HUMANIZED ANTI-INTERLEUKIN 3 RECEI'TOR ALPHA CHAIN ANTIBODIES RELATED APPLlCATlON DATA Tllc prcscnt application claims prio~ityk o ~ nU S Patent Applicatioll No. 611374,489 c~ltitled "Humanized Anti-lntcrleukin 3 Receptor Alpha Clvairl Antibodies" filed on 17 August 2010 and from Inte~~iationdPla tent Application No: PCTlAU2011/000155 entitled "Con~positioos and Methods for Targeting 'Type 1 Interfero~Pl roducing Cells". The cntire conte~ltso f tllesc applications alc llereby incorporated by reference. rn Thc present disclosure relates to allti-interleukin 3 receptor alpha c l ~ a i ~ l antibodies and uscs thereof. BACKGROUND The functional interleukin 3 receptor is a heterodimer that coniprises a specific alpha chain (JL-3Ra; CD123) and a "co~nmon" LL-3 receptor beta chain (PC; CD13 1) that is shared with the receptors for granulocyte macrophage color~y stimulating factor (GM-CSF) and interleukin 5 (1L-5). IL-3Ra is a type I transmembra~le protein with a deduced Molecular Wcigllt of about 4lkDa conraining all extraccllolar dotnain involved in IL-3 binding, a transmctnbrt~~dlco ~ n aain~d~ a short cytoplasmic tail of t~bout5 0 nmino acids. 'Thc cxtraccllular domain is composed of two regions: an N-terminal regio~o~f about 100 amino acids, tllc scqucncc of which cxhibits similarity to equivalent regions of the GM-CSF and IL-5 rcccptor alpha-chains; and a rcgion pmxirnal to tllc tra~is~ncmbrandco main tllat contains four co~lscrvcd cystci~ic rcsiducs and a WSXWS motif, coii~rl~too~ olt llcr mcmbcrs oftllis cytoki~lcre ccptor family. The IL-3 binding domaio comprises about 200 amino acid rcsidue cytoltinc rcccptor motifs (CRMs) madc up of two Ig-likc foldi~lgd omains. Thc extraccllular dotnail1 of IL-3Ka is Iligllly glycosylatcd, wit11 N-glycosylation ncccssary for boll1 ligand binding a11d rcccptor signaling. IL-3Ra is cxprcsscd widcly tliroi~glloutt llc hematopoictic systc~lli ncluding liernatol)oictic progct~itors, mast cells, crythroid cclls, mcgakaryocytcs, basol~hils, cosinophils, ~nonocyteslrnacrophngcs, ncutropllils and CD5' U-lymphocytes. Non-hcmatopoictic cclls such as plas~l~acytoiddc ndritic cells (pIlCs), 12cydigc clls, cndothelial cells and stromal cells also cxprcss IL-3Ra. 1L-3Ra is also exprcsscd by cclls it~volvcd in ccrlain discasc states including myelodysplastic syndrome, myeloid Icokernia (for example, acute inyeloge~~ous lcuke~nia (AML)), tnalignanl lymphoprolifcrativc disorders such as Iympl~oma, allergies and autoimmu~le disease, such as lupus, Sjogren's syndrome or sclcradcma. Accortlingly, anti-1L-3Ra antibodies arc desirable for therapeutic applications SUMMARY Tllc present disclosure is based on tlic i~~vcntorp'rso duction of a hurnanizcd antibody that binds spccifically to IL-3Ra. Following I~umanizdtioti, tlic iavcntor found that the afiinity of the antibody for IL-3Ra was reduced. Accordingly, tllc inve~ltopr erfornied affinity maturation to improvc the affinity of thc antibody for I - a . Unpredictably, tlie affinity matured antibody included mutations in the framework regions (FRs) of tlie heavy chain variable region (VII) and ligllt clrdin variable region (VI.), as well as in CDRI of tlie light chain. The inventor also produced folms of this antibody cdpablc of inducing cnh.dllccd lcvels of effectov function. Thc invc~itor also found that a particular modification to induce enhanced effector ft~~lctiorrcl sultcd in an additio~vdl desirable property in that following adininistratio~l of thc inodificd alltibody to a mammal the number of NK cclls in tlic mammal were initially rcduccd, howcve~th~e n expanded to levels greatcr than prior to administration. The inventor has also show11 that thcrc is a correlation between the ~lurnbeor f NK cells and lysis of targct cells, c.g., leukc~niac ells. The present disclosure is broadly directed to an immunoglobulin bilsed on a musine antibody capable of specifically binding to an 1L-3Ra chain. In one cxample, the present disclosure provides an isolatcd or recombinant in~~nui~oglobutlhinat spccifically binds to an 1L-3Rtx chain a~ldc oinprises complcmcntarity dctcrmining rcgions (CURS) of a V1, comprising a scqucncc sct fo~llin SEQ ID NO: 8 and CDRs of a VIIs et for111 it1 SEQ ID NO: 9. Thc prcsent disclosurc additio~vdlly or alternatively provides an isolatcd or recombinant antibody or antigen binding fragment thereof, the antibody or antigen binding fiagmcnt capablc of spccifically birldi~lgt o 1L-311a clrditl and comprising CDRs ofa V~,coniprisitiga sequelice set fo~tliln SEQ ID NO: 8 and CDRs oTa Vrr sct fort11 in SEQ Ill NO: 9. Tlic prcscnt disclosurc additio~vdlly or allelrlatively provides an isolatcd or rcco~nbinatlt liumanizcd antibody or antigcn binding fragment tlicrcof, tllc antibody or antigcn bindi~lgf ~dgtncntc al~ablco f spccifically binding to IL-3Ra chain and comprising CDRs of a VI, comprising a scquence sct forlli in SriQ ID NO: X and CDRs ofa VII set fo1.111 in SEQ ID NO: 9. In onc cxa~nple.t he prcscnt disclosorc providcs an isolnted or recombinant i~nmunoglobulint hat spccifically binds to an 11.-311a chain and compsises amino acid sequcnces according to SEQ ID Nos: 2-7, respectively. The present disclosure additionally or alternatively provides an isolated or recombinant antibody or antigen binding fi.agment thereof, the antibody or a~itigcn binding fragment capable of specifically binding to 1L-3Ra chain and comprising amino acid sequcnces according to SEQ ID NOS: 2-7. The prcsent disclosure additionally or alternatively yrovidcs an isolated or rcco~i~bi~hiau~m~a~t iizcd antibody or atitigcn binding fiagmcnt tlicrcof, tlic antibody or antigc11 binding fragment calsable of specifically binding to IL-3Ra chain and cornp~isinga mino acid sequcnccs according to SEQ ID NOS: 2-7. For cxample, tlic inimunoglobuli~o~r antibody comprises: (i) a liglit cliai~vi ariablc rcgioa (V1.J comprising CDRs 1, 2 and 3 as sct fo~thin SEQ ID NOS: 2,3 and 4, respectively; and (ii) a lleav)~c hain variable region (VII)c omprising