DUA L V A R IA B L E DO MA IN IMMUNO G LO B U LI NS A N D U S ES T HE R EOF Cross Reference to Related Applications [001] This application is a non-provisional application claiming priority to U.S. Provisional Application Serial No. 61/370,269, filed August 3, 2010, and U.S. Provisional Application Serial No. 61/377,134, filed August 26, 2010, the entire contents of which are hereby incorporated by reference. Field [002] Multivalent and multispecific binding proteins that bind IL-1 b and IL-17, methods of making, and specifically to their uses in the, diagnosis, prevention and/or treatment of acute and chronic inflammatory diseases, cancer, and other diseases are provided. Background [003] Engineered proteins, such as multispecific antibodies that bind to two or more antigens are known in the art. Such multispecific binding proteins can be generated using cell fusion, chemical conjugation, or recombinant DNA techniques. [004] Bispecific antibodies have been produced using quadroma technology (see Milstein, C. and Cuello, A.C. (1983) Nature 305(5934):537-40) based on the somatic fusion of two different hybridoma cell lines expressing murine monoclonal antibodies (mAbs) with the desired specificities of the bispecific antibody. Because of the random pairing of two different immunoglobulin (Ig) heavy and light chains within the resulting hybrid-hybridoma (or quadroma) cell line, up to ten different Ig species are generated, of which only one is the functional bispecific antibody. The presence of mispaired by-products, and significantly reduced production yields, means sophisticated purification procedures are required. [005] Bispecific antibodies can also be produced by chemical conjugation of two different mAbs (see Staerz, U.D., et al. (1985) Nature 314(6012): 628-31). This approach does not yield homogeneous preparation. Other approaches have used chemical conjugation of two different mAbs or smaller antibody fragments (see Brennan, M., et al. (1985) Science 229(4708): 81-3). [006] Another method used to produce bispecific antibodies is the coupling of two parental antibodies with a hetero-bifunctional crosslinker, but the resulting bispecific antibodies suffer from significant molecular heterogeneity because reaction of the crosslinker with the parental antibodies is not site-directed. To obtain more homogeneous preparations of bispecific antibodies two different Fab fragments have been chemically crosslinked at their hinge cysteine residues in a site-directed manner (see Glennie, M.J., et al. (1987) J. Immunol. 139(7): 2367-75). But this method results in Fab'2 fragments, not a full IgG molecule. [007] A wide variety of other recombinant bispecific antibody formats have been developed (see Kriangkum, J., et al. (2001) Biomol. Engin. 18(2): 31-40). Amongst them tandem single-chain Fv molecules and diabodies, and various derivatives thereof, are the most widely used. Routinely, construction of these molecules starts from two singlechain Fv (scFv) fragments that recognize different antigens (see Economides, A.N., et al. (2003) Nat. Med. 9(1): 47-52). Tandem scFv molecules (taFv) represent a straightforward format simply connecting the two scFv molecules with an additional peptide linker. The two scFv fragments present in these tandem scFv molecules form separate folding entities. Various linkers can be used to connect the two scFv fragments and linkers with a length of up to 63 residues (see Nakanishi, K., et al. (2001) Ann. Rev. Immunol. 19: 423-74). Although the parental scFv fragments can normally be expressed in soluble form in bacteria, it is, however, often observed that tandem scFv molecules form insoluble aggregates in bacteria. Hence, refolding protocols or the use of mammalian expression systems are routinely applied to produce soluble tandem scFv molecules. In a recent study, in vivo expression by transgenic rabbits and cattle of a tandem scFv directed against CD28 and a melanoma-associated proteoglycan was reported (see Grade, J.A., et al. (1999) J. Clin. Invest. 104(10): 1393-401). In this construct, the two scFv molecules were connected by a CH1 linker and serum concentrations of up to 100 mg/L of the bispecific antibody were found. Various strategies including variations of the domain order or using middle linkers with varying length or flexibility were employed to allow soluble expression in bacteria. A few studies have now reported expression of soluble tandem scFv molecules in bacteria (see Leung, BP., et al. (2000) J . Immunol. 164(12): 6495-502; Ito, A., et al. (2003) J. Immunol. 170(9): 4802-9; Kami, A., et al. (2002) J. Neuroimmunol. 125(1-2): 134-40) using either a very short Ala3 linker or long glycine/serine-rich linkers. In a recent study, phage display of a tandem scFv repertoire containing randomized middle linkers with a length of 3 or 6 residues was employed to enrich for those molecules that are produced in soluble and active form in bacteria. This approach resulted in the isolation of a tandem scFv molecule with a 6 amino acid residue linker (see Arndt, M. and Krauss, J. (2003) Methods Mol. Biol. 207: 305-21). It is unclear whether this linker sequence represents a general solution to the soluble expression of tandem scFv molecules. Nevertheless, this study demonstrated that phage display of tandem scFv molecules in combination with directed mutagenesis is a powerful tool to enrich for these molecules, which can be expressed in bacteria in an active form. [008] Bispecific diabodies (Db) utilize the diabody format for expression. Diabodies are produced from scFv fragments by reducing the length of the linker connecting the VH and VL domain to approximately 5 residues (see Peipp, M. and Valerius, T. (2002) Biochem. Soc. Trans. 30(4): 507-1 1). This reduction of linker size facilitates dimerization of two polypeptide chains by crossover pairing of the VH and VL domains. Bispecific diabodies are produced by expressing, two polypeptide chains with, either the structure VHA-VLB and VHB-VLA (VH-VL configuration), or VLA-VHB and VLB-VHA (VL-VH configuration) within the same cell. A large variety of different bispecific diabodies have been produced in the past and most of them are expressed in soluble form in bacteria. However, a recent comparative study demonstrates that the orientation of the variable domains can influence expression and formation of active binding sites (see Mack, M. et al.(1995) Proc. Natl. Acad. Sci. USA 92(15): 7021-5). Nevertheless, soluble expression in bacteria represents an important advantage over tandem scFv molecules. However, since two different polypeptide chains are expressed within a single cell inactive homodimers can be produced together with active heterodimers. This necessitates the implementation of additional purification steps in order to obtain homogenous preparations of bispecific diabodies. One approach to force the generation of bispecific diabodies is the production of knob-into-hole diabodies (see Holliger, P., et al. (1993) Proc. Natl. Acad. Sci. USA 90(14): 6444-8.18). This was demonstrated for a bispecific diabody directed against HER2 and CD3. A large knob was introduced in the VH domain by exchanging Val37 with Phe and Leu45 with Trp and a complementary hole was produced in the VL domain by mutating Phe98 to Met and Tyr87 to Ala, either in the anti- HER2 or the anti-CD3 variable domains. By using this approach the production of bispecific diabodies could be increased from 72% by the parental diabody to over 90% by the knob-into-hole diabody. Importantly, production yields did only slightly decrease as a result of these mutations. However, a reduction in antigen-binding activity was observed for several analyzed constructs. Thus, this rather elaborate approach requires the analysis of various constructs in order to identify those mutations that produce heterodimeric molecule with unaltered binding activity. In addition, such approach requires mutational modification of the immunoglobulin sequence at the constant region, thus creating non-native and non-natural form of the antibody sequence, which may result in increased immunogenicity, poor in vivo stability, as well as undesirable pharmacokinetics. [009] Single-chain diabodies (scDb) represent an alternative strategy for improving the formation of bispecific diabody-like molecules (see Holliger, P. and Winter, G. (1997) Cancer Immunol. Immunother. 45(3-4): 128-30; Wu, A.M., et al. (1996) Immunotechnology 2(1): p. 21-36). Bispecific single-chain diabodies are produced by connecting the two diabody-forming polypeptide chains with an additional middle linker with a length of approximately 15 amino acid residues. Consequently, all molecules with a molecular weight corresponding to monomeric single-chain diabodies (50-60 kDa) are bispecific. Several studies have demonstrated that bispecific single chain diabodies are expressed in bacteria in soluble and active form with the majority of purified molecules present as monomers (see Holliger, P. and Winter, G. (1997) Cancer Immunol. Immunother. 45(3-4): 128-30; Wu, A.M., et al. (1996) Immunotechnol. 2(1): 21-36; Pluckthun, A. and Pack, P. (1997) Immunotechnol. 3(2): 83-105; Ridgway, J.B., et al. (1996) Protein Engin. 9(7): 617-21). Thus, single-chain diabodies combine the advantages of tandem scFvs (all monomers are bispecific) and diabodies (soluble expression in bacteria). [010] More recently diabodies have been fused to Fc to generate more Ig-like molecules, named di-diabodies (see Lu, D., et al. (2004) J. Biol. Chem. 279(4): 2856-65). In addition, multivalent antibody constructs comprising two Fab repeats in the heavy chain of an IgG and that bind four antigen molecules have been described (see WO 0177342A1 , and Miller, K., et al. (2003) J. Immunol. 170(9): 4854-61). [01 1] There is a need in the art for improved multivalent binding proteins that bind two or more antigens. U.S. Patent No. 7,612,181 provides a novel family of binding proteins that bind two or more antigens with high affinity, and which are called dual variable domain immunoglobulins (DVD-lg™). The present disclosure provides further novel binding proteins that bind two or more antigens. Summary [012] Multivalent binding proteins that bind two or more antigens are provided. A novel family of binding proteins capable of binding two or more antigens with high affinity are also provided. [013] In one embodiment, a binding protein comprising a polypeptide chain, wherein the polypeptide chain comprises VD1-(X1)n-VD2-C-(X2)n, wherein VD1 is a first variable domain, VD2 is a second variable domain, C is a constant domain, X 1 represents an amino acid or polypeptide, X2 represents an Fc region and n is 0 or 1 is provided. In an embodiment the VD1 and VD2 in the binding protein are heavy chain variable domains. In another embodiment, the heavy chain variable domain is a murine heavy chain variable domain, a human heavy chain variable domain, a CDR grafted heavy chain variable domain, or a humanized heavy chain variable domain. In yet another, embodiment VD1 and VD2 bind the same antigen. In another embodiment VD1 and VD2 bind different antigens. In still another embodiment, C is a heavy chain constant domain. For example, X 1 is a linker with the proviso that X 1 is not CH1 . For example, X 1 is AKTTPKLEEGEFSEAR (SEQ ID NO: 1); AKTTPKLEEGEFSEARV (SEQ ID NO: 2); AKTTPKLGG (SEQ D NO: 3); SAKTTPKLGG (SEQ ID NO: 4); SAKTTP (SEQ ID NO: 5); RADAAP (SEQ ID NO: 6); RADAAPTVS (SEQ ID NO: 7); RADAAAAGGPGS (SEQ ID NO: 8); RADAAAA(G4S)4 (SEQ ID NO: 9);SAKTTPKLEEGEFSEARV (SEQ ID NO: 10); ADAAP (SEQ ID NO: ) ; ADAAPTVSIFPP (SEQ ID NO: 12); TVAAP (SEQ ID NO: 13); TVAAPSVFIFPP (SEQ ID NO: 14); QPKAAP (SEQ D NO: 15); QPKAAPSVTLFPP (SEQ D NO: 16); AKTTPP (SEQ ID NO: 17); AKTTPPSVTPLAP (SEQ ID NO: 18); AKTTAP (SEQ D NO: 19); AKTTAPSVYPLAP (SEQ ID NO: 20); ASTKGP (SEQ D NO: 21); ASTKGPSVFPLAP (SEQ ID NO: 22), GGGGSGGGGSGGGGS (SEQ ID NO: 23); GENKVEYAPALMALS (SEQ ID NO: 24); GPAKELTPLKEAKVS (SEQ ID NO: 25); GHEAAAVMQVQYPAS (SEQ ID NO: 26) ; TVAAPSVFIFPPTVAAPSVFIFPP (SEQ ID NO: 27); or ASTKGPSVFPLAPASTKGPSVFPLAP (SEQ ID NO: 28). In an embodiment, X2 is an Fc region. In another embodiment, X2 is a variant Fc region. [014] In an embodiment the binding protein disclosed herein comprises a polypeptide chain, wherein the polypeptide chain comprises VD1-(X1)n-VD2-C-(X2)n, wherein VD1 is a first heavy chain variable domain, VD2 is a second heavy chain variable domain, C is a heavy chain constant domain, X 1 is a linker with the proviso that it is not CH1 , and X2 is an Fc region. [015] In an embodiment, VD1 and VD2 in the binding protein are light chain variable domains. In an embodiment, the light chain variable domain is a murine light chain variable domain, a human light chain variable domain, a CDR grafted light chain variable domain, or a humanized light chain variable domain. In one embodiment VD1 and VD2 bind the same antigen. In another embodiment VD1 and VD2 bind different antigens. In an embodiment, C is a light chain constant domain. In another embodiment, X 1 is a linker with the proviso that X 1 is not CL1 . In an embodiment, X 1 is AKTTPKLEEGEFSEAR (SEQ ID NO: 1); AKTTPKLEEGEFSEARV (SEQ ID NO: 2); AKTTPKLGG (SEQ ID NO: 3); SAKTTPKLGG (SEQ ID NO: 4); SAKTTP (SEQ ID NO: 5); RADAAP (SEQ D NO: 6); RADAAPTVS (SEQ ID NO: 7); RADAAAAGGPGS (SEQ ID NO: 8); RADAAAA(G S) (SEQ ID NO: 9);SAKTTPKLEEGEFSEARV (SEQ ID NO: 10); ADAAP (SEQ ID NO: 11); ADAAPTVSIFPP (SEQ ID NO: 12); TVAAP (SEQ ID NO: 13); TVAAPSVFIFPP (SEQ ID NO: 14); QPKAAP (SEQ ID NO: 15); QPKAAPSVTLFPP (SEQ D NO: 16); AKTTPP (SEQ ID NO: 17); AKTTPPSVTPLAP (SEQ ID NO: 18); AKTTAP (SEQ D NO: 19); AKTTAPSVYPLAP (SEQ ID NO: 20); ASTKGP (SEQ ID NO: 21); ASTKGPSVFPLAP (SEQ ID NO: 22) GGGGSGGGGSGGGGS (SEQ ID NO: 23); GENKVEYAPALMALS (SEQ ID NO: 24); GPAKELTPLKEAKVS (SEQ ID NO: 25); GHEAAAVMQVQYPAS (SEQ ID NO: 26) ; TVAAPSVFIFPPTVAAPSVFIFPP (SEQ ID NO: 27); or ASTKGPSVFPLAPASTKGPSVFPLAP (SEQ ID NO: 28. In an embodiment, the binding protein does not comprise X2. [016] In an embodiment, both the variable heavy and variable light chain comprise the same linker. In another embodiment, the variable heavy and variable light chain comprise different linkers. In another embodiment, both the variable heavy and variable light chain comprise a short (about 6 amino acids) linker. In another embodiment, both the variable heavy and variable light chain comprise a long (greater than 6 amino acids) linker. In another embodiment, the variable heavy chain comprises a short linker and the variable light chain comprises a long linker. In another embodiment, the variable heavy chain comprises a long linker and the variable light chain comprises a short linker. [017] In an embodiment the binding protein disclosed herein comprises a polypeptide chain, wherein said polypeptide chain comprises VD1-(X1)n-VD2-C-(X2)n, wherein VD1 is a first light chain variable domain, VD2 is a second light chain variable domain, C is a light chain constant domain, X 1 is a linker with the proviso that it is not CH1 , and X2 does not comprise an Fc region. [018] In another embodiment, a binding protein comprising two polypeptide chains, wherein said first polypeptide chain comprises VD1-(X1)n-VD2-C-(X2)n, wherein VD1 is a first heavy chain variable domain, VD2 is a second heavy chain variable domain, C is a heavy chain constant domain, X 1 is a linker with the proviso that it is not CH1 , and X2 is an Fc region; and said second polypeptide chain comprises VD1-(X1)n- VD2-C-(X2)n, wherein VD1 is a first light chain variable domain, VD2 is a second light chain variable domain, C is a light chain constant domain, X 1 is a linker with the proviso that it is not CH1 , and X2 does not comprise an Fc region is provided. In a particular embodiment, the Dual Variable Domain (DVD) binding protein comprises four polypeptide chains wherein the first two polypeptide chains comprises VD1-(X1)n-VD2- C-(X2)n, respectively wherein VD1 is a first heavy chain variable domain, VD2 is a second heavy chain variable domain, C is a heavy chain constant domain, X 1 is a linker with the proviso that it is not CH1 , and X2 is an Fc region; and the second two polypeptide chain comprises VD1-(X1)n-VD2-C-(X2)n respectively, wherein VD1 is a first light chain variable domain, VD2 is a second light chain variable domain, C is a light chain constant domain, X 1 is a linker with the proviso that it is not CH1 , and X2 does not comprise an Fc region. Such a Dual Variable Domain (DVD) protein has four antigen binding sites. [019] In another embodiment the binding proteins disclosed herein are capable of binding one or more targets. Accordingly, in some embodiments, the binding proteins comprise at least two variable domain sequences (e.g., VD1 and VD2) capable of binding at least two different targets. In some embodiments, VD1 and VD2 are independently chosen. Therefore, in some embodiments, VD1 and VD2 comprise the same SEQ ID NO and, in other embodiments, VD1 and VD2 comprise different SEQ ID NOS. [020] In another embodiment the binding proteins disclosed herein bind one or more targets. In an embodiment, the target is a cytokine, a cell surface protein, an enzyme, or a receptor. In another embodiment, the binding protein modulates a biological function of one or more targets. In another embodiment, the binding protein neutralizes one or more targets. In yet another embodiment, the cytokine is a lymphokine, monokine, polypeptide hormone, receptor, or tumor marker. For example, in some embodiments, the binding protein is capable of binding two or more of the following: II_-1 b (seq. 1), II_-1 b (seq. 2), L- p (seq. 3), IL- I b (seq. 4), L- b (seq. 5), IL-17 (seq. 1), IL-17 (seq. 2), or IL-17 (seq. 3). [021] In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 50 or SEQ ID NO. 52; and a DVD light chain amino acid sequence SEQ ID NO. 5 1 or SEQ ID NO. 53. In an embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO.50 and a DVD light chain amino acid sequence of SEQ ID NO: 5 1. In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 52 and a DVD light chain amino acid sequence of SEQ ID NO: 53. [022] In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 54 or SEQ ID NO. 56; and a DVD light chain amino acid sequence SEQ ID NO. 55 or SEQ ID NO. 57. In an embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 54 and a DVD light chain amino acid sequence of SEQ ID NO: 55. In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ D NO. 56 and a DVD light chain amino acid sequence of SEQ ID NO: 57. [023] In another embodiment, the binding protein capable of binding II_- b (seq. 3) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 58 or SEQ ID NO. 60; and a DVD light chain amino acid sequence SEQ ID NO. 59 or SEQ ID NO. 61. In an embodiment, the binding protein capable of binding IL- b (seq. 3) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 58 and a DVD light chain amino acid sequence of SEQ ID NO: 59. In another embodiment, the binding protein capable of binding 1L-1 b (seq. 3) and IL-17 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 60 and a DVD light chain amino acid sequence of SEQ ID NO: 61. [024] In another embodiment, the binding protein capable of binding L- b (seq. 4) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ D NO. 62 or SEQ ID NO. 64; and a DVD light chain amino acid sequence SEQ ID NO. 63 or SEQ ID NO. 65. In an embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 62 and a DVD light chain amino acid sequence of SEQ ID NO: 63. In another embodiment, the binding protein capable of binding IL- I (seq. 4) and IL-17 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 64 and a DVD light chain amino acid sequence of SEQ ID NO: 65. [025] In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 66 or SEQ ID NO. 68; and a DVD light chain amino acid sequence SEQ ID NO. 67 or SEQ ID NO. 69. In an embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 66 and a DVD light chain amino acid sequence of SEQ ID NO: 67. In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 68 and a DVD light chain amino acid sequence of SEQ ID NO: 69. [026] In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 70 or SEQ ID NO. 72; and a DVD light chain amino acid sequence SEQ ID NO. 7 1 or SEQ ID NO. 73. In an embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 70 and a DVD light chain amino acid sequence of SEQ ID NO: 7 1. In another embodiment, the binding protein capable of binding L- b (seq. 1) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 72 and a DVD light chain amino acid sequence of SEQ D NO: 73. [027] In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 74 or SEQ ID NO. 76; and a DVD light chain amino acid sequence SEQ ID NO. 75 or SEQ ID NO. 77. In an embodiment, the binding protein capable of binding IL-1 p (seq. 2) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 74 and a DVD light chain amino acid sequence of SEQ ID NO: 75. In another embodiment, the binding protein capable of binding IL-1 p (seq. 2) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 76 and a DVD light chain amino acid sequence of SEQ ID NO: 77. [028] In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 78 or SEQ ID NO. 80; and a DVD light chain amino acid sequence SEQ ID NO. 79 or SEQ ID NO. 81. In an embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 78 and a DVD light chain amino acid sequence of SEQ ID NO: 79. In another embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 80 and a DVD light chain amino acid sequence of SEQ ID NO: 8 1. [029] In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 4) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 82 or SEQ ID NO. 84; and a DVD light chain amino acid sequence SEQ ID NO. 83 or SEQ ID NO. 85. In an embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 82 and a DVD light chain amino acid sequence of SEQ ID NO: 83. In another embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 84 and a DVD light chain amino acid sequence of SEQ ID NO: 85. [030] In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 86 or SEQ ID NO. 88; and a DVD light chain amino acid sequence SEQ ID NO. 87 or SEQ ID NO. 89. In an embodiment, the binding protein capable of binding L-1 b (seq. 5) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 86 and a DVD light chain amino acid sequence of SEQ ID NO: 87. In another embodiment, the binding protein capable of binding IL- I b (seq. 5) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 88 and a DVD light chain amino acid sequence of SEQ ID NO: 89. [031] In another embodiment, the binding protein capable of binding IL- I b (seq. 1) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 90 or SEQ ID NO. 92; and a DVD light chain amino acid sequence SEQ ID NO. 9 1 or SEQ ID NO. 93. In an embodiment, the binding protein capable of binding L- b (seq. 1) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 90 and a DVD light chain amino acid sequence of SEQ D NO: 91. In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 92 and a DVD light chain amino acid sequence of SEQ ID NO: 93. [032] In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 94 or SEQ ID NO. 96; and a DVD light chain amino acid sequence SEQ ID NO. 95 or SEQ ID NO. 97. In an embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 94 and a DVD light chain amino acid sequence of SEQ ID NO: 95. In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 96 and a DVD light chain amino acid sequence of SEQ ID NO: 97. [033] In another embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 98 or SEQ ID NO. 100; and a DVD light chain amino acid sequence SEQ ID NO. 99 or SEQ ID NO. 101 . in an embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 98 and a DVD light chain amino acid sequence of SEQ ID NO: 99. In another embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-17 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 00 and a DVD light chain amino acid sequence of SEQ ID NO: 10 1. [034] In another embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 102 or SEQ ID NO. 104; and a DVD light chain amino acid sequence SEQ ID NO. 103 or SEQ ID NO. 105. In an embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 102 and a DVD light chain amino acid sequence of SEQ ID NO: 103. In another embodiment, the binding protein capable of binding - b (seq. 4) and IL-17 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 104 and a DVD light chain amino acid sequence of SEQ ID NO: 105. [035] In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 106 or SEQ ID NO. 108; and a DVD light chain amino acid sequence SEQ D NO. 107 or SEQ ID NO. 109. In an embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 106 and a DVD light chain amino acid sequence of SEQ ID NO: 107. In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 108 and a DVD light chain amino acid sequence of SEQ ID NO: 109. [036] In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 110 or SEQ ID NO. 112; and a DVD light chain amino acid sequence SEQ ID NO. 111 or SEQ ID NO. 113. In an embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO.1 10 and a DVD light chain amino acid sequence of SEQ ID NO: 111. In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 1 2 and a DVD light chain amino acid sequence of SEQ ID NO: 113. [037] In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 114 or SEQ ID NO. 116; and a DVD light chain amino acid sequence SEQ ID NO. 115 or SEQ ID NO. 117. In an embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 114 and a DVD light chain amino acid sequence of SEQ ID NO: 15. In another embodiment, the binding protein capable of binding L- b (seq. 2) and IL-17 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ D NO. 1 6 and a DVD light chain amino acid sequence of SEQ ID NO: 117. [038] In another embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ D NO. 118 or SEQ ID NO. 120; and a DVD light chain amino acid sequence SEQ ID NO. 119 or SEQ ID NO. 121 . In an embodiment, the binding protein capable of binding L- b (seq. 3) and IL-1 7 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 118 and a DVD light chain amino acid sequence of SEQ ID NO: 119. In another embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-1 7 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 120 and a DVD light chain amino acid sequence of SEQ ID NO: 121. [039] In another embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-1 7 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 122 or SEQ ID NO. 124; and a DVD light chain amino acid sequence SEQ D NO. 123 or SEQ ID NO. 125. In an embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL- 7 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 122 and a DVD light chain amino acid sequence of SEQ ID NO: 123. In another embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-1 7 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 124 and a DVD light chain amino acid sequence of SEQ ID NO: 125. [040] In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-1 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 126 or SEQ D NO. 128; and a DVD light chain amino acid sequence SEQ ID NO. 127 or SEQ ID NO. 129. In an embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-1 7 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 126 and a DVD light chain amino acid sequence of SEQ ID NO: 127. In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-1 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 128 and a DVD light chain amino acid sequence of SEQ ID NO: 129. [041] In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-1 7 (seq. 2) comprises a DVD heavy chain amino acid sequence SEQ D NO. 130 or SEQ ID NO. 132; and a DVD light chain amino acid sequence SEQ ID NO. 131 or SEQ ID NO. 133. In an embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-1 7 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 130 and a DVD light chain amino acid sequence of SEQ ID NO: 131 . In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-1 7 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 132 and a DVD light chain amino acid sequence of SEQ ID NO: 133. [042] In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and 1L-17 (seq. 2) comprises a DVD heavy chain amino acid sequence SEQ D NO. 134 or SEQ D NO. 136; and a DVD light chain amino acid sequence SEQ ID NO. 135 or SEQ ID NO. 137. In an embodiment, the binding protein capable of binding 1L-1 b (seq. 2) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 134 and a DVD light chain amino acid sequence of SEQ ID NO: 135. In another embodiment, the binding protein capable of binding L- b (seq. 2) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ D NO. 136 and a DVD light chain amino acid sequence of SEQ D NO: 137. [043] In another embodiment, the binding protein capable of binding IL- I b (seq. 2) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 138 or SEQ ID NO. 140; and a DVD light chain amino acid sequence SEQ ID NO. 139 or SEQ ID NO. 141. In an embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 138 and a DVD light chain amino acid sequence of SEQ ID NO: 139. In another embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 140 and a DVD light chain amino acid sequence of SEQ ID NO: 141. [044] In another embodiment, the binding protein capable of binding IL- b (seq. 2) and IL-17 (seq. 4) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 142 or SEQ ID NO. 144; and a DVD light chain amino acid sequence SEQ ID NO. 143 or SEQ ID NO. 145. In an embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 142 and a DVD light chain amino acid sequence of SEQ D NO: 143. In another embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 144 and a DVD light chain amino acid sequence of SEQ ID NO: 145. [045] In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence SEQ D NO. 146 or SEQ ID NO. 148; and a DVD light chain amino acid sequence SEQ ID NO. 147 or SEQ ID NO. 149. In an embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 146 and a DVD light chain amino acid sequence of SEQ ID NO: 147. In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 148 and a DVD light chain amino acid sequence of SEQ ID NO: 149. [046] In another embodiment, the binding protein capable of binding L- b (seq. 1) and IL-1 7 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 150 or SEQ ID NO. 152; and a DVD light chain amino acid sequence SEQ ID NO. 151 or SEQ ID NO. 153. In an embodiment, the binding protein capable of binding IL-1 b (seq. 1) and 1L-17 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 150 and a DVD light chain amino acid sequence of SEQ D NO: 151 . In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-1 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 152 and a DVD light chain amino acid sequence of SEQ ID NO: 153. [047] In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-1 7 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 154 or SEQ D NO. 56; and a DVD light chain amino acid sequence SEQ ID NO. 155 or SEQ ID NO. 157. In an embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-1 7 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 154 and a DVD light chain amino acid sequence of SEQ ID NO: 155. In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-1 7 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ D NO. 156 and a DVD light chain amino acid sequence of SEQ ID NO: 157. [048] In another embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-1 7 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 158 or SEQ D NO. 160; and a DVD light chain amino acid sequence SEQ D NO. 159 or SEQ ID NO. 161. In an embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-1 7 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ D NO. 158 and a DVD light chain amino acid sequence of SEQ ID NO: 159. In another embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-1 7 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 160 and a DVD light chain amino acid sequence of SEQ ID NO: 161. [049] In another embodiment, the binding protein capable of binding L-1 b (seq. 4) and IL-1 7 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 162 or SEQ ID NO. 164; and a DVD light chain amino acid sequence SEQ ID NO. 163 or SEQ ID NO. 165. In an embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-1 7 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 162 and a DVD light chain amino acid sequence of SEQ ID NO: 163. In another embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-1 7 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 164 and a DVD light chain amino acid sequence of SEQ ID NO: 165. [050] In another embodiment, the binding protein capable of binding II_-1 b (seq. 5) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 166 or SEQ ID NO. 168; and a DVD light chain amino acid sequence SEQ ID NO. 167 or SEQ ID NO. 169. In an embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 166 and a DVD light chain amino acid sequence of SEQ ID NO: 167. In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 168 and a DVD light chain amino acid sequence of SEQ ID NO: 169. [051] In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 170 or SEQ ID NO. 172; and a DVD light chain amino acid sequence SEQ ID NO. 171 or SEQ ID NO. 173. In an embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 170 and a DVD light chain amino acid sequence of SEQ ID NO: 171 . In another embodiment, the binding protein capable of binding L-1b (seq. 1) and IL-17 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 172 and a DVD light chain amino acid sequence of SEQ D NO: 173. [052] In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 174 or SEQ ID NO. 176; and a DVD light chain amino acid sequence SEQ ID NO. 175 or SEQ ID NO. 177. In an embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 174 and a DVD light chain amino acid sequence of SEQ ID NO: 175. In another embodiment, the binding protein capable of binding L- b (seq. 2) and IL-17 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 176 and a DVD light chain amino acid sequence of SEQ ID NO: 177. [053] In another embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 78 or SEQ ID NO. 180; and a DVD light chain amino acid sequence SEQ ID NO. 179 or SEQ ID NO. 181 . In an embodiment, the binding protein capable of binding L-1 b (seq. 3) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 178 and a DVD light chain amino acid sequence of SEQ ID NO: 179. In another embodiment, the binding protein capable of binding L- b (seq. 3) and IL-17 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ D NO. 180 and a DVD light chain amino acid sequence of SEQ ID NO: 181 . [054] In another embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 182 or SEQ D NO. 184; and a DVD light chain amino acid sequence SEQ ID NO. 183 or SEQ ID NO. 185. In an embodiment, the binding protein capable of binding L- 1b (seq. 4) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 182 and a DVD light chain amino acid sequence of SEQ ID NO: 183. In another embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-17 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 184 and a DVD light chain amino acid sequence of SEQ ID NO: 185. [055] In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ D NO. 186 or SEQ ID NO. 188; and a DVD light chain amino acid sequence SEQ ID NO. 187 or SEQ ID NO. 189. In an embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 186 and a DVD light chain amino acid sequence of SEQ ID NO: 187. In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 188 and a DVD light chain amino acid sequence of SEQ ID NO: 189. [056] In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 190 or SEQ ID NO. 192; and a DVD light chain amino acid sequence SEQ ID NO. 191 or SEQ ID NO. 193. In an embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 90 and a DVD light chain amino acid sequence of SEQ ID NO: 191. In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 192 and a DVD light chain amino acid sequence of SEQ ID NO: 193. [057] In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 194 or SEQ ID NO. 196; and a DVD light chain amino acid sequence SEQ ID NO. 195 or SEQ ID NO. 197. In an embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 94 and a DVD light chain amino acid sequence of SEQ ID NO: 195. In another embodiment, the binding protein capable of binding L- b (seq. 2) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 196 and a DVD light chain amino acid sequence of SEQ ID NO: 197. [058] In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 98 or SEQ ID NO. 200; and a DVD light chain amino acid sequence SEQ ID NO. 99 or SEQ ID NO. 201. In an embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 198 and a DVD light chain amino acid sequence of SEQ ID NO: 199. In another embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ D NO. 200 and a DVD light chain amino acid sequence of SEQ ID NO: 201. [059] In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 4) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 202 or SEQ ID NO. 204; and a DVD light chain amino acid sequence SEQ ID NO. 203 or SEQ ID NO. 205. In an embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 202 and a DVD light chain amino acid sequence of SEQ ID NO: 203. In another embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 204 and a DVD light chain amino acid sequence of SEQ ID NO: 205. [060] In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 206 or SEQ ID NO. 208; and a DVD light chain amino acid sequence SEQ ID NO. 207 or SEQ ID NO. 209. In an embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 206 and a DVD light chain amino acid sequence of SEQ ID NO: 207. In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 208 and a DVD light chain amino acid sequence of SEQ ID NO: 209. [061 ] In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 210 or SEQ ID NO. 212; and a DVD light chain amino acid sequence SEQ D NO. 2 1 or SEQ D NO. 213. In an embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ D NO. 210 and a DVD light chain amino acid sequence of SEQ ID NO: 2 1 . In another embodiment, the binding protein capable of binding L- b (seq. 1) and IL- 7 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 212 and a DVD light chain amino acid sequence of SEQ D NO: 213. [062] In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ D NO. 214 or SEQ D NO. 216; and a DVD light chain amino acid sequence SEQ ID NO. 215 or SEQ ID NO. 217. In an embodiment, the binding protein capable of binding IL-1 p (seq. 2) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 214 and a DVD light chain amino acid sequence of SEQ D NO: 215. In another embodiment, the binding protein capable of binding IL-1 (seq. 2) and IL-17 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 216 and a DVD light chain amino acid sequence of SEQ ID NO: 217. [063] In another embodiment, the binding protein capable of binding IL-1 p (seq. 3) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 218 or SEQ ID NO. 220; and a DVD light chain amino acid sequence SEQ ID NO. 219 or SEQ ID NO. 221. In an embodiment, the binding protein capable of binding IL- I b (seq. 3) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 218 and a DVD light chain amino acid sequence of SEQ ID NO: 219. In another embodiment, the binding protein capable of binding IL-1 p (seq. 3) and IL-17 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 220 and a DVD light chain amino acid sequence of SEQ ID NO: 221 . [064] In another embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 222 or SEQ ID NO. 224; and a DVD light chain amino acid sequence SEQ ID NO. 223 or SEQ ID NO. 225. In an embodiment, the binding protein capable of binding IL-1 p (seq. 4) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 222 and a DVD light chain amino acid sequence of SEQ ID NO: 223. In another embodiment, the binding protein capable of binding IL-1 p (seq. 4) and IL-17 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 224 and a DVD light chain amino acid sequence of SEQ ID NO: 225. [065] In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 226 or SEQ ID NO. 228; and a DVD light chain amino acid sequence SEQ ID NO. 227 or SEQ D NO. 229. In an embodiment, the binding protein capable of binding IL- I (seq. 5) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ D NO. 226 and a DVD light chain amino acid sequence of SEQ D NO: 227. In another embodiment, the binding protein capable of binding L- b (seq. 5) and IL-17 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 228 and a DVD light chain amino acid sequence of SEQ ID NO: 229. [066] In another embodiment, the binding protein capable of binding !L-1 p (seq. 1) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 230 or SEQ ID NO. 232; and a DVD light chain amino acid sequence SEQ ID NO. 231 or SEQ ID NO. 233. In an embodiment, the binding protein capable of binding IL- b (seq. 1) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO.230 and a DVD light chain amino acid sequence of SEQ ID NO: 231. In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 232 and a DVD light chain amino acid sequence of SEQ ID NO: 233. [067] In another embodiment, the binding protein capable of binding IL-1 p (seq. 2) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ D NO. 234 or SEQ D NO. 236; and a DVD light chain amino acid sequence SEQ ID NO. 235 or SEQ ID NO. 237. In an embodiment, the binding protein capable of binding IL-1 p (seq. 2) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 234 and a DVD light chain amino acid sequence of SEQ ID NO: 235. In another embodiment, the binding protein capable of binding IL- I b (seq. 2) and IL-17 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 236 and a DVD light chain amino acid sequence of SEQ ID NO: 237. [068] In another embodiment, the binding protein capable of binding IL-1 p (seq. 3) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 238 or SEQ ID NO. 240; and a DVD light chain amino acid sequence SEQ ID NO. 239 or SEQ ID NO. 241. In an embodiment, the binding protein capable of binding IL-1 p (seq. 3) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 238 and a DVD light chain amino acid sequence of SEQ ID NO: 239. In another embodiment, the binding protein capable of binding IL-1 p (seq. 3) and IL-17 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 240 and a DVD light chain amino acid sequence of SEQ ID NO: 241. [069] In another embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 242 or SEQ ID NO. 244; and a DVD light chain amino acid sequence SEQ ID NO. 243 or SEQ ID NO. 245. In an embodiment, the binding protein capable of binding L- b (seq. 4) and IL-1 7 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 242 and a DVD light chain amino acid sequence of SEQ ID NO: 243. In another embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL- (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 244 and a DVD light chain amino acid sequence of SEQ D NO: 245. [070] In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 246 or SEQ ID NO. 248; and a DVD light chain amino acid sequence SEQ ID NO. 247 or SEQ ID NO. 249. In an embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 1) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 246 and a DVD light chain amino acid sequence of SEQ ID NO: 247. In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 1) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 248 and a DVD light chain amino acid sequence of SEQ ID NO: 249. [071] In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 250 or SEQ D NO. 252; and a DVD light chain amino acid sequence SEQ ID NO. 251 or SEQ ID NO. 253. In an embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 250 and a DVD light chain amino acid sequence of SEQ ID NO: 251. In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 252 and a DVD light chain amino acid sequence of SEQ ID NO: 253. [072] In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 254 or SEQ ID NO. 256; and a DVD light chain amino acid sequence SEQ ID NO. 255 or SEQ ID NO. 257. In an embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 254 and a DVD light chain amino acid sequence of SEQ ID NO: 255. In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 256 and a DVD light chain amino acid sequence of SEQ ID NO: 257. [073] In another embodiment, the binding protein capable of binding IL- b (seq. 2) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 258 or SEQ ID NO. 260; and a DVD light chain amino acid sequence SEQ D NO. 259 or SEQ ID NO. 261 . In an embodiment, the binding protein capable of binding L- b (seq. 3) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 258 and a DVD light chain amino acid sequence of SEQ ID NO: 259. In another embodiment, the binding protein capable of binding IL-1 p (seq. 3) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 260 and a DVD light chain amino acid sequence of SEQ ID NO: 261. [074] In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-17 (seq. 4) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 262 or SEQ ID NO. 264; and a DVD light chain amino acid sequence SEQ D NO. 263 or SEQ ID NO. 265. In an embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 262 and a DVD light chain amino acid sequence of SEQ ID NO: 263. In another embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 264 and a DVD light chain amino acid sequence of SEQ ID NO: 265. [075] In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-1 (seq. 2) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 266 or SEQ ID NO. 268; and a DVD light chain amino acid sequence SEQ ID NO. 267 or SEQ ID NO. 269. In an embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 2) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 266 and a DVD light chain amino acid sequence of SEQ ID NO: 267. In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-17 (seq. 2) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 268 and a DVD light chain amino acid sequence of SEQ ID NO: 269. [076] In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 270 or SEQ ID NO. 272; and a DVD light chain amino acid sequence SEQ ID NO. 271 or SEQ ID NO. 273. In an embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 270 and a DVD light chain amino acid sequence of SEQ ID NO: 271. In another embodiment, the binding protein capable of binding IL-1 b (seq. 1) and IL-17 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 272 and a DVD light chain amino acid sequence of SEQ ID NO: 273. [077] In another embodiment, the binding protein capable of binding L- b (seq. 2) and IL-1 7 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 274 or SEQ ID NO. 276; and a DVD light chain amino acid sequence SEQ ID NO. 275 or SEQ ID NO. 277. In an embodiment, the binding protein capable of binding IL-1p (seq. 2) and IL-1 7 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 274 and a DVD light chain amino acid sequence of SEQ D NO: 275. In another embodiment, the binding protein capable of binding IL-1 b (seq. 2) and IL-1 7 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 276 and a DVD light chain amino acid sequence of SEQ ID NO: 277. [078] In another embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-1 7 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 278 or SEQ D NO. 280; and a DVD light chain amino acid sequence SEQ ID NO. 279 or SEQ ID NO. 281 . In an embodiment, the binding protein capable of binding IL-1 b (seq. 3) and IL-1 7 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 278 and a DVD light chain amino acid sequence of SEQ ID NO: 279. In another embodiment, the binding protein capable of binding L-1 b (seq. 3) and IL-1 7 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 280 and a DVD light chain amino acid sequence of SEQ ID NO: 281 . [079] In another embodiment, the binding protein capable of binding L-1 b (seq. 4) and IL-1 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 282 or SEQ ID NO. 284; and a DVD light chain amino acid sequence SEQ ID NO. 283 or SEQ ID NO. 285. In an embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-1 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 282 and a DVD light chain amino acid sequence of SEQ D NO: 283. In another embodiment, the binding protein capable of binding IL-1 b (seq. 4) and IL-1 7 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 284 and a DVD light chain amino acid sequence of SEQ ID NO: 285. [080] In another embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-1 7 (seq. 3) comprises a DVD heavy chain amino acid sequence SEQ ID NO. 286 or SEQ ID NO. 288; and a DVD light chain amino acid sequence SEQ ID NO. 287 or SEQ ID NO. 289. In an embodiment, the binding protein capable of binding IL-1 b (seq. 5) and IL-1 7 (seq. 3) comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 286 and a DVD light chain amino acid sequence of SEQ ID NO: 287. In another embodiment, the binding protein capable of binding 1L-1 b (seq. 5) and IL-17 (seq. 3) has a reverse orientation and comprises a DVD heavy chain amino acid sequence of SEQ ID NO. 288 and a DVD light chain amino acid sequence of SEQ ID NO: 289. [081] In another embodiment, a binding protein comprising a polypeptide chain, wherein said polypeptide chain comprises VD1-(X1)n-VD2-C-(X2)n, wherein; VD1 is a first heavy chain variable domain obtained from a first parent antibody, or antigen binding portion thereof; VD2 is a second heavy chain variable domain obtained from a second parent antibody, or antigen binding portion thereof, which can be the same or different from the first parent antibody; C is a heavy chain constant domain; (X1)n is a linker with the proviso that it is not CH1 , wherein said (X1)n is either present or absent; and (X2)n is an Fc region, wherein said (X2)n is either present or absent is provided. In an embodiment, the Fc region is absent from the binding protein. [082] In another embodiment, a binding protein comprising a polypeptide chain, wherein said polypeptide chain comprises VD1-(X1)n-VD2-C-(X2)n, wherein, VD1 is a first light chain variable domain obtained from a first parent antibody or antigen binding portion thereof; VD2 is a second light chain variable domain obtained from a second parent antibody or antigen binding portion thereof, which can be the same or different from the first parent antibody; C is a light chain constant domain; (X1)n is a linker with the proviso that it is not CH1 , wherein said (X1)n is either present or absent; and (X2)n does not comprise an Fc region, wherein said (X2)n is either present or absent is provided. In an embodiment, (X2)n is absent from the binding protein. [083] In another embodiment, the binding protein comprises first and second polypeptide chains, wherein said first polypeptide chain comprises a first VD1-(X1)n- VD2-C-(X2)n, wherein VD1 is a first heavy chain variable domain obtained from a first parent antibody or antigen binding portion thereof; VD2 is a second heavy chain variable domain obtained from a second parent antibody or antigen binding portion thereof, which can be the same or different from the first parent antibody; C is a heavy chain constant domain; (X1)n is a linker with the proviso that it is not CH1 , wherein said (X1)n is either present or absent; and (X2)n is an Fc region, wherein said (X2)n is either present or absent; and wherein said second polypeptide chain comprises a second VD1-(X1)n- VD2-C-(X2)n, wherein VD1 is a first light chain variable domain obtained from a first parent antibody or antigen binding portion thereof; VD2 is a second light chain variable domain obtained from a second parent antibody or antigen binding portion thereof, which can be the same or different from the first parent antibody; C is a light chain constant domain; (X1)n is a linker with the proviso that it is not CH1 , wherein said (X1)n is either present or absent; and (X2)n does not comprise an Fc region, wherein said (X2)n is either present or absent. In another embodiment, the binding protein comprises two first polypeptide chains and two second polypeptide chains. In yet another embodiment, (X2)n is absent from the second polypeptide. In still another embodiment, the Fc region, if present in the first polypeptide is a native sequence Fc region or a variant sequence Fc region. In still another embodiment, the Fc region is an Fc region from an lgG1, an Fc region from an lgG2, an Fc region from an lgG3, an Fc region from an lgG4, an Fc region from an IgA, an Fc region from an IgM, an Fc region from an IgE, or an Fc region from an IgD. [084] In another embodiment, the binding protein is a DVD-lg that binds two antigens comprising four polypeptide chains, wherein, each of the first and third polypeptide chains comprise VD1-(X1)n-VD2-C-(X2)n, wherein,VD1 is a first heavy chain variable domain obtained from a first parent antibody, or antigen binding portion thereof; VD2 is a second heavy chain variable domain obtained from a second parent antibody, or antigen binding portion thereof, which can be the same as or different from the first parent antibody; C is a heavy chain constant domain; (X1)n is a linker with the proviso that it is not CH1, wherein said (X1)n is either present or absent; and (X2)n is an Fc region, wherein said (X2)n is either present or absent; and wherein each of the second and fourth polypeptide chains comprise VD1-(X1)n-VD2-C-(X2)n, wherein VD1 is a first light chain variable domain obtained from a first parent antibody or antigen binding portion thereof; VD2 is a second light chain variable domain obtained from a second parent antibody, or antigen binding portion thereof, which can be the same as or different from the first parent antibody; C is a light chain constant domain; (X1)n is a linker with the proviso that it is not CH1 , wherein said (X1)n is either present or absent; and (X2)n does not comprise an Fc region, wherein said (X2)n is either present or absent. [085] A method of making a DVD-lg binding protein by preselecting the parent antibodies is provided. In an embodiment, the method of making a Dual Variable Domain Immunoglobulin that binds two antigens comprises the steps of a) obtaining a first parent antibody, or antigen binding portion thereof, that binds a first antigen; b) obtaining a second parent antibody or antigen binding portion thereof, that binds a second antigen; c) constructing first and third polypeptide chains, each of which comprises VD1-(X1)n- VD2-C-(X2)n, wherein, VD1 is a first heavy chain variable domain obtained from said first parent antibody, or antigen binding portion thereof; VD2 is a second heavy chain variable domain obtained from said second parent antibody or antigen binding portion thereof, which can be the same as or different from the first parent antibody; C is a heavy chain constant domain; (X1)n is a linker with the proviso that it is not CH1 , wherein said (X1)n is either present or absent; and (X2)n is an Fc region, wherein said (X2)n is either present or absent; ) constructing second and fourth polypeptide chains each of which comprises VD1-(X1)n-VD2-C-(X2)n, wherein, VD1 is a first light chain variable domain obtained from said first parent antibody, or antigen binding portion thereof; VD2 is a second light chain variable domain obtained from said second parent antibody, or antigen binding thereof, which can be the same as or different from