ml of fresh DMEM/F12 supplemented with 10% (v/v) heat-inactivated PCS or DCS, 4 mM L-glutamjne, 10 mM HEPES, and 1% (v/v) Penicillin-Streptomycin. Calcium phosphate / DNA precipitate was prepared by adding 1200 µg of pIRESbleo3 (Invitrogen) plasmid DNA harboring the gene for human TNFRJ-Fc and 3720 µl of 2 M calcium chloride solution (BD Biosciences) in sterile HzO to a final volume of 30 ml (solution A), Alternatively, the same amount of plasmid DNA was added to 3000 µl of 2.5 M CaCl2 in sterile IxTE was to a final volume of 30 ml (solution A). Solution A was added drop-wise to 30 ml of 2 x HEPES Buffered Saline (HBS) (solution B) (BD Biosciences) with a 10 ml pipette, During the course of addition, bubbles were gently blown through solution B. The mixture was incubated at 25 °C for 20 minutes and vortexed, 12 ml of the mixture was added drop-wise to each plate. The plates were incubated at 37 °C and 5% COz overnight. Alternatively, after 4 hours incubation the medium containing the transfection mixture was removed and 100 ml of DMEM/F12 supplemented with 10% (v/v) DCS, 4 mM L-glutamine, 1% (v/v) Penicillin-Streptomycin, and a final concentration of 3,5-4.0 mM HC1, with the medium having a final pH of 7, was added to each plate. The plates were incubated at 37°C and 5% CO; overnight. At day 2, the cell culture supernatant was discarded. The contents in the plates were washed twice with 50 ml of DMEM/F12 medium per plate and 100 ml of fresh serum-free DMEM/F12 medium, supplemented with 40 mM N-acetyl-D-mannosamine (New Zealand Pharmaceuticals), 7 or 10 mM L-Glutamine, 15 mM HEPES, 0.5 or 4.1 g/L Mannose (Sigma), 1% (v/v) Penicillin-Streptomycin,, and ITS solution (5 mg/L bovine insulin, 5 mg/L partially iron saturated human transferrin and 5 fig/ml selenium) (Sigma) (alternatively, without ITS solution) was added to each plate. The plates were incubated at 37 °C and 5% CO2 overnight. At day 3, the cell culture supernatant was collected and 100 ml fresh serum-free DMEM/F12 medium., supplemented with 40 mM N-acetyl-D-mannosamine, 7 or 10 mM L-Glutamine, 15 mM HEPES (alternatively, without HEPES), 0,5 or 4.1 g/L Mernnose, 1% (v/v) Penicillin-Streptomycin, and ITS solution (alternatively, without ITS solution) was added to each plate, The plates were incubated at 37°C and 5% CO2 overnight. 100 mM PMSF (1% (v/v)) and 500 mM EDTA (1% (v/v)) were added to the collected cell culture supernatant and the mixture was stored at 4°C. At day 4, the serum free DMEM/F12 medium in the plates were collected. 100 mM PMSF, 1 % (v/v) and 500 mM EDTA, 1 % (v/v) were added to the collected medium and the mixture was combined with the day 3 serum free • collection, The combined cell culture media collections were filtered using 0.45 mm low-protein binding filters (Durapore, Millipore). The mixture was either stored at -70°C or used immediately, (ii) Isolation and Purification of TNFRI-Fc of the Present Invention Medium was collected, pH adjusted to pH 8 by the addition of 2 M Tris-HCl pH 8 (Sigma) to a final concentration of 100 mM and filtered (Durapore, 0.45µm, Millipore. One litre of pH adjusted medium containing TNFRI-Fc was passed under gravity flow over a Protein A Sepharose column (Pharmacia) with a ] ml bed volume which had been pre-equilibrated to pH 8 with 100 mM Tris-Cl (Sigma), After washing with 20 column volumes of column buffer (100 mM Tris-Cl pH 8) TNFRI-Fc was eluted with 0,1 M Citric Acid (Sigma) pH 4.4 followed by elution with 0.1 M Citric Acid (Sigma) pH 2.2 and immediately neutralised by the addition of 100 µl and 400 µl respectively of 2 M Tns-HCl pH 9 (Sigma). Fractions were analysed by silver stained SDS PAGE using 4-20 % gradient Tris-Glycine gels (Invitrogen).Pure fractions containing TNFRI-Fc were pooled and concentrated to less than 1 ml for size exclusion chromatography using a centrifugal filter device (Amicon Ultra, Millipore). Size exclusion chromatography was performed on the concentrated sample using Superdex 200 prep grade 16/70 (Pharmacia, Uppsala, Sweden) column. An isocratic flow of 1% Ammonium Bicarbonate was used at a flow rate of Iml/min. Total run time was 120 min with peaks eluting between 20 and 100 minutes. The eluted fractions were assayed by silver stained SDS PAGE using 4-20 % Tris-Glycine gels (Invitrogen). Fractions containint TNFRI-Fc were pooled and concentrated to less than 2 ml using a centrifugal filter device (Amicon Ultra, Millipore). The purified TNFRI-Fc was found to have an apparent MW of 45-85 kDa and to be at least 99 % pure by silver stained SDS PAGE. The final concentration of the TNFRI-Fc was found to be 213,86µg/ as determined by absorption at 280 run using a molar extinction coefficient of 51725 M'1 cm'1. (d) Production, Isolation and Purification of TNFRII-Fc of the Present Invention (i) Production of TNFRII-Fc of the Present Invention At day 0, five 500 cm2 tissue culture dishes (Coming) were seeded with 3 x 107 cells from a transformed embryonal human kidney cell line, for example HEK 293, HEK 293 c!8, HEK 293T, 293 CEN4, HEK 293F, HEK 293E, HEK 293FT, AD-293 (Stratagene) 293A (Invitrogen). Cells were seeded in 90 ml per plate of Dulbecco's Modified Eagle's Medium/Ham's Nutrient Mixture F12 (DMEM/F12) (JRH Biosciences), the medium being supplemented with 10% (v/v) heat-inactivated foetal calf serum (FCS, JRH Biosciences), 10mM HEPES (Sigma), 4mM L-glutamine (Ameresco) and l%(v/v) Penicillin-Streptomycin (JRH), At day 1, transfection was performed using calcium phosphate. Before transfection, the medium in. each plate was replaced with 120 ml of fresh DMEM/F12 (JRH Biosciences) containing 10% Foetal Calf Serum (JRH). Calcium phosphate / DNA precipitate was prepared by adding 1200 µg of pIRESbleo (Clonetech, BD Biosciences) plasmid DNA harbouring the gene for human TNFRII-Fc and 3720 µl CaCl2 to sterile H2O to a final volume of 30ml (solution A). Solution A was added drop wise to 30ml of 2 x HEPES Buffered Saline (HBS) (solution B) with a 10 ml pipette. During the course of addition, bubbles were gently blown through solution B via a pipette. The mixture was incubated at 25°C for 20 minutes and vortexed. 12 ml of the mixture was added drop wise to each plate via a pipette. After 4 hours the medium containing the transfection mixture was removed and 100 ml per plate of DMEM/F12 pH7 supplemented with 10% (v/v) heat-inactivated foetal calf serum (JRH Biosciences), lOmM HEPES, 4mM L-glutamine, }%(v/v) Penicillin-Streptomycin and 3.5 or 4.0 mM HCl was added and incubated overnight At day 3, the cell culture supernatant was collected and 100 ml fresh serum-free DMEM/F12 medium supplemented with 40 mM N-acetyl-D-mannosamine, 7 mM L-Glutamme. 0.5 g/L Manuose, and 1% (v/v) Penicillin-Streptomycin was added to each plate, The plates were incubated at 37 °C and 5% C02 overnight. 100 mM PMSF (1% (v/v)) and 500 mM EDTA (1% (v/v)) were added to the collected cell culture supernatant and the mixture was stored at 4 °C. At day 5, the serum-free DMEM/F12 was collected and 100ml of fresh serum-free DMEM/F12 was added to each plate. 100mM PMSF, 1% (v/v) and 500mM EDTA, 1% (v/v) were added to the collected medium and the mixture was stored at 4°C. Al day 4, the serum-free DMEM/F12 in the plates were collected. 100mM PMSF, 1% (v/v) and 500mM EDTA. 1% (v/v) were added to the collected medium and the mixture was combined with the first serum free collection. The combined cell culture supernatant collections were filtered using 0.45 mm low-protein binding filters (Durapore, Millipore). The mixture was either stored at -70°C or used immediately. (ii) Isolation and Purification of TNFRII-Fc of the Present Invention Medium was collected, pH adjusted to pH 8 by the addition of 2 M Tris-HCl pH 8 (Sigma) to a final concentration of 100 mM and filtered (Durapore, 0.45µm, Millipore. One litre of pH adjusted medium containing TNFRII-Fc was passed under gravity flow over a Protein A Sepharose column (Pharmacia) with a 1 ml bed volume which had been pre-equilibrated to pH 8 with 100 mM Tris-Cl (Sigma). After washing with 20 column volumes of column buffer (300 mM Tris-Cl pH 8) TNFRII-Fc was eluted with 0.1 M Citric Acid (Sigma) pH 4.4 followed by elution with 0.1 M Citric Acid (Sigma) pH 2.2 and immediately neutralised by the addition of 100 µl and 400 µl respectively of 2 M Tris-HCl pH 9 (Sigma). Fractions were analysed by silver stained SDS PAGE using 4 - 20 % gradient Tris-Glycine gels (Invitrogen). Pure fractions containing TNFRII-Fc were pooled and concentrated to less than 1 ml for size exclusion chromatography using a centrifugal filter device (Amicon Ultra, Millipore), Size exclusion chromatography was performed on the concentrated sample using Superdex 200 prep grade 36/70 (Pharmacia, Uppsala. Sweden) column. An isocratic flow of 1% Ammonium Bicarbonate was used at a flow rate of Iml/min. Total run time was 120 min with peaks eluting between 20 and 100 minutes. The eluted fractions were assayed by silver stained SDS PAGE using 4-20 % Tris-Glycine gels (Invitrogen). Fractions containint TNFRII-Fc were pooled and concentrated to less than 2 ml using a centrifugal filter device (Amicon Ultra, Millipore). The purified TNFRII-Fc was found to have an apparent MW of 45 - 100 kDa and to be at least 99 % pure by silver stained SDS PAGE. The final concentration of the TNFRII-Fc was found to be 1321 µg/ml as determined by absorption at 280 run using a molar extinction co-efficient of 61110 M-1 cm-1.. (e) Production, Isolation and Purification of BAFF of the Present Invention (i) Production of BAFF of the Present Invention At day 0, five 500 cm2 tissue culture dishes (Corning) were seeded with 3 x 107 cells of a transformed embryonal human kidney cell line, for example HEK 293, HEK 293 c!8, HEK 293T, 293 CEN4, HEK 293F, HEK 293E, HEK 293FT, AD-293 (Stratagene), or 293A (Invitrogen). Cells were seeded in 90 ml per plate of Dulbecco's Modified Eagle's Medium/Ham's Nutrient Mixture F12 (DMEM/F12) (JRH Biosciences), the medium being supplemented with 10% (v/v) donor calf serum (DCS, JRH Biosciences), 4 mM L-glutamine (Amresco) and 1% (v/v) Penicillin-Streptomycin (Penicillin G 5000 U/ml, Streptomycin Sulphate 5 mg/rni) (JRH Biosciences). The plates were incubated at 37 °C and 5% CO; overnight, At day 1, transfection was performed using calcium phosphate. Before transfection, the medium in each plate was replaced with 120 ml of fresh DMEM/F12 supplemented with 10% (v/v) heat-inactivated FCS or DCS, 4 mM L-glutamine, 10 mM HEPES, and 1% (v/v) Penicillin-Streptomycin. Calcium phosphate / DNA precipitate was prepared by adding 1200 fig of pIRESbleo3 (Invitrogen) plasmid DNA harboring the gene for human BAFF and 3720 ul of 2 M calcium chloride solution (BD Biosciences) in sterile H2O to a final volume of 30 ml (solution A), Alternatively, the same amount of plasmid DNA was added to 3000 fil of 2.5 M CaCl2 in sterile IxTE was to a final volume of 30 ml (solution A). Solution A was added drop-wise to 30 ml of 2 x HEPES Buffered Saline (HBS) (solution B) (BD Biosciences) with a 10 ml pipette. During the course of addition, bubbles were gently blown through solution B. The mixture was incubated at 25 °C for 20 minutes and vortexed. 12 ml of the mixture was added drop-wise to each plate. The plates were incubated at 37 °C and 5% C02 overnight. Alternatively, after 4 hours incubation the medium containing the transfection mixture was removed and 100 ml of DMEM/F12 supplemented with 10% (v/v) DCS, 4 mM L-glutamine, 1% (v/v) Penicillin-Streptomycin, and a final concentration of 3.5-4.0 mM HC1, with the medium having a final pH of 7, was added to each plate. The plates were incubated at 37°C and 5% CO2 overnight. Al day 2, the cell culture supernatant was discarded, The contents in the plates were washed twice with 50 ml of DMEM/F12 medium per plate and 100 ml of fresh serum-free DMEM/F12 medium, supplemented with 40 mM N-acetyl-D-maruiosamine (New Zealand Pharmaceuticals), 7 or 10 mM L-Glutamine, 0.5 or 4.] g/L Mannose (Sigma), and 1% (v/v) Penicillin-Streptomycin, was added to each plate. The plates were incubated at 37 °C and 5% CO2 overnight. At day 3, the cell culture supernatant was collected and 100 ml fresh serum-free DMEM/F12 medium, supplemented with 40 mM N-acetyJ-D-mannosamine, 7 or 30 mM L-Glutamine, 0.5 or 4.1 g/L Mannose, and 1% (v/v) Penicillin-Streptomycin, was added to each plate. The plates were incubated at 37 °C and 5% CO3 overnight. 100 mM PMSF (1% (v/v)) and 500 mM EDTA (1% (v/v)) were added to the collected cell culture supernatant and the mixture was stored at 4 °C. At day 4, the cell culture supernatant was collected. 100 mM PMSF (1% (v/v)) and 500 mM EDTA (1% (v/v)) was added to the collected cell culture supernatant and combined with the day 3 collection before particulate removal using a 0,45 micron low-protein binding filter (Durapore, Millipore). The mixture was either stored at -70 °C or used immediately. (ii) Isolation and Purification of BAFF of the Present Invention 950 ml of filtered cell culture supernatant was concentrated approximately 20 fold using a tangential flow filtration (TFF) device (Peiicon XL, Ultracell, Millipore). The sample was pumped at 350 ml/min across 150 cm2 of regenerated cellulose membrane, with a nominal molecular weighl cut-off of 5 KDa until the sample had concentrated down to a volume of 30 ml. The concentrated sample was diafiltered by the addition of 70 ml of 50 mM HEPES pH 8 followed by another concentration down to 30 ml. This diafiltration step was repeated twice with a final concentration to 50 ml. The concentrated diafiltered sample was then filtered through a 0.45 micron low-protein binding filter (Durapore, Millipore). Purification of BAFF was achieved by passing the concentrated cell culture supernatant from the TFF over an Ion Exchange column (Bio-Rad Laboratories, MacroPrep HS) pre-equilibrated with 50 mM HEPES pH 8. The bound BAFF was then eluted from the column with a linear gradient from 50 mM HEPES pH 8 to 80 % 50 mM HEPES pH 8 containing 1M NaCl. The resulting fractions were analysed for apparent molecular weight and level of purity by BUS A and ID SDS PAGE using 4 - 20 % gradient Tris-Glycine gels (Invitrogen) and quantitated by anti-BAFF ELISA (R & D Systems). BAFF was found to elute from the anion exchange column as two distinct ionic forms. Fractions containing pure BAFF were combined and concentrated to less than 1 ml for size exclusion chromatography using a centrifugal filter device (Amicon Ultra, Millipore). Size exclusion chromatography was performed on the combined anion exchange fractions using a Superdex 75 prep grade 16/70 column (Pharmacia, Uppsala, Sweden). An isocratic buffer of 1 % ammonium bicarbonate was used at a flow rate of 1 ml/min. Total run time was 120 min with peaks eluting between 20 and 100 minutes. The eluted fractions -were assayed by silver stained 4 - 20 % gradient Tris-Glycine gels (Invitrogen) and by BAFF ELISA.. Fractions containing BAFF were combined and concentrated to less than 2 ml using a centrifugal filter device (Amicon Ultra, Millipore). The purified BAFF was found to have an apparent MW of around 16-17 kDa. The final concentration of the BAFF was found to be 50 ug/ml as determined by absorption at 280 nm using a molar extinction co-efficient of 14565 M"1 cm"1. (f) Production, Isolation and Purification of NGFR-Fc of the Present Invention (i) Production of NGFR-Fc of the Present Invention At day 0, five 500 cm* tissue culture dishes (Coming) were seeded with 3 x 107 cells of a transformed embryonal human kidney cell line, for example HEK 293, FtEK 293 c!8, HEK 293T, 293 CEN4, HEK 293F, HEK 293E, HER. 293FT, AD-293 (Stratagene), or 293A (Invitrogen). Cells were seeded in 90 ml per plate of Dulbecco's Modified Eagle's Medium/Ham's Nutrient Mixture F12 (DMEM/F12) (JRH Biosciences), the medium being supplemented with 10% (v/v) heat-inactivated fetal calf serum (PCS, JRH Biosciences), 4 mM L-glutamme (Amresco) and 1% (v/v) Penicillin-Streptomycin (Penicillin G 5000 U/ml, Streptomycin Sulphate 5 mg/ml) (JRH Biosciences). The plates were incubated at 37°C and 5% CO: overnight. At day 1, transfection was performed using calcium phosphate. Before transfection, the medium in each plate was replaced with 120 ml of fresh DMEM/F12 supplemented with 10% (v/v) heat-inactivated PCS, 4 mM L-glutamine, and 1% (v/v) Penicillin-Streptomycin. Calcium phosphate / DNA precipitate was prepared by adding 1200 µg of pIRESbleoS (Invitrogen) plasmid DNA harboring the gene for human NGFR-Fc and 3720 µl of 2.5 M CaCl2 in sterile H2O to a final volume of 30 ml (solution A). Solution A was added drop-wise to 30 ml of 2 x HEPES Buffered Saline (HBS) (solution B) with a 10 ml pipette. During the course of addition, bubbles were gently blown through solution B. The mixture was incubated at 25 °C for 20 minutes and vortexed. 12 ml of the mixture was added drop-wise to each plate. After 4 hours the medium containing the transfection mixture was removed and 100 ml of DMEM/F12 supplemented with 10% (v/v) heat-inactivated PCS, 4 mM L-glutamine, 1% (v/v) Penicillin-Streptomycin, and a final concentration of 3.5 mM HC1, with the medium having a final pH of 7, was added to each plate. The plates were incubated at 37 °C and 5% CO2 overnight. At day 2, the cell culture supernatant was discarded. The contents in the plates were washed twice with 50 ml of DMEM/F12 medium per plate and 100 ml of fresh serum-free DMEM/F12 medium, supplemented with 40 mM N-acetyl-D-marmosamine (New Zealand Pharmaceuticals), 10 mM L-Glutamine, 0.5 g/L Mannose (Sigma), and 1% (v/v) Penicillin-Streptomycin, was added to each plate. The plates were incubated at 37 °C and 5% CO2 overnight. At day 3, the cell culture supernatant was collected and 100 ml fresh serum-free DMEM/F12 medium, supplemented with 40 mM N-acetyl-D-mannosamine, 10 mM L-Glutamine, 0.5 g/L Mannose, and 1% (v/v) Penicillin-Streptomycin, was added to each plate. The plates were incubated at 37 °C and 5% CO2 overnight. 100 mM PMSF (1% (v/v)) and 500 mM EDTA (1% (v/v)) were added to the collected cell culture supernatant and the mixture was stored at 4 °C- At day 4, the cell culture supernatant was collected. 100 mM PMSF (3% (v/v)) and 500 mM EDTA (1% (v/v)) was added to the collected cell culture supernatant and combined with the day 3 collection. The combined collections were adjusted to pH 8 by the addition of 2 M Tris-HCl pH 8 (Sigma) to a final concentration of 100 mM before particulate removal using a 0.45 micron low-protein binding filter (Durapore, Millipore), The mixture was either stored at -70 oC or used immediately. (ii) Isolation and Purification of NGFR-Fc of the Present Invention Medium was collected. pH adjusted to pH 8 by the addition of 2 M Tris-HCl pH 8 (Sigma) to a final concentration of 100 mM and filtered (Durapore, 0.45 µrn, Millipore. One litre of pH adjusted medium containing NGFR-Fc was passed under gravity flow over a Protein A Sepharose column (Pharmacia) with a 1 ml bed volume which had been pre-equilibrated to pH 8 with 100 mM Tris-Cl (Sigma). After washing with 20 column volumes of column buffer (100 mM Tris-Cl pH 8) NGFR-Fc was eluted with 0.1 M Citric Acid (Sigma) pH 4.4 followed by elution with 0.1 M Citric Acid (Sigma) pH 2.2 and immediately neutralised by the addition of 100 ul and 400 ul respectively of 2 M Tris-HCl pH 9 (Sigma). Fractions -were analysed by silver stained SDS PAGE using 4-20 % gradient Tris-Glycine gels (Invitrogen). Pure fractions containing NGFR-Fc were pooled and concentrated to ]ess than 1 ml for size exclusion chromatography using a centrifugal filter device (Amicon Ultra, Millipore). Size exclusion chromatography was performed on the concentrated sample using Superdex 200 prep grade 16/70 (Pharmacia, Uppsala, Sweden) column. An isocratic flow of 1% Ammonium Bicarbonate was used at a flow rate of Iml/min. Total run time was 120 min with peaks eluting between 20 and 100 minutes. The eluted fractions were assayed by silver stained SDS PAGE using 4-20 % Tris-Glycine gels (Invitrogen). Fractions containint NGFR-Fc were pooled and concentrated to less than 2 ml using a centrifugal filter device (Amicon Ultra, Millipore), The purified NGFR-Fc was found to have an apparent MW of 50-110 kDa and to be at least 95 % pure by silver stained SDS PAGE. The final concentration of the NGFR-Fc was found to be 1259 µg/ as determined by absorption at 280 nm using a molar extinction coefficient of 55735 M'1 cm'1. (g) Production, Isolation and Purification of Fas Ligand of the Present Invention (i) Production ol Fas Ligand of the Present Invention At day 0, five 500 cm" tissue culture dishes (Corning) were seeded with 3 x 107 cells of a transformed embryonal human kidney cell line, for example HEK 293, HEK 293 c!83 HEK 293T. 293 CEN4, HEK 293F, HEK 293E, HEK 293FT, AD-293 (Stiatagene), or 293A (Invitrogen). Cells were seeded in 90 ml per plate of Dulbecco's Modified Eagle's Medium/Ham's Nutrient Mixture F12 (DMEM/F12) (JRH Biosciences), the medium being supplemented with 10% (v/v) donor calf serum PCS, JRH Biosciences), 4 mM L-glutamine (Amresco) and 3% (v/v) Penicillin-Streptomycin (Penicillin G 5000 U/ml, Streptomycin Sulphate 5 mg/ml) (JRH Biosciences). The plates were incubated at 37 °C and 5% CO2 overnight. At day 1, transfection was performed using calcium phosphate. Before transfection, the medium IE each plate was replaced with 120 ml of fresh DMEM/F12 supplemented with 10% (v/v) DCS, 4 mM L-glutamine, and 1% (v/v) Penicillin-Streptomycin. Calcium phosphate / DNA precipitate was prepared by adding 1200 µg of pIRESbleoS (Invitrogen) plasmid DNA harboring the gene for human Fas Ligand and 3720 µl of 2.5 M CaCl2 in sterile H20 to a final volume of 30 ml (solution A). Solution A was added drop-wise to 30 ml of 2 x HEPES Buffered Saline (HBS) (solution B) with a 10 ml pipette. During the course of addition, bubbles were gently blown through solution B. The mixture was incubated at 25 oC for 20 minutes and vortexed. 12 ml of the mixture was added drop-wise to each plate. After 4 hours the medium containing the transfection mixture was removed and 100 ml of DMEM/F12 supplemented with 10% (v/v) DCS, 4 mM L-glutamine, 3% (v/v) Penicillin-Streptomycin, and a final concentration of 3.5 mM HC1, with the medium having a final pH of 7, was added to each plate. The plates were incubated at 37°C and 5% CO2 overnight. At day 2, the cell culture supernatant was discarded, The contents in the plates were washed twice with 50 ml of DMEMJF12 medium per plate and 100 ml of fresh serum-free DMEM/F12 medium, supplemented with 40 mM N-acetyJ-D~mannosamine (New Zealand Pharmaceuticals), 10 mM L-Glutamine, 0.5 g/L Mannose (Sigma), and 1% (v/v) Penicillin-Streptomycin, was added to each plate. The plates were incubated at 37 °C and 5% CO; overnight, At day 3, the cell culture supernatant was collected and 100 ml fresh serum-free DMEM/F32 medium, supplemented with 40 mM N-acetyl-D-mannosamine. 10 mM L-Glutamine, 0.5 g/L Mannose, and 1% (v/v) Penicillin-Streptomycin, was added to each plate. The plates were incubated at 37 °C and 5% CO2 overnight. 100 mM PMSF (1% (v/v)) and 500 mM EDTA (1% (v/v)) were added to the collected cell culture supernatant and the mixture was stored at 4 °C. At day 4, the cell culture supernatant was collected. 100 mM PMSF (1% (v/v)) and 500 mM EDTA (1% (v/v)) was added to the collected cell culture supernatant and combined with the day 3 collection. The combined collections were adjusted to pH 6 by the addition of a one tenth volume of 200 mM MES/ 50 mM MgCl2 pH6 before particulate removal using a 0.45 micron low-protein binding filter (Durapore, Millipore). The mixture was either stored at -70 °C or used immediately. (ii) Isolation and Purification of Fas Ligand of the Present Invention The process of Dye-ligand chiomatography (DLC) was used as the primary step in the purification of Fas ligand. A library of immobilised reactive dye was used to screen Fas ligand for efficient binding and release in a batch purification microtitre format. Suitable dye-protein combinations were then tested in a small scale column format. In small scale purification 5 ml samples of thawed cell culture supernatant were passed through 0,5 ml dye-ligand columns at a pH of either 6 or 7.3. In this optimisation step optimal reactive dye-cytokine and pH combinations were selected for maximal recover,' in fractions for up scaling in bulk DLC. For bulk scale DLC reactive dye number 8 High (Zymatrix) was selected as the reactive dye with the best binding and elution properties for Fas ligand. The filtered cell culture supernatant was passed under gravity flow over 4.0 ml or 8.0 ml column bodies (Alltech, Extract Clean Filter columns) with 3 ml or 6 ml respectively of DLC resin pre-equilibrated to pH 6 with 50 mM MES/5 mM MgCl2, The column was washed with Buffer A (20 mM MES/5 mM MgCl2 pH 6) until fractions were free of protein as monitored by colourmetric protein assay (Biorad protein assay). Fas ligand was eluted using three Elution Buffers in the following order: Elute 1: Buffer C (50 mM Tris-Cl/' 10 mM EDTA pH 8) Elute 2: EN 1.0 (50 mM Tris-Cl/10 mM EDTA/1.0 MNaCI pH 8) Elute 3; EN2.0 (50 mM Tris-Cl/10 mM EDT A/2.0 M NaCl pH 8) The eiuted fractions were assayed by silver stained SDS PAGE using 4 - 20% Tris-Glycine gels (Invitrogen) and by anti-Fas ligand ELISA (R&D systems). Fas ligand was found to bind to reactive dye 8 High and was found to elute in Buffer EN1.0. It was estimated by SDS PAGE analysis that 90% of the contaminating proteins were removed in this primary purification step. DLC fractions containing Fas ligand were desalted using a PD10 column (Amersham Biosciences) and pooled for cation exchange chromatography. Purification was achieved by passing the desalted fractions from the PD10 column over a cation exchange column (Bio-Rad Laboratories, Uno SI) pre-equilibrated to pH 6.5 with 50 mM MES pH 6.5 (Sigma). The bound Fas ligand was then eluted from the column with a linear gradient from 50 mM MES pH 6.5 to 50 mM MES pH 6.5 containing 1 M NaCl. The resulting fractions were analysed for apparent molecular weight and level of purity by EL1SA and ID SDS PAGE using 4-20 % gradient Tris-G3ycine gels (Invitrogen) and quantitated by anti-Fas ligand ELISA (R&D systems). Fractions containing the cytokine were Size exclusion chromatograpliy was performed on the concentrated sample using Superdex 75 prep grade 16/70 (Pharmacia, Uppsala, Sweden) column. An isocratic flow of 1% Ammonium Bicarbonate was used at & flow rate of Iml/min. Total run time was 120 min with peaks eluting between 20 and 100 minutes. The eluted fractions were assayed by silver stained SDS PAGE using 4-20 % Tris-Glycine gels (Invitrogen). The purified Fas Ligand was found to have an apparent MW of around 25-36 kDa. The final concentration of the Fas Ligand was found to be 94.8 µg/ml as determined by absorption at 280 nm using a molar extinction co-efficient of 27515 M-1 cm-1. (h) Production, Isolation and Purification of a Further Embodiment of TNFRII-Fc of the Present Invention (Batch 003) (i) Production of TNFRII-Fc (Batch 003) of the Present Invention Freestyle 293F cell cultures were prepared with a minimum total cell number of 5xl07 cells. Freestyle 293F cell density and total cell number was determined by trypan blue exclusion. 3x10' cells were added to 28ml of Freestyle expression medium (Invitrogen) in a 125mL Erlemneyer flask. Cells were then incubated at 37°C with shaking, while transfection mixes were prepared. 30µg of plasmid DNA harbouring the TNFRII-Fc sequence (pCEP-4-TNFRII-Fc) in a 25µl volume was added to 975µl Opti-MEM (Invitrogen)(Solution A). 40µl of 293fectin (Invitrogen) was added to 960µl Opti-MEM (Solution B). Solution A and Solution B were incubated at room temperature for 5 minutes, then mixed together gently and incubated at room temperature for a further 30 minutes. The transfection mix was added to 28ml of the 293F cell suspension. Expression cultures were maintained by sub-culturing until TNFRII-Fc expression ceased. Large-scale expression of protein was carried out in either shaker flasks or MantaRay culture vessels (Fisher Scientific). Five hundred ml or 1000ml cultures of Freestyle 293F cells transfected with the pCEP'4-TNFRII-Fc vector were prepared in Freestyle Expression Medium at a cell density of 4xl05cells/ml as follows, Transfected cells were then pelleted at 1000rpm for 10min, washed with 5ml of pre-warmed sterile PBS then pelleted at 1000rpm for 10 min and resuspend in 10ml of fresh Freestyle Expression Medium. Cells were added to either a MantaRay vessel or shaker flasks at a density of 4.0x 105 cell/ml in either 500ml or 1000ml pre-warmed Freestyle Expression Medium The cell culture was incubated 37°C, 5% CO2 humidified incubator with stirring. Cell viability was assessed every 24 hours using trypan blue exclusion. Once the cell density reached 1.5x]06 cells/ml (usually within 5 days after inoculation) the supernatant was harvested. (ii) Isolation and Purification of TNFRH-Fc (Batch 003) of the Present Invention (a) Purification of TNFRH-Fc of the present invention (Batch 003) was performed under sterile conditions in a biohazard hood and was performed in two chromatographic steps. The expression culture supernatant (Batch 003) was clarified by centrifugation and applied to a Protein A Sepharose Column (RN040633, Repligen) at a flow rate of 5 ml/min. The column was then washed with 10 bed volumes (200 ml) of 0.1 M Tris-Cl pH 8.0. Bound TNFRII-Fc (Batch 003) was eiuted with cold 0.1 M Citric Acid pH 4.0 and 20 ml fractions were collected jr. 8 labeled 50 ml Falcon tubes. Eiuted samples were incubated at 4*C for 1 hour to inactivate viruses and then the elutions were neutralized with 2M Tris-Cl pH 8.5. The TNFRII-Fc eluied from the protein A column was further purified over a over a Q Sepharose Column anion exchange column equilibrated with 80 mM citric acid 400mM Tris-Cl pH 9.0. The Protein A elution was applied at a flow rate of 5 ml/min the peak was collected and stored at 4°C. Bound protein was eluted equilibration buffer containing 1 M NaCl. The flow through peak was concentrated using four Centriprep YM-10 Centrifugal filter units (Millipore) according to the manufacturer's instructions. After 3 fold concentration, the fractions were buffer exchanged into 1 x DPBS pH 7.0 (2.7 mM KC1, 1.5 mM KH2PO4 137 mM NaCl and 8 mM Na2HPO4, pH 7.0). The final yield of TNFRII-Fc (Batch 003) was 60 ml of 1.45 mg/ml (i.e. 87 mg of total protein) as determined by UV280 and Fc ELISA. The silver stained gel revealed a greater than 95% purity, Bioassay results revealed TNFRII-Fc Batch 003 was active and able to inhibit cell toxicity from TNF-a in proliferation assays of WEHI164 cells. (b) Alternatively. TNFRII-Fc was purified using a 2 ml IP A-400HC rProtein A column (Repligen RN040633). Expression culture supernatant containing TNFRII-Fc was loaded to the column for about 4 hours at room temperature, and overnight at 4°C. The column was washed with buffer (12.5 ml 1M NaCl, 0.1M Tris, pH S.O) and bound TNFRII-Fc was eluted with 14 ml 0.1 M Citric Acid, pH 4.0 and neutralised with 6 ml of Tris, pH 9.0. The elution was concentrated using Centriprep YM-10 Centrifugal filter units according to manufacturers instructions. TNFRII-Fc (approximately 3 mg/ml) was detected by methods described above. EXAMPLE 3 (a) Characterization of TNF-a of the Present Invention (i) Two-Dimensional Polyacrylamide Electropboresis The sample collected from Example 2(a) was buffer exchanged by dialysis or desalting column (Pharmacia HR 10/10 Fast Desalting Column) into re-purified (18 MOhm) water and dried using a SpeedVac concentrator. Alternatively the collected sample undergwent TCA or acetone precipitation using methods known in the art. The sample was then re-dissolved into 240µl MSD buffer (5M urea, 2M thiourea, 65mM DTT, 2% (w/v) CHAPS, 2% (w/v) sulfobetame 3-10, 0.2% (v/v) carrier ampholytes, 40mM Tris, 0.002% (w/v) bromophenol blue, water) and centrifuged at ISOOOg for 8 minutes. Isoelectric focusing (IEF) was performed using either precast 11 cm or precast 17 cm gel pH 3-10 immobolised pH gradient IEF strips (BioRad). The IEF strips were re-hydrated in the sample in a sealed tube at room temperature for at least 6 hours. The IEF strips were placed into the focusing chamber and covered with paraffin oil. IEF was carried out at 100 V for 1 hour.. 200V for ] hour, 600V for 2 hours, 1000 V for 2 hours, 2000 V for 2 hours, 3500 V for 12 hours and 100 V for up to 12 hours in the case of 11cm strips or for 85kV hours in the case of 17cm strips (using the same V ramp up procedure). Following isoelectnc focusing the strips were reduced and alkylated before being applied to a second dimension gel. The strips were incubated in 1 x Tris/HCl pH 8.8, 6M urea, 2% (w/v) SDS, 2% (v/v) glycerol, 5mM tributylphosphine (TBP), 2.5% (v/v) acrylamide solution for at least 20 minutes. The 11cm strips were separated on .the.second dimension by Criterion pre poured (11 x 8cm; 1mm thick) 10-20% Tris glycine gradient gels (BioRad). 17cm strips were separated on 17 x ]7 cm, 1.5mm thick, self poured 10-20% Tris glycine gradient gels. Precision or Kaleidoscope molecular weight markers (BioRad) were also applied to the gel. The strip was set into place using 0.5% Agarose containing bromophenol blue as a tracking dye. The SDS-PAGE was run using either a Criterion or Protean II electrophoresis system (BioRad) (200 V for; hour (until the buffer front was about to run off the end of the gel) for ] ] cm gels and 15mA constant current per gel for 21 hours for 17cm gels). The buffer used was 192 mM glycine, 0.1% (w/v) SDS, 24.8 mM Tris base at pH 8.3. The completed second dimension gels were fixed for 30 minutes- overnight in 10% methanol (MeOH and 1% acetic acid (Hac). The gel was then stained using Sypro Ruby ge] stain (BioRad) for at least 3 hours and destained with 10% MeOH and 7% HAc for at least 30 minutes. Alternatively after fixing the gels were stained using Deep Purple fluorescent stain. The gels were incubated in 300mM Na2CO3, 35 mM NaHCO3 for 2 x 30 min, then incubated in 1:200 dilution Deep Purple stain for at least 1 hour in the dark. The gels were then destained by 2 x 15 minute incubations in 10% MeOH, 7% HAc. In both cases the gel was imaged using a FX laser densitometer (BioRad) and the appropriate filter. Analysis of Two-Dimensional Electropboresis Protein Maps Using Image Analysis Software Image! (http://rsb.info.nih.gov/ij/) was used to analyse the relative intensities of the protein spots on each gel. Densitometry was performed on the spots within a selected area of each gel and a background subtraction was conducted using the appropriate region of the gel lacking protein spots. A volume integration was performed on each protein spot of interest. Relative percentage intensities were calculated for each protein spot and by normalising the combined value of the intensities of all spots to 100%, the intensity of each protein spot relative to the other spots in each gel was determined. t The molecular weights of the respective spots were determined by measuring the respective distance of the spots from the base of each gel and comparing the distance shown by Precision or Kaleidoscope molecular weight markers that were also applied to each gel. A 4th order polynomial and exponential function was fitted to the precision markers to interpolate protein spot locations respectively. In this way, the molecular weights of the respective spots could be accurately determined. The charge of the isoforms (pKa values) were determined by measuring the respective distance of the spots from the left side of each gel using Image! Since the relationship between the pJ values of the strip and the physical distance of each gel is linear, the pi values corresponding to the different pKa values of the isoform spots were readily determined. Each protein spot corresponds to a "unique isoform of TNF-a. Tables 9 and 10 show The major protein spots in each resulting gel corresponds to isoforms of TNF-a. The low intensity spots may be TNF-a or low level contaminants, however, these canot be confirmed by PMF due to the low intensity. Examination of the gels revealed that TNF-a of the present invention contains 10 to 30 isoforms. Tables 9 and 10 show key properties of these isoforms: the pi values (± 1.0), the apparent molecular weights (± 20%), and the relative intensities (+ 20% of the actual value or ^ 2% of the total, whichever is larger). The values listed correspond to the intensity weighted center within the selected area of each gel containing the spot and hence, are only reflective of the pi and molecular weight of the protein at one particular reading within the selected area of each gel. Taking into consideration the inherent variability7 of size and position of protein spots within 2D gels, the pi values for the molecule are determined to range from about 4-8.5 based on the values listed in Tables 9 and 10; and the apparent molecular weights of the molecule are determined to range from 10-30 kDa based on the values listed in Tables 9 and 10. TABLE 9 Molecular weights and pi values of isoforms of TNF-a (Table Removed) TABLE 10 Molecular weights and pi values of isoforms of TNF-a (Table Removed) (ii) One-Dimensional Polyacrylamide Electropboresis The sample collected from Example 2(a) was dried and then re-solubilised into 60 µl of ID sample buffer (10% glycerol, 0.1% SDS, 10mM DTT, 63mM tris-HCl) and heated at 1 00°C for 5 minutes. For PNGaseF treatment, a 30 µL aliquot of the sample was taken and NP40 added to a final concentration of 0.5 %. 5 µL of PNGaseF was added and the sample was incubated at 37 °C for 3 hours. For glycosidase cocktail treatment of the sample, an aliquot was taken and NP 40 is added to a final concentration of 0.5%. 1 µX of PNGase F, and 1µL each of Sialidase A (neuramidase), 0-Glycanase, |3 (l-4)-Galactosidase and ß-N-Acetylglucosaminidase was added. Treated and untreated samples were incubated at 37 °C for 3 hours. Treated and untreated samples were run on a pre-cast Tris gel, for example, a Tris 4-20% gradient gel (BioRad) or Tris HC1 gradient gel (Invitrogen). Precision molecular weight markers (BioRad catalogue number 161-0363) were also applied to the gel. Criterion 4-20% or 18% gels were used for ID SDS-PAGE (BioRad catalogue numbers: 345-0033 or 345-0024). The SDS-PAGE was run using either a Mini Protean 11 or a Criterion electrophoresis system (BioRad) at 200 V for approximately 1 hour or until the buffer front was about to run off the end of the gel. The buffer used was 192 mM glycine, 0.1% (w/v) SDS, 24.8 mM Tris base at pH 8.3. The completed gels were fixed for at teast 30 minutes in 10% MeOH and 7% HAc. The gel was then stained using Sypro Ruby gel stain (BioRad) for at least 3 hours and destained with 10% MeOH and 7% HAc for at least 30 minutes. Alternatively the gels were stained using Deep Purple (Araersham) as per the manufacturers instructions. The gel was imaged using a FX laser densitometer (BioRad) and the appropriate filter. The apparent molecular weight of the TNF-a (as observed by SDS-PAGE) following the release of N-lmked oligosaccharides (by PNGase treatment) was between 8 and 30 kDa. The apparent molecular weight of the TNF-a (as observed by SDS-PAGE) following the release of of N-linked and O-linked oligosaccharides (by glycosidase treatment) was between 10 and 20 kDa. (Hi) N-Terminal Sequencing Protein bands are cut from the gel prepared above (either from a two-dimensional gel or a one-dimensional gel) and are placed into a 0.5ml tube and 100m] extraction buffer is added (100mM Sodium acetate, 0.1%SDS, SOrnM DTT pH 5.5). The gel slices are incubated at 37'C for 16 hours with shaking. The supernatant is applied to a ProSorb membrane (ABI) as per the manufacturers instruction and sequenced using an automated 494 Protein Sequencer (Applied Biosystems) as per the manufacturers instructions. The sequence generated is used to confirm the identity of the protein. (iv) Peptide Mass FiageiTprinting Protein bands were cut from the gel prepared above (either from a two-dimensional gel or a one-dimensional gel) and washed with 25µl of wash buffer (50% acetonitrile in 50mM NH4HCO3). The ge! pieces were left at room temperature for at least 1 hour and dried by vacuum centrifugation for 30 minutes. The gel pieces and 12ul of trypsin solution (20u,g trypsin, 1200 µl NH4HCO3) was placed in each sample well and incubated at 4°C for 1 hour. The remaining trypsin solution was removed and 20 µl 50mM NH4HCO3 was added. The mixture was incubated overnight at 37°C with gentle shaking. The peptide samples were concentrated and desalted using CIS Zip-Tips (Millipore, Bedford, MA) or prefabricated micro-columns containing Poros R2 (Perseptive Biosystems, Framingham, MA) chromatography resm. Bound peptides were eluted in 0.8 µ1 of matrix solution (a-cyano-4-hydroxy cinnamic acid (Sigma), 8 mg/ml in 70% acetonitrile / 1% formic acid) directly onto a target plate. Peptide mass fingerprints of tryptic peptides were generated by matrix-assisted laser desorption / ionisation thne-of-flight mass spectrometry (MALDI-TOF MS) using a Perseptive Biosystems Voyager DE-STR. Spectra were obtained in reflection mode using an accelerating voltage of 20 kV. Mass calibration was performed using trypsin autolysis peaks, 2211.13 Da and 842.51 Da as internal standards. Data generated from peptide mass fingerprinting (PMF) was used to confirm the identity of the protein. Searches (primarily of Homo sapien (Human) and mammalian entries) were performed in databases such the SWISS-PROT and TrEMBL, via the program Peptldent (www.expasy.ch/tools/peptident.html). Identification parametres included peptide mass tolerance of 0.1 Da, a maximum of one missed tryptic cleavage per peptide, and the methionine sulfoxide and eystebe-acrylamide modifications, Identifications were based on the number of matching peptide masses and the total percentage of the amino acid sequence that those peptides covered, in comparison to other database entries. Generally, a peptide match with at least 30% total sequence coverage was required for confidence in identification, but very low and high mass proteins, and those resulting from protein fragmentation, may not always meet this criterion, therefore requiring further identification, Where inconclusive or no protein identification could be obtained from MALDI-TOF PMF analysis, the remaining peptide mixture or the identical spot cut from a replicate gel was subjected to tryptic digest and analysed by electrospray ionization tandem MS (ESI-MS/MS), For ESI-MS/MS, peptides were eluted from Poros R2 micro-columns in 1-2 jol of 70% acetonitrile. 