CDRs 1, 2 and 3 as set forth in SEQ ID NOS: 5,6 and 7, respectively. For cxample, tlie immunoglobulin or antibody comprises: (i) a VIc~o mprising: a) a CDRI co~nprisi~a ~scgq i~cnccs ct forth it1 SEQ ID NO: 2 (or encoded by a sequencc sct forth in SEQ ID NO: 14); b) a CUR2 comprising a sequence set fort11 in SEQ ID NO: 3(or encoded by a scqucncc set forlh in SEQ ID NO: 15); and c) a CDR3 cotnprisi~iga sequence set foitli in SEQ ID NO: 4 (or encoded by a scqucncc set forth in SEQ ID NO: 16); and (ii) a VII comprising: d) a CDRl comprising a sequence set forth in SEQ ID NO: 5 (or cncodcd by a sequence set forth in SEQ ID NO: 17); e) a CDR2 comprising a sequence set forth in SEQ ID NO: 6 (or c~~coded by a sequcnce sct forth in SEQ ID NO: 18); and i) a CDR3 comprising a sequence set forth in SEQ ID NO: 7 (or cncoded by a scqucncc sct fort11 in SEQ ID NO: 19). The preselit disclosurc additionally or altclndtivcly pro\~ides an isolatcd or rccombinaot l~unia~~izacndt ibody or a~itige~bii llding fragment thcrcof, tlic antibody or antigcn'binding fragmcnt capablc of specifically binding to 1L-3Ra cl~aia~nid comprisi~iga VI, comprising ail a~ninoa cid scqucncc accordi~igto SEQ ID NO: 8 (or cncoded by a scquc~iccs cr fort11 in SEQ ID NO: 20) and/or a VII comprisi~iga n amino acid scquc~icca ccording to SEQ ID NO: 9 (or cncoded by a scqueticc sct forth in SEQ 1U NO: 2 1). 'l'hc prcsc~~dits closurc additionally or altcmativcly provides an isolatcd or recombinant humanized alltibody or antigcn bindi~ig fragmcnt tlicrcof, tl~c antibody or antigcn bintliag fragmcnt capablc of s~~ecificallbyin ding to IL-3Ra chain and coniprisi~ig a VI. comprising an amino acid scquencc according to SEQ ID NO: 8 (or cncodcd by a scquelicc set fort11 io SEQ ID NO: 20) and a VII comprising an amino acid scqucncc accordi~igto SEQ 111 NO: 9 (or encoded by a sequencc set forth in SEQ ID NO: 21). Exemplary aritigcrl biriditig fragments conteniplatcd by tlie present disclosule includc: (i) a domain alltibody (dAb); (ii) a Fv; (iii) a scFv or stabilized fonn tlicrcof (c.g., a disulfidc stabilized scFv); (iv) a dimcric scFv or stabilized form thcrcof; (v) a diabody, triabody, tctrabody or higlicr ordcr multimer; (vi) Fab fmgnicnt; (vii) a Fab' fragment; (viii) a F(ab3) f~agtncnt; (ix) a F(ab')z tkagment; (x) ally one of (i)-(ix) fuscd to a Fc rcgion of an antibody; (xi) any one of (i)-(ix) fused to an antibody or antigen binding fragment thereof that binds to an immut~ee ffector cell. In onc example, tlie immunoglobulin or antibody depletes or at least partly eliminates cells to which it binds, e.g., leukemic cclls andlor basopliils andlor pDCs. As will be apparent to thc skilled artisan from the disclosurc herein, cxcmplary immunoglobulins or antibodics arc capable of depleting or at least partly eliminating cells to wliich it binds without being conjugated to a toxic con~pound. In one examplc, tlic immunoglobulin or antibody is capable of inducing an effector functioti, c.g., an cffector fu~~ctitohat~t ~ s u l tisn killing a cell to which thc i~nrnunoglobulino r antibody binds. Exempla~yc ffector functions include ADCC, antibody-depende~~t cell-mediated phagocytosis (ADCP) an(Uor complcmcnt-dcpc~idc~ciyt totoxicity (CDC). In one example, the immonoglobulin or antibody is cal~able of inducing ADCC. In one cxamplc, tlie im~iiunoglobulino r antibody conipriscs an antibody Fc region capable of inducing an cffcctor function. For example, the efkctor function is Fc-mediated cffector function. In onc example, tlie Fc region is an lgG l Fc rcgio~o~r a n lgG3 Fc rcgiot~o r a hybrid lgGlllgG2 Fc region. In one example, tlie i1i1111unoglobulil1111oglobuoli1ri antibody is capable of inducing a similar (e.g., not sig~~ifica~d~ilt'flcyrc nt or within about 10%) or tl~csa me Icvcl of effcctor fu~~ctioasn a wild-type human 1gG1 andlor human lgG3 Fc legion. In onc cxaml~lct,h e inimunoglobuli~io r antibody is capablc of indi~ciiiga 11 enhanced lcvcl of cffector fuoction. In one example, tlie level of cffcctor funoglobulil111otio11 induced by tlic immunoglobulin or antibody is enhanced rclative to that of tl~cim munoglobulin or alltibody when it co~npriscsa wild-typc lgGl Fc rcgion. In one exa~iiplct he immuooglobulin or a~~tiboilyis afucosylated or comprises a Fc rcgion that is afucosylatcd. III another example, tlic i~nmunoglobulin or antibody has a lower level of fucosylation compared to an immunoglobulin or antibody produced by a human or a CHO cell that has not been altered to reduce tl~ele vel offi~cosylaliono f proteins. hi accordance with this example, a lower level of fucosylation will be understood to mean that in a composition comprising the im~nu~ioglobulionr antibody the pcrccntagc of fucosylatcd immunoglobulins (c.g., glycosyl groups attachcd to As11297 of an antibody cornprisi~lgf ucose) is lower than l~roducedb y a human or a C1-10 cell that llas not been altercd to rcduce thc lcvcl of fucosylation ofprotcins. For example, the immu11oglobulin or antibody is an afucosylatcd humanized antibody co~nl~risitalg V I. conlprising a scquc~~csect forth it1 SEQ ID NO: 8 (or encoded by a sequence set fort11 in SEQ ID NO: 20) and a VII comprising a sequence set forth in SEQ ID NO: 9 (or encoded by a scquc~lccs ct fort11 io SEQ ID NO: 21). For example, the immunoglobulin or antibody is an afucosylatcd Ilumanized antibody comprising a light chain comprising a sequencc set forth in SEQ ID NO: 13 (or cncodcd by a syucncc set forth in SEQ ID NO: 23) and a hcavy chain co1ilprisil1g a sequence set forth in SEQ ID NO: 10 (or encoded by a scqucnce sct forth in SEQ ID NO: 22). In one example, the i~~~mu~~ogloobr uanlitinb ody is a humatlizcd antibody comprisi~lg a light chai11 cotnprising a sequence set forth in SEQ ID NO: 13 (or encoded by a syucnce sct forth in SEQ ID 30: 23) and a licavy chain comprisi~ig a sequcncc set forth in SEQ ID NO: 10 (or e~~codebdy a seqoence sct forth in SEQ ID NO: 22) expressed by a u~ammdlia~cle ll (e.g., a CHO ccll) Ihal does not cxprcss detectable lcvels of (or cxprcsses rcduccd lcvcls ol) a-1,6-fucosyltransferasc (FUT8). 