the first parent antibody; C is a light chain constant domain; (X1)n is a linker with the proviso that it is not CH1 , wherein said (X1)n is either present or absent; and (X2)n does not comprise an Fc region, wherein said (X2)n is either present or absent; and e) expressing said first, second, third and fourth polypeptide chains; such that a DVD-lg binds said first antigen and said second antigen is generated. [086] In still another embodiment, a method of generating a DVD-lg that binds two antigens with desired properties comprising the steps of a) obtaining a first parent antibody, or antigen binding portion thereof, that binds a first antigen and possessing at least one desired property exhibited by the DVD-lg; b) obtaining a second parent antibody, or antigen binding portion thereof, which can be the same as or different from the first parent antibody, can bind to a second antigen and possesses at least one desired property exhibited by the Dual Variable Domain Immunoglobulin; c) constructing first and third polypeptide chains comprising VD1-(X1)n-VD2-C-(X2)n, wherein; VD1 is a first heavy chain variable domain obtained from said first parent antibody, or antigen binding portion thereof; VD2 is a second heavy chain variable domain obtained from said second parent antibody, or antigen binding portion thereof; C is a heavy chain constant domain; (X1)n is a linker with the proviso that it is not CH1 , wherein said (X1)n is either present or absent; and (X2)n is an Fc region, wherein said (X2)n is either present or absent; d) constructing second and fourth polypeptide chains comprising VD1-(X1)n- VD2-C-(X2)n, wherein; VD1 is a first light chain variable domain obtained from said first parent antibody, or antigen binding portion thereof; VD2 is a second light chain variable domain obtained from said second parent antibody, or antigen binding portion thereof), which can be the same as or different from the first parent antibody; C is a light chain constant domain; (X1)n is a linker with the proviso that it is not CH1 , wherein said (X1)n is either present or absent; and (X2)n does not comprise an Fc region, wherein said (X2)n is either present or absent; e) expressing said first, second, third and fourth polypeptide chains; such that a Dual Variable Domain Immunoglobulin capable of binding said first and said second antigen with desired properties is generated is provided. [087] In one embodiment, the VDI of the first and second polypeptide chains disclosed herein are obtained from the same parent antibody or antigen binding portion thereof. In another embodiment, the VDI of the first and second polypeptide chains disclosed herein are obtained from different parent antibodies or antigen binding portions thereof. In another embodiment, the VD2 of the first and second polypeptide chains disclosed herein are obtained from the same parent antibody or antigen binding portion thereof. In another embodiment, the VD2 of the first and second polypeptide chains disclosed herein are obtained from different parent antibodies or antigen binding portions thereof. [088] In one embodiment the first parent antibody or antigen binding portion thereof, and the second parent antibody or antigen binding portion thereof, are the same antibody. In another embodiment the first parent antibody or antigen binding portion thereof, and the second parent antibody or antigen binding portion thereof, are different antibodies. [089] In one embodiment the first parent antibody or antigen binding portion thereof, binds a first antigen and the second parent antibody or antigen binding portion thereof, binds a second antigen. In a particular embodiment, the first and second antigens are the same antigen. In another embodiment, the parent antibodies bind different epitopes on the same antigen. In another embodiment the first and second antigens are different antigens. In another embodiment, the first parent antibody or antigen binding portion thereof, binds the first antigen with a potency different from the potency with which the second parent antibody or antigen binding portion thereof, binds the second antigen. In yet another embodiment, the first parent antibody or antigen binding portion thereof, binds the first antigen with an affinity different from the affinity with which the second parent antibody or antigen binding portion thereof, binds the second antigen. [090] In another embodiment the first parent antibody or antigen binding portion thereof, and the second parent antibody or antigen binding portion thereof, are human antibodies, CDR grafted antibodies, or humanized antibodies. In an embodiment, the antigen binding portions are Fab fragments, F(ab')2 fragments, bivalent fragments comprising two Fab fragments linked by a disulfide bridge at the hinge region, Fd fragments consisting of the VH and CH1 domains; Fv fragments consisting of the VL and VH domains of a single arm of an antibody, dAb fragments, isolated complementarity determining regions (CDR), single chain antibodies, or diabodies. [091] In another embodiment, the binding protein possesses at least one desired property exhibited by the first parent antibody or antigen binding portion thereof, or the second parent antibody or antigen binding portion thereof. Alternatively, the first parent antibody or antigen binding portion thereof and the second parent antibody or antigen binding portion thereof possess at least one desired property exhibited by the Dual Variable Domain Immunoglobulin. In an embodiment, the desired property is selected from one or more antibody parameters. In another embodiment, the antibody parameters are antigen specificity, affinity to antigen, potency, biological function, epitope recognition, stability, solubility, production efficiency, immunogenicity, pharmacokinetics, bioavailability, tissue cross reactivity, or orthologous antigen binding. In an embodiment the binding protein is multivalent. In another embodiment, the binding protein is multispecific. The multivalent and or multispecific binding proteins described herein have desirable properties particularly from a therapeutic standpoint. For instance, the multivalent and or multispecific binding protein may (1) be internalized (and/or catabolized) faster than a bivalent antibody by a cell expressing an antigen to which the antibodies bind; (2) be an agonist antibody; and/or (3) induce cell death and/or apoptosis of a cell expressing an antigen to which the multivalent antibody binds. The "parent antibody," which provides at least one antigen binding specificity of the multivalent and/ or multispecific binding proteins, may be one which is internalized (and/or catabolized) by a cell expressing an antigen to which the antibody binds; and/or may be an agonist, cell death-inducing, and/or apoptosis-inducing antibody, and the multivalent and or multispecific binding protein as described herein may display improvement(s) in one or more of these properties. Moreover, the parent antibody may lack any one or more of these properties, but may be endowed with them when constructed as a multivalent binding protein as described herein. [092] In another embodiment, the binding protein has an on rate constant (Kon) to one or more targets of: at least about 0 MV 1;at least about 103MV ;at least about 10 M s ; at least about 0 M s 1 ; or at least about 106M V ,as measured by surface plasmon resonance. In an embodiment, the binding protein has an on rate constant (Kon) to one or more targets between about 102MV1and about 103M1s 1 ; between about 103M V and about 104M s 1 ; between about 10 M_ s 1 and about 10 M s ; or between about 10 M 1s 1 and about 10 MV 1,as measured by surface plasmon resonance. [093] In another embodiment the binding protein has an off rate constant (Koff) for one or more targets of: at most about 0 3s ; at most about 0V1;at most about 10 V ;or at most about 10 s 1 , as measured by surface plasmon resonance. In an embodiment, the binding protein has an off rate constant (Koff) to one or more targets of from about 10 3s 1 to about 0 V ;of from about 10 4s 1 to about 10 V ;or of from about 10 5s to about 10 s , as measured by surface plasmon resonance. [094] In another embodiment the binding protein has a dissociation constant (KD) to one or more targets of: at most about 0 7M; at most about 10 M; at most about 0 M; at most about 10 M; at most about 0 M; at most about 10 2M; or at most about 10 13M. In an embodiment, the binding protein has a dissociation constant (KD) to its targets of from about 10 M to about 10 8M; of from about 0 8M to about 0 9 ; of from about 10 to about 10 M; of fromabout 10 M to about 10 M; of from about 10 M to about 10 2M; or of from about 10 2M to about 10 M. [095] In another embodiment, the binding protein described herein is a conjugate further comprising an agent. In some embodiments, the agent is an immunoadhesion molecule, an imaging agent, a therapeutic agent, or a cytotoxic agent. In an embodiment, the imaging agent is a radiolabel, an enzyme, a fluorescent label, a luminescent label, a bioluminescent label, a magnetic label, or biotin. In another embodiment, the radiolabel is: 3H, C 3 S, 0Y, "Tc, 1ln, 2 l , 3 l , 1 Lu, Ho, or 3Sm. In yet another embodiment, the therapeutic or cytotoxic agent is an anti-metabolite, an alkylating agent, an antibiotic, a growth factor, a cytokine, an anti-angiogenic agent, an anti-mitotic agent, an anthracycline, toxin, or an apoptotic agent. [096] In another embodiment, the binding protein described herein is a crystallized binding protein and exists as a crystal. In an embodiment, the crystal is a carrier-free pharmaceutical controlled release crystal. In yet another embodiment, the crystallized binding protein has a greater half life in vivo than the soluble counterpart of said binding protein. In still another embodiment, the crystallized binding protein retains biological activity. [097] In another embodiment, the binding protein described herein is glycosylated. For example, the glycosylation is a human glycosylation pattern. [098] An isolated nucleic acid encoding any one of the binding proteins disclosed herein is provided. A further embodiment provides a vector comprising the isolated nucleic acid disclosed herein wherein said vector is pcDNA; pTT (Durocher et al. (2002) Nucl. Acids Res. 30: 2); pTT3 (pTT with additional multiple cloning site; pEFBOS (Mizushima, S. and Nagata, S. (1990) Nucl. Acids Res. 18: 17); pBV; pJV; pcDNA3.1 TOPO; pEF6 TOPO; or pBJ. In an embodiment, the vector is a vector disclosed in U.S. Patent Publication No. 2009/0239259. [099] In another aspect a host cell is transformed with the vector disclosed herein. In an embodiment, the host cell is a prokaryotic cell. In another embodiment, the host cell is E.coli. In a related embodiment the host cell is a eukaryotic cell. In another embodiment, the eukaryotic cell is a protist cell, an animal cell, a plant cell, or a fungal cell. In yet another embodiment, the host cell is a mammalian cell including, but not limited to, CHO, COS; NSO, SP2, PER.C6 or a fungal cell, such as Saccharomyces cerevisiae; or an insect cell such as Sf9. [0100] In an embodiment, two or more DVD-lgs, e.g., with different specificities, are produced in a single recombinant host cell. For example, the expression of a mixture of antibodies has been called Oligoclonics™ (Merus B.V., The Netherlands); U.S. Patent Nos. 7,262,028; 7,429,486. [0101] A method of producing a binding protein disclosed herein comprising culturing any one of the host cells also disclosed herein in a culture medium under conditions sufficient to produce the binding protein is provided. In an embodiment, 50%- 75% of the binding protein produced by this method is a dual specific tetravalent binding protein. In a particular embodiment, 75%-90% of the binding protein produced by this method is a dual specific tetravalent binding protein. In a particular embodiment, 90%- 95% of the binding protein produced is a dual specific tetravalent binding protein. [0102] One embodiment provides a composition for the release of a binding protein wherein the composition comprises a formulation that in turn comprises a crystallized binding protein, as disclosed herein, and an ingredient, and at least one polymeric carrier. In another embodiment, the polymeric carrier comprises one or more polymers. In some embodiments, the polymers are poly (acrylic acid), poly (cyanoacrylates), poly (amino acids), poly (anhydrides), poly (depsipeptide), poly (esters), poly (lactic acid), poly (lactic-co-glycolic acid) or PLGA, poly (bhydroxybutryate), poly (caprolactone), poly (dioxanone); poly (ethylene glycol), poly ((hydroxypropyl) methacrylamide, poly [(organo)phosphazene], poly (ortho esters), poly (vinyl alcohol), poly (vinylpyrrolidone), maleic anhydride- alkyl vinyl ether copolymers, pluronic polyols, albumin, alginate, cellulose and cellulose derivatives, collagen, fibrin, gelatin, hyaluronic acid, oligosaccharides, glycaminoglycans, sulfated polysaccharides, or blends or copolymers thereof. In some embodiments, the ingredient is albumin, sucrose, trehalose, lactitol, gelatin, hydroxypropyl- b- cyclodextrin, methoxypolyethylene glycol or polyethylene glycol. Another embodiment provides a method for treating a mammal comprising the step of administering to the mammal an effective amount of the composition disclosed herein. [0103] A pharmaceutical composition comprising a binding protein, as disclosed herein and a pharmaceutically acceptable carrier is provided. In a further embodiment the pharmaceutical composition comprises at least one additional therapeutic agent for treating a disorder. In some embodiments, the additional agent is: a therapeutic agent, an imaging agent, a cytotoxic agent, an angiogenesis inhibitor (including but not limited to an anti-VEGF antibody or a VEGF-trap), a kinase inhibitor (including but not limited to a KDR and a TIE-2 inhibitor), a co-stimulation molecule blocker (including but not limited to anti-B7.1, anti-B7.2, CTLA4-lg, anti-CD20), an adhesion molecule blocker (including but not limited to an anti-LFA-1 antibody, an anti-E/L selectin antibody, a small molecule inhibitor), an anti-cytokine antibody or functional fragment thereof (including but not limited to an anti-IL-18, an anti-TNF, and an anti-IL-6/cytokine receptor antibody), methotrexate, cyclosporin, rapamycin, FK506, a detectable label or reporter, a TNF antagonist, an antirheumatic, a muscle relaxant, a narcotic, a non-steroid anti¬ inflammatory drug (NSAID), an analgesic, an anesthetic, a sedative, a local anesthetic, a neuromuscular blocker, an antimicrobial, an antipsoriatic, a corticosteriod, an anabolic steroid, an erythropoietin, an immunization, an immunoglobulin, an immunosuppressive, a growth hormone, a hormone replacement drug, a radiopharmaceutical, an antidepressant, an antipsychotic, a stimulant, an asthma medication, a beta agonist, an inhaled steroid, an epinephrine or analog, a cytokine, or a cytokine antagonist. [0104] A method for treating a human subject suffering from a disorder in which the target, or targets, that can be bound by the binding protein disclosed herein is/are detrimental, comprising administering to the human subject a binding protein disclosed herein such that the activity of the target, or targets in the human subject is inhibited and one of more symptoms is alleviated or treatment is achieved is provided. For example, the disorder is arthritis, osteoarthritis, juvenile chronic arthritis, septic arthritis, Lyme arthritis, psoriatic arthritis, reactive arthritis, spondyloarthropathy, systemic lupus erythematosus, Crohn's disease, ulcerative colitis, inflammatory bowel disease, insulin dependent diabetes mellitus, thyroiditis, asthma, allergic diseases, psoriasis, dermatitis scleroderma, graft versus host disease, organ transplant rejection, acute or chronic immune disease associated with organ transplantation, sarcoidosis, atherosclerosis, disseminated intravascular coagulation, Kawasaki's disease, Grave's disease, nephrotic syndrome, chronic fatigue syndrome, Wegener's granulomatosis, Henoch-Schoenlein purpurea, microscopic vasculitis of the kidneys, chronic active hepatitis, uveitis, septic shock, toxic shock syndrome, sepsis syndrome, cachexia, infectious diseases, parasitic diseases, acquired immunodeficiency syndrome, acute transverse myelitis, Huntington's chorea, Parkinson's disease, Alzheimer's disease, stroke, primary biliary cirrhosis, hemolytic anemia, malignancies, heart failure, myocardial infarction, Addison's disease, sporadic polyglandular deficiency type I and polyglandular deficiency type II, Schmidt's syndrome, adult (acute) respiratory distress syndrome, alopecia, alopecia areata, seronegative arthopathy, arthropathy, Reiter's disease, psoriatic arthropathy, ulcerative oolitic arthropathy, enteropathic synovitis, chlamydia, yersinia and salmonella associated arthropathy, spondyloarthopathy, atheromatous disease/arteriosclerosis, atopic allergy, autoimmune bullous disease, pemphigus vulgaris, pemphigus foliaceus, pemphigoid, linear IgA disease, autoimmune haemolytic anaemia, Coombs positive haemolytic anaemia, acquired pernicious anaemia, juvenile pernicious anaemia, myalgic encephalitis/Royal Free Disease, chronic mucocutaneous candidiasis, giant cell arteritis, primary sclerosing hepatitis, cryptogenic autoimmune hepatitis, Acquired Immunodeficiency Disease Syndrome, Acquired Immunodeficiency Related Diseases, Hepatitis B, Hepatitis C, common varied immunodeficiency (common variable hypogammaglobulinaemia), dilated cardiomyopathy, female infertility, ovarian failure, premature ovarian failure, fibrotic lung disease, cryptogenic fibrosing alveolitis, post¬ inflammatory interstitial lung disease, interstitial pneumonitis, connective tissue disease associated interstitial lung disease, mixed connective tissue disease associated iung disease, systemic sclerosis associated interstitial lung disease, rheumatoid arthritis associated interstitial lung disease, systemic lupus erythematosus associated lung disease, dermatomyositis/polymyositis associated lung disease, Sjogren's disease associated lung disease, ankylosing spondylitis associated lung disease, vasculitic diffuse lung disease, haemosiderosis associated lung disease, drug-induced interstitial lung disease, fibrosis, radiation fibrosis, bronchiolitis obliterans, chronic eosinophilic pneumonia, lymphocytic infiltrative