1% formic acid directly into borosilicate nanoelectrospray needles (Micromass, Manchester, UK). Tandem MS was performed using a Q-Tof hybrid quadrupole/orthogonal-acceleration TOP mass spectrometer (Micromass). Nanoelectrospray needles containing the sample were mounted in the source and stable flow obtained using capillary voltages of 900-1200V. Precursor ion scans were performed to detect mass to charge ratio (m/z) values for peptides within the mixture. The mJz of each individual precursor ion was selected for fragmentation and collided with argon gas using collision energies of !8-30eV. Fragment ions (corresponding to the loss of amino acids from the precursor peptide) were recorded and processed using MassLynx Version 3.4 (Micromass). Ammo acid sequences were deduced by the mass differences between y- or b-'ion 'ladder1 series using the program MassSeq (Micromass) and confirmed by manual interpretation. Peptide sequences were then used to search the NCBI and TrEMBL databases using the program BLASTP "short nearly exact matches". A minimum of two matching peptides were required to provide confidence in a given identification. The identity of the gels spots were confirmed to be TNF-a. (b) Characterization of LT-a of the Present Invention (i) Two-Dimensional Polyacrylamide Electrophoresis The sample collected from Example 2(b) was treated and analysed as described above in Example 3(a)(i). The major protein spots in the resulting gels correspond to isoforms of LT-a, The low intensity spots may be LT-a or low level contaminants, however, these canot be confirmed by PMF due to the low intensity. Examination of the gel revealed that LT-a of the present invention contains 7 to 33 isoforms. Tables 11 and 12 show key properties of these isoforms; the pi values (± 1.0), the apparent molecular weights (± 20%), and the relative intensities (± 20% of the actual value or ± 2% of the total, whichever is larger). The values listed correspond to the intensity weighted center within the selected area of each gel containing the spot and hence, are only reflective of the pi and molecular weight of the protein at one particular reading within the selected area of each gel. Taking into consideration the inherent variability of size and position of protein spots within 2D gels, the pi values for the molecule are determined to range from about 5-11 based on the values listed in Tables 11 and 12; and the apparent molecular weights of the molecule are determined to range from 15- 32 kDa based on the values listed in Tables 11 and 12. TABLE 11 (Table Removed Molecular weights and pi values of isoforms of LT-a (Table Removed) TABLE 12 Molecular weights and pl values of isoforms of LT-a (Table Removed) (ii) One-Dimensional Polyacrylamide Electrophoresis The collected sample from Example 2(b) was treated as described above in Example 3(a)(ii). The apparent molecular weight of the LT-a (as observed by SDS-PAGE) following the release of N-linked oligosaccharides (by PNGase treatment) was between 12 and 25 kDa. The apparent molecular weight of the LT-a (as observed by SDS-PAGE) following the release of of N-linked and 0-linked oligosaccharides (by glycosidase treatment) was between 12 and 23 kDa. (iii) N-Terminal Sequencing of Proteins N-termina! sequencing of the LT-a of the present invention is performed as described above in Example 3(a)(iii). (iv) Peptide Mass Fingerprinting Peptide mass fingerprinting of the LT-a of the present invention was performed as described above in Example 3(a)(iv). The identity of the gel spots were confirmed to be LT-a. (c) Characterization of TNFRI-Fc of the Present Invention (i) Two-Dimensional Polyacrylamide Electrophoresis The sample collected from Example 2(c) was treated and analysed as described above in Example 3(a)(i). The major protein spots in the resulting gels correspond to isoforms of TNFRI-Fc. The low intensity spots may be TNFRI-Fc or low level contaminants, however, these canot be confirmed by PMF due to the low intensity, Examination of the gel revealed that TNFRI-Fc of the present invention contains 8 to 16 isoforms. Tables 13 and 14 show key properties of these isoforms: the pi values (± 1.0), the apparent molecular weights (± 20%), and the relative intensities (± 20% of the actual value or ± 2% of the total, whichever is larger). The values listed correspond to the intensity weighted center within the selected area of each gel containing the spot and hence, are only reflective of the pi and molecular weight of the protein at one particular reading within the selected area of each gel. Taking into consideration the inherent variability of size and position of protein spots within 2D gels, the pi values for the molecule are determined to range from about 5.5 - 9.5 based on the values listed in Tables 13 and 14; and the apparent molecular weights of the molecule are determined to range from 45 - 75 kDa based on the values listed in Tables 13 and 14. TABLE 13 Molecular weights and pl values of isoforms of TNFRI-Fc (Table Removed) TABLE 14 Molecular weights and pi values of isoforms of TNFRI-Fc (Table Removed) One-Dimensional PolyacrylamideElectrophoresis The collected sample from Example 2(c) was treated as described above in Example 3(a)(ii). The apparent molecular weight of the TNFRI-Fc (as observed by SDS-PAGE) following the release of N-linked oligosaccharides (by PNGase treatment) was between 36 and 60 kDa. The apparent molecular weight of the TNFRI-Fc (as observed by SDS-PAGE) follovring the release of of N-linked and 0-linked oligosaccharides (by glycosidase treatment) was between 36 and 60 kDa. (iii) N-Terminal Sequencing of Proteins N-termina! sequencing of the TNFRI-Fc of the present invention is performed as described above in Example 3(a)(iii). (iv) Peptide Mass Fingerprinting Peptide mass fingerprinting of the TNFRl-Fc of the present invention was performed as described above in Example 3(a)(iv). The identity of the gel spots were confirmed to be TNFRI-Fc. Further, an observed IDa shift in the masses of tryptic peptides indicated the asparagine residues (N) of 1 NX(S/T/C) motif found in the theoretical amino acid sequence of human TNFRI-Fc was modified to aspartic acid (D), consistent with the known ability of PNGase F to induce an Ts1 to D residue modification upon removal of associated N-linked oligosaccharides. Hence, a confirmed site of N-glycosylation of the TNFRI-Fc of the present invention is N-299 (when numbered from the start of the signal sequence). (d) Characterization of TNFRII-Fc of the Present Invention (i) Two-Dimensional Polyacrylamide Electropboresis The sample collected from Example 2(d) or 2(h) was treated and analysed as described above inExampie 3(a)(i). The major protein spots in the resulting gel corresponds to isoforms of TNFRII-Fc, The low intensity spots may be TNFRII-Fc or low level contaminants, however, these canot be confirmed by PMF due to the low intensity. Examination of the gel revealed that TNFRII-Fc of the present invention contains 10 to 40 isoforms. Tables 15 and 15(a) shows key properties of these isoforms: the pi values (± 1.0), the apparent molecular weights (± 20%), and the relative intensities (± 20% of the actual value or ± 2% of the total, whichever is larger). The values listed correspond to the intensity weighted center within the selected area of gel containing the spot and hence, are only reflective of the pi and molecular weigh! of the protein at one particular reading within the selected area of the gel. Taking into consideration the inherent variability of size and position of protein spots within 2D gels, the pi values for the molecule are determined to range from about 4-10 based on the values listed in Tables 15 and 15(a); and the apparent molecular weights of the molecule are determined to range from 46- 118 kDa based on the values listed in Tables 15 and TABLE 15 Molecular weights and pi values of isoforms of TNFRll-Fc (Table Removed) TABLE 15(a) Molecular weights and pi values of isoforms of TNFRII-Fc (Batch 003) (Table Removed) (ii) One-Dimensional Polyacrylamide Electrophoresis The collected sample from Example 2(h)(ii)(b) (Batch 003) was treated as described above in Example 3(a)(ii). The apparent molecular weight of the TNFRII-Fc (as observed by SDS-PAGE) following the release of N-linked oligosaccharides (by PNGase treatment) was between 46 and 87 kDa. The apparent molecular weight of the TNFRII-Fc (as observed by SDS-PAGE) following the release of of N-linked and O-linked oligosaccharides (by glycosidase treatment) was between 42 and 80 kDa. (iii) N-Terminal Sequencing of Proteins N-terminal sequencing of the TNFRII-Fc of the present invention was performed as described above in Example 3(a)(iii). The sequence generated (PAQVAFTPYA) was used to confirm the identity of the TNFRII-Fc. (iv) Peptide Mass Fingerprinting Peptide mass fingerprinting of the TNFRII-Fc of the present invention was performed as described above in Example 3(a)(iv). The identity of the gel spots were confirmed to be TNFRII-Fc. Further, the detection of a IDa shift in the masses of tryptic peptides indicates the asparagine residues (N) of one or more MX(S/T/C) motifs in the theoretical amino acid sequence of human TNFRII-Fc are modified to aspartic acid (D), hence confirming one or more sites of N-glycosylation of the TNFRII-Fc of the present invention. (e) Characterization of OX40-Fc of the Present Invention (i) Two-Dimensional Polyacrylamide Electrophoresis The sample collected from Example 2(e) was treated and analysed as described above in Example 3(a)(i). The major protein spots in the resulting gel corresponds to isoforms of OX40-Fc. The low intensity spots may be OX40-Fc or low level contaminants, however, these canot be confirmed by PMF due to the low intensity. Examination of the gel revealed that OX40-Fc of the present invention contains 8 to 16 isoforms. Table 16 shows key properties of these isoforms: the pl values (= 1.0). the apparent molecular weights (± 20%), and the relative intensities (+ 20% of the actual value or ± 2% of the total, whichever is larger). The values listed correspond to the intensity weighted center within the selected area of gel containing the spot and hence, are only reflective of the pi and molecular weight of the protein at one particular reading within the selected area of the gel. Taking into consideration the inherent variability of size and position of protein spots within 2D gels, the pl values for the molecule are determined to range from about 4-9 based on the values listed in Table 16; and the apparent molecular weights of the molecule are determined to range from 46- 75 kDa based on the values listed in Table 16. TABLE 16 Molecular weights and pl values of isoforms of OX40-Fc (Table Removed) (ii) One-Dimensional Polyacrylamide Electrophoresis The sample collected from Example 2(e) was treated as described above in Example 3(a)(ii). The apparent molecular weight of the OX40-Fc (as observed by SDS-PAGE) following the release of N-liriked oligosaccharides (by PNGase treatment) was between 44 and 72 kDa. The apparent molecular weight of the OX40-Fc (as observed by SDS-PAGE) following the release of N-linked oligosaccharides (by PNGase treatment) and 0-linked oligosaccharides (by glycosidase cocktail) was between 41 and 70 kDa. (iii) N-TerminaJ Sequencing N-terminal sequencing of the OX40-Fc of the present invention is performed as described above in Example 3(a)(iii). (iv) Peptide Mass Fingerprinting Peptide mass fingerprinting of the OX40-Fc of the present invention was performed as described above in Example 3(a)(iv). The identity of the gel spots were confirmed to be OX40-Fc. Further, an observed IDa shift in the masses of tryptic peptides indicated the asparagine residues (N) of 2 NX(S/T/C) motifs in the theoretical; amino acid sequence of human QX40-Fc were modified to aspartic acid (D). Herice, the confirmed sites of N-glycosylation of the OX40-Fc of the present invention include N-160 and N-298 (when numbered from the start of the signal sequence). (f) Characterization of BAFF of the Present Invention (i) Two-Dimeasioaal Polyacrylamide Electrophoresis; The sample collected from Example 2(f) was treated and analysed as described above in Example 3(a)(i), The major protein spots in the gel corresponds to isofbrms of BAFF. The low intensity spots may be BAFF or low level contaminants, however; these canot be confirmed by PMF due to the low intensity. Examination of the gel revealed that BAFF of the present invention contains 5 to 10 isoforms. Table 17 shows key properties of these isoforms: the pl values (± 1.0), the apparent molecular weights (± 20%), and the relative intensities (± 20% of the actual value or ± 2% of the total, whichever is larger), The values listed correspond to the intensity weighted center within the selected area of gel containing the spot and hence, are only reflective of the pi and molecular weight of the protein at one particular reading within the selected area of the gel. Taking into consideration the inherent variability of size and position of protein spots within 2D gels, the pl values for the molecule are determined to range from about 4-8 based on the values listed in Table 17; and the apparent molecular weights of the molecule are determined to range from 10- 22 kDa based on the values listed in Table 17. TABLE 17 Molecular weights and pl values of isoforms of BAFF (Table Removed) (ii) One-Dimensional Polyacrylamide Electrophoresis The collected sample from Example 2(f) was treated as described above in Example 3(a)(ii). The apparent molecular weight of the 3BAFF (as observed by SDS-PAGE) following the release of N-linked oligosaccharides (by PNGase treatment) was between 8 and 22 kDa. The apparent molecular weight of the BAFF (as observed by SDS-PAGE) following the release of N-linked oligosaccharides (by PNGase treatment) and O-linked oligosaccharides (by glycosidase cocktail) was between 8 and 22 kDa. (Hi) N-Termina) Sequencing N-termina] sequencing of theBAFF of the present invention is performed as described above in Example 3(a)(iii). (iv) Peptide Mass Fingerprinting Peptide mass fingerprinting of the BAFF of the present invention was performed as described above in Exampl e 3 (a) (iv). The identity of the gel spots were confirmed to be BAFF. (g) Characterkation of NGFR-Fc of the Present Invention (i) Two-Dimension a] Polyacrylamide Electropboresis The sample collected from Example 2(f) was treated and analysed as described above in Example 3(a)(i). The major protein spots in the resulting gel corresponds to isofonns of NGFR-Fc. The low intensity spots may be NGFR-Fc or low level contaminants, however, these canot be confirmed by PMF due to the low intensity. Examination of the gel revealed that NGFR-Fc of the present invention contains 8 to 36 isoforms. Table 18 shows key properties of these isoforms: the pl values (± 1.0), the apparent molecular weights (± 20%), and the relative intensities (± 20% of the actual value or ± 2% of the total, whichever is larger). The values listed correspond to the intensity weighted center within the selected area of gel containing the spot and hence, are only reflective of the pl and molecular weight of the protein at one particular reading within the selected area of the gel. Taking into consideration the inherent variability of size and position of protein spots within 2D gels, the pi values for the molecule are determined to range from about 3-6 based on the values listed in Table 18; and the apparent molecular weights of the molecule are determined to range from 55- 105 kDa based on the values listed in Table 18. TABLE 18 Molecular weights and pl values of isoforms of NGFR-Fc; (Table Removed) (ii) One-Dimensional PoJyacrylamide Electropboresis The sample collected from Example 2(g) was treated as described above in Example The apparent molecular weight of the NGFR-Fc (as observed by SDS-PAGE) was found to be between 55 and 105 kDa. The apparent molecular weight of the NGFR-Fc (as observed by SDS-PAGE) following the release of N-linked oligosaccharides by PNGase treatment was between 48 and 90 kDa. The apparent molecular weight of the NGFR-Fc (as observed by SDS-PAGE) following the release of N -inked oligosaccharides (by PNGase treatment) and 0-linked oligosaccharides (by glycosidase cocktail) was between 48 and 85 kDa, (Hi) N-Terminal Sequencing N-termina] sequencing of the NGFR-Fc of the present invention is performed as described above in Example 3{a)(iii). (iv) Peptide Mass Fingerprinting Peptide mass fingerprinting of the NGFR-Fc of the present invention was performed as described above in Example 3(a)(iv), The identity of the gel spots were confirmed to be NGFR-Fc. (h) Characterization of Fas Ligand of the Present Invention (i) Two-Dimensional Polyacrylamide Elecrropboresis The sample collected from Example 2(h) is treated and analysed as described above in Example 3(a)(i). (ii) One-Dimensional Polyacrylamide Electropboresis The sample collected from Example 2(h) was treated as described above in Example 3(a)(ii). The apparent molecular weight of the Fas Ligand (as observed by SDS-PAGE) was found to be between 15-35 kDa. The apparent molecular weight of the Fas Ligand (as observed by SDS-PAGE) following the release of N-linked oligosaccharides (by PNGase treatment) was between 12 and 23 kDa, (iii) N-Terminal Sequencing N-tennina] sequencing of the Fas Ligand of the present invention is performed as described above in Example 3(a)(iii). (rv) Pep tide Mass Fingerprinting Peptide mass fingerprinting of the Fas Ligand of the present invention was performed as described above in Example 3(a)(iv), The identity of the gel spots were confirmed to be Fas Ligand. An observed IDa shift in the masses of tryptic peptides indicated the asparagine residues (N) of 1 NX(S/T/C) motif in the theoretical amino acid sequence of human Fas Ligand was modified to aspartic acid (D). Hence, a confirmed site of N-glycosylaiion of the Fas Ligand of the present invention includes N-384 (when numbered from the start of the signal sequence). EXAMPLE 4 (a) Analysis of Araino Acid, Monosaccharide, Oligosaccbaride, Phosphate, Sulfate and Isoform Composition of TNF-a of the Present Invention. (i) Preparation of Samples for Amino Acid, Monosaccharide, Oligosaccharide, Phosphate, Sulfate and Isoform Analysis. For characterisation of monosaccharide and Oligosaccharide glycosylation and phosphate and sulfate post-translationai modifications, the saccharides are first removed from the polypeptide backbone by hydroJytic or enzymatic meats. The sample buffer components are also removed and exchanged with water to avoid inhibition of the hydrolysis and enzymatic reactions before analysis began. A solution of purified TNF-a in PBS is dialysed extensively against 4 litres of deionised ultrafiltered water (18 MOhrn) for four days with two changes per day using a regenerated cellulose dialysis membrane (Spectrapore) with a nominal molecular weight cut-off (NMWC) of 5 KDa. After dialysis the solution is dried using a Savant Speed Vac (New York, JUS A). The dried down sample is then resuspended in 2 ml of deionised ultrafihered watei| (18 MOhm) and divided into aliquots for the various analyses. (ii) Analysis of Amine Acid Composition by the Gas Phase Hydrolysis Method Amino acids in the samples are analysed using precfrlumn derivatisation with 6-ammoquinolyl-A'-hydroxysuccmimidy] carbamate (AQC). (The stable fluorescent ammo acid derivatives are separated and quantified by reverjsed phise (CIS) HPLC. The procedure employed is based on the Waters AccQTag aminp acid analysis methodology. Three 100 µl samples of the TNF-a preparation are taken and dried in a Speed Vac . The dried samples are then hydrolysed for 24 hours at 110°C. After hydrolysis the samples are dried again before derivatisation as follows. The dried samples are re-dissolved in 10 µL of an internal amino acid standard solution (a-aminobutyric acid, AABA), 35 µL of borate buffer is added followed by 15 µL of AQC derivatising reagent. The reaction mix is heated at 50oC for 12 minutes in a heating block. The derivatised amino acid sample is transferred to the autosampler of a HPLC system consisting of a Waters Alliance 2695 Separation Module, a Waters 474 Fluorescence Detector and a -Waters 2487 Dual λ Absorbance Detector in series. The control and analysis software is Waters Empower Pro Module (Waters Corporation, Milford, MA, USA). The samples were passed over a Waters AccQTag column (15cm x 3.9mm ID) using chromatographic parameters (i.e. suitable eluents and gradient flows) known in the an. (iii) Analysis of Neutral and Amino Monosaccharide composition Two 100 µl samples of the TNF-a preparation are taken and treated in two different ways to liberate monosaccharides. Each treatment, as described below, is performed in triplicate. 