111 one example, the immunoglobulin or antibody comprises all Fc region conlprisi~lg o~lc or morc amino acid seclucncc substitutions that cnhancc thc cficctor function induccd by tllc immunoglobulin. For examplc, tl~co ne or inore a~ninoa cid scquc~~csucb stitutiolls iilcrcasc thc affinity of thc Fc rcgiotl for a Fcy reccptor (FcyR) coniparcd to tl Fc rcgion not comprising the s~~bstitutions. For cxample, thc onc or more atnillo acid si~bstitutionsc nhance incrcasc tl~caf finity of thc Fc region for a FcyR selected from the group consisting of FcyRI, FcyRlla, FcyRlIc ;ind FcyRIEa compared to a Fc region not comprising tllc substitutions. In one examplc, thc ~ I I Co r lnorc arnino ;icid sequence substitutio~~arse : (i) S239DDA, 330L and 1332E accot.di11g to tllc EU nu~nbcringsy stcm of Kdbat; or (ii) S239D and 1332E according to tllc EU numbering systcm of Kabat. For CXRI~IPIC, thc i m n ~ ~ ~ ~ o g loor ban~ti~boldiy~ i~s a hutnmizcd mtibody cornprisieg a VL cotnprisit~git S ~ U C I I C Csc t fort11 ill SEQ ID NO: 8 (or c~lcodedb y a scquolcc set forth in SEQ ID NO: 20) and a VII comp~.isiog a sequence set fort11 in SEQ ID NO: 9 (or c~lcodcdb y a scquence set Corl11 in SEQ ll) NO: 21), wllcrein thc aotiboily cotr~prisesa Fc regio~ti~u tnprisi~lgo nc or nlorc amino acid scquc~~cc substitutio~lss clcctcd from the group cot~sistillgo f: (i) S239D, A330L and I332E according to the EU numbering systcm of Kabat; and (ii) S239D and 1332E according to the EU numberirrg system of Kabal. In onc example, the Fc rcgio11 compriscs a sequence set forth between residues 234-450 of SEQ ID NO: 11 (comprising the S239D and I332E s~~bstitutioancsc ording to thc EU nuinbcring systcm of Kabat). 111 one cxainple, the Fc regioo comprises a sequence set furth betweeit rcsidues 234-450 of SEQ TD NO: 12 (comprising the S239D, A330L and 1332E substitutions according to lllc EU numbering system of Kabat). 5 111 onc cxamplc, thc immunoglobulin or antibody is sclcctcd from thc group consisting of: (i) an antibody comprising a light chain co~np~isina gsc quence set fo~lhin SEQ ID NO: 13 and a heavy chaitl comprising a sequence set f o ~ i~n hS EQ ID NO: 1 1; (ii) an antibody comprising a comprising a light chain comprising a sequcncc 10 sct foiih in SEQ ID NO: 13 and a heavy chain comprising a sequence set forth in SEQ ID NO: 12. As discusscd herein abovc, thc i~lventor has determined that following administration of an antibody described herein, the number of NK cells in ciizulation in a mammal are initially reduccd aud then illcreased co~nparcd to the 15 number of NK cells in circulation in the ma~nmal piior to administration. The iovcntor has also shown that increasing the number of NK cells relativc to target cells results in increased efficacy, is., a greater number of targct cclls arc killcd. This effect is induced by an antibody comprising a constant rcgion or Fc rcgion comprising amino acid substitutions S239D and 1332E according to the EU 20 nutnbering systeni of Kabat. Thns, in onc cxamplc, thc present disclosure provides an isolated or recoinbina~~ant tibody, which is capable ol spccifi~allyb inding Lo IL-3Ra clvaii~ and comprising: (i) a ligl~ct hill variable rcgion (Vl,) colnprising CDRs 1, 2 and 3 as set forth in 25 SEQ ID NOS: 2, 3 and 4, respectively; (ii) a hcavy chain variahlc region (VII) comprising CDRq 1, 2 and 3 as set forth in SEQ ID NOS: 5,6 and 7, rcspcctivcly; and (iii) a hcavy chain constant region cotnprisiilg ainiuo acid substitutions S239D and 1332E according to the EU numbering sysicrn of Kabat. 30 I11 onc exainl)lc, thc prcscnt disclosure provides an isolated or recombina~li Immanizcd antibody, thc antibody capablc of specifically binding to 11,-3Ra chaitl and cotnprising: (i) a Vr. comprising: a) a CDRI comprisitlg a scquc~~sccct forth in SEQ 11) NO: Z (01.e ncoded 35 by a sequcnce sct forth in SDQ ID NO: 14); b) a CDK2 comprising a scqucncc sct fort11 in SEQ ID NO: 3(01. cncodcd by a sequencc set forth in SEQ ID NO: 15); and c) a CDR3 comprising a sequence set forth in SEQ ID NO: 4 (or cncoded by a sequence set forth in SEQ ID NO: 16); 40 (ii) a VH comprising: d) a CDR 1 comprising a sequence set forth in SEQ ID NO: 5 (or encoded by a sequence set forth in SEQ ID NO: 17); C) a CDR2 cotnprising a scqucncc sct forth in SEQ ID NO: 6 (or c~~codcd by a scquence set forth in SEQ TD NO: 18); a ~ ~ d f ) a CDR3 comprisilig a sequence set forth in SEQ ID NO: 7 (or encodcd by a acqucnce set forth in SEQ ID NO: 19); and (iii) a hcavy clrain co11sta11t rcgion con~prising amino acid substitutions S239D and 1332E according to the EU numbcriag system of Kabat. In onc example, the heavy chain co~lstar~eg~ito n is a hybrid of a hurnan lgG1 and a human IgG2 constant regions. In o11e cxamplc, thc constant rcgion comprises a scc~ucnccs ct fortli between residues 121-450 (inclusive) of SEQ ID NO: 11. The present disclosurc additio~lallyo r alternatively providcs an isolated or recombinant humanizcd antibody, the antibody capablc of spccifically binding to IL-3Ra chain and cotnptising: (i) a VI. comprisi~~agn a~ninoa cid sequence according to SEQ ID NO: 8 (or encoded by a sequence set forth in SEQ ID NO: 20) aildior a VI* co~nprisi~la1g1 amino acid sequence according to SEQ ID NO: 9 (or encoded by a sequeticc set forth in SEQ ID NO: 2 1); and (ii) a hcavy chain constant region comprising amino acid substitutions S239D and 1332E accordi~lgto the EU numbering system of Kabat. 111 o~ice xample, the heavy cl~aic~oln stant region is a hybrid of a human IgG 1 and a human lgG2 constant rcgions. 