lung disease, postinfectious interstitial lung disease, gouty arthritis, autoimmune hepatitis, type-1 autoimmune hepatitis (classical autoimmune or lupoid hepatitis), type-2 autoimmune hepatitis (anti-LKM antibody hepatitis), autoimmune mediated hypoglycemia, type B insulin resistance with acanthosis nigricans, hypoparathyroidism, acute immune disease associated with organ transplantation, chronic immune disease associated with organ transplantation, osteoarthrosis, primary sclerosing cholangitis, psoriasis type 1, psoriasis type 2, idiopathic leucopaenia, autoimmune neutropaenia, renal disease NOS, glomerulonephritides, microscopic vasulitis of the kidneys, lyme disease, discoid lupus erythematosus, male infertility idiopathic or NOS, sperm autoimmunity, multiple sclerosis (all subtypes), sympathetic ophthalmia, pulmonary hypertension secondary to connective tissue disease, Goodpasture's syndrome, pulmonary manifestation of polyarteritis nodosa, acute rheumatic fever, rheumatoid spondylitis, Still's disease, systemic sclerosis, Sjorgren's syndrome, Takayasu's disease/arteritis, autoimmune thrombocytopaenia, idiopathic thrombocytopaenia, autoimmune thyroid disease, hyperthyroidism, goitrous autoimmune hypothyroidism (Hashimoto's disease), atrophic autoimmune hypothyroidism, primary myxoedema, phacogenic uveitis, primary vasculitis, vitiligo acute liver disease, chronic liver diseases, alcoholic cirrhosis, alcohol-induced liver injury, choleosatatis, idiosyncratic liver disease, Drug-Induced hepatitis, Non-alcoholic Steatohepatitis, allergy and asthma, group B streptococci (GBS) infection, mental disorders (e.g., depression and schizophrenia), Th2 Type and Th1 Type mediated diseases, acute and chronic pain (different forms of pain), and cancers such as lung, breast, stomach, bladder, colon, pancreas, ovarian, prostate and rectal cancer and hematopoietic malignancies (leukemia and lymphoma), Abetalipoprotemia, Acrocyanosis, acute and chronic parasitic or infectious processes, acute leukemia, acute lymphoblastic leukemia (ALL), acute myeloid leukemia (AML), acute or chronic bacterial infection, acute pancreatitis, acute renal failure, adenocarcinomas, aerial ectopic beats, AIDS dementia complex, alcoholinduced hepatitis, allergic conjunctivitis, allergic contact dermatitis, allergic rhinitis, allograft rejection, alpha-l- antitrypsin deficiency, amyotrophic lateral sclerosis, anemia, angina pectoris, anterior horn cell degeneration, anti cd3 therapy, antiphospholipid syndrome, anti-receptor hypersensitivity reactions, aortic and peripheral aneuryisms, aortic dissection, arterial hypertension, arteriosclerosis, arteriovenous fistula, ataxia, atrial fibrillation (sustained or paroxysmal), atrial flutter, atrioventricular block, B cell lymphoma, bone graft rejection, bone marrow transplant (BMT) rejection, bundle branch block, Burkitt's lymphoma, Burns, cardiac arrhythmias, cardiac stun syndrome, cardiac tumors, cardiomyopathy, cardiopulmonary bypass inflammation response, cartilage transplant rejection, cerebellar cortical degenerations, cerebellar disorders, chaotic or multifocal atrial tachycardia, chemotherapy associated disorders, chronic myelocytic leukemia (CML), chronic alcoholism, chronic inflammatory pathologies, chronic lymphocytic leukemia (CLL), chronic obstructive pulmonary disease (COPD), chronic salicylate intoxication, colorectal carcinoma, congestive heart failure, conjunctivitis, contact dermatitis, cor pulmonale, coronary artery disease, Creutzfeldt-Jakob disease, culture negative sepsis, cystic fibrosis, cytokine therapy associated disorders, Dementia pugilistica, demyelinating diseases, dengue hemorrhagic fever, dermatitis, dermatologic conditions, diabetes, diabetes mellitus, diabetic ateriosclerotic disease, Diffuse Lewy body disease, dilated congestive cardiomyopathy, disorders of the basal ganglia, Down's Syndrome in middle age, drug- induced movement disorders induced by drugs which block CNS dopamine receptors, drug sensitivity, eczema, encephalomyelitis, endocarditis, endocrinopathy, epiglottitis, epstein-barr virus infection, erythromelalgia, extrapyramidal and cerebellar disorders, familial hematophagocytic lymphohistiocytosis, fetal thymus implant rejection, Friedreich's ataxia, functional peripheral arterial disorders, fungal sepsis, gas gangrene, gastric ulcer, glomerular nephritis, graft rejection of any organ or tissue, gram negative sepsis, gram positive sepsis, granulomas due to intracellular organisms, hairy cell leukemia, Hallerrorden-Spatz disease, hashimoto's thyroiditis, hay fever, heart transplant rejection, hemachromatosis, hemodialysis, hemolytic uremic syndrome/thrombolytic thrombocytopenic purpura, hemorrhage, hepatitis (A), His bundle arrythmias, HIV infection/HIV neuropathy, Hodgkin's disease, hyperkinetic movement disorders, hypersensitity reactions, hypersensitivity pneumonitis, hypertension, hypokinetic movement disorders, hypothalamic-pituitary-adrenal axis evaluation, idiopathic Addison's disease, idiopathic pulmonary fibrosis, antibody mediated cytotoxicity, Asthenia, infantile spinal muscular atrophy, inflammation of the aorta, influenza a, ionizing radiation exposure, iridocyclitis/uveitis/optic neuritis, ischemiareperfusion injury, ischemic stroke, juvenile rheumatoid arthritis, juvenile spinal muscular atrophy, Kaposi's sarcoma, kidney transplant rejection, legionella, leishmaniasis, leprosy, lesions of the corticospinal system, lipedema, liver transplant rejection, lymphederma, malaria, malignamt Lymphoma, malignant histiocytosis, malignant melanoma, meningitis, meningococcemia, metabolic/idiopathic diseases, migraine headache, mitochondrial multi.system disorder, mixed connective tissue disease, monoclonal gammopathy, multiple myeloma, multiple systems degenerations (Mencel Dejerine- Thomas Shi-Drager and Machado-Joseph), myasthenia gravis, mycobacterium avium intracellulare, mycobacterium tuberculosis, myelodyplastic syndrome, myocardial infarction, myocardial ischemic disorders, nasopharyngeal carcinoma, neonatal chronic lung disease, nephritis, nephrosis, neurodegenerative diseases, neurogenic muscular atrophies, neutropenic fever, non- hodgkins lymphoma, occlusion of the abdominal aorta and its branches, occlusive arterial disorders, okt3 therapy, orchitis/epidydimitis, orchitis/vasectomy reversal procedures, organomegaly, osteoporosis, pancreas transplant rejection, pancreatic carcinoma, paraneoplastic syndrome/hypercalcemia of malignancy, parathyroid transplant rejection, pelvic inflammatory disease, perennial rhinitis, pericardial disease, peripheral atherosclerotic disease, peripheral vascular disorders, peritonitis, pernicious anemia, Pneumocystis carinii pneumonia, pneumonia, POEMS syndrome (polyneuropathy, organomegaly, endocrinopathy, monoclonal gammopathy, and skin changes syndrome), post perfusion syndrome, post pump syndrome, post-MI cardiotomy syndrome, preeclampsia, Progressive supranucleo Palsy, primary pulmonary hypertension, radiation therapy, Raynaud's phenomenon and disease, Raynoud's disease, Refsum's disease, regular narrow QRS tachycardia, renovascular hypertension, reperfusion injury, restrictive cardiomyopathy, sarcomas, scleroderma, senile chorea, Senile Dementia of Lewy body type, seronegative arthropathies, shock, sickle cell anemia, skin allograft rejection, skin changes syndrome, small bowel transplant rejection, solid tumors, specific arrythmias, spinal ataxia, spinocerebellar degenerations, streptococcal myositis, structural lesions of the cerebellum, Subacute sclerosing panencephalitis, Syncope, syphilis of the cardiovascular system, systemic anaphalaxis, systemic inflammatory response syndrome, systemic onset juvenile rheumatoid arthritis, T-cell or FAB ALL, Telangiectasia, thromboangitis obliterans, thrombocytopenia, toxicity, transplants, trauma/hemorrhage, type III hypersensitivity reactions, type IV hypersensitivity, unstable angina, uremia, urosepsis, urticaria, valvular heart diseases, varicose veins, .vasculitis, venous diseases, venous thrombosis, ventricular fibrillation, viral and fungal infections, vital encephalitis/aseptic meningitis, vital-associated hemaphagocytic syndrome, Wernicke- Korsakoff syndrome, Wilson's disease, xenograft rejection of any organ or tissue, acute coronary syndromes, acute idiopathic polyneuritis, acute inflammatory demyelinating polyradiculoneuropathy, acute ischemia, adult Still's disease, alopecia areata, anaphylaxis, anti-phospholipid antibody syndrome, aplastic anemia, arteriosclerosis, atopic eczema, atopic dermatitis, autoimmune dermatitis, autoimmune disorder associated with streptococcus infection, autoimmune enteropathy, autoimmune hearing loss, autoimmune lymphoproliferative syndrome (ALPS), autoimmune myocarditis, autoimmune premature ovarian failure, blepharitis, bronchiectasis, bullous pemphigoid, cardiovascular disease, catastrophic antiphospholipid syndrome, celiac disease, cervical spondylosis, chronic ischemia, cicatricial pemphigoid, clinically isolated syndrome (cis) with risk for multiple sclerosis, conjunctivitis, childhood onset psychiatric disorder, chronic obstructive pulmonary disease (COPD), dacryocystitis, dermatomyositis, diabetic retinopathy, diabetes mellitus, disk herniation, disk prolaps, drug induced immune hemolytic anemia, endocarditis, endometriosis, endophthalmitis, episcleritis, erythema multiforme, erythema multiforme major, gestational pemphigoid, Guillain-Barre syndrome (GBS), hay fever, Hughes syndrome, idiopathic Parkinson's disease, idiopathic interstitial pneumonia, IgE-mediated allergy, immune hemolytic anemia, inclusion body myositis, infectious ocular inflammatory disease, inflammatory demyelinating disease, inflammatory heart disease, inflammatory kidney disease, IPF/UIP, iritis, keratitis, keratojuntivitis sicca, Kussmaul disease or Kussmaul-Meier disease, Landry's paralysis, Langerhan's cell histiocytosis, livedo reticularis, macular degeneration, microscopic polyangiitis, morbus bechterev, motor neuron disorders, mucous membrane pemphigoid, multiple organ failure, myasthenia gravis, myelodysplastic syndrome, myocarditis, nerve root disorders, neuropathy, non-A non-B hepatitis, optic neuritis, osteolysis, ovarian cancer, pauciarticular JRA, peripheral artery occlusive disease (PAOD), peripheral vascular disease (PVD), peripheral artery, disease (PAD), phlebitis, polyarteritis nodosa (or periarteritis nodosa), polychondritis, polymyalgia rheumatica, poliosis, polyarticular JRA, polyendocrine deficiency syndrome, polymyositis, polymyalgia rheumatica (PMR), post-pump syndrome, primary Parkinsonism, prostate and rectal cancer and hematopoietic malignancies (leukemia and lymphoma), prostatitis, pure red cell aplasia, primary adrenal insufficiency, recurrent neuromyelitis optica, restenosis, rheumatic heart disease, SAPHO (synovitis, acne, pustulosis, hyperostosis, and osteitis), scleroderma, secondary amyloidosis, shock lung, scleritis, sciatica, secondary adrenal insufficiency, silicone associated connective tissue disease, sneddon-wilkinson dermatosis, spondilitis ankylosans, Stevens-Johnson syndrome (SJS), systemic inflammatory response syndrome, temporal arteritis, toxoplasmic retinitis, toxic epidermal necrolysis, transverse myelitis, TRAPS (tumor necrosis factor receptor, type 1 allergic reaction, type I I diabetes, urticaria, usual interstitial pneumonia (UIP), vasculitis, vernal conjunctivitis, viral retinitis, Vogt-Koyanagi- Harada syndrome (VKH syndrome), wet macular degeneration, wound healing, yersinia and salmonella associated arthropathy. [0105] In an embodiment, diseases that can be treated or diagnosed with the compositions and methods provided include, but are not limited to, primary and metastatic cancers, including carcinomas of breast, colon, rectum, lung, oropharynx, hypopharynx, esophagus, stomach, pancreas, liver, gallbladder and bile ducts, small intestine, urinary tract (including kidney, bladder and urothelium), female genital tract (including cervix, uterus, and ovaries as well as choriocarcinoma and gestational trophoblastic disease), male genital tract (including prostate, seminal vesicles, testes and germ cell tumors), endocrine glands (including the thyroid, adrenal, and pituitary glands), and skin, as well as hemangiomas, melanomas, sarcomas (including those arising from bone and soft tissues as well as Kaposi's sarcoma), tumors of the brain, nerves, eyes, and meninges (including astrocytomas, gliomas, glioblastomas, retinoblastomas, neuromas, neuroblastomas, Schwannomas, and meningiomas), solid tumors arising from hematopoietic malignancies such as leukemias, and lymphomas (both Hodgkin's and non-Hodgkin's lymphomas). [0106] In an embodiment, the antibodies provided or antigen-binding portions thereof, are used to treat cancer or in the prevention or inhibition of metastases from the tumors described herein either when used alone or in combination with radiotherapy and/or other chemotherapeutic agents. [0107] A method of treating a patient suffering from a disorder comprising the step of administering any one of the binding proteins disclosed herein before, concurrently, or after the administration of a second agent, as discussed herein is provided. In a particular embodiment the second agent is budenoside, epidermal growth factor, corticosteroids, cyclosporin, sulfasalazine, aminosalicylates, 6-mercaptopurine, azathioprine, metronidazole, lipoxygenase inhibitors, mesalamine, olsalazine, balsalazide, antioxidants, thromboxane inhibitors, IL-1 receptor antagonists, anti-IL-1 b mAbs, anti-IL-6 or IL-6 receptor mAbs, growth factors, elastase inhibitors, pyridinylimidazole compounds, antibodies or agonists of TNF, LT, IL-1, IL-2, IL-6, IL-7, IL-8, IL- 12, IL-13, IL-15, IL-16, IL-18, IL-23, EMAP-II, GM-CSF, FGF, and PDGF, antibodies of CD2, CD3, CD4, CD8, CD-19, CD25, CD28, CD30, CD40, CD45, CD69, CD90 or their ligands, methotrexate, cyclosporin, FK506, rapamycin, mycophenolate mofetil, leflunomide, NSAIDs, ibuprofen, corticosteroids, prednisolone, phosphodiesterase inhibitors, adenosine agonists, antithrombotic agents, complement inhibitors, adrenergic agents, IRAK, NIK, IKK, p38, MAP kinase inhibitors, IL-1 b converting enzyme inhibitors, TNFa converting enzyme inhibitors, T-cell signalling inhibitors, metalloproteinase inhibitors, sulfasalazine, azathioprine, 6-mercaptopurines, angiotensin converting enzyme inhibitors, soluble cytokine receptors, soluble p55 TNF receptor, soluble p75 TNF receptor, slL-1RI, slL-1RII, slL-6R, antiinflammatory cytokines, !L-4, IL-10, IL-1 1, IL- 13, or TGFp. [0108] In a particular embodiment the pharmaceutical compositions disclosed herein are administered to the patient by at least one mode selected from parenteral, subcutaneous, intramuscular, intravenous, intrarticular, intrabronchial, intraabdominal, intracapsular, intracartilaginous, intracavitary, intracelial, intracerebellar, intracerebroventricular, intracolic, intracervical, intragastric, intrahepatic, intramyocardial, intraosteal, intrapelvic, intrapericardiac, intraperitoneal, intrapleural, intraprostatic, intrapulmonary, intrarectal, intrarenal, intraretinal, intraspinal, intrasynovial, intrathoracic, intrauterine, intravesical, bolus, vaginal, rectal, buccal, sublingual, intranasal, and transdermal. [0109] At least one anti-idiotypic antibody to at least one binding protein provided herein is also provided. The anti-idiotypic antibody includes any protein or peptide containing molecule that comprises at least a portion of an immunoglobulin molecule such as, but not limited to, at least one complementarity determining region (CDR) of a heavy or light chain or a ligand binding portion thereof, a heavy chain or light chain variable region, a heavy chain or light chain constant region, a framework region, or any portion thereof, that can be incorporated into a binding protein provided herein. Brief Description of the Drawings [01 10] Figure 1A is a schematic representation of Dual Variable Domain (DVD)- Ig constructs and shows the strategy for generation of a DVD-lg from two parent antibodies; [01 11] Figure B, is a schematic representation of constructs DVD1-lg, DVD2-lg, and two chimeric mono-specific antibodies from hybridoma clones 2D13.E3 (anti-IL-la) and 13F5.G5 (anti-IL- b) . Detailed Description [01 12] Multivalent and/or multispecific binding proteins that bind two or more antigens are provided. Specifically, dual variable domain immunoglobulins (DVD-lg), and pharmaceutical compositions thereof, as well as nucleic acids, recombinant expression vectors and host cells for making such DVD-lgs are provided. Methods of using the DVD-lgs to detect specific antigens, either in vitro or in vivo are also provided. [01 13] Unless otherwise defined herein, scientific and technical terms used herein shall have the meanings that are commonly understood by those of ordinary skill in the art. The meaning and scope of the terms should be clear, however, in the event of any latent ambiguity, definitions provided herein take precedent over any dictionary or extrinsic definition. Further, unless otherwise required by context, singular terms shall include pluralities and plural terms shall include the singular. In this application, the use of "or" means "and/or" unless stated otherwise. Furthermore, the use of the term "including," as well as other forms, such as "includes" and "included," is not limiting. Also, terms such as "element" or "component" encompass both elements and components comprising one unit and elements and components that comprise more than one subunit unless specifically stated otherwise. [01 14] Generally, nomenclatures used in connection with, and techniques of, cell and tissue culture, molecular biology, immunology, microbiology, genetics and protein and nucleic acid chemistry and hybridization described herein are those well known and commonly used in the art. The methods and techniques discussed herein are generally performed according to conventional methods well known in the art and as described in various general and more specific references that are cited and discussed throughout the present specification unless otherwise indicated. Enzymatic reactions and purification techniques are performed according to manufacturer's specifications, as commonly accomplished in the art or as described herein. The nomenclatures used in connection with, and the laboratory procedures and techniques