1. Hydrolysed with 2 M trifluroacetic acid (TFA) heated to 100° C for four hours to release neutral sugars (galactose, glucose, fucose and mannose). 2. Hydroiysed with 4 M HCS heated to 100° C for four hours to release amino sugars (N-acetyl-galactosamine, N-acetyl-glucosamine). All of the hydroiysates are lyophilised using a Speed Vac system, redissolved in 200 µl water containing 0.8 nmols of internal standard. For neutral and amino sugars the internal standard is 2-deoxy-glucose. The samples are then centrifuged at 10,000 g for 30 minutes to remove protein debris. The supernatant is transferred to a fresh tube and analysed by high pH anion exchange chromatography using a Dionex LC 50 system with a GP50 pump and an ED50 pulsed amperometric detector (Dionex Ltd). Analysis of neutral and amino sugars is performed using a Dionex CarboPac PA-20 column. Eiution is performed with an isocratic hydroxide concentration of 10 mM over 20 minutes. This is achieved with the Dionex EG50 eluent generation system. (iv) Analysis of Acidic Monosaccharide Composition A 100 µl sample of the TNF-a preparation is taken and: treated in the following way to liberate sialic acid rnonosaccharides. The treatment is performed in triplicate. The sample is hydrolysed with 0.1 M TFA at 80° C for 40 minutes to release N-Acety3 and N-Glycolyl neurarninic .acid. The hydroiysates are lyophilised using a Speed Vac, redissolved in 200 ul water containing 0.8 nmols of internal standard. For sialic acid analysis the internal standard is lactobionic acid. Samples are then centrifuged at 10,000 g for 30 minutes to remove protein debris. The supernatant is transferred to a fresh tube and analysed by high pH anion exchange chromatography using a Dionex LC 50 system with a GP50 pump and an ED50 pulsed amperometric detector. Analysis of sialic acids was performed using a Dionex CarboPac PA1 using using chromatographic parameters (i.e. suitable eluents and gradient flows) known in the art. (v) Analysis of Oligosaccbaride Composition For analysis of oiigosaccharide composition two 300 ul samples of the TNF-a preparation are taken in triplicate and treated in one of the following ways: Release of N-Iinked oligosaccharides is achieved with the enzyme Peptide-N4-(N- acetyl-p-D-glucosaminyl) Asparagine Amidise (PNGase). First, a 1/5°' volume of denaturation solution (2 % SDS (Sigma)/1 M (3-mercaptoethanol (Sigma)) is added to the sample. The. sample is heated to 100 °C for 5 minutes. A 1/10th volume of 15 % Triton- X100 (Sigma) is added to the sample. The sample is mixed gently and allowed to cool to room temperature, 25 Units of PNGase (Sigma) is added and incubated overnight at 37°C. 1. Release of O-linked oligosaccharides is achieved by the process of ß-elimination. First, a 1/2 volume of 4M sodium borohydride (freshly made) (Sigma) solution is added to the sample. A 1/2 volume of 0.4 M NaOH (BDH, HPLC grade) is added to the sample. The sample is incubated at 50° C for 16 hours. The sample is cooled on ice and a 1/2 volume of 0.4 M acetic acid (Sigma) is added to the sample. Both the N-linked and O-linked samples are further processed to remove buffer components using a Carbo Pac graphitised carbon SPE column. The column equilibration and elution conditions are is follows: Firstly, the column is pre-equilibrated with 1 column volume of 80 % acetonitrile (Sigma) followed by two column volumes of H2O. The sample is loaded under gravity flow and the column washed with two column volumes of H2O, To elute neutral oligosaccharides 2 ml of 50 % acetonitrile is applied to the column. To elute acidic oligosaccharides 2 ml of 50 % acetonitrile/0,1% formic acid is applied to the column. Any remaining oligosaccharides are eluted by the addition of 2 ml of 80 % acetonitrile/0.1 % formic acid. Individual fractions from the SPE columns containing the neutral or acidic N-linked oligosaccharides and the neutral or acidic O-linked oligosaccharides are dried down to completion using a Speed Vac. The samples are redissolved in 200 µl water and analysed by high pH anion exchange chromatography using a Dionex LC 20 system with a GP50 pump and an ED50 pulsed amperometric detector. Analysis of neutral and acidic oligosaccharides is performed using a CarboPac PA100 column and chromatographic parameters (i.e. suitable eluents and gradient flows) known in the art. (vi) Analysis of Suliate and Phosphate Composition Siilfate/phosphate analysis is performed essentially by the method described by Harrison and Packer (Harrison and Packer Methods Mol Biol 125:211-216, 2000). A 100 µl sample of the TNF-a preparation is taken for sulfate/phosphate analysis and hydroJysed in 4 M HCJ at 100 °C for four hours. The HC1 is removed by drying the samples in a Speed Vac system. Samples are then redissalved into 200 u,l H^O. 24 |j.l of sample is injected onto a Dionex LC 50 system with a GP50 pump and a ED50 conductivity detector. Separation is performed by a Dionex lonPac IS 11 Anion exchange column using using chromatographic parameters (i.e. suitable eluents and gradient flows) known in the art, (vii) Further Separation of Protein Isoforms Further separation of TNF-a isoforms is performed using a pellicular anion exchange column. A suitable volume of sample, for example, 24 µl, is separated through a ProPac SAX-10 column (Dionex Ltd) using a Dionex SUMMIT system with UV-Vis detector (Dionex Ltd). Separation is performed using suitable eluents and gradients known in the art. TNF-a isoforms are found to elute in a pattern of distinct peaks. (b) Analysis of Araino Acid, Monosaccbaride, Oligosaccharide, Phosphate, Sulfate and isoform composition of LT-a of the Present Invention (i) Preparation of Samples for Amino Acid, Monosaccharide, Oligosaccharide, Phosphate, Sulfate and Isoforni Analysis A solution of purified LT-a in PBS is treated as described above in Example 4(a)(i). (ii) Analysis of Amino Acid Composition by the Gas Phase Hydrolysis Method Samples of the LT-a preparation are treated as described above in Example 4(a)(ii). (iii) Analysis of Neutral and Amino Monosaccharide composition Samples of the LT-a preparation are treated as described above in Example 4(a)(iii). (iv) Analysis of Acidic Monosaccharide Composition A sample of the LT-a preparation is treated as described above in Example 4(a)(iv). (v) Analysis of Oligosaccharide Composition Samples of the LT-a preparation are treated as described above in Example 4(a)(v). (vi) Analysis of Sulfate and Phosphate Composition A sample of the LT-a preparation is treated as described above in Example 4(a)(vi). (vii) Further Separation of Protein Isoforrns A sample of the LT-a preparation is treated as described above in Example 4(a)(vii). LT-a isoforms are found to elute in a pattern of distinct peaks. (c ) Analysis of Amino Acid, Monosaccharide, Oligosaccharide, Phosphate, Sulphate and Isoform Composition of TNFRI-Fc of the Present Invention (i) Preparation of Samples for Amino Acid, Monosaccharide, Oligosaccharide, Phosphate, Sulfate and Isoform Analysis A solution of purified TNFRI-Fc in PBS was treated as described above in Example (ii) Analysis oi Amino Acid Composition by the Gas Phape Hydrolysis Method Samples of the TNFRl-Fc preparation were treated as described above in Example 4(a)(ii). (iii) Analysis of Neutral and Atnino Monosaccharide composition Samples of the TNFRI-Fc preparation were treated as described above in Example 4{a)(iii). (iv) Analysis of Acidic Monosaccharide Composition A sample of the TNFRI-Fc preparation was treated as described above in Example 4(a)(iv). (v) Analysis of Oligosaccharide Composition Samples of the TNFRI-Fc preparation are treated as described above in Example 4(a)(v). (vi) Analysis of Sulfate and Phosphate Composition. A sample of the TNFRI-Fc preparation was treated as described above in Example (vii) Further Separation of Protein Isoforms A sample of the TNFRI-Fc preparation is treated as described above in Example 4(a)(vii). TNFRI-Fc isoforms are found to elute in B pattern of distinct peaks. (viii) Results Amino acid composition The TNFRI-Fc was hydrolysed. derivatised and analysed by reversed phase high performance liquid chromatography as described to give the following amino acid composition (Table 19). Results are expressed as the number of occurrences of that amino acid in the sequence given as a percentage. TABLE 19 (Table Removed) Monosaccharides and Sulfate The individual monosaccharides and sulfate was hydrolysed froro the amino acid backbone of TNFRl-Fc and analysed by High pH anion exchange chromatography (HP ABC) as described to give the following compositional analysis. Results from the samples are normalised to GalNAc and three times mannose respectively (Table 20-22), Table 23 is a summary of results from the three samples. TABLE 20 (Table Removed) TABLE 21 (Table Removed) Monosaccharide Composition Run 2 (Table Removed) TABLE 22 Monosaccharide Composition Run 3 (Table Removed) TABLE 23 (Table Removed) Taking into consideration the inherent variability of the above-described chromatographic procedures, the monosaccharide, sialic acid and sulfate contents of the TNFRI-Fc of the present invention, when normalized to GalNAc, is determined to be about 1 to 1-4.5 fucose, 1 to 10-18 GlcNAc, 1 to 3-9 galactose, 1 to 4-11 mannose,] to 0.1-2 NeuNAc and 1 tc 1.5-34 sulfate: and when normalized to 3 times of mannose, is determined to be about 3 to 0.1-1,5 fucose, 3 to 0.1-1 GalNAc, 3 to 3-11 GlcNAc, 3 to 1-2.5 galactose, 3 to 0-2 NeuNAc and 3 to 0.5-4 sulfate. The amino acid composition data were combined with the monosaccharide and sulfate data to give the content .of the various species (Table 24). Taking into consideration the inherent variability of the above-described chromatographic procedures, the percentage acidic monosaccharide content of the TNFRI-Fc of the present invention is determined to range from about 0-10%, the sulfation as a percentage of the monosaccharide content of the TNFRI-Fc of the present invention is determined to range from about 10-16 %, the acidic percentage of N-linked oligosaccharide of the TNFRI-Fc of the present invention is determined to range from about 3-6% and the acidic percentage of O-linked oligosaccharide of the TNFRI-Fc of the present invention is determined to range from about 43-66%. TABLE 24 (Table Removed) (d ) Analysis of Amino Acid, Monosaccharide, Oligosaccbaride, Phosphate, Sulphate and Isoform Composition of TNFRH-Fc of the Present Invention. (i) Preparation of Samples for Amino Acid, Monpsaccharide, Oligosaccharide, Phosphate, Sulfate and Isoform Analysis A solution of purified TNFRII-Fc in PBS was treated as described above in Example (ii) Analysis of Amino Acid Composition by the Gas Phase Hydrolysis Method Samples of the TNFRII-Fc preparation were treated as described above in Example (iii) Analysis of Neutral and Amino Monosaccharide composition Samples of the TNFRII-Fc preparation were treated as described above in Example (iv) Analysis of Acidic Mooosaccharide Composition A sample of the TNFRII-Fc preparation was treated as described above in Example 4(a)(iv). (v) Analysis of Oligosaccbaride Composition Samples of the TNFRII-Fc preparation are treated as described above in Example 4(a)(v). (vi) Analysis of Sulfate and Phosphate Composition A sample of the TNTFRU-Fc preparation was treated as described above in Example 4(a)(vi). (vii) Further Separation of Protein Isoforms A sample of the TNFRD-Fc preparation is treated as described above in Example 4(a)(vii). TNFRII-Fc isoforms are found to elute in a pattern of distinct peaks. (viii) Results Amioo acid composition The TNFRII-Fc preparation was hydrolysed, derivatised and analysed by reversed phase high performance liquid chromatography as described to give the amino acid composition (Table 25). Results are expressed as amount by weight and the percentage occurrence of each amino acid in the sequence (including SD), TABLE 25 (Table Removed) Monosaccbarides and Sulfate The individual monosaccharidesand sulfate was hydrolysed from the amino acid backbone of TNFRII-Fc and analysed by High pH anion exchange chromatography (HP AEC) as described to give the following compositional analysis. Results are normalised to GalNAc and three times of mannose, respectively (Table 26-28). Table 29 is a summary of results from the three samples. TABLE 26 Monosaccharide Composition Run 1 (Table Removed) TABLE 27 IMcfnosatcbariae Composition Run 2 (Table Removed) TABLE 28 (Table Removed) TABLE 29 (Table Removed) Taking into consideration the inherent variability of the above-described chiomatographic procedures, the monosaccharide, sialic acid and sulfate contents of the TNFRII-Fc of the present invention, when normalized to GalNAc, is determined to be about 1 to 0.01-2 fucose, 1 to 0.1-3 GlcNAc, 1 to 0.1-2 galactose, 1 to 0.1-2 mannose,! to 0.01-2 NeuNAc and ! to 1-4 sulfate; and when normalized to 3 times of mannose, is determined to be about 3 to 0.1-2 fucose. 3 to 3-11 GalNAc, 3 tc 5-21 GlcNAc, 3 to 3-6 galactose, 3 to 0.1-2 NeuNAc and 3 to 9-19 sulfate. The ammo acid composition data were combined with the monosaccharide and phosphate and sulfate data to give the content of the various species .as a percent by weight (Table 30), Taking into consideration the inherent variability of the above-described chromatographic procedures, the percentage acidic mOnosaccharide content of the TNFRII-Fc of the present invention is determined to range from about 1-10%, the sulfation as a percentage of the monosaccharide content of the TNFRII-Fc of the present invention is determined to range from about 27-41%, the acidic percentage of N-linked oligosaccharide of the TNFRII-Fc of the present invention is determined to range from about 16-26% and the acidic percentage of 0-linked oligosaccharide of the TNFRII-Fc of the present invention is determined to range from about 51-78%. TABLE 30 (Table Removed) (e) Analysis of Amino Acid, Monosaecharide, Oligosaccharide, Phosphate, Sulphate and isoform composition of OX40-Fc of the Present Invention (a) Preparation of Samples for Amino Acid, Monosacchsride, Oligosaccharide, Phosphate, Sulfate and Isoform Analysis A solution of purified OX40-Fc in PBS was treated as described above in Example 4(a)(i). (ii)Analysis of Amino Acid Composition by the Gas Phase Hydrolysis Method Samples of the OX40-Fc preparation were treated as described above in Example 4(a)(ii). (iii) Analysis of Neutral and Amino Monosaccharide composition Samples of the OX40~Fc preparation were treated as described above in Example 4(a)(iii). (iv) Analysis of Acidic Monosaccharide Composition A sample of the OX40-Fc preparation was treated as described above in Example 4(a)(iv). (v) Analysis of Oligosaccharide Composition Samples of the OX40-Fc preparation are treated as described above in Example 4(a)(v). (vi) Analysis of Sulfate and Phosphate Composition A sample of the OX40-Fc preparation was treated as described above in Example 4(a)(vi). (vii) Further Separation of Protein Isoforms A sample of the OX40-Fc preparation is treated as described above in Example 4(a)(vii). OX40-Fc isoforms are found to elute in a pattern of distinct peaks. (viii) Results Amino acid composition The OX40-Fc was hydrolysed, derivatised and analysed by reversed phase high performance liquid chromatography as described to give the following amino acid composition (Table 31). Results are expressed as the number of occurrences of that amino acid in the sequence given as a percentage. Glycine is a known contaminant in amino acid analysis that can artificially alter the amino acid composition. With this taken into account, the results are comparable to the theoretical values. TABLE 31 (Table Removed) Monosacchandes and Sulfate The individual monosacchandes, phosphate and sulfatewas hydrolysed from the amino acid backbone of OX40-Fc and analysed by High pH anion exchange cnromatography (HP AEC) as described to give the following compositional analysis. Results from the samples are normalised to GalNAc and three times mannose respectively (Table 32-34). Table 35 is a summary of results from the three samples. Glucose is a common contaminant and is not normally a component of N- or 0-linked oligosacchrides. TABLE 32 (Table Removed) TABLE 33 (Table Removed) TABLE 34 Monosaccharide "Composition Run 3 (Table Removed)427 TABLE 35 (Table Removed) Taking into consideration the inherent variability of the above-described chromatographic procedures, the monosaccharide, sialic acid and sulfate contents of the OX40-Fc of the present invention, when normalized to GalNAc, is determined to be about 1 to 0.1-1 fucose, 1 to 2-3 GlcNAc, 1 to 0.5-2 galactose, 1 to 0.5-1 mannose, 1 to 0-2 NeuNAc and 1 to 0.30-2 sulfate; and when normalized to 3 times of mannose, is determined to be about 3 to 0.5-2 fucose, 3 to 3-5 GalNAc, 3 to 6-10 GlcNAc, 3 to 4-5 galactose, 3 to 0-2 NeuNAc and 3 to 1-5 sulfate. For each OX40-Fc the amino acid composition data were combined with the monosaccharide and sulfate data to give the content of the various species (Table 36). Taking into consideration the inherent variability of the above-described chromatographic procedures, the sialic acidic as a percentage of the monosaccharide content of the OX40-Fc of the present invention is determined to range from about 0-10%, the sulfation as a percentage of the monosaccharide content of the OX40-Fc of the present invention is determined to range from about 9-15%, the acidic percentage of N-linked oligosaccharide of the OX40-Fc of the present invention is determined to range from about 5-21% and the acidic percentage of O-linked oligosaccharide of the OX40-Fc of the present invention is determined to range from about 20-55%. TABLE 36 (Table Removed) (f) Analysis of Amino Acid, Monosaccharide, Oligosaccharide, Phosphate, Sulphate and isoform composition of BAFF of the Present Invention (i) Preparation of Samples for Amino Acid, Monosaccharide, Oligosaccharide, Phosphate, Sulfate and Isoform Analysis A solution of purified BAFF in PBS is treated as described above in Example 4(a)(i). (ii)Analysis of Amino Acid Composition by the Gas Phase Hydrolysis Method Samples of the BAFF preparation are treated as described above in Example 4(a)(ii). (iii) Analysis of Neutral and Amiao Monosaccharide composition Samples of the BAFF preparation are treated as described above in Example 4(a)(iii). (iv) Analysis of Acidic Monosaccharide Composition A sample of the BAFF preparation is treated as described above in Example 4(a)(iv). (v) Analysis of Oligosaecharide Composition Samples of the BAFF preparation are treated as described above in Example 4(a)(v). (vi) Analysis of Sulfate and Phosphate Composition A sample of the BAFF preparation is treated as described above in Example 4(a)(vi). (vii) Further Separation of Protein Isoforms A sample of the BAFF preparation is treated as described above in Example 4(a)(vii). BAFF isoforms are found to elute in a pattern of distinct peaks. (g) Analysis of Amino