111 onc exa~nplcL, lic c u ~ ~ s lrdc~g~iut~ c~or ll]~riscsa sequcncc set l'orll~b etween rcsiducs 121.450 (i~lclusivc)o f SEQ ID NO: 1l The present disclosurc additio~lallyo r altcr~iativclyp rovidcs an isolatcd or rccornbinant huma~iizcd antibody, the antibody capable of spccifically binding to IL-3Ra chain atid comprising a VI. comprising at1 amino acid scqucncc according to SEQ ID NO: 8 (or cncodcd by a scqucncc set forth in SEQ ID NO: 201, a VII comprising an amino acid scqucncc according to SEQ ID NO: 9 (or c~icodcd by a scquence set forth ill SEQ ID NO: 21) ant1 a l~cavy cliain cotistiant rcgion comprising a ~ l i i ~a~ciod substitutions S239D and I332E accordi~lgt o the EU numbering systcrn of Kabat. III o~lcx amplc, the hcavy chaitl constant region is a hybrid of a human lgG1 and a Iiu~nunlg G2 constant regions. 111 one example, thc constant region conipriscs a scqucncc sct forth between rcsiducs 121-450 (i~lclusive)o f SDQ ID NO: I1 111 one cxamplc, the prcscnt disclosurc providcs an isolatcd or rccornbinant humanized antibody, the antibody capable of specifically binding to IL-3Ra chain and comprising a light chait~c omprisir~ga sequencc set forth in SEQ ID NO: 13 and a hcavy cliain comprising a sequence set forth in SEQ ID NO: I I . la onc examplc, an immn~~noglobulionr antibody or a~itigcb~iln ding Gagment thereof of the presellt disclosure iieutralizes 1L-3 signaling. 111 one example, an imn~unoglobulino r antibody of the present disclosure is a nakcd im~nu~loglobulioilr an alltibody or antigcn bitiding fragmcnt thcrcof of the prcsc~ldt isclosure is a i~alieda ntibody or antigel1 binding fragment thcreof In onc cxample, an imn~u~loglobulionr alltibody of tlic present tlisclosure is a full length antibody. In onc cxamplc, an im~nutioglob~~olri ~ani tibody of the prcscnt disclosurc binds to IL-311a cl~ainw ith at1 equilibrium dissociatiot~c onstaut (Ko) of 1 x 1 0 ~ ~ ~ or Icss, such as 5 x 1 0 .o~r ~Ics s, for cxamplc, 3 x 1 0 . ' ~o r Icss, such as 2 . 5 ~ 1 0 ~ ~ or less. In one cxample, an immunoglobulin or antibody of the prcsent disclosure binds to 1L-3Ra chain with a KI, of about 2 . 2 ~ 1 0 ~or' l~es s. In one cxample, the KI, is bctween about 1 x 1 0 ~ 'a~nd about 2.5x10~'~f,o r examplc is about 2 . 2 ~ 1 0 " ~ . In one cxample, an immu~ioglobulin or antibody of thc prcsent disclosure binds to IL-3Ra chain with a KD of about 9 x 1 0 . ' ~o~r l ess, for cxample, about 8x10."'~o r less. 111o ne example, the K,, is between about 5 x 1 0 ~an' d~ a~bo ut 9 x 1 0 . ' ~f~or, e xample is about 7 . 8 ~ 1 0 ~ ' ~ ~ . The disclosure also includes fsagrncnts, variants and derivatives of the itnmunoglobuli~o~r antibody of the disclosurc. I11 one example, an im~nu~loglobuloi~r ia lltibody of the present disclosure is capablc of rcducing the nunibcr ofNK cclls whcn administered to a ti~a~iiri(~c.agl. , a non-human primate, snch as a cynomolyls monkey). For example, the irnmu~~oglobuloinr antibody is capablc of rcducing tllc nurnbcr of NK cells whco adtiii~iistcrctlt o tlic liiat~nni~byl $11 ]cast about 20%, such as at l a s t about 30% or 40% within 12 liours or 10 horns or 8 hours of administration. For cxamplc, tllc immunoglobulin or anti1)ody is capable of reducing tbc numbcr of NK cclis when adn~inistcrcd to ll~c mammal by at least about 50% within 6 hours of administration. In ouc cxamplc, thc i~nmunoglobulin or alltibody is capablc of reducing tlic tlumbcr of NK cells when administered at a dosc of betwceli 0.0001mg/kg and SOmglkg, ssucl~ as between about 0.0005rngikg and about 40mg/kg, for cxamplc, bctween about 0.001mg/kg and about 301ng/kg, such as about 0.0051ngikg and about 20mg/kg, such as about 0.0lmdkg and about IOmg/kg. For cxamplc, thc i~n~nunoglobulionr alltibody is capablc of reducing tlrc numbcr of NK cclls wl1e11 administered to the mammnl by at least about 50% within 6 hours of administration whcn adtninisterect at a dose of about O.OImg/kg or O.lmg/kg or lmglkg or lOmg/kg. In one example, thc dosc is about 0.01 mg/kg or 0. Imgikg. In one examplc, thc nurnbcr of NK cells in the mammal is increased about 7 or8or9or10or11or12or13or14or15orI6or17or18or19or20or22or 29 or 57 days after administeri~igth e immu~ioglobulio~rl antibody coml~aredto the number of NK cclls in the mammal prior to admi~iistrationo f the immunoglobulin or antibody. For cxatnple, the tmmnbcr of NK cells is increased at least about 8 or 1 1 or 17 or 22 or 29 days after administration. For example, the number of NK cclls in tllc mani~iiali s i~icrcascdb y about 10% or 20% or 30% or 50% or 60% or 70% or 80% compared to the uumber of NK cells in tlie mammal prior. to administration of tlie inimu~~oglobuloinr antibody. For example, the number of NK cclls in thc mammal is increased by about 20% at least 8 days after admi~listratioo~fi thc antibody or i~n~iiunoglobulait~ ai dose bctwcc~i0 .0011ngikg and O.lmg/kg compared to the ~iumbcr of NK cells in tllc ~iiai?ltlial prior lo administratio11 of the immunoglobulin or antibody. For example, the ~iu~i~obfe r NK cells in the mammal is incrcaed by about 50% at lcast l I , 17, 22 or 29 days after administration of the alltibody or immunoglobulin at a dose between 0.001mgikg and O.lmg/kg compared to the number of NK cells in tlle mammal prior to administration of the imlnulloglobulin or a~itibody. In oue example, the antibody or immunoglobulin is administered at a dose of between O.Olmg/kg and 0.lmdkg. For example, the itn~i?unoglobulino r antibody is adnii~lislercda t a dose of O.Olmg/kg or O.lmg/kg. Based on the disclosurc herein, it will bc apparent to the skilled artisan that the pleseut disclosure providcs an immunoglobulin or antibody that, wlle~i administered to a mammal, causcs an increase in the number of NK cells in the mammal. For example, the immunoglobulin or antibody, whco administered to a mammal, causes a reduction in the number of NK cells in the mammal followed by an incrcase in the number of NK cells. 111 one example, the number of NK cells is incrcascd or reduced comparcd to the number of NK cells in the rnammal prior to adtninistration ol'thc immunoglobulin or antibody. I11 one cxamplc, thc immu~ioglobulin or antibody is capablc of rcducing thc number of NK cells in the mammal by at lcast about 50% within 6 hours of adminisfration when administered at a dosc of about 0.0lmg/kg or O.lmg/kg and the number of NK cells in the mammal is increased by about 20% at lcast X days aflcr administration of thc antibody or immunoglobulio at a dosc bclwcct~ 0.001m~kgan d O.lnig/kg compared to tlie numbcr of NK cclls in thc ma~liilral prior to adtninistration of the in?munoglobulin or antibody. 