of, analytical chemistry, synthetic organic chemistry, and medicinal and pharmaceutical chemistry described herein are those well known and commonly used in the art. Standard techniques are used for chemical syntheses, chemical analyses, pharmaceutical preparation, formulation, and delivery, and treatment of patients. [01 15] Select terms are defined below: [01 16] The term "polypeptide" as used herein, refers to any polymeric chain of amino acids. The terms "peptide" and "protein" are used interchangeably with the term polypeptide and also refer to a polymeric chain of amino acids. The term "polypeptide" encompasses native or artificial proteins, protein fragments and polypeptide analogs of a protein sequence. A polypeptide may be monomeric or polymeric. Use of "polypeptide" herein is intended to encompass polypeptide and fragments and variants (including fragments of variants) thereof, unless otherwise stated. For an antigenic polypeptide, a fragment of polypeptide optionally contains at least one contiguous or nonlinear epitope of polypeptide. The precise boundaries of the at least one epitope fragment can be confirmed using ordinary skill in the art. The fragment comprises at least about 5 contiguous amino acids, such as at least about 0 contiguous amino acids, at least about 5 contiguous amino acids, or at least about 20 contiguous amino acids. A variant of polypeptide is as described herein. [01 17] The term "isolated protein" or "isolated polypeptide" is a protein or polypeptide that by virtue of its origin or source of derivation is not associated with naturally associated components that accompany it in its native state; is substantially free of other proteins from the same species; is expressed by a cell from a different species; or does not occur in nature. Thus, a polypeptide that is chemically synthesized or synthesized in a cellular system different from the cell from which it naturally originates will be "isolated" from its naturally associated components. A protein may also be rendered substantially free of naturally associated components by isolation, using protein purification techniques well known in the art. [01 18] The term "recovering" as used herein, refers to the process of rendering a chemical species such as a polypeptide substantially free of naturally associated components by isolation, e.g., using protein purification techniques well known in the art. [0119] "Biological activity " as used herein, refers to any one or more inherent biological properties of a molecule (whether present naturally as found in vivo, or provided or enabled by recombinant means). Biological properties include but are not limited to binding a receptor; inducing cell proliferation, inhibiting cell growth, inducing other cytokines, inducing apoptosis, and enzymatic activity. Biological activity also includes activity of an Ig molecule. [0120] The terms "specific binding" or "specifically binding," as used herein, in reference to the interaction of an antibody, a protein, or a peptide with a second chemical species, mean that the interaction is dependent upon the presence of a particular structure (e.g., an antigenic determinant or epitope) on the chemical species; for example, an antibody recognizes and binds to a specific protein structure rather than to proteins generally. If an antibody is specific for epitope "A," the presence of a molecule containing epitope A (or free, unlabeled A), in a reaction containing labeled "A" and the antibody, will reduce the amount of labeled A bound to the antibody. [0121] The term "antibody," as used herein, broadly refers to any immunoglobulin (Ig) molecule comprised of four polypeptide chains, two heavy (H) chains and two light (L) chains, or any functional fragment, mutant, variant, or derivation thereof, which retains the essential epitope binding features of an Ig molecule. Such mutant, variant, or derivative antibody formats are known in the art. Nonlimiting embodiments of which are discussed below. [0122] In a full-length antibody, each heavy chain is comprised of a heavy chain variable region (abbreviated herein as HCVR or VH) and a heavy chain constant region. The heavy chain constant region is comprised of three domains, CH1 , CH2 and CH3. Each light chain is comprised of a light chain variable region (abbreviated herein as LCVR or VL) and a light chain constant region. The light chain constant region is comprised of one domain, CL. The VH and VL regions can be further subdivided into regions of hypervariability, termed complementarity determining regions (CDR), interspersed with regions that are more conserved, termed framework regions (FR). Each VH and VL is composed of three CDRs and four FRs, arranged from aminoterminus to carboxy-terminus in the following order: FR1, CDR1, FR2, CDR2, FR3, CDR3, and FR4. Immunoglobulin molecules can be of any type (e.g., IgG, IgE, IgM, IgD, IgA and IgY), class (e.g., IgG 1, lgG2, IgG 3, lgG4, lgA1 and lgA2) or subclass. [0123] The term "Fc region" is used to define the C-terminal region of an immunoglobulin heavy chain, which may be generated by papain digestion of an intact antibody. The Fc region may be a native sequence Fc region or a variant Fc region. The Fc region of an immunoglobulin generally comprises two constant domains, a CH2 domain and a CH3 domain, and optionally comprises a CH4 domain. Replacements of amino acid residues in the Fc portion to alter antibody effector function are known in the art (US Patent Nos. 5,648,260 and 5,624,821). The Fc portion of an antibody mediates several important effector functions e.g., cytokine induction, ADCC, phagocytosis, complement dependent cytotoxicity (CDC) and half-life/ clearance rate of antibody and antigen-antibody complexes. In some cases these effector functions are desirable for a therapeutic antibody but in other cases might be unnecessary or even deleterious, depending on the therapeutic objectives. Certain human IgG isotypes, particularly lgG1 and lgG3, mediate ADCC and CDC via binding to F Rs and complement C1q, respectively. Neonatal Fc receptors (FcRn) are the critical components determining the circulating half-life of antibodies. In still another embodiment at least one amino acid residue is replaced in the constant region of the antibody, for example the Fc region of the antibody, such that effector functions of the antibody are altered. The dimerization of two identical heavy chains of an immunoglobulin is mediated by the dimerization of CH3 domains and is stabilized by the disulfide bonds within the hinge region (Huber et al. (1976) Nature 264: 415-20; Thies et al. (1999) J. Mol. Biol. 293: 67-79). Mutation of cysteine residues within the hinge regions to prevent heavy chain-heavy chain disulfide bonds will destabilize dimeration of CH3 domains. Residues responsible for CH3 dimerization have been identified (Dall'Acqua (1998) Biochem. 37: 9266-73). Therefore, it is possible to generate a monovalent half-lg. Interestingly, these monovalent half Ig molecules have been found in nature for both IgG and IgA subclasses (Seligman (1978) Ann. Immunol. 129: 855-70; Biewenga et al. (1983) Clin. Exp. Immunol. 51: 395-400). The stoichiometry of FcRn: Ig Fc region has been determined to be 2:1 (West et al. (2000) Biochem. 39: 9698-708), and half Fc is sufficient for mediating FcRn binding (Kim et al. (1994) Eur. J. Immunol. 24: 542-548). Mutations to disrupt the dimerization of CH3 domain may not have greater adverse effect on its FcRn binding as the residues important for CH3 dimerization are located on the inner interface of CH3 b sheet structure, whereas the region responsible for FcRn binding is located on the outside interface of CH2-CH3 domains. However, the half -Ig molecule may have certain advantages in tissue penetration due to its smaller size in comparison to that of a regular antibody. In one embodiment at least one amino acid residue is replaced in the constant region of the binding protein provided herein, for example the Fc region, such that the dimerization of the heavy chains is disrupted, resulting in half DVD Ig molecules. The anti-inflammatory activity of IgG is completely dependent on sialylation of the N-linked glycan of the IgG Fc fragment. The precise glycan requirements for anti-inflammatory activity has been determined, such that an appropriate lgG1 Fc fragment can be created, thereby generating a fully recombinant, sialylated lgG1 Fc with greatly enhanced potency (Anthony, R.M., et al. (2008) Science 320: 373-376). [0124] The term "antigen-binding portion" of an antibody (or simply "antibody portion"), as used herein, refers to one or more fragments of an antibody that retain the ability to bind specifically to an antigen. It has been shown that the antigen-binding function of an antibody can be performed by fragments of a full-length antibody. Such antibody embodiments may also be bispecific, dual specific, or multi-specific formats; specifically binding to two or more different antigens. Examples of binding fragments encompassed within the term "antigen-binding portion" of an antibody include (i) a Fab fragment, a monovalent fragment consisting of the VL, VH, CL and CH1 domains; (ii) a F(ab')2 fragment, a bivalent fragment comprising two Fab fragments linked by a disulfide bridge at the hinge region; (iii) a Fd fragment consisting of the VH and CH1 domains; (iv) a Fv fragment consisting of the VL and VH domains of a single arm of an antibody, (v) a dAb fragment (Ward (1989) Nature 341:544-546; PCT Publication No. WO 90/05144 A1), which comprises a single variable domain; and (vi) an isolated complementarity determining region (CDR). Furthermore, although the two domains of the Fv fragment, VL and VH, are coded for by separate genes, they can be joined, using recombinant methods, by a synthetic linker that enables them to be made as a single protein chain in which the VL and VH regions pair to form monovalent molecules (known as single chain Fv (scFv); see e.g., Bird et al. (1988) Science 242: 423-426; and Huston et al. (1988) Proc. Natl. Acad. Sci. USA 85: 5879-5883). Such single chain antibodies are also intended to be encompassed within the term "antigen-binding portion" of an antibody. Other forms of single chain antibodies, such as diabodies are also encompassed. Diabodies are bivalent, bispecific antibodies in which VH and VL domains are expressed on a single polypeptide chain, but using a linker that is too short to allow for pairing between the two domains on the same chain, thereby forcing the domains to pair with complementary domains of another chain and creating two antigen binding sites (see e.g., Holliger, P., et al. (1993) Proc. Natl. Acad. Sci. USA 90:6444-6448; Poljak, R.J., et al. (1994) Structure 2: 1121-1 123). Such antibody binding portions are known in the art (Kontermann and Dubel eds., Antibody Engineering (2001) Springer- Verlag. New York p. 790 (ISBN 3-540-41354-5). In addition single chain antibodies also include "linear antibodies" comprising a pair of tandem Fv segments (VH-CH1-VH-CH1) which, together with complementary light chain polypeptides, form a pair of antigen binding regions (Zapata et al. (1995) Protein Eng. 8(10): 1057-1 062; and US Patent No. 5,641 ,870). [0125] The term "multivalent binding protein" is used throughout this specification to denote a binding protein comprising two or more antigen binding sites. In an embodiment, the multivalent binding protein is engineered to have the three or more antigen binding sites, and is generally not a naturally occurring antibody. The term "multispecific binding protein" refers to a binding protein that binds two or more related or unrelated targets. Dual variable domain (DVD) binding proteins provided herein comprise two or more antigen binding sites and are tetravalent or multivalent binding proteins. DVDs may be monospecific, i.e., bind one antigen or multispecific, i.e., capable of binding two or more antigens. DVD binding proteins comprising two heavy chain DVD polypeptides and two light chain DVD polypeptides are referred to as DVD-lg. Each half of a DVD-lg comprises a heavy chain DVD polypeptide, and a light chain DVD polypeptide, and two antigen binding sites. Each binding site comprises a heavy chain variable domain and a light chain variable domain with a total of 6 CDRs involved in antigen binding per antigen binding site. [0126] The term "bispecific antibody," as used herein, refers to full-length antibodies that are generated by quadroma technology (see Milstein, C. and Cuello, A.C. (1983) Nature 305(5934): p. 537-540), by chemical conjugation of two different monoclonal antibodies (see Staerz, U.D. et al. (1985) Nature 314(6012): 628-631), or by knob-into-hole or similar approaches, which introduce mutations in the Fc region (see Holliger, P. et al. (1993) Proc. Natl. Acad. Sci USA 90(14): 6444-6448), resulting in multiple different immunoglobulin species of which only one is the functional bispecific antibody. By molecular function, a bispecific antibody binds one antigen (or epitope) on one of its two binding arms (one pair of HC/LC), and binds a different antigen (or epitope) .on its second arm (a different pair of HC/LC). By this definition, a bispecific antibody has two distinct antigen binding arms (in both specificity and CDR sequences), and is monovalent for each antigen it binds to. [0127] The term "dual-specific antibody," as used herein, refers to full-length antibodies that can bind two different antigens (or epitopes) in each of its two binding arms (a pair of HC/LC) (see PCT Publication No. WO 02/02773). Accordingly a dualspecific binding protein has two identical antigen binding arms, with identical specificity and identical CDR sequences, and is bivalent for each antigen to which it binds. [0128] A "functional antigen binding site" of a binding protein is one that binds a target antigen. The antigen binding affinity of the antigen binding site is not necessarily as strong as the parent antibody from which the antigen binding site is derived, but the ability to bind antigen must be measurable using any one of a variety of methods known for evaluating antibody binding to an antigen. Moreover, the antigen binding affinity of each of the antigen binding sites of a multivalent antibody herein need not be quantitatively the same. [0129] The term "cytokine" is a generic term for proteins released by one cell population, which act on another cell population as intercellular mediators. Examples of such cytokines are lymphokines, monokines, and traditional polypeptide hormones. Included among the cytokines are growth hormone such as human growth hormone, Nmethionyl human growth hormone, and bovine growth hormone; parathyroid hormone; thyroxine; insulin; proinsulin; relaxin; prorelaxin; glycoprotein hormones such as follicle stimulating hormone (FSH), thyroid stimulating hormone (TSH), and luteinizing hormone (LH); hepatic growth factor; fibroblast growth factor; prolactin; placental lactogen; tumor necrosis factor-alpha and - beta; mullerian-inhibiting substance; mouse gonadotropinassociated peptide; inhibin; activin; vascular endothelial growth factor; integrin; thrombopoietin (TPO); nerve growth factors such as NGF-alpha; platelet-growth factor; placental growth factor, transforming growth factors (TGFs) such as TGF- alpha and TGF-beta; insulin-like growth factor-1 and - ; erythropoietin (EPO); osteoinductive factors; interferons such as interferon-alpha, -beta and -gamma colony stimulating factors (CSFs) such as macrophage-CSF (M-CSF); granulocyte macrophage-CSF (GMCSF); and granulocyte-CSF (G-CSF); interleukins (ILs) such as IL-1, IL-2, IL-3, IL-4, IL-5, IL-6, IL-7, IL-8, IL-9, IL-10, IL- , IL-12, IL- 3, IL-15, IL-18, IL-21, IL-22, IL-23, and IL-33; a tumor necrosis factor such as TNF-alpha or TNF-beta; and other polypeptide factors including LIF and kit ligand (KL). As used herein, the term cytokine includes proteins from natural sources or from recombinant cell culture and biologically active equivalents of the native sequence cytokines. [0130] The term "linker" is used to denote polypeptides comprising two or more amino acid residues joined by peptide bonds and are used to link one or more antigen binding portions. Such linker polypeptides are well known in the art (see e.g., Holliger, P., et al. (1993) Proc. Natl. Acad. Sci. USA 90:6444-6448; Poljak, R.J., e a/. (1994) Structure 2:112 1- 1 23). Exemplary linkers include, but are not limited to, AKTTPKLEEGEFSEAR (SEQ ID NO: 1); AKTTPKLEEGEFSEARV (SEQ ID NO: 2); AKTTPKLGG (SEQ ID NO: 3); SAKTTPKLGG (SEQ ID NO: 4); SAKTTP (SEQ ID NO: 5); RADAAP (SEQ ID NO: 6); RADAAPTVS (SEQ ID NO: 7); RADAAAAGGPGS (SEQ ID NO: 8); RADAAAA(G S) (SEQ ID NO: 9) SAKTTPKLEEGEFSEARV (SEQ ID NO: 10); ADAAP (SEQ ID NO: 11); ADAAPTVSIFPP (SEQ ID NO: 12); TVAAP (SEQ ID NO: 13); TVAAPSVFIFPP (SEQ ID NO: 14); QPKAAP (SEQ D NO: 15); QPKAAPSVTLFPP (SEQ ID NO: 16); AKTTPP (SEQ ID NO: 17); AKTTPPSVTPLAP (SEQ ID NO: 18); AKTTAP (SEQ ID NO: 19); AKTTAPSVYPLAP (SEQ ID NO: 20); ASTKGP (SEQ ID NO: 21); ASTKGPSVFPLAP (SEQ ID NO: 22), GGGGSGGGGSGGGGS (SEQ ID NO: 23); GENKVEYAPALMALS (SEQ ID NO: 24); GPAKELTPLKEAKVS (SEQ ID NO: 25); GHEAAAVMQVQYPAS (SEQ ID NO: 26), TVAAPSVFIFPPTVAAPSVFIFPP (SEQ ID NO: 27); and ASTKGPSVFPLAPASTKGPSVFPLAP (SEQ ID NO: 28. [0131] An "immunoglobulin constant domain" refers to a heavy or light chain constant domain. Human IgG heavy chain and light chain constant domain amino acid sequences are known in the art. [0132] The term "monoclonal antibody" or "mAb" 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 antigen. Furthermore, in contrast to polyclonal antibody preparations that typically include different antibodies directed against different determinants (epitopes), each mAb is directed against a single determinant on the antigen. The modifier "monoclonal" is not to be construed as requiring production of the antibody by any particular method. # AttOlllcy Docket No. 1016.56-304 We claim: 1. A binding protein capable of binding at least one target comprising a polypeptide chain, wherein said polypeptide chain comprises VD1-(X1)n-VD2-C-(X2)n, wherein VD1 is a first heavy chain variable domain; V02 is a second heavy chain variable domain; C is a heavy chain constant domain; X1 is a linker with the proviso that it is not CH1; X2 is an Fc region; n is 0 or 1; and wherein the binding protein binds IL-1J3 and IL-17; and wherein the heavy chain variable domain binding IL-1J3 comprises at least one CDR from SEQ 10 NO: 30, 32, 34, 36, or 38, and/or wherein the heavy chain variable domain binding IL-17 comprises at least one CDR from SEQ 10 NO: 40, 42, or 44. 