Acid, Monosaccharide, Oligosaccharide, Phosphate, Sulphate and isoform composition of NGFR-Fc of the Present Invention (i) Preparation of Samples for Amino Acid, Mooosaccharide, Oligosaccharide, Phosphate, Sulfate and Isoform Analysis A solution of purified NGFR-Fc in PBS is treated as described above in Example 4(a)(i). (ii) Analysis of Atnico Acid Composition by the Gas Phase Hydrolysis Method Samples of the NGFR-Fc preparation are treated as described above in Example 4(a)(ii). (iii) Analysis of Neutral and Amino Monosaccharide composition Samples of the NGFR-Fc preparation are treated as described above in Example 4(a)(iii). (iv) Analysis of Acidic Mooosaccharide Composition A sample of the NGFR-Fc preparation is treated as described above in Example 4(a)(iv). (v) Analysis of Oligosaccharide Composition Samples of the NGFR-Fc preparation are treated as described above in Example 4(a)(v). (vi) Analysis of Sulfate and Phosphate Composition A sample of the NGFR-Fc preparation is treated as described above in Example 4(a)(vi). (vii) Further Separation of Protein Isoforms A sample of the NGFR-Fc preparation is treated as described above in Example 4(a)(vii). NGFR-Fc isoforms are found to elute in a pattern of distinct peaks. (f) Analysis of Amino Acid, Monosaccharide, Oligosaccharide, Phosphate, Sulphate and Isoform Composition of BAFF of the Present Invention (i) Preparation of Samples for Amino Acid, Mooosaccharide, Oligosaccharide, Phosphate, Sulfate and Isoform Analysis. A solution of purified BAFF in PBS is treated as described above in Example 4(a)(i). (ii)Analysis of Amino Acid Composition by the Gas Phase Hydrolysis Method Samples of the BAFF preparation are treated as described above in Example 4(a)(ii). (iii) Analysis of Neutral and Amino Monosaccharide Composition Samples of the BAFF preparation are treated as described above in Example 4(a)(iii). (iv) Analysis of Acidic Mooosaccbaride Composition A sample of the BAFF preparation is treated as described above in Example 4(a)(iv). (v) Analysis of Oligosaccharide Composition Samples of the BAFF preparation are treated as described above in Example 4(a)(v). (vi) Analysis of Suliate and Phosphate Composition A sample of the BAFF preparation is treated as described above in Example 4(a)(vi), (vii) Further Separation of Protein Isofonns A sample of the BAFF preparation is treated as described above in Example 4(a)(vii). BAFF isoforms are found to elute in a pattern of distinct peaks. (b) Analysis of Amino Acid, Monosaccbaride, Oligosaccharide, Phosphate, Sulphate and isoform composition of Fas Ligand of the Present Invention (j) Preparation of Samples for Amino Acid, Monosaccharide, Oligosaccharide, Phosphate, Sulfate and Isoform Analysis A solution of purified Fas Ligand in PBS is treated as described above in Example 4(a)(i). (ii)Analysis of Amino Acid Composition by the Gas Phase Hydrolysis Method Samples of the Fas Ligand preparation are treated as described above in Example 4(a)(ii). (Hi) Analysis of Neutral and Amioo Monosaccharide composition Samples of the Fas Ligand preparation are treated as described above in Example 4(a)(iii). (iv) Analysis of Acidic Monosaccharide Composition A sample of the Fas Ligand preparation is treated as described above in Example 4(a)(iv). (v) Analysis of Oligosaccharide Composition. Samples of the Fas Ligand preparation are treated as described above in Example 4(a)(v). (vi) Analysis of Sulfate and Phosphate Composition A sample of the Fas Ligand preparation is treated as described above in Example 4(a)(vi). (vii) Further Separation of Protein Isoforms A sample of the Fas Ligand preparation is treated as described above in Example 4(a)(vii). Fas Ligand isofonns are found to elute in a pattern of distinct peaks. EXAMPLE 5 Glyco Mass Fingerprinting (a) Comparison of Glyco Mass Fingerprints between a Protein of the Present Invention and a corresponding human protein expressed using non-human cells The protein of the present invention is separated using 2D gel electrophoretic techniques as in Example 3 and blotted onto polyvinyl difluorethane (PVDF) membrane. The spots are stained using one of a standard array of protein stains (Colloidal Coomassie Blue, Sypro Ruby or Deep Purple), and the isoform relative amounts quantified using densitometry algorithms. The individual spots are excised and treated with an array of deglycosylating enzymes and/or chemical means, as appropriate, to remove the oligosaccharides present according to methods described in this document. Once the oligosaccharides are removed, they are separated and analysed on a liquid chromatograpby-electrospray mass spectrometry system (LC-MS) using a graphitised carbon column and organic solvent (MeCN) gradient elution system. The generated peak profile that is generated is a "fingerprint" of the oligosaccharides present on the isoform. Furthermore, the mass spectrometn system simultaneously generates information on the mass of each of the sugars present in the sample which is used to identify their structure through pattern matching with the GlycoSuite database, In addition, individual mass peaks can be fragmented multiple times to give MS" spectra. These fragments allow structural prediction using methods known in the art, for example, by the use of the GiycosidlQ software package. The above separation, deglycosyiation and analysis procedures are repeated using a corresponding protein expressed in a non*hurnan cell system, e.g. E. coli, yeast or CHO cells and the respective glyco mass fingerprints are found to be significantly different. At a structural level, such a result indicates different patterns of glycan structures present on the protein of the present invention and the corresponding non-human cell expressed protein. (b) Comparison of Glyco Mass Fingerprints between TTSGFRII-Fc of the Present InveatioD and a human TNFRII-Fc expressed using CHO cells The TNFRII-Fc of the present invention was separated using 2D gel electrophoretic techniques as in Example 3 and blotted onto polyvinyl difluorethane (PVDF) membrane. The spots were stained using one of a standard array of protein stains (Colloidal Coomassie Blue, Sypro Ruby or Deep Purple), and the isoform relative amounts quantified using densitometry algorithms. Individual spots were excised and treated with an array of deglycosylating enzymes and/or chemical means, as appropriate, to remove the oligosaccharides present according to methods described above in Example 4(a)(v). Once the oligosaccharides were removed, they were separated and analysed on a liquid chromatography-electrospray mass spectrometry system (LC-MS) using a graphitized carbon column and organic solvent (MeCN) gradient elution system. The generated peak profile represents a "fingerprint" of the N-linked and 0-linked oligosaccharides present on TNFRIl-Fc of the present invention (Figures 2(a) and 2(e), respectively). In addition, individual mass peaks were fragmented multiple times to give MSn spectra (Figures 2(b) and 2(f)). These fragments allowed a structural prediction using the GlycosidlQ software (Tables 37(a) and 37(b)). TABLE 37(a) (Table Removed) Predicted structures of the N-glycans present in the TNFRII-Fc of the present invention using GlycosidlQ (Table Removed) TABLE 37(b) Predicted structures of the O-glycans present in the TNFRII-Fc of the present invention using GlycosidlQ (Table Removed) The above separation, deglycosylation and analysis procedures were repeated using a human TNFRII-Fc expressed in Chinese hamster ovary (or CHO) cells (Figures 2(c), 2(d), 2(g) and 2(h); Tables 38(a) and 38(b)) and then compared with the corresponding results described above for TNFRII-Fc of the present invention. The respective glyco mass fingerprints were found to be significantly different. At a structural level, such a result indicates different patterns of glycan structures present on the TNFRII-Fc of the present invention and a human TNFRIl-Fc expressed in CHO cells. TABLE 38(a) Predicted structures of the N-glycans present in TNFRII-Fc expressed in Chinese Hamster Ovary cells (Enbrel) using GlycosidlQ (Table Removed) TABLE 38(b) Predicted structures of the 0-glycans present in TNFRII-Fc expressed in Chinese Hamster Ovary cells (Enbrel) using GlycosidlQ (Table Removed) EXAMPLE 6 Fluorophore Assisted Carbohydrate Electrophoresis Oligosaccharide profiles of the target molecule are derived using the fluorophore assisted carbohydrate electrophoresis protocols (FACE protocols). The oligosaccharides from the target cytokine are hydrolysed from the amino acid backbone using ammonium hydroxide and subsequently labelled using the fluorophore 8-aminonaphthalene-l,3,6-trisulfonic acid (ANTS). Polyacrylamide gel electrophoresis is used to separate the species and standards used to identify1 an oligosaccharide profile that is typical of the target molecule. Further, the oligosaccharides are identified using matrix assisted laser desorption and ionisation -time of flight mass spectrometry (MALDI-TOF) relying On the fluorophore and a specific matrix to ionise each sugar. The mass of each sugar is determined and potential structures identified using the GlycoSuite database. The potential sugar structures are further characterised by tandem mass spectrometric techniques, which allows partial or complete characterisation of the oligosaccharides present and their relative amounts. Further, the process is repeated using the isoforms identified by 2D gel electrophoresis to generate a profile of the oligosaccharides present on each of the isoforms isolated. EXAMPLE 7 QCM and SPR The binding characteristics and activity of the target molecule is determined using either quartz crystal microbalance (QCM) or surface plasmon resonance (SPR). In both cases a suitable receptor for the molecule is bound to a wafer using the chemistry described by the manufacturer. The target molecule is dissolved into a suitable biological buffer and allowed to interact with the receptor on the chip by passing the buffer over it. Changes in the total protein mass on the surface of the wafer are measured either by change of oscillation frequency (in the case of QCM) or changes in the light scattering qualities of the chip (in the case of SPR). The chip is then treated with the biological buffer alone to observe the release of the target molecule back into solution. The rate at which the receptors reach saturation and complete disassociation is then used to calculate the binding curve of the targe: molecule. EXAMPLE 8 Generation of a Transgenic Host Cell Line (a) Transgenic Host Cell Line with alpha"2,6-sialyltrausferase The cDNA coding for alpha-2,6-sialyltransferase (alpha 2.6ST) is amplified by PCR from poly(A)-primed cDNA. The PCR product is ligated into a suitable vector, for instance pIRESpuro4 or pCEP4, to generate an alpha 2,6ST plasmid. The cloned cDNA is sequenced and its identity verified by comparison with the published alpha-2,6ST cDNA sequence, DNA sequencing is performed using known methods. Mammalian host ceils, including cell clones of the same lineage that express high levels of target molecule (cell line-target molecule) are transfected with the alpha 2,6ST plasmid, which also carries an antibiotic resistance marker. Selection of stably transfected cells is performed by incubaton of the cells in the presence of the antibiotic; colonies of antibiotic-resistant cells that appear subsequent to transfection are pooled and examined for intracellular alpha 2.6ST activity. To isolate individual cell clones expressing alpha 2,6ST, cell pools are cloned by a limiting dilution process as described by Kronman (Gene 727:295-304, 1992). Individual cell clones are chosen at random, cells expanded and clones tested for alpha 2,6ST activity. Cell pellets are washed, resuspended in lysis buffer and left on ice prior to sonication. The cell lysate is centrifuged and the clear supernatant is assayed for protein concentration (via known methods) and sialyltransferase activity. Sialyltransferase activity is assayed by known methods, for example the method detailed by Datta el al. (J Biol Chem 270:1497-1500, 1995). Expressed target molecule is purified from high-expressing alpha 2,6ST cell line-target molecule cells and subjected to in vitro and/or in vivo half-life bioassays (see Example 10), Target molecule from high-expressing alpha 2,6ST cell displays an increased in vitro and/or vivo half-life in comparison to target molecule derived from the same parent cell line without any subsequent transgene manipulation or target molecule derived from other cell lines. (b) Transgenic Host Cell Line with fucosyltransferase The cDNA coding for a fucosyltransferase (FT) such as FUT1, FUT2, FUT3, FUT4, FUT5, FUT6, FUT7, FUT8, FUT9, FUT10, FUT11 is amplified by PCR from poly(A)-primed cDNA. The PCR product is ligated into a suitable vector, for instance pIRESpuro4 or pCEP4, to generate an alpha 2,6ST plasmid. The cloned cDNA is sequenced and its identity verified by comparison with the published FT cDNA sequence. DNA sequencing is performed using known methods. Human host cells, including cell clones of the same lineage that express high levels of target molecule molecule (cell line-target molecule) are transfected with the FT plasmid, which also carries an antibiotic resistance marker. Selection of stably transfected cells is performed by incubation of the cells in the presence of the antibiotic; colonies of antibiotic-resistant cells that appear subsequent to transfection are pooled and examined for intracellular FT activity. To isolate individual cell clones expressing FT, cell pools are cloned by a limiting dilution process as described by Kronman (Gene 121: 295-304, 1992); Individual cell clones are chosen at random, cells expanded and clones tested for FT activity. Cell pellets are washed, resuspended in lysis buffer and left on ice prior to sonication. The cell lysate is centrifuged and the clear supernatant is assayed for protein concentration (via known methods) and FT activity. FT activity is assayed by known methods, for example the method detailed by Mas et al (Glycobiology 8(6):605-13, 1998). Expressed target molecule is purified from high-expressing FT cell line-target molecule cells. A Lewis x-specific antibody, such as L5 and a sialyl Lewis x-specific antibody such as KM93, HECA493, 2H5 or CSLEX are used to test the presence of Lewis x or sialyl Lewis x structures according to methods known in the art, for example, as detailed in Lucka el al (Glycobiology 15(1):87, 2005). Alternatively, the presence of Lewis x or sialyl Lewis x structures may be detected by treating the sample with appropriate glycosidases and detecting the effect of the glycosidases on parameters such as mass using MS or retention time using HPLC. Glyco mass fingerprinting, as described in Example 5, may also be employed to predict the presence of Lewis x or sialyl Lewis x structures. EXAMPLE 9 Differential Gene Expression Differences in gene expression can be analyzed using a target cell line of the target molecule. The target cells are grown to the appropriate density and treated with a range of concentration of target molecule or buffer control for a number of hours,, for instance, 72 hours. At various time points RNA is harvested, purified, and reverse transcribed according to Affymetrix protocols. Labelled cRNA (e.g. biotin labelled) is then prepared and hybridised to expression arrays e.g. U133 GeneChips. Following washing and signal amplification, the GeneChips are scanned using a GeneChip scanner (Affymetrix) and the hybridisation intensities and fold change information at various time points is obtained using GeneChip software (Affymetrix). The target molecule induces unique gene expression and results in different mRNA profiles upon comparison with profiles induced by cytokines or receptors produced from different sources e.g. E. coli, yeast or CHO cells. EXAMPLE 10 Determining the Half-Life of the Target Molecule of the Present Invention The half-life of the target molecule is determined in an in vitro system. Composition containing target molecule is mixed into human serum/plasma and incubated at a particular temperature for a particular time (e.g. 37 degrees for 4 hours, 12 hours etc). The amount of target molecule remaining after this treatment is determined by ELISA methods or dot blot methods known in the art. The biological activity of the remaining target molecule is determined by performing a suitable bioassay chosen by a person skilled in the relevant art. The serum chosen may be from a variety of human blood groups (eg A, B, AB, O etc.). The half-life of target molecule is also determined in an in vivo system. Composition containing target molecule is labelled by a radioactive tracer (or other means) and injected intravenously, subcutaneousiy, retro-orbitally, intramuscularly or intraperitonally into the species of choice for the study, for instance, mouse, rat, pig, primate or human, Blood samples are taken at time points after injection and assayed for the presence of target molecule (either by ELISA methods, dot blot methods or by trichloroacetic acid (TCA)-precipitable label e.g. radioactive counts). A comparison composition consisting of target molecule produced from other sources eg E. coli, yeast, or CHO cells can be run as a control. EXAMPLE 11 (a) In Vivo Studies using the Target Molecule of the Present Invention The individual subjects of the in vivo studies described herein are warm-blooded vertebrate animals, which includes humans. The clinical trial is subjected to rigorous controls to ensure that individuals are not unnecessarily put at risk and that they are fully informed about their role in the study. Preferably to account for the psychological effects of receiving treatments, the trial is conducted in a double-blinded fashion. Volunteers are randomly assigned to placebo or target molecule treatment groups. Furthermore, the relevant clinicans are blinded as to the treatment regime administered to a given subject to prevent from being biased in their post-treatment observations. Using this randomization approach, each volunteer has the same chance of being given either the new treatment or the placebo. Volunteers receive either the target molecule or placebo for an appropriate period with biological parameters associated with the indicated disease state or condition being measured at the beginning (baseline measurements before any treatment), end (after the final treatment), and at regular intervals during the study period. Such measurements include the levels of target molecule in body fluids, tissues or organs compared to pre-treatment levels. Other measurements include, but are not limited to, indices of the disease state or condition being treated, body weight, blood pressure, serum tilers of pharmacologic indicators of disease such as specific disease indicators or toxicity as well as ADME (absorption, distribution, metabolism and excretion) measurements. Information recorded for each patient includes age (years), gender, height (cm), family history of disease state or condition (yes/no), motivation rating (some/moderate/great) and number and type of previous treatment regimens for the indicated disease or condition. Volunteers taking part in this study are adults aged 18 to 65 years and roughly an equal number of males and females participate in the study. Volunteers with certain characteristics are equally distributed for placebo and target molecule treatment. In general, the volunteers treated with placebo have little or no response to treatment, whereas the volunteers treated with the target molecule show positive trends in their disease state or condition index at the conclusion of the study. (b) Treatment of Human Psoriatic Skin Using a Topical Preparation of TNFRI-Fc The individual subjects of the in vivo studies described herein are warm-blooded vertebrate animals, which includes humans. The clinical trial is subjected to rigorous controls to ensure that individuals are not unnecessarily put at risk and that they are fully informed about their role in the study. To account for the psychological effects of receiving treatments, volunteers are randomly assigned to topical placebo or topical TNFRI-Fc treatment groups. Furthermore, to prevent the doctors from being biased in treatments, they are not informed as to whether the medication they are administering is topical TNFRI-Fc or topical placebo. Using this randomization approach, each volunteer has the same chance of being given either the new treatment or the placebo. Volunteers receive either the topical TNFRJ-Fc (without thalidomide the