111 one cxamplc, the disclosure provides a pl~armaccutical compositio~i comprising an imm~moglobulin or antibody accordirlg to tlic present disclosurc and a pl~ar~iiaccuticallayc ccptablc carricr, diluc~tot r cxcipictit. The preseot disclosure also provides all isolated nuclcic acid cncoding an immunoglobulin or alltibody of the present tlisclosure. ExempLary sequences of nucleic acids arc discussed in thc co~~tcxotf c~~codiuangt ibodies or immt~oogloboli~o~f st he disclosure and arc to bc tahe~Lo~ apply nzurtrtis nzutcmdis to the prcsc~lt cxamplc of the disclosurc. The present disclosurc also providcs a nuclcic acid capablc of hybridizing to a nuclcic acid of thc disclosurc under high stringci~cyh ybridization conditions. The disclosure also includes kagments, llornologs atid derivatives of an isolated 11ucleic acid of the disclosore. The present disclosure also provides a genetic construct comprising an isolatcd ~iuclcic acid of thc disclosurc and onc or morc additior~al nuclcotitlc sequences, such as a promoter operably linked to the nuclcic acid. In one example, the gcnctic construct is an expression construct comprisi~~g ail expressio~v~a lor and an isolated nucleic acid of thc disclosurc, wherein said isolatcd nuclcic acid is opcrably liiikcd to onc or niorc rcgulato~yn uclcic acids in said expressio~vi ector. In one examplc, the genetic construct of the disclosure cotnprises a ~iuclcic acid encoding a polpcptidcs (e.g., comprising a VII) operably linked to a promoter and a nucleic acid encoding ar~othcrp olypeptidc (e.g., comprisi~iga V1j operably litlked to a promotcr. 111 another example, the getictic colistruct is a bicistronic genetic constluct, e.g., comprising the following opcrably linked components in 5' to 3' order: (i) a promoter (ii) a t~ucleica cid encodi~iga first polypeptidc; (iii) an internal ribosonie entiy site; and (iv) a ~luclcica cid encoding a sccond polypeptidc. For examplc, tlic first polypeptide comprises a VII and the second polypeptidc compriscs a VI., or the first polypeptide comprises a VL and thc second polypeptide compriscs a VH. Tlic prcscnt disclosurc also contemplates separate gcnetic constructs onc of which cncodcs a first polypcptide (e.g., comprising a Vrr) and another of whicli cncadcs a sccond poly1)el)lid~(c .g., conrprising a VI). FUI-e xan~ple,t he prcsent disclosurc also providcs a cornpositio~ci ompvising: (i) a first expression constmct comprising a nuclcic acid cncoding a polypeptidc (c.g., comprising a Vli) operably li~iltedt o a promotcr; and (ii) a seco~id expression construct comprising a nuclcic acid encoding a polypcptidc (c.g., comprising a Vl.) opcrably litlkcd to a prornotcr. The disclosure also providcs a host ccll co~nprising a gctictic construct i~ccordingto thc prcsent disclosure. 111 one example, the prcsent disclosurc provides an isolatcd cell cxprcssing an immunoglobulin or antibody or antigcn binding fragtncnt of tlic disclosurc or a rcconibinant ccll gcnctically-modificd to cxprcss tlic itnmunoglobulin, antibody or antigcn binding fingincnt. In one example, the ccll compriscs thc gcnctic cotistruct of thc disclosnre 01.: (i) a first gcnctic construct comprising a ~~ucleaici d encoding a polypcptidc (c.g., comprisi~~a gV H) opcrt~blyli nkcd to a prornotcr; and (ii) a. second genetic constnlct co~nprising$ 1n ucleic acid encoding a polypeptide (c.g., comprising a VI,) operably linked to a promoter, whereit1 the first and second polypeptides form an immunoglobulin, antibody or antigcn binding fragmcat of the prcscnt disclosure. The genetic co~istmctc an be integrated into the cell or remain cpisomal. Exa~nplcs of cclls of thc prcscnt disclosurc i~icludc bacterial cclls, yeast cells, insect cclls or mannlialian cclls. The present disclosure additio~~allpyr ovides a method for producing an immunoglobulin, antibody or a~ltigcll binding fragment of the disclosure, thc mcthod comprising maintaining thc gc~~ctciocn struct(s) of thc disclosurc under conditions sufficient for thc immunoglobulin, antibody or antigc~b~i nding fragment to bc produced. 111 one example, tlie method for producing an immu~~oglobulinan, tibody or atitigen binding fragrne~it of the disclosure comprises culturing the cell of the disclosure under conditions sufficient for tlie irnmunoglobulin, antibody or alltigel1 binding Fagment to be produced and, optionally, secreted. hl one example, the method for producing an immunoglobulin, antibody or antigen binding Fagment of the disclosure additio~lally comprises isolating the itntnunoglobulin, antibody or antige~bi illding fragment. The present disclosure additio~lally provides a method of producing a recombioat~ti mmunoglobuli~o~r antibody of the disclosure, the ~nctllodi ~~cluding the stcps oC (i) culturing a 11ost ccll containing an exprcssio~v~e ctor according to the disclosure such that the recombinant immu~loglobuloi~r~ a ntibody is expressed in said Ilost cell; and (ii) isolating tllc rccombioant immunoglobulin. In one examplc, a mcthod for producing an irnmunoglobulin, antibody or antigen binding fragmcnt of thc disclosurc additionally coml~riscsf ormulating thc immunoglobulin, antibody or antigen binding fii~gtnclttw ith a plra~~nr~ceutically acceptablc carrier. The present disclosure also provides a method of prophylactic or therapeutic trcatmcnt of a disease or co~iditioni ll a mammal, tl~cm cthod including tl~csi c]) of administering the immunoglobulin or antibody of the disclosore to the mammal to tlicreby trcat or prcvent the disease or condition. In one exnmple, the rnammal is a l~uman. 111 onc cxatnplc, thc tna~iimali s in ~lcedo f trcatmcnt or prophylaxis. 