2. The binding protein according to claim 1, wherein V01 and/or V02 comprise three CORs from SEQ 10 NO: 30, 32, 34, 36, 38, 40, 42, or 44, respectively. 3. A binding protein capable of binding at least one target comprising a polypeptide. chain, wherein said polypeptide chain comprises VD1-(X1)n-V02-C-(X2)n, wherein V01 is a first light chain variable domain; V02 is a second light chain variable domain; C is a light chain constant domain; X1 is a linker with the proviso that it is not CH1; X2 does not comprise an Fc region; n is 0 or 1; and wherein the binding protein binds IL-1J3 and IL-17; and wherein the light chain variable domain binding IL-1J3 comprises at least one CDR from SEQ 10 NO: 31, 33, 35, 37, or 39, and/or wherein the light chain variable domain binding IL-17 comprises at least one CDR from SEQ 10 NO: 41, 43, or 45. 309 AUo•. ,cy Docket No.1 016.56-304 4. The binding protein according to claim 3, wherein the VD1 and/or VD2 light chain variable domains comprise three CDRs from SEQ ID NO: 31, 33, 35, 37, 39, 41, 43, or 45, respectively. 5. The binding protein according to claim 1 or 3, wherein (X1)n on the heavy and/or light chain is (X1)0 and/or (X2)n on the heavy and/or light chain is (X2)0. 6. A binding protein capable of binding at least one target comprising first and second polypeptide chains, wherein said first polypeptide chain comprises V01-(X1)n-VD2-C-(X2)n, wherein VD1 is a first heavy chain variable domain; VD2 is a second heavy chain variable domain; C is a heavy chain constant domain; X1 is a first linker with the proviso that it is not CH1; X2 is an Fc region; n is 0 or 1; and wherein said second polypeptide chain comprises V01-(X1)n-V02-C-(X2)n, wherein VD1 is a first light chain variable domain; VD2 is a second light chain variable domain; C is a light chain constant domain; X1 is a second linker with the proviso that it is not CH1; X2 does not comprise an Fc region; and n is 0 or 1; and wherein the binding protein binds IL-113 and IL-17; and wherein the heavy chain variable domain binding IL-113 comprises at least one CDR from SEQ ID NO: 30, 32, 34,36, or 38, and/or the light chain variable domain binding IL-113 comprises at least one CDR from SEQ 10 NO: 31, 33, 35, 37, or 39; and/or wherein the heavy chain variable domain binding IL-17 comprises at least one CDR from SEQ ID NO: 40,42, or 44, and/or the light chain variable domain binding IL-17 comprises at least one CDR from SEQ 10 NO: 41, 43, or 45. 7. The binding protein according to claim 6, wherein the VD1 and/or VD2 heavy chain variable domains comprise three CORs from SEQ 10 NO: 30, 32, 34, 36, 38, 40, 42, or 44, respectively, 310 Attoilley Oocket No. 1016.56-304 and/or wherein the V01 and/or V02 light chain variable domains comprise SEQ 10 NO: 31, 33, 35,37,39,41,43, or 45, respectively. 8. The binding protein according to claim 1,3, or 6, wherein X1 is SEQ 10 NO: 1-29. 9. The binding protein according to claim 6, wherein the binding protein comprises two first polypeptide chains and two second polypeptide chains. 10. The binding protein according to claim 1, 3, or 6, wherein the Fc region is a variant sequence Fc region. 11. The binding protein according to claim 1, 3, or 6, wherein the Fc region is from an IgG1, IgG2, IgG3, IgG4, IgA, IgM, IgE, or IgO. 12-17. (Canceled) 18. The binding protein according to claim 1, 3, or 6, wherein said VD1 binds a first target with an affinity and/or potency different from the affinity and/or potency with which said V02 binds a second target. 19. The binding protein according to claim 1, 3, or 6, wherein said first parent antibody or binding portion thereof, and said second parent antibody or binding portion thereof, are a human antibody, a CDR grafted antibody, or a humanized antibody. 20-23. (Canceled) 24. A binding protein capable of binding at least one target comprising four polypeptide chains, wherein two polypeptide chains comprise VD1-(X1)n-VD2-C-(X2)n, wherein VD1 is a first heaVy chain variable domain; VD2 is a second heavy chain variable domain; C is a heavy chain constant domain; X1 is a first linker with the proviso that it is not CH1; X2 is an Fc region; n is 0 or 1; and wherein two polypeptide chains comprise VD1-(X1)n-VD2-C-(X2)n, wherein VD1 is a first light chain variable domain; VD2 is a second light chain variable domain; C is a light chain constant domain; 311 AttOlllCY Docket No. 1016.56-304 X1 is a second linker with the proviso that it is not CH1; X2 does not comprise an Fc region; n is 0 or 1; and wherein the binding protein binds IL-1J3 and IL-17; and wherein the heavy chain variable domain binding IL-1J3 comprises at least one CDR from SEQ 10 NO: 30, 32, 34, 36, or 38, and/or the light chain variable domain binding IL-1(3 comprises at least one COR from SEQ 10 NO: 31, 33, 35, 37, or 39; and/or wherein the heavy chain variable domain binding IL-17 comprises at least one COR from SEQ 10 NO: 40, 42, or 44, and/or the light chain variable domain binding IL-17 comprises at least one CDR from SEQ 10 NO: 41, 43, or 45. 25. The binding protein according to claim 24, wherein the V01 and/or VD2 heavy chain variable domains comprise three CDRs from SEQ 10 NO: 30, 32, 34, 36, 38, 40, 42, or 44, respectively; and/or wherein the VD1 and/or V02 light chain variable domains comprise three CORs from SEQ 10 NO: 31,33,35,37,39,41,43, or 45, respectively. 26. The binding protein according to claim 1, 3, 6, or 24, wherein said binding protein has an on rate constant (Kon) to at least one target of: at least about 102M-1s-1 ; at least about 103M-1s-1 ; at least about 104M-1s-1 ; at least about 105M<1S·1; or at least about 106M- 1s-1 , as measured by surface plasmon resonance. 27. The binding protein according to claim 1, 3, 6, or 24, wherein said binding protein has an off rate constant (Kerr) to at least one target of: at most about 10-3S<1; at most about 10-4S-1; at most about 10·5 S- 1 ; or at most about 10-6s·" as measured by surface plasmon resonance. 28. The binding protein according to claim 1, 3, 6, or 24, wherein said binding protein has a dissociation constant (Ko) to at least one target of: at most about 10·7M; at most about 10-8M; at most about 10-9M; at most about 10·10M; at most about 1Q-11M; at most about 10·12M; or at most 10-13M, as measured by surface plasmon resonance. 29. A binding protein conjugate comprising a binding protein according to claims 1, 3, 6, or 24, said binding protein conjugate further comprising an immunoadhesion molecule, an imaging agent, a therapeutic agent, or a cytotoxic agent. 30. The binding protein conjugate according to claim 29, wherein said imaging agent is a radiolabel, an enzyme, a fluorescent label, a luminescent Jabel, a bioluminescent label, a magnetic label, or biotin. 312 AUol"ey Docket No. 1016.56-304 31. The binding protein conjugate according to claim 30, wherein said radiolabel is: 3H, 14C, 35S, 9OY, 99Tc, 1111n, 1251, 131 1, 177Lu, 166Ho, or 153Sm. 32. The binding protein conjugate according to claim 29, wherein said therapeutic or cytotoxic agent is an anti-metabolite, an alkylating agent, an antibiotic, a growth factor, a cytokine, an anti-angiogenic agent, an anti-mitotic agent, an anthracycline, toxin, or an apoptotic agent. 33. The binding protein according to claim 1, 3, 6, or 24, wherein said binding protein is a crystallized binding protein. 34-36. (Canceled) 37. An isolated nucleic acid encoding a binding protein amino acid sequence according to claims 1, 3, 6, or 24. 38. A vector comprising an isolated nucleic acid according to claim 37. 39. The vector according to claim 38, wherein said vector is pcDNA, pTT, pTT3, pEFBOS, pBV, pJV, pcDNA3.1 Tapa, pEF6 Tapa, pHybE, or pBJ. 40. A host cell comprising a vector according to claim 38. 41. The host cell according to claim 40, wherein said host cell is a prokaryotic cell. 42. The host cell according to claim 41, wherein said prokaryotic cell is E. coli. 43. The host cell according to claim 40, wherein said host cell is a eukaryotic cell. 44. The host cell according to claim 43, wherein said eukaryotic cell is a protist cell, an animal cell, a plant cell, or fungal cell. 45. The host cell according to claim 44, wherein said animal cell is a mammalian cell, an avian cell, or an insect cell. 46. The host cell according to claim 45, wherein said mammalian cell is a CHO cell. 47. The host cell according to claim 45, wherein said mammalian cell is a COS cell. 48. The host cell according to claim 44, wherein said host cell is a yeast cell. 49. The host cell according to claim 48, wherein said yeast cell is S. cerevisiae. 50. The host cell according to claim 45, wherein said insect cell is an S19 cell. 51. A method of producing a binding protein, comprising culturing a host cell according to claims 40-50 in culture medium under conditions sufficient to produce the binding protein. 313 · Attoilley Docket NO.1 016.56-304 52-54. (Canceled) 55. A binding protein produced according to the method of claim 51. 56. A pharmaceutical composition comprising the binding protein according to claims 1, 3, 6, 24. or 91-94. and a pharmaceutically acceptable carrier. 57. The pharmaceutical composition according to claim 56 further comprising at least one additional therapeutic agent. 58. The pharmaceutical composition according to claim 57. wherein said additional therapeutic agent is an imaging agent, a cytotoxic agent. an angiogenesis inhibitor, a kinase inhibitor, a costimulation molecule blocker, an adhesion molecule blocker, an anti-cytokine antibody or functional fragment thereof, methotrexate, cyclosporin, rapamycin, FK506, a detectable label or reporter, a TNF antagonist, an antirheumatic, a muscle relaxant. a narcotic, a non-steroid antiinflammatory drug (NSAID), an analgesic, an anesthetic, a sedative, a local anesthetic, a neuromuscular blocker, an antimicrobial, an antipsoriatic, a corticosteriod, an anabolic steroid, an erythropoietin, an immunization, an immunoglobulin. an immunosuppressive, a growth hormone, a hormone replacement drug, a radiopharmaceutical, an antidepressant, an antipsychotic, a stimulant. an asthma medication, a beta agonist, an inhaled steroid, an epinephrine or analog, a cytokine, or a cytokine antagonist. 59. Use of the binding protein according to claims 1, 3,6, 24, or 91-94, in treating a subject for a disease or a disorder by administering to the subject the binding protein such that treatment is achieved. 60. The use according to claim 59, wherein said disorder is rheumatoid arthritis, osteoarthritis, juvenile chronic arthritis, septic arthritis, Lyme arthritis, psoriatic arthritis, reactive arthritis, spondyloarthropathy, systemic lupus erythematosus, Crohn's disease, ulcerative colitis, inflammatory bowel disease, insulin dependent diabetes mellitus, thyroiditis, asthma, allergic diseases, psoriasis, dermatitis scleroderma, graft versus host disease, organ transplant rejection, acute or chronic immune disease associated with organ transplantation, sarcoidosis, atherosclerosis, disseminated intravascular coagulation, Kawasaki's disease, Grave's disease, nephrotic syndrome, chronic fatigue syndrome, Wegener's granulomatosis, Henoch-Schoenlein purpurea, microscopic vasculitis of the kidneys, chronic active hepatitis, uveitis, septic shock, toxic shock syndrome, sepsis syndrome, cachexia, infectious diseases. parasitic diseases, acute transverse myelitis, Huntington's chorea, Parkinson's disease, Alzheimer's disease. stroke, primary biliary cirrhosis, hemolytic anemia, malignancies, heart failure, myocardial 314 Attoilley Docket No.1 016.56-304 infarction, Addison's disease. sporadic polyglandular deficiency type I and polyglandular deficiency type II, Schmidt's syndrome, adult (acute) respiratory distress syndrome, alopecia. alopecia areata, seronegative arthopathy, arthropathy, Reiter's disease. psoriatic arthropathy, ulcerative colitic arthropathy, enteropathic synovitis, chlamydia, yersinia and salmonella associated arthropathy, spondyloarthopathy, atheromatous disease/arteriosclerosis, atopic allergy, autoimmune bullous disease, pemphigus vulgaris, pemphigus foliaceus, pemphigoid, linear IgA disease, autoimmune haemolytic anaemia, Coombs positive haemolytic anaemia, acquired pernicious anaemia. juvenile pernicious anaemia, myalgic encephalitis/Royal Free Disease, chronic mucocutaneous candidiasis, giant cell arteritis, primary sclerosing hepatitis, cryptogenic autoimmune hepatitis, acquired immunodeficiency related diseases, hepatitis B, hepatitis C, common varied immunodeficiency (common variable hypogammaglobulinaemia), dilated cardiomyopathy, female infertility, ovarian failure, premature ovarian failure, fibrotic lung disease, cryptogenic fibrosing alveolitis, post-inflammatory interstitial lung disease, interstitial pneumonitis, connective tissue disease associated interstitial lung disease, mixed connective tissue disease associated lung disease, systemic sclerosis associated interstitial lung disease, rheumatoid arthritis associated interstitial lung disease, systemic lupus erythematosus associated lung disease, dermatomyositis/polymyositis associated lung disease, SjOgren's disease associated lung disease, ankylosing spondylitis associated lung disease, vasculitic diffuse lung disease, haemosiderosis associated lung disease, drug-induced interstitial lung disease, fibrosis, radiation fibrosis, bronchiolitis obliterans, chronic eosinophilic pneumonia. lymphocytic infiltrative lung disease, postinfectious interstitial lung disease, gouty arthritis, autoimmune hepatitis, type-1 autoimmune hepatitis (classical autoimmune or lupoid hepatitis), type-2 autoimmune hepatitis (anti-LKM antibody hepatitis), autoimmune mediated hypoglycaemia, type B insulin resistance with acanthosis nigricans, hypoparathyroidism, acute immune disease associated with organ transplantation, chronic immune disease associated with organ transplantation, osteoarthrosis, primary sclerosing cholangitis, psoriasis type 1, psoriasis type 2, idiopathic leucopaenia, autoimmune neutropaenia, renal disease NOS, glomerulonephritides, microscopic vasulitis of the kidneys, Iyme disease, discoid lupus erythematosus, male infertility idiopathic or NOS, sperm autoimmunity, multiple sclerosis (all subtypes), sympathetic ophthalmia, pulmonary hypertension secondary to connective tissue disease, Goodpasture's syndrome, pulmonary manifestation of polyarteritis nodosa, acute rheumatic fever, rheumatoid spondylitis, Still's disease, systemic sclerosis, SjOrgren's syndrome, Takayasu's disease/arteritis, autoimmune thrombocytopaenia, idiopathic thrombocytopaenia, autoimmune thyroid disease, hyperthyroidism, goitrous autoimmune 315 Attol'ley Docket No. 1016.56-304 hypothyroidism (Hashimoto's disease), atrophic autoimmune hypothyroidism, primary myxoedema, phacogenic uveitis, primary vasculitis, vitiligo acute liver disease, chronic liver diseases, alcoholic cirrhosis, alcohol-induced liver injury, cholestasis, idiosyncratic liver disease, drug-induced hepatitis, non-alcoholic steatohepatitis, allergy and asthma, group B streptococci (GBS) infection, mental disorders; depression; schizophrenia, Th2 Type and Th1 Type mediated diseases, acute and chronic pain; pain, cancers, lung cancer, breast cancer, stomach cancer, bladder cancer, colon cancer, pancreatic cancer, ovarian cancer, prostate cancer, rectal cancer, hematopoietic malignancies, leukemia, lymphoma, abetalipoproteinemia, acrocyanosis, acute and chronic parasitic or infectious processes, acute leukemia, acute lymphoblastic leukemia (All), acute myeloid leukemia (AML), acute or chronic bacterial infection, acute pancreatitis, acute renal failure, adenocarcinomas, aerial ectopic beats, AIDS dementia complex, alcoholinduced hepatitis, allergic conjunctivitis, allergic contact dermatitis, allergic rhinitis, allograft rejection, alpha-I- antitrypsin deficiency, amyotrophic lateral sclerosis, anemia, angina pectoris, anterior horn cell degeneration, anti cd3 therapy, antiphospholipid syndrome, anti-receptor hypersensitivity reactions, aortic and peripheral aneuryisms, aortic dissection, arterial hypertension, arteriosclerosis, arteriovenous fistula, ataxia, atrial fibrillation, sustained atrial fibrillation, paroxysmal atrial fibrillation, atrial flutter, atrioventricular block, B cell lymphoma, bone graft rejection, bone marrow transplant (BMT) rejection, bundle branch block, Burkitt's lymphoma, burns, cardiac arrhythmias, cardiac stun syndrome, cardiac tumors, cardiomyopathy, cardiopulmonary bypass inflammation response, cartilage transplant rejection, cerebellar cortical degenerations, cerebellar disorders, chaotic or multifocal atrial tachycardia, chemotherapy associated disorders, chronic myelocytic leukemia (CMl), chronic alcoholism, chronic inflammatory pathologies, chronic lymphocytic leukemia (Cll), chronic obstructive pulmonary disease (COPO), chronic salicylate intoxication, colorectal carcinoma, congestive heart failure, conjunctivitis, contact dermatitis, cor pulmonale, coronary artery disease, Creutzfeldt-Jakob disease, culture negative sepsis, cystic fibrosis, cytokine therapy associated disorders, dementia pugilistica, demyelinating diseases, dengu~ hemorrhagic fever, dermatitis, dermatologic conditions, diabetes, diabetes mellitus, diabetic ateriosclerotic disease, diffuse lewy body disease, dilated congestive cardiomyopathy, disorders of the basal ganglia, Down's syndrome in middle age, drug-induced movement disorders induced by drugs which block eNS dopamine receptors, drug sensitivity, eczema, encephalomyelitis, endocarditis, endocrinopathy, epiglottitis, epstein-barr virus infection, erythromelalgia, extrapyramidal and cerebellar disorders, familial hematophagocytic Iymphohistiocytosis, fetal thymus implant rejection, Friedreich's ataxia, functional peripheral arterial disorders, fungal sepsis, gas gangrene, gastric ulcer, graft 316 Atto...cy Docket No. 1016.56-304 rejection of any organ or tissue, gram negative sepsis, gram positive sepsis, granulomas due to intracellular organisms, hairy cell leukemia, Hallerrorden-Spatz disease, hashimoto's thyroiditis, hay fever, heart transplant rejection, hemachromatosis, hemodialysis, hemolytic uremic syndrome/thrombolytic thrombocytopenic purpura, hemorrhage, hepatitis A, His bundle arryhthmias, HIV