formulation of which is described in Example I9(c)) or topical placebo for an appropriate period, for example, a single 0.8ml application on one psoriatic lesion (total skin area of 20 cm*) with a 7 day follow-up or, alternatively, multiple 0.8ml applications on the same target lesion 9 times (every second day) over a 21 day period. Biological parameters associated with the indicated disease state or condition, for example, psoriasis, will be measured at the beginning (baseline measurements before any treatment), end (after the final treatment), and at regular intervals during the study period. Such measurements include the levels of TNF alpha in body fluids, tissues or organs compared to pre-treatment levels. Other measurements include, but are not limited to, indices of the disease state or condition being treated, body weight, blood pressure, serum liters of pharmacologic indicators of disease or toxicity as well as ADME (absorption, distribution, metabolism and excretion) measurements. In particular, the topical TNFRJ-Fc of the present invention is given to voluntary psoriasis patients, who have been assigned to the TNFRI-Fc treatment group. Information recorded for each patient includes age (years), gender, height (cm), family history7 of disease state or condition (yes/no), motivation rating (some/moderate/great) and number and type of previous treatment regimens for the indicated disease or condition. Volunteers taking part in this study are adults aged 18 to 65 years and roughly an equal number of males and females participate in the study. Volunteers with certain characteristics are equally distributed for topical placebo and topical TNFRI-Fc treatment. Evaluation of treatment is graded by four categories, namely, cured, obviously effective, effective and non-effective. "Cured" is where the inflammatory area on the plaque is diminished completely and the pruritus disappeared. "Obviously effective" is where the inflammatory area on the plaque is diminished by more than 60% and the pruritus is slighted and softened. "Effective" is where the inflammatory area on the plaque is diminished by 20 to 60% and the pruritus is slighted and softened. "Non-effective" is where the inflammatory area on the plaque is diminished by less than 20 % or there is exacerbation of psoriasis. Alternatively, treatment evaluation is graded by the Local Plaque Severity Index (LPSI), whereby each target plaque is assessed and rated for erthema, induration and dessquamation using a five-point scale by the supervising clinician at the time of the specified clinic visits, An example of an appropriate clinical visit timetable for the "multiple application" treatment regime is on days 0, 11 and 21. The five-point scale is defined as follows: 0 = no symptoms; 1 = slight; 2 = moderate; 3 = marked; 4 = very marked. Scores for erthema, induration and desquamation are totalled. LPSI ranges from 0 to 12 with the higest score representing the more severe disease state. In general, the volunteers treated with topical placebo have little or no response to treatment, whereas the volvsnteers treated with the topical TNFRI-Fc cream of the present invention show positive trends in their disease state or condition index at the conclusion of the study. In particular, the topical preparation of the present invention is obviously effective on most patients in the TNFRI-Fc treatment group. No visible side-effects are observed. (c) Treatment of Human Rheumatoid Arthritis Using TNFRI-Fc The individual subjects of the 177 vivo studies described'herein are warm-blooded vertebrate animals, which includes humans. The clinical trial is subjected to rigorous controls to ensure that individuals are not unnecessarily put at risk and that they are fully informed about their role in the study. During the clinic visits, investigators will obtain multiple blood samples; and be given comprehensive physical examination, including the assessment of swollen, tender, and painful joints. To account for the psychological effects of receiving treatments, volunteers are randomly assigned to placebo or TMFRI-Fc treatment groups. Furthermore, to prevent the doctors from being biased in treatments, they are not informed as to whether the medication they are administering is TNFRI-Fc or a placebo. Using this randomization approach, each volunteer has the same chance of being given either the new treatment or the placebo. Volunteers receive either the TNFRI-Fc or placebo for an appropriate period with biological parameters associated with the indicated disease state or condition, such as the extent of joint swelling, being measured at the beginning (baseline measurements before any treatment), end (after the final treatment), and at regular intervals during the study period. Measurements include the levels of inflammatory parameters such as TNF alpha in body fluids, tissues or organs compared to pre-treatment levels. Other measurements include, but are not limited to, indices of the disease state or condition being treated, body weight, blood pressure, serum titers of pharmacologic indicators of disease or toxicity as well as ADME (absorption, distribution, metabolism and excretion) measurements. In particular, the TNFRI-Fc of the present invention is given to voluntary rheumatoid arthritis patients, who have been assigned to the TNFRI-Fc treatment group, in the form of a twice weekly subcutaneous injection of TNFRI-Fc for eight weeks. Information recorded for each patient includes age (years); gender, height (cm), family history of disease state or condition (yes/no), motivation rating (some/moderate/great) and number and type of previous treatment regimens for the indicated disease or condition, Volunteers taking part in this study are adults aged 18 to 65 years and roughly an equal number of males and females participate in the study, Volunteers with certain characteristics are equally distributed for placebo and TNFRI-Fc treatment. Evaluation of treatment is graded by four categories, namely, cured, obviously effective, effective and non-effective. "Cured'1 is where the joint or joints show no sign of swelling or associated pain/tenderness. "Obviously effective" is where the joint or joints show a substantial diminution of swelling (more than 60%) accompanied by a marked reduction of joint pain and tenderness, "Effective51 is where the joint or joints show a diminution of swelling of between 20 to 60% accompanied by a mild diminution of associated joint pain and tenderness, "Non-effective" is where the swelling of the joint or joints is diminished by less than 20 % and there is no perceived improvement to associated joint pain. In general, the volunteers treated with placebo have little or no response to treatment, whereas the volunteers treated with TNFRI-Fc of the present invention show positive trends in their disease state or condition index at the conclusion of the study. In particular, the preparation of the present invention is obviously effective or effective on most patients in the TNFRI-Fc treatment group. No visible side-effects are observed. (d) Treatment of Human Psoriatic Skin Using Topical TNFRII-Fc Preparation The individual subjects of the in vivo studies described herein are warm-blooded vertebrate animals, which includes humans. The clinical trial is conducted as described above in Example 11(b) except that the non-placebo treatment consists of the administration of a topical preparation of TNFRII-Fc without the addition of thalidomide, the formulation of which is described in Example In general, the volunteers treated with placebo have little or no response to treatment, whereas the volunteers treated with the TNFRII-Fc cream of the present invention show positive trends in thsir disease state or condition index, as described above in Example 11(b), at the conclusion of the study. In particular, the topical preparation of the present invention is obviously effective on most patients in the TNFRII-Fc treatment group. No visible side-effects are observed. (e) Treatment of Human Rheumatoid Arthritis Using TNFRII-Fc The individual subjects of the in vivo studies described herein are warm-blooded vertebrate animals, which includes humans. The clinical trial is conducted as described above in Example 11(c) except that the non-placebo treatment consists of the administration of TNFRII-Fc of the present invention. In general, the volunteers treated with placebo have little or no response to treatment, whereas the volunteers treated with TNFRII-Fc of the present invention show positive trends in their rheumatoid arthritis, as described above in Example 1 l(c), at the conclusion of the study. In particular, the preparation of the present invention is obviously effective or effective on most patients in the TNFRII-Fc treatment group. No visible side-effects are observed. (i) Treatment of Human Pityriasis Rubria Pilaris Using Topical TNFRH-Fc Preparation The topical preparation of TNFRII-Fc of the present invention containing TNFRII-Fc (250 lag/ml) and thalidomide (20 mg/ml) was applied to a voluntary pityriasis rubria pilaris patient. The inflammation area was treated once every second day for two weeks, by applying 2 ml of the topical preparation. The hand of the voluntary patient prior to the first treatment is shown in Figure 3 (a) and the same hand after the two week treatment regimen is shown in Figure 3(b). The topical preparation obviously reduced the patches. No visible side-effects were observed. EXAMPLE 12 (a) Bioactiviry of TNF-a of the present invention TNF-a induces cytotoxicity and cell death in the mouse fibrosarcoma cell line WEHI 164. WEHI 164 cells were pre-treated with actinomycin D (2|o.g/ml) which inhibits transcription. This increases the sensitivity of WEHI 164 to TNF-a. In a 96 well plate, 0-10 ng/ml TNF-a was incubated with 50,000 WEHI 164 cells/ well for 18 hours at 37°C. Cytotoxicity of TNF-a was subsequently measured using the CellTiter 96 Aqueous One Solution Cell Proliferation Assay (Promega). In this assay a tetrazolium compound MTS (3-(4,5-dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium) in the presence of an electron coupling reagent (phenazine methosulfate) is bioreduced by cells into a formazan product. The concentration of the formazan is determined by reading the absorbance of the resultant solution at 490nm by a spectrophotometer (BioRad microplate reader), ED50 of the present invention was calculated from a curve fit of absorbance versus the concentration into a four parameter equation and was found to be 0.012-0.018 ng/ml (Figure 4). (b) Bioactivity of LT-a of the present invention LT-a induces cytotoxicity and cell death in the mouse fibrosaicoma cell line WEHI 164 pre-treated with the transcription inhibitor actinomycin D. WEHI 164 cells were pre-treated with actinomycin D (2µg/ml) then in a 96 well plate, 0-400 ng/ml LT-a was incubated with 50,000 WEHI 164 cells/ well and incubated for 18 hours at 37°C. Cytotoxocity was subsequently measured using the CellTiter 96 Aqueous One Solution Cell Proliferation Assay (Promega). In this assay a tetrazolium compound MTS (3-(4,5-dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium) in the presence of an electron coupling reagent (phenazine methosulfate) is bioreduced by cells into a formazan product, The concentration of the formazan was determined by reading the absorbance of the resultant solution at 490nm by a spectrophotometer (E max precision microplate reader, Molecular Devices). The ED50 of the present invention was calculated from a curve fit of absorbance versus the concentration into a four-parameter equation and was found to be 0.038-0.055 ng/ml (Figure 5), (c) Bioactivity of TNFRI-Fc of the present invention. The activity of TNFRI-Fc is measured by its ability to neutralise TNF-a mediated cytotoxicity in the WEH1-164 cell line, Serial dilutions of TNFRI-Fc ranging from 0.006 to 100 ng/mi were incubated with 5 ng/ml TNF-a for 1 hour at 37°C to allow TNFRI-Fc binding to TNF-a. 5x104 WEHI-164 cells, pre-treated with 2ug/ml Actinomycin D, which increases the sensitivity of the cells to TNF-a by inhibiting transcription, were then added to each well. Plates were then incubated for 20 hours (37°C, 5%CCO2), followed by addition of 10% cell Titre96® AQueous One solution reagent (Promega) which contains the tetrazolium compound MTS [3~(4,5-dimethylthiazol-2-y3)- 5- (3- carboxymethoxypheny3)-2-(4-sulfophenyl)-2H-tetrazoiium, inner salt] and an electron coupling agent (phenazine ethaosulfate ; PES). Absorbance was measured at 490nm, which reflects the number of cells present in the well. ED50 was calculated from a curve fit of absorbance versus the concentration into a four-parameter equation and found to be 14-20 ng/ml (Figure 6). (d) Bioactivity ofTNFRII-Fc of the present invention The activity of TNFRII-Fc is measured by its ability to neutralise TNF-a mediated cytotoxicity in the WEHI-164 cell line. Serial dilutions of TNFRII-Fc ranging from 0.006 to 100 ng/ml were incubated with 5 ng/ml TNF-a for 1 hour at 37°C to allow TNFRII-Fc binding to TNF-a, 5xl04 WEHI-164 cells, pre-treated with 2 µg/ml Actinomycin D, which increases the sensitivity of the cells to TNF-a by inhibiting transcription, were then added to each well. Plates were then incubated for 20 hours (37°C, 5%CO2), followed by addition of 10% cell Titre96® AQueous One solution reagent (Promega) which contains the tetrazolium compound MTS [3-(4,5-dimethylthiazol-2-yl)- 5- (3- carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium, inner salt] and an electron coupling agent (phenazine ethaosulfate ; PES. Absorbance was measured at 490nm, which reflects the number of cells present in the well. ED50 of the present invention was calculated from a curve fit of absorbance versus the concentration into a four parameter equation and found to be 14-20 ng/ml (Figure 7). (e) Comparing tbe bioactivities of TNFRII-Fc of the present invention and TNFRII- Fc expressed using non-human systems Biological activity of TNFRII-Fc expressed in E. coll (PeproTech, Cat #310-12) and TNFRII-Fc of the present invention (1500 M-g/ml) were determined by the inhibitory effect of the TNF-a mediated cytotoxicity in murine L-929 cells. The respective results were compared. Lyophilized TNFRII-Fc (PeproTech) was reconstituted and stored at -80°C. L-929 cells were resuspended in culture media. The suspension was transferred to an assay plate (8,000cells/well; passage # 7) with 100 ml added per well. The plate was incubated overnight at 37°C. In a separate plate, TNFRII-Fc (PeproTech) was serially diluted in assay media. Each dilution was added in duplicate to the assay plate, with 40 ul of each dilution added per well. 60 uJ of assay media containing 4ng/ml TNF-a (PeproTech) was added to each well. The total volume of each well was 100 µl The plate was incubated for one hour. The TNF-a-TNFRII-Fc complex was transferred to the assay plate containing the L-929 cells. 100 µl of the complex was transferred to each well. Hence, the final volume per well was 200 µl, containing Ing/ml TNF-a. The assay plate and its contents were incubated for 17 hours. 20 ul of Promega substrate cell titre 96 aqueous solution was added to each well. The mixture was incubated at 37DC and -absorbance at 490nm was read after 6 hours. The above experiment was repeated using TNFRII-Fc of the present invention. As another control (not shown), the assay was repeated using TNFRII-Fc of the present invention in the absence of TNF-a. L-929 cells were resuspended in culture media. The suspension was transferred to an assay plate (8,000cells/well; passage # 7) with 100 µl added per well. The plate was incubated overnight at 37°G. In a separate plate, TNFRII-Fc of the present invention was serially diluted in assay media, with each well containing 100 µl of the respective dilutions, The dilutions were added to the L-929 cells in the first place. Hence, the final volume per well was 200 ul The plate was incubated for 17 hours. 20 µl of Promega substrate cell titre 96 aqueous solution was added to each well. The mixture was incubated at 37°C and absorbance at 490nm was read after 6 hours. The concentration effective dosages at 50% (Cone. ED50) for TNFRII (PeproTech) and TNFRII-Fc of the present invention are determined by plotting their A(490nm) against the respective log concentrations and fitting the values to a function of the following form, using GnuPiot. a graphical program which facilitates the visualization of mathematical functions and data (http://www.gnuplot.info): f(x) = cauchy (x) where cauchy (x) = a0 + al (a tan((x-a2)/a3)/n where n = 3.1416 The EDso corresponds to the saddle point of the cauchy function, which is identical to fitting-parameter "a2" and a y-value (A(490nm) halfway between the asymptotic minima and maxima of the cauchy function (Figure 8). ED50 for TNFRII-Fc was determined to be 3.2-4.8 ng/ml, The ED50 for TNFRII (PeproTech) was determined to be 39 - 59 ng/ml. TNFRI!-Fc was found to be 8-18 fold more active than TNFRJI (PeproTech), with a lower EDso and hence more biologically active. (d) Comparing the activities of OX40-Fc of the present invention and OX40-Fc expressed using con-human systems 0X40 has been reported to inhibit OX40L-induced IL-2 secretion in mouse T cell line CTLL2. IL-2 is a proliferate and survival factor for CTLL2 cells. The addition of 0X40 hence inhibits the proliferative effect of OX40L. In 96-well plates, 2 ng/ml OX40L is incubated with 0- 100 ng/ml of OX40-Fc of the present invention for 1 hour at 37DC to allow binding to occur. 10000 CTLL2 cells / well are then added for 72 hours at 37°C, Cell numbers are then measured using the CellTiter 96 Aqueous One Solution Cell Proliferation Assay (Promega). In this assay a tetrazolium compound MTS (3-(4,5-dimethylthiazol-2-yl)-5-(3-caTboxymethoxyphenyl)-2-(4-sulfopheriyl)-2H-tetrazolium) in the presence of an electron coupling reagent (phenazine methosulfate) is bioreduced by cells into a formazan product. The concentration of the formazan is determined by reading the absorbance of the resultant solution at 490nm by a spectrophotometer (E max precision microplate reader, Molecular Devices). The above assay is repeated using OX40-Fc expressed in non-human cell systems, e.g. E. coli, yeast or CHO cells. The respective ED50s are calculated after curve fitting the absorbance and the OX40-Fc concentration values using a 4 parameter equation. The EDSOs are found to be significantly different. (e) Comparing the activities of BAFF of the present invention and BAFF expressed using non-human systems BAFF has been reported to induce proliferation in RPMI 2886 cells. In a 96-well plate, 10000 RPMI 2886 cells/ well were treated with 0-250 ng/ml BAFF of the present invention for 114 hours at 37°C. Cell numbers were then measured using the CellTiter 96 Aqueous One Solution Cell Proliferation Assay (Promega). In this assay a tetrazolium compound MTS ((3-(4,5-dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium) in the presence of an electron coupling reagent (phenazine methosulfate) is bioreduced by cells into a formazan product. The concentration of the formazan was determined by reading the absorbance of the resultant solution at 490run by a spectrophotometer (E max precision microplate reader, Molecular Devices). The above assay was repeated a recoinbinant human BAFF molecule (Peprotech) expressed in E. coli, The EDso for the BAFF of the present invention was found to be 50 - 75 ng/ml using, whereas the EDso for Peprotech (E.coli expressed) BAFF was found to be 80 - 120 ng/ml (Figure 9). Thus, the BAFF of the present invention induced a 1.1 - 2,4 fold more potent proliferation of RPMI 8226 cells than a BAFF molecule expressed in E. coli. (e) Bioactivity of NGFR-Fc of the present invention NGF-beta has been reported to induce proliferation in TF-1 cells. NGFR-Fc blocks the activity of NGF-beta by binding to NGF-beta and competitively inhibiting the binding of these molecules to their cellular NGF-beta receptor sites, rendering NGF-beta biologically inactive. Incubating NGF-beta with NGFR-Fc will therefore inhibit NGF-beta stimulated TF-1 cell proliferation. In 96-well plates, 1 ng/ml NGF-beta was incubated with 0-100 ng/ml of NGFR-Fc of the present invention for 2 hours at 37°C to allow binding to occur. 