111 o~icx amplc, thc mammal in need suffcrs from thc discasc or condition. 111 one exa~nple!,h e mammal it1 oeed is at risk of developing the discasc or condition or a rclapsc thereof. 'l'hc present disclosurc also provides for usc ol'an immunoglobuli~~an, tibody or allligc~b~it rding k a g ~ n eo~f ~thtc disclosorc or a cotnposition oftlle disclosurc ill medicine. The present disclosure additionally or altern'dtively provides for usc of an immunoglobulin, antibody or antigen binding fragmcnt of the disclosure in the rnanuftdcture ofa medicament for drc treatment ofa disease or co~~ditiion ~ai mammal. The present disclosure also provides an im~nu~ioglobuliann, tibody or antigcn bindi~igf ragment of tlic disclosure for usc in the trcdtnietit of a dismsc or conditio~iin a mammal. In one examplc, the discase or condition is an L-3Ra-mediatcd disease or cotidition. 5 In one cxamplc, thc discasc or condition is myclodysplastic syndrome. In one examplc, tlic diseasc or co~iditiois~ c~a ncer, such as a Iicmdtologic caiiccr, for cxample, lcukcmia, such as an acutc lcukemia (c.g., acute ~nyelogc~ious leukemia) or a chronic leukemia (e.g., chronic myclomo~iocyticle ukemia). 111 one example, tlie disease or condition is an IL-3Ra-associated canccr, c.g., 10 leukernid, i.e., the canccr (or lcukcmia) is characterized by cancer (or icukcmia) cells expressing IL-3Ra. 111 another examplc, the canccr is a malignant lympl~oprolifcrativcd isordcr such as ly~nplioma. hi one exatnplc, thc discase or condition is an a~ctoimmunec ondition or an IS inflammato~yc ondition. For example, the co~iditiotis lupus, c.g., systemic lupus erytlirematosus, Sjogren's syndrome or sclerode~ma(e .g., systemic scerodcrma). I11 one example, the method comprises administering an effective amount of the immu~ioglobulin, such as a therapeutically effective anioulit of thc 20 immunoglobulin, atitibody or antigen billding fragment. In one example, tlic method compriscs administering betwccn about 0.00011nglkg arid 50mgikg of immunoglobulin, antibotiy or antigen biildi~ig ftagmcnt to the tnammal. For cxatiiplc, thc mcthod cotllpriscs administcring between about 0.000Smdkg to about 401ndkg. For cxamplc, tlic mctliod 25 comprises administering between about 0.0005mglkg to about 30mglkg. For example, the mcthod compriscs adrninisteritig betwec~i about 0.001mgikg to about 201nglkg. For cxdmplc, tl~c mcthod compriscs ad~ninistcring bctwccn about 0.001mglkg to about IOmgiIcg. For exiimple, tl~c mcthod co~~ipriscs administering betwccn about O.Olmg/kg to about Smglkg. For examplc, the 30 method cornprises administcri~igb etweell about 0.001mglkg to &out Imdkg. lo onc cxamplc, tlic nictl~od co~iipriscs administcring bctwcc~l about O.lnlg/kg to about IOmdkg of tbc immunoglobulin, antibody or a~itigclib illding fiagiient. For examplc, tlic inctl~od comprises administcrit~g bctweet~ about 0.lmglkg to about 51nglkg. I'or cxarnple, tlic mcthod compriscs administeritig 35 between about 0. I mg/kg to about ImpJkg. I11 olic cxamplc, ihe nictliod co~iipt.ises ad~iii~iiatcriribgc twcei~ about I01ndkg to about 30mpJkg of the immunoglobulin, antibody or antigen binding fragment. For cxample, tlie method cornprises administering between about 20mglkg to about 30mgiky. 40 111 one example, the immunoglobuli~i, antibody or antigct~ binding fragment is ad~ni~iistcrcadt a dose of 0.0lmgkg. In one example, the im~nunoglobulin, antibody or antigen binding fragmcnt is administcrcd at a dosc of 0. lmgikg. Jn one example, tile irnmunoglobulin, antibody or a~tigen binding fragmcnt is administered at a dosc of Imdkg. 111 one cxatnple, the immunoglobulin, antibody or antigen binding fragmcnt is adrninistcrcd at a dosc of IOmdkg. In one examplc, the immunoglobulin, antibody or antigen binding fiagncnt is administcred at a dosc of 301ng/kg. In one example, the im~nnnoglobulio~r~ a ntibody is administered to the mammal a plurality of times. 111 one example, thc pcriod bctwccn administrations is at least about 7 days, such as at least about 8 days, for cxample, at lcast about 9 days or 10 days. In onc cxamplc, tlic pcriod bctwccn administrations is at lcast about 11 days. 111 anothcr examplc, the pcriod bctwcen administrations is at least about 15 days, such as at least about 16 days, for example, at lcast about 18 days or 20 days. In one cxample, tlie period betwcen administrations is at least about 22 days. In anothcr example, the period between administrations is at least about 25 days, such as at least about 30 days, for example, at least about 40 days or 45 days. In one example, tlie period between administrations is at lcast about 57 or 60 days. For example, thc immunoglobulin, antibody or atitigen binding do~nai~isi administered at a dosc of bctwecn 0.00011ndkg and Snidkg, such as between 0.0005mg/kg and Srndkg, for cxamplc, between 0.001mg/kg and Smdkg, and tlie peliod bctwccn admin~stmtions is at lcast about 7 tlays or 8 ddys or 9 days or I0 days or 11 days or 14 days or 17 days or 21 days or 22 days or 28 days or 20 days or 30 days or 1 cnlcnd;a month. For cxa~nplct,h c in~munoglobulin,a ntibody or antigen bioding domain is administcrcd at a dosc of bctwccn 0.0lmylkg and 5mg/kg and the period betwcen ad~ninistrationsi s at lcast about 7 days or X days or 0 days or 10 days or 11 days or 14 days. For cxamplc, tllc irnmunoglobulin, antibody or antige~b~i llding do~nain is administcred at a dosc of betwccn 0.01 mdkg and 2mdIcg and tlic period bctwcen admioist~ations is at least about 7 days or 8 days or 9 days or 10 days or 11 tlays or 14 days. For example, tlle immunoglobulin, antibody or antigcn binding dotnain is administcrcd at a dosc of bctwccn 0.Olm~kikga nd I nidkg and tlic pcriod bctwccn administrations is at lcast about 7 days or 8 days or 9 days or 10 days or 11 days or 14 days. 111 sotnc cxamplcs, tlic pcriod between ~dministrationsis at lcast about 7 days and lcss thar~ about 22 days, sucli as at last about 11 days or 15 ddys and lcss than about 20 days, for example at least about 13 days and lcss