infection/HIV neuropathy, Hodgkin's disease, hyperkinetic movement disorders, hypersensitity reactions, hypersensitivity pneumonitis, hypertension, hypokinetic movement disorders, hypothalamic-pituitary-adrenal axis evaluation, idiopathic Addison's disease, idiopathic pulmonary fibrosis, antibody mediated cytotoxicity, asthenia, infantile spinal muscular atrophy, inflammation of the aorta, influenza a, ionizing radiation exposure, iridocyclitis/uveitis/optic neuritis, ischemia- reperfusion injury, ischemic stroke, juvenile rheumatoid arthritis, juvenile spinal muscular atrophy, Kaposi's sarcoma, kidney transplant rejection, legionella, leishmaniasis, leprosy, lesions of the corticospinal system,lipedema, liver transplant rejection, Iymphederma, malaria, malignamt lymphoma, malignant histiocytosis, malignant melanoma, meningitis, meningococcemia, metaboliclidiopathic, migraine headache, mitochondrial multLsystem disorder, mixed connective tissue disease, monoclonal gammopathy, multiple myeloma, multiple systems degenerations (Mencel Dejerine-Thomas Shy-Drager and Machado-Joseph), myasthenia gravis, mycobacterium avium intracellulare, mycobacterium tuberculosis, myelodyplastic syndrome, myocardial ischemic disorders, nasopharyngeal carcinoma, neonatal chronic lung disease, nephritis, nephrosis, neurodegenerative diseases, neurogenic I muscular atrophies, neutropenic fever, nonhodgkins lymphoma, occlusion of the abdominal aorta and its branches, occulsive arterial disorders, okt3 therapy, orchitis/epidydimitis, orchitis/vasectomy reversal procedures, organomegaly, osteoporosis, pancreas transplant rejection, pancreatic carcinoma, paraneoplastic syndrome/hypercalcemia of malignancy, parathyroid transplant rejection, pelvic inflammatory disease, perennial rhinitis, pericardial disease, peripheral atherlosclerotic disease, peripheral vascular disorders, peritonitis, pernicious anemia, pneumocystis carinii pneumonia, pneumonia, POEMS syndrome (polyneuropathy, organom~galy, endocrinopathy, monoclonal gammopathy, and skin changes syndrome), post perfusion syndrome, post pump syndrome, post-MI cardiotomy syndrome, preeclampsia, progressive supranucleo palsy, primary pulmonary hypertension, radiation therapy, Raynaud's phenomenon and disease, Raynoud's disease, Refsum's disease, regular narrow QRS tachycardia, renovascular hypertension, reperfusion injury, restrictive cardiomyopathy, sarcomas, scleroderma, senile chorea, senile dementia of Lewy body type, seronegative arthropathies, shock, sickle cell anemia, skin allograft rejection, skin changes syndrome, small bowel transplant rejection, solid tumors, 317 AUollley Docket No.1 016.56-304 specific arrythmias, spinal ataxia, spinocerebellar degenerations, streptococcal myositis, structural lesions of the cerebellum, subacute sclerosing panencephalitis, syncope, syphilis of the cardiovascular system, systemic anaphalaxis, systemic inflammatory response syndrome, systemic onset juvenile rheumatoid arthritis, T-cell or FAB ALL, telangiectasia, thromboangitis obliterans, thrombocytopenia, toxicity, transplants, trauma/hemorrhage, type III hypersensitivity reactions, type IV hypersensitivity, unstable angina, uremia, urosepsis, urticaria, valvular heart diseases, varicose veins, ,vasculitis, venous diseases, venous thrombosis, ventricular fibrillation, viral and fungal infections, vital encephalitis/aseptic meningitis, vital-associated hemaphagocytic syndrome, Wernicke-Korsakoff syndrome, Wilson's disease, xenograft rejection of any organ or tissue, acute coronary syndromes, acute idiopathic polyneuritis, acute inflammatory demyelinating polyradiculoneuropathy, acute ischemia, adult Still's disease, anaphylaxis, anti-phospholipid antibody syndrome, aplastic anemia, atopic eczema, atopic dermatitis, autoimmune dermatitis, autoimmune disorder associated with streptococcus infection, autoimmune enteropathy, autoimmune hearing loss, autoimmune Iymphoproliferative syndrome (ALPS), autoimmune myocarditis, autoimmune premature ovarian failure, blepharitis, bronchiectasis, bullous pemphigoid, cardiovascular disease, catastrophic antiphospholipid syndrome, celiac disease, cervical spondylosis, chronic ischemia, cicatricial pemphigoid, clinically isolated syndrome (cis) with risk for multiple sclerosis, childhood onset psychiatric disorder, dacryocystitis, dermatomyositis, diabetic retinopathy, disk herniation, disk prolaps, drug induced immune hemolytic anemia, endometriosis, endophthalmitis, episcleritis, erythema multiforme, erythema multiforme major, gestational pemphigoid, Guillain-Barre syndrome (GBS), hay fever, Hughes syndrome, idiopathic Parkinson's disease, idiopathic interstitial pneumonia, IgE-mediated allergy, immune hemolytic anemia, inclusion body myositis, infectious ocular inflammatory disease, inflammatory demyelinating disease, inflammatory heart disease, inflammatory kidney disease, IPF/UIP, iritis, keratitis, keratoconjunctivitis sicca, Kussmaul disease or Kussmaul-Meier disease, Landry's paralysis, Langerhan's cell histiocytosis, livedo reticularis, macular degeneration, microscopic polyangiitis, morbus bechterev, motor neuron disorders, mucous membrane pemphigoid, multiple organ failure, myelodysplastic syndrome, myocarditis, nerve root disorders, neuropathy, non-A non-B hepatitis, optic neuritis, osteolysis, ovarian cancer, pauciarticular JRA, peripheral artery occlusive disease (PAOD), peripheral vascular disease (PVD), peripheral artery, disease (PAD), phlebitis, polyarteritis nodosa (or periarteritis nodosa), polychondritis, polymyalgia rheumatica, poliosis, polyarticular JRA, polyendocrine deficiency syndrome, polymyositis, post-pump syndrome, primary Parkinsonism, prostatitis, pure red cell aplasia, primary adrenal insufficiency, recurrent neuromyelitis optica, 318 · AUol"ey Docket No. 1016.56-304 restenosis, rheumatic heart disease, sapho (synovitis, acne, pustulosis, hyperostosis, and osteitis), scleroderma, secondary amyloidosis, shock lung, scleritis, sciatica, secondary adrenal insufficiency, silicone associated connective tissue disease, sneddon-wilkinson dermatosis, spondilitis ankylosans, Stevens-Johnson syndrome (SJS), systemic inflammatory response syndrome, temporal arteritis, toxoplasmic retinitis, toxic epidermal necrolysis, transverse myelitis, TRAPS (tumor necrosis factor receptor, type 1 allergic reaction, type II diabetes, usual interstitial pneumonia (UIP), vernal conjunctivitis, viral retinitis, Vogt-Koyanagi-Harada syndrome (VKH syndrome), wet macular degeneration, or wound healing. 61. The use according to claim 60, wherein said administering to the subject is parenteral, subcutaneous, intramuscular, intravenous, intrarticular, intrabronchial, intraabdominal, intracapsular, intracartilaginous, intracavitary, intracelial, intracerebellar, intracerebroventricular, intracolic, intracervical, intragastric, intrahepatic, intramyocardial, intraosteal, intrapelvic, intrapericardiac, intraperitoneal, intrapleural, intraprostatic, intrapulmonary, intrarectal, intrarenal, intraretinal, intraspinal, intrasynovial, intrathoracic, intrauterine, intravesical, bolus, vagil:1al, rectal, buccal, sublingual, intranasal, or transdermal. 62. A method for generating a binding protein capable of binding at least one target comprising the steps of a) obtaining a first parent antibody or binding portion thereof,; b) obtaining a second parent antibody or binding portion thereof; c) constructing the polypeptide chain or chains according to claims 1, 3, 6, 24, or 91-94; and d) expressing the polypeptide chain or chains such that a binding protein capable of binding at least one target is generated. 63. The method according to claim 62, wherein the V01 and/or V02 heavy chain variable domains comprise three CORs from SEQ 10 NO: 30, 32, 34, 36, 38. 40, 42, or 44; and/or wherein the V01 and/or V02 light chain variable domains comprise three CORs from SEQ 10 NO: 31. 33, 35, 37, 39,41,43, or 45. 64. The method according to claim 62, wherein said first parent antibody or binding portion thereof, and said second parent antibody or binding portion thereof, are a human antibody, a CDR grafted antibody, or a humanized antibody. 65-67. (Canceled) 319 Attollley Docket NO.1 016.56-304 68. The method according to claim 62, wherein the Fc region is a variant sequence Fc region. 69. The method according to claim 62, wherein the Fc region is from an IgG1, IgG2, IgG3, IgG4, IgA, IgM, IgE, or IgO. 70-73. (Canceled) 74. The method according to claim 62, wherein said first parent antibody or binding portion thereof, binds a first target with a different affinity than the affinity with which said second parent antibody or binding portion thereof, binds a second target. 75. The method according to claim 62, wherein said first parent antibody or binding portion thereof, binds a first target with a different potency than the potency with which said second parent antibody or binding portion thereof, binds a second target. 76. A method of determining the presence of at least one target or fragment thereof in a test sample by an immunoassay, wherein the immunoassay comprises contacting the test sample with at least one binding protein and at least one detectable label, wherein the at least one binding protein comprises the binding protein according to claim 1,3,6, or 24, or 91-94. 77. The method according to claim 76 further comprising: (i) contacting the test sample with the at least one binding protein, wherein the binding protein binds to an epitope on the target or fragment thereof so as to form a first complex; (ii) contacting the complex with the at least one detectable label, wherein the detectable label binds to the binding protein or an epitope on the target or fragment thereof that is not bound by the binding protein to form a second complex; and (iii) detecting the presence of the target or fragment thereof in the test sample based on the signal generated by the detectable label in the second complex, wherein the presence of the target or fragment thereof is directly correlated with the signal generated by the detectable label. 78. The method according to claim 76 further comprising: (i) contacting the test sample with the at least one binding protein, wherein the binding protein binds to an epitope on the target or fragment thereof so as to form a first complex; 320 Atto"ley Docket NO.1 016.56-304 (ii) contacting the complex with the at least one detectable label, wherein the detectable label competes with the target or fragment thereof for binding to the binding protein so as to form a second complex; and (iii) detecting the presence of the target or fragment thereof in the test sample based on the signal generated by the detectable label in the second complex, wherein the presence of the target or fragment thereof is indirectly correlated with the signal generated by the detectable label. 79. The method according to claims 76-78, wherein the test sample is from a patient and the method further comprises diagnosing, prognosticating, or assessing the efficiency of therapeutic/prophylactic treatment of the patient, and wherein if the method further comprises assessing the efficacy of therapeutic/prophylactic treatment of the patient, the method optionally further comprises modifying the therapeutic/prophylactic treatment of the patient as needed to improve efficacy. 80. The method according to claims 76-78, wherein the method is adapted for use in an automated system or a semi-automated system. 81. The method according to claims 76-78, wherein the method determines the presence of more than one target in the sample. 82. A method of determining the amount or concentration of an target or fragment thereof in a test sample by an immunoassay, wherein the immunoassay (a) employs at least one binding protein and at least one detectable label and (b) comprises comparing a signal generated by the detectable label with a control or calibrator comprising the target or fragment thereof, wherein the calibrator is optionally part of a series of calibrators in which each calibrator differs from the other calibrators in the series by the concentration of the target or fragment thereof, and wherein the at least one binding protein comprises the binding protein according to claim 1, 3, 6, or 24, or 91-94. 83. The method according to claim 82 further comprising: (i) contacting the test sample with the at least one binding protein, wherein the binding protein binds to an epitope on the target or fragment thereof so as to form a first complex; 321 Attollley Docket No. 1016.56-304 (ii) contacting the complex with the at least one detectable label, wherein the detectable label binds to an epitope on the target or fragment thereof that is not bound by the binding protein to form a second complex; and (iii) determining the amount or concentration of the target or fragment thereof in the test sample based on the signal generated by the detectable label in the second complex, wherein the amount or concentration of the target or fragment thereof is directly proportional to the signal generated by the detectable label. 84. The method according to claim 82 further comprising: (i) contacting the test sample with the at least one binding protein, wherein the binding protein binds to an epitope on the target or fragment thereof so as to form a first complex; (ii) contacting the complex with the at least one detectable label, wherein the detectable label competes with the target or fragment thereof for binding to the binding protein so as to form a second complex; and (iii) determining the amount or concentration of the target or fragment thereof in the test sample based on the signal generated by the detectable label in the second complex, wherein the presence of the target or fragment thereof is indirectly proportional to the signal generated by the detectable label. 85. The method according to claims 82-84, wherein the test sample is from a patient and the method further comprises diagnosing, prognosticating, or assessing the efficiency of therapeutic/prophylactic treatment of the patient, and wherein if the method further comprises assessing the efficacy of therapeutic/prophylactic treatment of the patient, the method optionally further comprises modifying the therapeutic/prophylactic treatment of the patient as needed to improve efficacy. 86. The method according to claims 82-84, wherein the method is adapted for use in an automated system or a semi-automated system. 87. The method according to claims 82-84, wherein the method determines the amount or concentration of more than one target in the sample. 88. A kit for assaying a test sample for the presence, amount, or concentration of an target or fragment thereof, 322 Altol/ley Docket No. 1016.56-304 said kit comprising (a) instructions for assaying the test sample for the target or fragment thereof and (b) at least one binding protein comprising the binding protein according to claim 1, 3, 6, or 24, or 91-94. 89. The binding protein according to claim 1, 3, 6, or 24, wherein the V01 and V02 heavy chain variable domains, if present, comprise three CDRs from SEQ 10 NO: 30, 32, 34, 36, 38, 40, 42, or 44, respectively, and wherein the V01 and V02 light chain variable domains, if present, comprise three CORs from SEQ 10 NO: 31, 33, 35, 37, 39, 41, 43, or 45, respectively. 90. The binding protein according to claim 1, 3, 6, or 24, wherein the V01 and/or V02 heavy chain variable domains, if present, comprise SEQ 10 NO: 30, 32, 34, 36, 38, 40, 42, or 44, respectively, and/or wherein the V01 and/or V02 light chain variable domains, if present, comprise from SEQ 10 NO: 31, 33, 35,37,39,41,43, or 45, respectively. 91. A binding protein capable of binding at least one target comprising a polypeptide chain, wherein said polypeptide chain comprises V01-(X1)n-V02-C-(X2)n, wherein V01 is a first heavy chain variable domain; VD2 is a second heavy chain variable domain; C is a heavy chain constant domain; X1 is a linker with the proviso that it is not CH1; X2 is an Fc region; n is 0 or 1; and wherein the binding protein binds IL-113 and IL-17; and further wherein the binding protein binds: (a) IL-113 and has an off rate constant (Kotr) of at most about 8.50 x 10-4 s'\ and/or has a dissociation constant (Ko) of at most 2.80 x 10.9 M, as measured by surface plasmon resonance; and/or (b) IL-17 and has an off rate constant (Kotr) of at most about 1.00 x 10-4 s'\ and/or has a dissociation constant (Ko) of at most 1.20 x 10.8 M. 92. A binding protein capable of binding at least one target comprising a polypeptide chain, wherein said polypeptide chain comprises V01-(X1)n-V02-C-(X2)n, wherein VD1 is a first light chain variable domain; 323 Attol ney Docket No.1 016.56-304 VD2 is a second light chain variable domain; C is a light chain constant domain; X1 is a linker with the proviso that it is not CH1; X2 does not comprise an Fc region; n is 0 or 1; and wherein the binding protein binds IL-1~ and IL-17; and further wherein the binding protein binds: (a) IL-1~ and has an off rate constant (Koff) of at most about 8.50 x 10-4 s'" and/or has a dissociation constant (Ko) of at most 2.80 x 10-9 M, as measured by surface plasmon resonance; and/or (b) IL-17 and has an off rate constant (Koff) of at most about 1.00 x 10-4 S·1, and/or has a dissociation constant (Ko) of at most 1.20 x 10-8 M. 93. A binding protein capable of binding at least one target comprising first and second polypeptide chains, wherein said first polypeptide chain comprises VD1-(X1)n-VD2-C-(X2)n, wherein VD1 is a first heavy chain variable domain; VD2 is a second heavy chain variable domain; C is a heavy chain constant domain; X1 is a first linker with the proviso that it is not CH1; X2 is an Fc region;n is 0 or 1; and wherein said second polypeptide chain comprises VD1-(X1)n-VD2-C-(X2)n, wherein VD1 is a first light chain variable domain; VD2 is a second light chain variable domain; C is a light chain constant domain; X1 is a second linker with the proviso that it is not CH1; X2 does not comprise an Fc region; and n is 0 or 1; and 324 il I • AHo. ney Docket NO.1 016.56-304 wherein the binding protein binds IL-113 and IL-17; and further wherein the binding protein binds: (a) IL-113 and has an off rate constant (Koff) of at most about 8.50 x 10'4 S'1, and/or has a dissociation constant (Ko) of at most 2.80 x 10.9 M, as measured by surface plasmon resonance; and/or (b) IL-17 and has an off rate constant (!