18,000 TF-1 cells / well were then added and incubated for 65 hours at 37°C. Cell numbers were then measured using the CellTiter 96 Aqueous One Solution Cell Proliferation Assay (Promega). In this assay a tetrazolium compound MTS (3-(4,5-dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium) in the presence of an electron coupling reagent (phenazine methosulfate) is bioreduced by cells into a formazan product. The concentration of the formazan is determined by reading the absorbance of the resultant solution at 490mn by a spectrophotometer (E max precision microplate reader, Molecular Devices). The ED50 was calculated after curve fitting the absorbance and the NGFR-Fc concentration values using a 4-parameter equation. The ED50 of the present invention was calculated from a curve fit of absorbance versus the concentration into a four-parameter equation and was found to be 670 - 1000 ng/ml (Figure 10). (f) Comparing the bioactivities of Fas Ligand of the present invention to Fas Ligand expressed using non-human systems Fas Ligand has been reported to induce apoptosis in human T cell leukemia Jurkat cell line in the presence of 10 p.g/ml of a cross-linking antibody. In a 96-well plate, ] 0000 Jurkat cells / well are treated with 0- 1 fig/ml Fas Ligand of the present invention for 65 hours at 37°C. Cell numbers are then measured using the CellTiter 96 Aqueous One Solution Cell Proliferation Assay (Promega). In this assay a tetrazolium compound MTS ((3-(4,5- dimethylthia2o]-2-y])-5-(3-carboxyinethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium) in the presence of ari electron coupling reagent (phenazine methosulfate) is bioreduced by cells into a formazan product. The concentration of the fonnazan is determined by reading the absorbance of the resultant solution at 490nm by a spectrophotometei (E max precision microplate reader, Molecular Devices), ED50 is calculated after curve fitting the absorbance and the Fas Ligand concentration values using a 4-parameter equation. The above assay is repeated using Fas Ligand expressed in non-human cell systems, e.g. E. coli, yeast or CHO cells and the ED50s are found to be significantly different. EXAMPLE 13 (a) In vitro comparison of Immunoreactivity Profiles between TNF-a of the Present Invention and and human TNF-a expressed using non-human systems Protein estimation of TNF-a of the present invention was determined using was determined using the R&D Systems human TNF-a DuoSet® ELISA kit (Cat.#DY210) in accordance with the manufacturer's instructions. TNF-a of the present invention, standardised using the ELISA assay results, was diluted and tested in a R&D Systems human TNF-a DuoSet® ELISA kit in accordance with the manufacturer's instructions. The above-mentioned ELISA kit employs a human TNF-a expressed in E. coli as a standard.An R&D Systems E. coli expressed human TNF-a (Cat.#210-TA) and a WHO E. coli expressed human TNF-a (Cat # 87/650) were also assayed. The R&D Systems DuoSet® TNF-a ELISA kit results produced concentration curves for TNF-a of the present invention, the R&D Systems E. coli expressed human TNF-a and the WHO E. coli expressed human TNF-a at an OD450nm as well as the internal DuoSet TNF-a expressed in E coli standard curve (Figure 11). These results show an underestimation of the THF-a of the present invention concentration by the R&D Systems human TNF-a DuoSet* ELISA kit, a commercial kit employing a E. coli -expressed human TNF-a standard and antibodies against E. coli -expressed human TNF-a, that is used to evaluate levels of native human expressed TNF-a in laboratory samples and human patient samples. This result indicates different immunoreactivity profiles of TNF-a of the present invention and a non-human cell expressed human TNF-a molecule. (b) In vitro comparison of Imnmnoreactivity Profiles between LT-a of the Present Invention and LT-a expressed using a non-human system Protein estimation of LT-a of the present invention was determined by the A280 absorbance method using the calculated extinction coefficient (E) and the measured molecular mass based on SDS-PAGE analysis. LT-a of the present invention, standardised using the protein estimation results described above, was diluted and tested in an R&D Systems human TNF-beta DuoSet® ELISA kit (Cat # DY211) in accordance with the manufacturer's instructions. The above-mentioned ELISA kit uses as a standard a protein calibrated against & human LT-a (TNF-beta) expressed in £. coli cells. The R&D Systems DuoSet® TNF-beta ELISA kit results gave an interpolated concentration estimate of LT-a of the present invention of approximately 360 pg/ml at an OD450nm of 0.22 (Figure 12) when estimated from the E. coli expressed human recombinant LT-a standard curve. Whereas, the actual concentration of LT-a of the present invention was approximately 1000 pg/ml at a similar OD450nm value (Figure 12). These results represent a greater than 2-fold underestimate of the LT-a of the present invention concentration by the R&D Systems human TNF-beta DuoSet® ELISA kit, a commercial kit employing a E. coli -expressed human LT-a standard and antibodies against E. coli -expressed human LT-a, that is used to evaluate levels of native human expressed LT-a in laboratory samples and human patient samples. This result indicates different immunoreactivity profiles of LT-a of the present invention and a non-human cell expressed human LT-a molecule. (c) In vitro comparison of Immunoreactivity Profiles between TNFRI-Fc of the Present Invention and a soluble human TNFRI molecule expressed using a non-human system Protein estimation of TNFRI-Fc of the present invention is determined using a suitable method for the estimation of protein concentration, for example, the Lowry method of protein estimation with human IgG as a standard, TNFRI-Fc of the present invention, standardised using the above-mentioned protein estimation results, is diluted and tested in a R&D Systems soluble human TNF RI DuoSet® ELISA kit (Cat # DY225) in accordance with the manufacturer's instructions. The above-mentioned .ELISA kit uses as a standard a protein calibrated against a soluble human TNF RI expressed in E. Coli cells. The protein concentrations of TNFRI-Fc of the present invention (as a monomer) determined by the commercially available ELISA kit will differ from that determined by a standard protein assay method as the capture and/or detection antibodies employed in the commercially available ELISA kit or irnmunoassay procedure are raised against a non-human cell expressed soluble human TNFRI protein. It should be noted that the TNFRI-Fc of the present invention is expressed as a homodimer. This result indicates different immunoreactivity profiles of TNFRI-Fc of the present invention and a non-human cell expressed soluble human TNFRI molecule. (d) In vitro comparison of Immunoreactivity Profiles between TNFRII-Fc of the Present Invention and a soluble human TNFRII molecule expressed using a non- human system Protein estimation of TNFRII-Fc of the present invention is determined using a suitable method for the estimation of protein concentration, for example, the Lowry method of protein estimation with human IgG as a standard. TNFRJI-Fc of the present invention, standardised using the above-mentioned protein estimation method, is diluted and tested in a R&D Systems soluble human TNF RII DuoSet* ELISA kit (Cat # DY726) in accordance with the manufacturer's instructions. The above-mentioned ELISA kit uses as a standard a protein calibrated against a soluble human TNF RII expressed in E. Coli cells. The protein concentrations of TNFRII-Fc of the present invention (as a monomer) determined by the commercially available ELISA kit will differ from that determined by a standard protein assay method as the capture and/or detection antibodies employed in the commercially available ELISA kit or immunoassay procedure are raised against a non-human cell expressed soluble human TNFRII protein. It should be noted that the TNFRII-Fc of the present invention is expressed as a homodimer. This result indicates different immunoreactivity profiles of TNFRII-Fc of the present invention and a non-human cell expressed soluble human TNFRII molecule. (e) In vitro comparison of Immunoreactivity Profiles between OX40-Fc of the Present Invention and a soluble human OX40 molecule expressed using a non-human system Protein estimation of OX40-Fc of the present invention is determined using a suitable method for the estimation of protein concentration, for example, the Lowry method of protein estimation with human IgG as a standard. OX40-Fc of the present invention, standardised using the above-mentioned protein estimation method, is diluted and tested in an IBL-Hamburg soluble human 0X40 ELISA kit (Cat # BE59401) in accordance with the manufacturer's instructions. The above-mentioned ELISA kit uses as a standard a protein calibrated against a soluble human OX40 expressed in non-human cells. The protein concentrations of OX40-Fc of the present invention (as a monomer) determined by the commercially available ELISA kit will differ from that determined by a standard protein assay method as the capture and/or detection antibodies employed in the commercially available ELISA kit or immunoassay procedure are raised against a non-human cell expressed soluble human 0X40 protein. It should be noted that the OX40-Fc of the present invention is expressed as a homodimer. This result indicates different immunoreactivity profiles of OX40-Fc of the present invention and a non-human cell expressed soluble human 0X40 molecule. (f) In vitro comparison of Immunoreactivity Profiles between BAFF of the Present Invention and human BAFF expressed using non-human systems Protein estimation of BAFF of the present invention is determined using a standard protein assay technique, for example, the Bradford protein assay (Bradford Anal Biochem 72:248-254. 1976) or. alternatively, the A280 absorbance method using the calculated extinction coefficient (E) and the measured molecular mass based on SDS-PAGE analysis. BAFF of the present invention, standardised using the standard protein assay results, is diluted and tested in a commercially available ELISA kit, for example, a R&D Systems human BAFF Quantikine® ELISA kit (Cat # DBLYSO) in accordance with the manufacturer's instructions. The above-mentioned ELISA kit is calibrated against a human BAFF expressed in E. coll cells. The protein concentrations of BAFF of the present invention determined by the commercially available ELISA kit will differ from that determined by a standard protein assay method as the capture and/or detection antibodies employed in the commercially available ELISA kit are raised against a non-human cell expressed human BAFF protein. Al a structural level, such a result will indicate different immunoreactivity profiles of BAFF of the present invention and a non-human cell expressed human BAFF molecule. (g) In vitro comparison of Immunoreactivity Profiles between NGFR-Fc of the Present Invention and a NGFR-Fc molecule expressed using non-human systems Protein estimation of NGFR-Fc of the present invention is determined using a suitable protein assay method, for example, the Lowry method of protein estimation with human IgG as a standard. NGFR-Fc of the present invention, standardised using the standard protein assay results, is subjected to a quantitative immunoassay procedure developed using reagents available from a commercially available source. For example, an anti-NGFR-Fc-Fc ELISA is developed using a human NGFR-Fc Mab (R&D Systems Cat # MAB367) as a capture antibody, a biotinylated human NGFR-Fc Pab (R&D Systems Cat # BAF367) as a detection antibody and a recombinant human NGFR-Fc-Fc expressed in Sf 21 insect cells (R&D Systems Cat #367-NR-0.50/CF) as a protein standard. Protein concentrations of NGFR-Fc of the present invention, standardised using the standard protein assay results, are assayed with the above-mentioned reagents using ELISA methods known in the art. The protein concentrations of NGFR-Fc of the present invention determined by the quantitative immunoassay developed using sourced components will differ from that determined by a standard protein assay method as the capture and/or detection antibodies employed in the immunoassay procedure are raised against a non-human cell expressed human chimeric NGFR-Fc protein. At a structural level, such a result indicates different immunoreactivity profiles of NGFR-Fc of the present invention and a non-human cell expressed human chimeric NGFR-Fc molecule. h) In vitro comparison of Immunoreactivity Profiles between Fas Ligand of the Present Invention and human Fas Ligand expressed using non-human systems Protein estimation of Fas Ligand of the present invention is determined using a standard protein assay technique, for example, the Bradford protein assay (Bradford 1976 supra} or, alternatively, the A280 absorbance method using the calculated extinction coefficient (E) and the measured molecular mass based on SDS-PAGE analysis. Fas Ligand of the present invention, standardised using the standard protein assay results, is diluted and tested in a commercially available ELISA kit, for example, a R&D Systems human Fas Ligand DuoSet® ELISA kit (Cat # DYJ26) in accordance with the manufacturer's instructions. The above-mentioned ELISA kit employs a human Fas Ligand expressed in CHO cells as a standard. The protein concentrations of Fas Ligand of the present invention determined by the commercially available ELISA kit will differ from that determined by a standard protein assay method as the capture and/or detection antibodies employed in the commercially available ELISA kit are raised against a non-human cell expressed human Fas Ligand protein. A1 a structural level, such a result will indicate different immunoreactivity profiles of Fas Ligand of the present invention and a non-human cell expressed human Fas Ligand molecule. EXAMPLE 14 Further Purification of Target Molecule of the Present Invention and Peptide Mass Fingerprinting by ESJ-MS/MS In addition to the purification protocol as described in Example 2, purification of the target molecule of the present invention is further performed by RP-HPLC, using a commercially available column, Eluting proteins are monitored by the absorbance at 215 or 280 nm and collected with correction being made for the delay due to tubing volume between the flow cell and the collection port. A gel piece containing the protein sample from a ID or 2D gel is digested in trypsin solution as described in Example 3, Alternatively, a solution containing the protein sample is digested with trypsin in an ammonium bicarbonate buffer (10-25 mM, pH 7.5-9). The solution is incubated at 37° C overnight. The reaction is then stopped by adding acetic acid until the pH is in the range 4-5. The peptide samples are concentrated and desalted using C18 Zip-Tips (Millipore, Bedford, MA) or pre-fabricated micro-columns containing Poros R2 chromatography resin (Perspetive Biosystems, Framingham, MA) as described in Example 3. The protein sample (2-5 µl) is injected onto a micro C18 precolumn and washed with 0,1% formic acid at 30 ul/min to concentrate and desalt. After a 3 min wash the pre-column is switched into line with the analytical column containing C18 RP silica (Atlantis, 75µm x 100mm. Waters Corporation). Peptides are eluted from the column using a linear solvent gradient, with steps, from H2O:CH3CN (95:5; + 0.1% formic acid) to H2O:CH3CN (20:80, + 0.1% formic acid) at 200 nl/min over a 40 min period. The LC eluent is subject to positive ion nanoflow electrospray analysis on a Micromass QTOF Ultima mass spectrometer (Micromass, Manchester, UK). Tandem MS is performed using a Q-Tof hybrid quadrupole / orthogonal-acceleration TOF mass spectrometer (Micromass). The QTOF is operated in a data dependent acquisition mode (DDA). A TOFMS survey scan was acquired (m/z 400-2000, 1.0s), with the three largest multiply charged ions (counts >15) in the survey scan sequentially subjected to MS/MS analysis, MS/MS spectra were accumulated for 8 s (m/z 50-2000). The LC/MS/MS data are searched using Mascot (Matrix Science, London, UK) and Protein Lynx Global Server ("PLGS") (Micromass). The protein sample is anticipated to be the target molecule. EXAMPLE 15 (a) ImmuDogeuiciiy in non-human animals (i) Animal immunization with target protein Separate groups of non-human animals, for example, mice are immunized either sub-cutaneously, intramuscularly or intraperitoneally (IP) with l-100ug of protein of the present invention and the protein expressed in non-human cells, respectively. Animals receive a secondary immunization one month following immunization. Prior to immunization, protein is emulsified in an adjuvant, for example, complete Freud's adjuvant for the primary immunization and incomplete Freud's adjuvant for the secondary immunization. (ii) Detection of antibodies directed to target protein For the detection of antibody response, animals from each group are bled from the tail and sera pooled. Protein-specific antibodies are detected by a solid phase ELISA using 50ng/well of protein of the present invention. Different immunoglobulin isotypes are detected by using label-led detection antibodies raised against IgGl, IgG2, IgG2b, IgG3, IgM, IgA, IgD. Alternatively, antibody response is measured against protein of the present invention blotted onto a membrane either as a dot blot or Western blot. Detection of different immunoglobulin isotypes are detected as described above. It is anticipated that the protein of the present invention will elicit an antibody response that is distinct to that of protein expressed in non-human cells. (iii) T cell proliferation assay Immunised animals are euthariised and spleen cells prepared. A suitable number of spleen cells, for example, 5 x 105 cells, from animals immunized with protein of the present invention are cultured with various concentrations of protein of the present invention while and equivalent number of spleen cells from animals immunized with protein expressed in non-humar; cells are cultured with various concentrations of protein expressed in non-human cells. For T cell proliferation assays, spleen cells are cultured for 96 hours and treated with lµCi [3H] thymidine (6-7 |µCi/umol) during the final 16 hours. The cells are harvested onto filter strips and [3H] thymidine incorporation determined using standard methods. I; is anticipated that the protein of the present invention will elicit a different proliferation response compared to the protein expressed in non-human cells. (iv) IFN gamma assay For the IFN gamma assay, culture supernatant from spleen cells incubated with either the protein of the present invention or protein expressed in non-human cells are harvested at 96 hours and IFN gamma production is detected by a sandwich ELISA, for example, a R&D Systems anti-EFN gamma Quantikine® ELISA kit (Gat # DIF50) in accordance with the manufacturer's instructions. It is anticipated that IFN gamma production will be different in culture supernatant derived from cells incubated with protein of the present invention compared with culture supernatant derived from cells incubated with protein expressed in non-human cells. (b) In vitro Human Immunogenicity assays (i) Human T-Cell response assay Human dendritic cells and CD4+ T cells are prepared from human blood as described in Stickler et al. Toxicologica! Sciences 77:280-289,2004. Co-cultures of dendritic cells and CD4+ T cells are plated out in 96 well plates containing 2 x 104 dendritic cells and 2 x 105 CD4+ T cells. The protein of the present invention and protein expressed in non-human cells undergo enzymatic digestion into peptide fragments using a suitable enzyme determined by cleavage site prediction software, for example, Peptide Cutter (http://au.expasv.org/tools/peptidecutter). The resulting peptide fragments are purified by a suitable technique, for example, liquid chromatography and added to the co-cultures to a final concentration of 5ug/ml. Cultures are incubated for 5 days and 0.5uCi 3H thymidine is then added to each culture. The cells are harvested onto filter strips and cell proliferation is determined by [3H] thymidine incorporation. 