than about 18 daya. Jn one cxamplc, tlie i~nmunoglobulin,a ntibody or antigen binding domain is administered at a dose of O.Olnig/kg and the period between administrations is 6 days or 7 days or X days or 9 days or 10 days or 11 days or 14 days or 15 days. In one example, the immunoglobnlin, antibody or antigen binding domain is administered at a dose of 0.lmdkg and tlic period between administrations is 6 days or 7 days or 8 days or 9 days or 10 days or 11 days or 14 days or 15 days. I11 o~icx amplc, thc iiniiiunoglobuliu or antibody is administcrcd at a dosc of inig/lcg aiid the pcriod between administratio~isi s 6 days or 7 days or 8 days or 9 days or 10 days or 11 days or 14 days or 15 days or 20 days or 21 days or 22 days. For cxaniplc, thc immunoglobulin or antibody is adtiii~iistcrcd at a dosc of between 6mgikg and 501ngkg and the period between ad~liitiistratio~is~ sa t least about 15 days. For examplc, tlic immunoglobulin or antibody is administered at a dose of between 1 Omgikg and 30mgikg and thc period between administrations is at least about 14 or 15 days. For cxample, the immunoglobulin or antibody is adrni~~istcrcadt a dosc of bctwcc~i2 01iigikg aiid 30tngkg and the pcriod betweell administratioils is at lcast about 14 or15 days. I11 some examples, the period between administrations is at least about 20 days and less than about 70 days, such as at least about 21 or 22 days and less tlra~ia bout 65 days, for example at least about 25 days and less that1 about 57 days. I11 one examnple, the initnunoglobulin or ailtibody is administered at a dose of IOmgikg and tlic period between adtninistrations is 14 days or 15 days or 21 days or 22 days or 30 days or 48 days or 50 days or 56 days or 57 days or 60 days. oiie example, tlie immuiloglobuliii or antibody is adniiiiistered at a dose of 30mgkg and tlie period betwec~ia dmi~listratiollsi s 14 days or 15 days or 21 days or 22 days or 30 dnys or 48 days or 50 days or 56 days or 57 days or 60 days. As discossed abovc, tlic invcntor has found that following adrninistratioii of an immutioglobulin or antibody of thc disclostrre the number of NK cells is iiicrcascd abovc thc ~luiiibcr prcscnt bcforc administration within about 8 days. Tlie invcntor has also sliowt~ that increased ~iuiiibcrs of NK cclls incrcasc tllc efficacy of an antibody or immunoglobulin of thc disclosure in inducing death of target cells. Thus, once the number of NK cclls is increased, a further dose oftlic antibody or immunoglobulin call bc adniinistcrcd to inducc a tlicrapeutic/propliylactic effect. For example, an immonoglobulin, antibody or antigcn binding fiagmcnt of thc disclosure is administcrcd a plurality of times at a dosc of bctwcc~a~b out 0.0011ngikg and about l~ngikgw ith a pcriod betwccri adtninistrations of at lcast about 7 days, such as, at lcast about 8 (lays, for cxamplc, at lcast about 11 days, such as at lcast about 14 days, for cxamplc, at lcast about 17 days, sucl~a s at least about 21 days, for exatnplc, at least about 22 days, for cxamplc, 28 days or 29 dnys or onc calcadar niontli or 56 or 57 or 60 days. Tn one examplc, tlie period between tloses is about 7 days. In one cxamplc, the period bctwccn doses is about 8 days. I11 onc cxarnplc, the period belwce11 doses is about 11 days. In onc cxamplc, tlie period betwee11 doses is about 14 days. In one example, tlie period between doses is about 17 days, In olic cxample, the period betweell doses is about 21 days. hi one example, the period between doses is about 22 days. In one example, the period between doses is about 28 days. 111 one example, the period between doses is about 29 days. In onc example, tlie dose is betwce~a~bo ut 0.011ngkg and about O.lmgikg, such as a dose of about 0.0Imglkg or 0.ltngIkg. BRIEF DESCRlPTION OF TI-IE DRAWINGS Figure 1A is a graphical representation showing tllc number of ?4K cells in a saml~lcfr om a non-human primatc sul?jcct at various timc points (as indicatcd) following administratio~i of antibody CSL362X2. Tlic number of cells is represented as a percentage of thc number of cclls prior to admi~iisteri~itgli e antibody. Dosages of the antibody arc indicatcd. Figure 1B is a graphical representation showing the number of NK cclls in a sample from a non-human pri~nate subject at various time points (as indicatcd) following administ~ation of antibody CSL362B. The numbcr of cclls is represetlted as a percentage of the ouniber of cells prior to adnii~iistcring tlic antibody. Dosages of the antibody are indicatcd. Figure 1C is a gmpllical representation showing thc liurnber of NK cells in a sample from a non-Iinman primate subject at various timc points (as indicated) following adminiseation of a cliimcric antibody (designated CSL360) comprising a human IgGl constant domain and the variablc region of antibody 7G3. The number of cells is rcprcsetltcd as a percetltagc of tllc number of cells prior to administering tlic antibody. Dosages of tlie antibody are iiidicated. Figure 2A is a graphical reprcse~ilation showing tllc percentage of TF-I cells lysed in the presclicc of thc illdicatcd cell pol~ulation and antibody CSL302X1 at various concenuations (as indicatcd on the X axis). Figure 2B is a gral~hical rcl>rcscnlntion showi~lg tlic pcrccntegc of AML cells in the presence of various numbers of NK cells and antibody CSL362X1. The ratio of cffcctor cclls (NK cclls; E) to targct cells (leukemia cells; T) is indicated on the X axis. Results generated sui~igc ells from two paticms arc dcpictcd. DETAIL.ED DESCRIPTION Key to Seque~~Lcies tiug SEQ ID NO: I --amino acid scqucncc of ll.-311u cliai~~ SEQ ID NO: 2 - arliitio acid sequcncc of LCDRl of humanized anti- IL-3Rn cllain alltibody CS1.362 and modified forms thereof SEQ ID NO: 3 a m i n o acid sequence of LCDR2 of humanized anti- IT..