11 is anticipated that the peptides derived from protein of the present invention will elicit a weaker proliferation response compared to peptides derived from the protein expressed in non-human cells, (ii) Human antibody response assay Human donors undergoing treatment with protein expressed in non-human cells are bled and sera prepared. Protein-specific antibodies are detected by a solid phase ELISA against both SOng/well of protein of the present invention and protein expressed in non-human cells. Different immunoglobulin isotypes are detected by using labelled detection antibodies raised against human IgGl, IgG2, lgG3, IgG4, IgM, IgA, IgD. Alternatively, antibody response is measured against protein of the present invention and protein expressed in non-human cells blotted onto a membrane either as a dot blot or Western blot. Detection of different immunoglobulin isotypes are detected as described above. It is anticipated that the immunoglobulin present in the sera of people treated with protein expressed in non-human cells will bind to protein expressed in non-human cells while either binding weakly or not binding with protein of the present invention. EXAMPLE 16 Preparation of protein of the present invention from recombinant genomic constructs The genomic sequences encoding the TNF-a, LT-a or Fas Ligand of the present invention (SEQ ID NOs: 191, 192, 193, respectively) are amplified by PCR and cloned into appropriate expression vectors, for instance pIRESbleo3, pCMV-SPORT6, pUMCV3, pORF, pORF9, pcDNA3.1/GS, pCEP4, pIRESpuroS, pIRESpuro4, pcDNA3.1/Hygro(+), pcDNA3.1/Hygro(-), pEF6/V5-His. These recombinant constructs are then prepared for human cell transformation as described above in Example l(c). Production and purification of GM-CSF, IL-3, IL-4 and IL-5 of the present invention from the recombinanl DNA construct are carried OUT as described above in Example 2. EXAMPLE 17 In Vivo Comparison of the Inhibition of Colitis by OX40-Fc of the Present Invention and OX40-Fc Expressed from CHO Cells The potencies of OX40-Fc of the present invention and OX40-Fc expressed from CHO cells to inhibit immune responses in vivo are evaluated in a murine model of trinitrobenzene sulfonic acid (TNBS)-induced colitis (Taylor Journal of Leukocyte Biology 72:522-525, 2002). TNBS is prepared in a 50% ethanol solution diluted to give a final concentration of 2mg TNBS in 75 |4 total volume. The mice are lightly anesthetized and colitis is induced by intrarectal administration of 75 u.1 of the TNBS solution using a plastic catheter. Control mice receive 50% aqueous ethanol. On day 4-6, TNBS colitic mice and ethanol treated controls are each injected a suitable amount, for example, 100µg, of either OX40-Fc of the present invention or OX40-Fc expressed from CHO cells. The mice are sacrificed at day 7 and gut tissue is stained for CD4-+ T cell infiltration into the lamina propria, OX40-Fc of the present invention treated mice show a greater reduction in the number of infiltrating CD4+ T cells into the lamina propria. TNF-a mRNA transcript levels in gut tissue of mice from above are determined by real time reverse transcription polymerase chain reaction (RT-PCR). Total UNA is extracted from tissue using KNeasy Mini Kit (Qiagen, Australia) according to manufacturer's instructions and the KNA concentration is determined spectrophotometrically. After extraction, samples are stored at -80°C until use. Real time RT-PCR is prepared using the TaqMan One-Step RT-PCR Master Mix Reagents Kit (PE Appb'ed Biosystems). 100 ng of total RNA is analysed in a 25 µ1 reaction containing 1 x Master Mix, 1 x MultiScribe and Rnase Inhibitor Mix, 300 nM TNF-a forward primer, 300 nM TNF-a reverse primer, 100 nM TNF-a probe, i x 18srRNA Primer and Probe Mix. RT-PCR reaction is performed in the ABI Prism 7700 Sequence Detection System (PE Applied Biosystems). The thermal cycle conditions consisted of reverse transcription at 48°C for 30 minutes, denaturation at 95°C ior 10 minutes, followed by 40 cycles of 95°C for 15 seconds and 60°C for 1 minute. Data from the reaction is collected and analysed by appropriate computer software. TNF-a mRNA expression is reduced by OX40-Fc of the present invention to a larger extent that OX40-Fc expressed from CHO cells. EXAMPLE 18 (a) Production of a DNA construct expressing alpha 2,6 sialyltransferase The DNA sequence for alpha 2,6 sialyltransferase (a2,6ST) was amplified from an EST cDNA library (clone 3090115, Invitrogen) by PCR, using forward primer (SEQ ID NO: 194) and reverse primer (SEQ ID NO: 195) that incorporated restriction enzyme sites for Not 1 and BamHl, respectively. After amplification, the sequence was digested using Notl and BamHl enzymes and cloned into the corresponding restriction sites of expression vector pIRESbleo3 to produce the vector pIRESbleo3-a2,6ST, Digestion of pIRESbleo3-a2,6ST with Not 1 and BamHl resulted in the expected size fragment of 1315 bp. Alternatively, the DNA sequence for a2,6ST was amplified from an EST cDNA library (clone 3090115, Invitrogen) by PCR, using forward primer (SEQ ID NO: 196) and reverse primer (SEQ ID NO: 197) that incorporated restriction enzyme sites for BamHl and Not 1, respectively. After amplification, the sequence was digested using BamHl and Not 1 enzymes and cloned into the corresponding restriction sites of expression vector pIRESpuroS to produce the vector pIRESpuro3-a2,6ST. Digestion of pIRESpuroS- a2,6ST with BamHl and Not 1 resulted in the expected size fragment of 1310 bp. (b) Preparation of Megaprep of 2,6 Sialyltransferase expression vector 750ml of sterile LB broth containing ampicillin (120µg/ml) was inoculated with 750µl of overnight culture of pIRESbleo3-a2,6ST or pIRESpuro3-a2,6ST. The culture was incubated at 37°C with shaking for 16 hours. Plasmid was prepared using a Qiagen Endofree Plasmid Mega Kit (Qiagen Catalog number 12381). (c) Production and Purification of Highly Sialylated TNFRI-Fc Plasmid pIRESbleo3-a2,6ST or pIRESpuro3-a2,6ST harbouring the gene for a2,6ST and plasmid pIRESbleoS-TNFRI-Fc harbouring the gene for TNFRI-Fc were mixed in the ratio of 1:3. The mixture was transfected into cells and the resulting supernatant purified in accordance with Example 2(c) using with the exception that the pooled fractions containint TNFRI-Fc were not further concentrated. The purified highly sialylated TNFRI-Fc was found to have an approximate molecular weight range of 45-85 kDa and to be at least 99% pure by silver staining. (d) Characterization of Highly Sialylated TNFRI-Fc Two dimensional polyacrylamide electrophoresis was performed on the highly sialylated TNFRIl-Fc according to Example 3(c). Table 39 shows the apparent molecular weights, pi values and relative intensities of isoforms of TNFRI-Fc. The values listed correspond to the intensity weighted center within the selected area of the gel containing the spot and hence, are the most reflective of the pi and molecular weight of the protein. TABLE 39 Molecular weights and pi values of isoforms of highly sialylated TNFRI-Fc (Table Removed) EXAMPLE 19 (a) Formulation of a Topical Cream containing a Protein of the Present Invention Collected fractions of the target protein of the present invention, as described in Example 2, are collected into a syringe using a caanula. A suitable amount of protein solution is filtered into a Falcon tube, transferred into a low-protein binding tube and mixed with a suitable amount of topical cream, for example, Cetapbil Moisturising Cream (Galderma), resulting in a final target protein concentration of 10-1000 µg/ml. The cream was dispensed slowly into the falcon tube while stirring. The mixture was transferred from Falcon tube to syringe several times to mix the components. The cream was transferred to the 60mL syringe and a suitable amount of cream was taken in a syringe for analysis, The remaining homogenous mixture was then transferred into syringes. An airspace was introduced before the cream was transferred to avoid the cream from coming into direct contact with the rubber seal. (b) Formulation of Topical Cream containing TNFRII-Fc of the Present Invention Collected fractions of TNFRII-Fc of the present invention, as described in Example 2(d) or 2(h). were collected into a 20mL syringe using a cannula, 14,0 mL of Img/mL protein was 0,22um filtered into a 50mL Falcon tube; O.SmL was transferred into a low-protein binding tube as a sample for analysis. 43 mL of Cetaphil Moisturising Cream (Galderma) was transferred into a 60mL syringe using a cannula, resulting in a final TNFRII-Fc concentration of 250 ug/ml. The cream was dispensed slowly into the falcon tube while stirring. The mixture was transferred from Falcon tube to syringe several times to mix the components. A 0.5mL aliquot of this mixture was taken in a 1mL syringe for analysis (sample 1). The homogenous mixture was then transferred into 10mL syringes at 8mL per syringe. An airspace was introduced before the cream was transferred to avoid the cream from coming into direct contact with the rubber seal. Half of the cream was transferred .to the 60mL syringe.1.0g of thalidomide was then added to the Falcon tube and mixed in with remaining cream. The process of transferring cream from tube to syringe was repeated to thoroughly mix all components of the cream. A O.SmL aliquot of this mixture was taken in a ImL syringe for analysis (sample 2). The homogenous mixture was then transferred into 1 OmL syringes at 8mL per syringe, as described above. (c) Formulation of Topical Cream containing TNFRI-Fc of the Present Invention Collected fractions of TNFRI-Fc of the present invention, as described in Example 2(c), are collected, filtered and mixed with Cetaphii Moisturising Cream as described above in Example 19(b) to a final THFRI-Fc concentration of 250 µg/m.1. As described above in Example 19(b), separate homogenous mixtures containing 250 µg/ml TNFRI-Fc of the present invention and either no thalidomide or 20 mg/ml thalidomide are formulated and transferred into 10mL syringes at 8mL per syringe. EXAMPLE 20 (a) Biodistribution of TNFRII-Fc after topical application of pharmaceutical composition comprising TNFRII-Fc TNFRII-Fc of the present invention was 125I-labeled using the Chloramine T method. Briefly, a 20 (il aliquot of solution of TNFRII-Fc at 3.5 mg/ml, was added to 20 jil of 0.5 M Phosphate buffer pH 7.4. 2 µl of Na125 -l (0.2 mCi) was added, followed by 10 yl of Chloramine T (10 mg/ml) and mixed. After 30 seconds 10 \il sodium metabisulfite (10 mg/ml) was added to stop the reaction. Free 125I was removed from the reaction by chromatography on a Sephadex G10 column in the presence of 0.1 M Phosphate buffer pH 7.4. The eluted material was stored at 4°C until used in biodistributions studies. 125I-labeled-TNFRII-Fc was dissolved at 0.2 mg/ml and mixed 1:10 into the one of the four creams, namely Alpha Keri Moisturising Lotion (Mentholatum), DermaVeen Moisturing Lotion (DermaTech Laboratories), QV Skin Lotion (Lision Hong), Cetaphil Moisturing Lotion (Galderma Laboratories, L.P.) The topical pharmaceutical compositions were then applied to a 2 x 1 cm area of the shaved skin of anaesthetized Balb/C mice. The topical formulation was left on the mice and after 180 minutes the mice were euthanased and all the organs removed and counted in a gamma counter. Figure 13 shows the distribution of 125I-labeled TNFRII-Fc in mice following transdermal application of 125I-labeled TNFRII-Fc in a topical formulation of the present invention, wherein A is a topical formulation of 125l-labeled TNFRII-Fc in Alpha Keri Moisturising Lotion (Mentholatum); B is a topical formulation of 125l-labeled TNFRII-Fc in DermaVeen Moisturing Lotion (DermaTech Laboratories); C is a topical formulation of 125l-labeled TNFRII-Fc in QV Skin Lotion; and D is a topical formulation of 125I-labeled TNFRII-Fc in Cetaphil Moisturing Lotion (Galderma Laboratories, L.P.). As can be seen in Figure 13 there was rapid appearance of 125I-TNFRII-Fc in skin, muscle and the shaved area of the skin. Those skilled in the art will appreciate that the invention described herein is susceptible to variations and modifications other than those specifically described. It is to be understood that the invention includes all such variations and modifications. The invention also includes ali of the steps, features, compositions and compounds referred to, or indicated in this specification, individually or collectively, and any and all combinations of any two or more of said steps or features. IBLIOGRAPHY Ackland et at. Chromatogr 540:187-198, 1991 Aloj et al. J BiolChem 247:1146-1151, 1971 Altschul et o/. Nvcl Acids Res 25:389, 1997 Antibodies: A Laboratory Manual, Harlow and Lane (eds,), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, (1988). Aronsson et al. FEES Lev 411:359-364, 1997 Atherton and Shephard Synthetic Vaccines 9: Biackwell Scientific Publications Ausubel et al. In: Current Protocols in Molecular Biology John Wiley & Sons Inc. 1994-1998) Baneyx Current Opinion in Biotechnology, 70:411-421. 1999 Bernstein Methods Mo! Bio! 237:195-204, 2004 Bird Science 242:423, 1988 Blems and Resh Curr Opin Cell Bio! 5(6):9K4-9, 1993 Bonner and Laskey Eur J Biochem 46:83, 1974 Bradford Anal Biochem 72/248-254, 1976 Caprioli et al. 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An isolated protein comprising a profile of measurable physiochemical parameters, wherein said profile is indicative of, associated with or forms the basis of one or more distinctive pharmacological traits, wherein said isolated protein comprises a physiochemical profile comprising a number of measurable physiochemical parameters, {]~Px]i, [Pxk..-[PJn,}, wherein Px represents a measurable physiochemical parameter and "n" is an integer >1, wherein each of [Px]i to [Px]n is a different measurable physiochemical parameter, wherein the value of any one of the measurable physiochemical characteristics or an array of values of more than one measurable physiochemical characteristics is indicative of, associated with, or forms the basis of, a distinctive pharmacological trait, Ty, or an array of distinctive physiochemical traits {[Ty]i, [Ty]2, ....[Ty]m} wherein Ty represents a distinctive pharmacological trait and m is an integer >1 and each of [Ty]i to [Ty]m is a different pharmacological trait, wherein the isolated protein is selected from the group comprising TNF-a, LT-a, TNFRJ-Fc, TNFRII-Fc, OX40-Fc, BAFF, NGFR-Fc and Fas Ligand. 2. The isolated protein of Claim 1, wherein said protein comprises one or more of the measurable physiochemical parameters set forth in Table 2. 3. The isolated protein of Claim 1 wherein said protein comprises one or more of the distinctive pharmacological traits set forth in Table 3. 4. A chimeric molecule comprising the TNF-a, LT-a, BAFF or Fas Ligand of Claim 1, or fragment thereof, fused to one or more peptide, polypeptide or protein moieties. 5. The chimeric molecule of Claim 4 wherein the peptide, polypeptide or protein moiety comprises the constant (Fc) or framework region of a human immunoglobulin. 6. The chimeric molecule of Claim 4 wherein the chimeric molecule is selected from the group comprising TNF-a-Fc, LT-a-Fc, BAFF-Fc or Fas Ligand-Fc.A pharmaceutical composition comprising the isolated protein or chimeric molecule of any one of Claims 1 to 6. 7. The pharmaceutical composition of Claim 7, wherein the pharmaceutical composition further comprises a pharmaceutically acceptable topical carrier. 8. The pharmaceutical composition of Claim 8, wherein the pharmaceutical acceptable topical carrier is a cream or a lotion. 9. The pharmaceutical composition of Claims 7 to 9, wherein the chimeric molecule is TNFRI-Fc or TNFRII-Fc. 10. A method of treating or preventing a condition in a mammalian subject, wherein said condition can be ameliorated by increasing the amount or activity of a protein, said method comprising administering to said mammalian subject an effective amount of an isolated protein according to any one of Claims 1 to 3, a chimeric molecule according to any one of Claims 4 to 6 or the pharmaceutical composition of Claim 7-9. 11. A nucleotide sequence selected from the list consisting of SEQ ID NOs: 27, 29, 31, 33, 35, 37, 39, 43, 45, 47, 49, 51, 53, 55, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85,89,91,93,95,97,99, 101, 103, 105, 107,109, 111, 113, 115, 117, 119, 121, 127, 129, 131, 133, 135, 137, 139, 141, 143, 147, 149, 151, 153, 155, 157, 159, 163, 165, 167, 169, 171, 173, 175, 177,179, 183, 185, 187, 189, or a nucleotide sequence having at least about 90% identity to any one of the above-listed sequences or a nucleotide sequence capable of hybridizing to any one of the above sequences or their complementary forms under high stringency conditions. 12. An isolated protein or chimeric molecule encoded by a nucleotide sequence selected from the list consisting of SEQ ED NOs: 27, 29, 31, 33, 35, 37, 39, 43, 45, 47, 49, 51, 53, 55, 59.. 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107, 109, 111, 113, 115, 117, 119, 121, 127, 129, 131, 133, 135, 137, 139, 141, 143, 147, 149.. 151, 153, 155, 157, 159, 163, 165, 167, 169, 171, 173, 175, 177, 179, 183,185, 187, 189, or a nucleotide sequence having at least about 90% identity to any one of the above-listed sequence or a nucleotide sequence capable of hybridizing to any one of the above sequences or their complementary forms under high stringency conditions. 14. An isolated nucleic acid molecule encoding a protein or chimeric molecule or a functional part thereof comprising a sequence of nucleotides having at least 90% similarity SEQ ID NOs: 27, 29, 31, 33, 35, 37, 39, 43, 45, 47, 49, 51, 53, 55, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107, 109, 111, 113, 115, 117, 119, 121, 127, 129, 131, 133, 135, 137, 139, 141, 143, 147, 149, 151, 153, 155, 157, 159, 163, 165, 167, 169, 171, 173, 175, 177, 179, 183, 185, 187, 189 or after optimal alignment and/or being capable of hybridizing to one or more of SEQ ID NOs: 27, 29, 31, 33, 35, 37, 39, 43, 45, 47, 49, 51, 53, 55, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 89, 91, 93, 95, 97, 99, 101, 103, 105,107, 109, 111, 113, 115, 117, 119, 121, 127, 129, 131, 133, 135, 137, 139, 141, 143, 147, 149, 151, 153, 155, 157, 159, 163, 165, 167, 169, 171, 173, 175, 177, 179, 183, 185, 187, 189 or their complementary forms under high stringency conditions. 15. An isolated nucleic acid molecule comprising a sequence of nucleotides encoding a protein or chimeric molecule having an amino acid sequence substantially as set forth in one or more of SEQ ID NOs: 28, 30, 32, 34, 36, 38, 40, 44, 46, 48, 50, 52, 54, 56, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 90, 92, 94, 96, 98, 100, 102, 104, 106, 108, 110, 112, 114, 116, 118, 120, 122, 126, 130, 132, 134, 136, 138, 140, 142, 144, 148, 150, 152, 154,156, 158, 160,164,166, 168, 170, 172, 174, 176, 178,180, 184, 186,188, 190 or an amino acid sequence having at least about 90% similarity to one or more of SEQ ID NOs: 28, 30, 32, 34, 36, 38, 40, 44, 46, 48, 50, 52, 54, 56, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 90, 92, 94, 96, 98, 100, 102, 104, 106, 108, 110, 112, 114, 116, 118, 120, 122, 128, 130, 132, 134, 136, 138, 140, 142, 144, 148, 150, 152, 154, 156, 158, 160, 164, 166, 168, 170, 172, 174,176,178, 180, 184, 186,188, 190 after optimal alignment. 16. A kit for determining the level of human cell expressed human protein or chimeric molecule present in a biological preparation comprising (a) a solid phase support matrix; (b) one or more antibodies directed against a human protein according to any one ofClaims 1 to 3 or chimeric molecule according to any one of Claims 4 to 6; (c) a blocking solution; (d) one or more stock solutions of substrate; (e) a solution of substrate buffer; (f) a standard human protein or chimeric molecule sample; and (g) instructions for use. 17. The kit of Claim 16, wherein the standard human protein or chimeric molecule sample is a preparation of the isolated protein of any one of Claim 2 or 3 or the chimeric molecule of Claim 4. 18. The kit of Claim 16 or 17, wherein the or each antibody is derived from an immunization of a mammal with a preparation comprising the isolated protein of any one of Claims 2 or 3 or the chimeric molecule of Claim 4, 19. The kit of any of Claims 16 to 18, wherein the human cell expressed human protein is naturally occurring human TNF-a, LT-a, TNFRI, TNFRH, 0X40, BAFF, NGFR or Fas Ligand. 20. A method for treating a disease state characterized, or exacerbated, by or otherwise associated with an excess level of TNF-a in a subject, the method comprising topically administering to the subject a therapeutically effective amount* of the pharmaceutical composition of Claim 10. 21. The method of Claim 20, wherein the disease state is selected from the list consisting of: psoriasis, Behcet's disease, bullous dermatitis, eczema, fungal infection, leprosy, neutrophilic dermatitis, pityriasis maculara (or pityriasis rosea), pityriasis nigra (or tinea nigra), pityriasis rubra pilaris, systemic lupus erythematosus, systemic vascularitis and toxic epidermal necrolysis, erythema, erosion, ulceration, flaking, scaling, dryness, scabbing, crusting, weeping or exudating of skin or any side effects caused by the use of medication, such as the Aldara cream.