-3Rn cllaili a~~tiboiClyS L362 and ~liodificdf orms thcrcof SEQ ID NO: 4 - a~oinoa cid scquc~oco f LCDR3 of I~u~nanizeadn ti- 11,-3Rcx cllai~l antibody CSL362 and modified forms thereof SEQ ID NO: 5 - amino acid sccluence of HCDRl of humanized anti- 1L-3Ru cllain antibody CSL362 and modificd forms thcrcof SEQ ID NO: 6 - amino acid sequence of HCDR2 of humanized anti- IL-3Ra chain antibody CSL362 and modified forms thereof SEQ ID NO: 7 - a~ni~iaoci d sequence of HCDR3 of humanized anti- IL-3Ra chain antibody CSL362 and rnodificd forms thcrcof SEQ ID NO: 8 amino acid sequcnce of liglit chain variable region of liu~ivanized anti- IL-3Ra chai~ai ntibody CSL362 and modified forms thereof SEQ ID NO: 9 - amino acid sequcnce of heavy chain variable region of 5 hu~iiatiizcda nti- IL-3Ra chai~ain tibody CSL362 and ~iiodificdf orms thcrcof SEQ ID NO: 10 - arni~ioa cid sequence of lieavy cliain of Iiumanized anti- IL-3Ra chain antibody CSL362 and CSL362B SEQ ID NO: 11 a m i n o acid scqucnce of heavy chain of humanized anti- 11.-3Ra chain antibody CSL362Xl 10 SEQ ID NO: 12 - anii~ioa cid sequence of heavy chai~oi f humatiized anti- IL-3Ra chain a~itibodyC SL362X2 SEQ ID NO: 13 -amino acid scquence of light chain of huma~iized anti- IL-3Ra chain antibody CSL362 and modificd forms thcrcof SEQ ID NO: 14 - ~lucleotide sequence encoding a LCDRI of Iiuma~iized anti- 15 IL-3Ra chain antibotly CSL362 and modificd forms thereof SEQ ID NO: 15 - nucleotide sequencc ellcoding a LCDR2 of humariized anti- IL-3Ra chain antibotly CSL362 and modified forms thereof SEQ ID NO: 16 - ~iuclcotides equcnce e~icodi~aig L CDR3 of humanized anti- IL-3Ra chain antibody CSL362 and modified forms thereof 20 SEQ ID NO: 17 - ~iucleotides equence cncoding a HCDRI of hu~i~a~iizaendti - IL-3Ra chain antibody CSL362 aud modificd forms thereof SEQ IDN O: I X - ~n~clcotidscq ucnce cncoding a I-ICDRZ of humanized anti- IL-3Rr~c hain alltibody CSL362 and ~iiodificdf orms tlicrcof SEQ ID NO: 19 - ~lucleotides cqucncc encoding a HCDR3 of Iiurntuiized tunti- 25 IL-3Ra chain antibody CSL362 and ~nodificd hrms thcrcof SEQ ID NO: 20 -- nucleotidc sequence encoding a light chain variable region of humanized asti- IL-3Ra cliai~ai lltibody CSL362 and modificd fotrns thcrcof SEQ ID NO: 21 - nucleotide sequence encoding a licavy chain variable region of humanized anti- IL-3Ra chain antibody CSL362 aud modified forms thereof 30 SEQ ID NO: 22 - nucleotidc scqucncc encoding a hcavy chain of Iiumanized anti- JL-3Ra chain antibody CSL362 and CSL362B SEQ ID NO: 23 - nuclcotidc scqucncc encoding a light chain of Iiumanizcd anti- IL-3Ra chain alltibody CSL362 and modified for~rlsth crcof 35 General 'l'l~rougl~ootth is specification, u~ilcsss p~ificallys tatcd olllerwisc or tlie coiitcxt rcquilrs otlic~wisc, refcrc~icc to a single step, composition of matter, group of steps or group of compositiorls of matter shall bc takc~tio encompass one and a plurality (i.c. one or more) of those steps, compositions of matter, gro~lpso f 40 steps or groups of compositio~iso f matter. Those skilled in tlie art will appreciate that the present disclosure is susceptible to variatio~isa rid modificatio~iso ther than those specifically described. It is to bc understood that tlic disclosurc i~icludcs all sucl~ variations and modifications. The disclosure also includcs all of the stcps, features, co~npositions and compounds referred to or indicated in this specification, individually or collectively, and any and all combinatiot~s or any two or more of said steps or fcaturcs. Tlic present disclosure is not to bc limited in scope by the specific cxamplcs describcd hcrcin, which arc intcndcd for the purpose of exemplification only. Functionally-equivalent products, co~npositions and methods are clearly withiti the scope of the present disclosure. Any example of the present disclosure hereill shall bc taken to apply niufatis niurnndis to any other example of the disclosurc ul~lcss specifically stated othe~wise. Unlcss spccifically dcfi~~codth crwise, all technical and scientific terms uscd hcrein shall bc takcn to l~avcth c sarnc mcar~inga s cotnmonly u~~derstoobdy onc of ordinary skill in thc art (for example, in cell culture, ~nolecular genetics, immunology, immunohistochcmistry, protein chemistry, and biochemistry). Ullless othcrwise indicated, the recombi~rant protein, cell culture, and in~tnu~~ologictaclc hniqucs ntilizcd in thc preserlt disclosure are standard procedures, well kiiowl~t o those skilled in the art. Such techniqucs are described and cxplait~cdt hroughout tl~cli tcraturc in sources such as, J. Pcrbal, A Practical Guide to Molecular Cloning, John Wiley a11d Sons (1984), J. Sambrook el al. Molcc~rlarC loning: A '.aborato~y Manoal, (Cold Spring Harbour Laboratory Press (1989), T.A. Brown (editor), Essential Molecular Biology: A Practical Approach, Volu~ncs I and 2, IRL I'rcss (1991), D.M. Glovcr and B.D. Halncs (cditors), DNA Cloning: A I'ractical Approach, Volumcs 1-4, IRL Press (1995 and 1996), and F.M. Ausubel et nl. (cdito~s), Cumcnt Protocols in Molecular Biology, Gree~lc I'ub. Associates and Wilcy-lntcrscicncc (1988, including all updatcs until prcscnt), Ed Harlow and David Lane (cditors) Antibodies: A Laboratory Manual, Cold Spring Harbour Laboratory, (l988), and J.E. Coligan et ~ 1(.cd itors) Currc~it Protocols in Immunology, Joht~ Wilcy & Sons (including all updates ut~til prcscnt). Tl~c description and dcfi~litions of variablc rcgions and Darts thcrcof, immunoglobuli~~asn, tibodies and fragments thcrcof hcrcin may bc further clarilicd by thc discussioll in Kabat S(!(~ucnc;c!osf ' Proteins oj' I~iiriiunologicnl Intcriscs a Fc. In a light chain, a constant rcgion gclicmlly comprise one constant dornain (a CI,~). The tenn "fragment c~ystalizable" or "Fc" or "PC region" or "Fc portion" (which call bc used intcrchdngcably Ilerein) rcfers to a rcgion of an antibody co~ilprising at least one constant domain and wllicl~ is generally (Lhoogh not ncccssarily) glycosylatcd and which is capable of binding to onc or more FC receptors and/or co~lipolle~itosf tllc co~~iple~ilcea~slcta de. The 11eavy chain constant region call bc sclected from any of thc five isotypes: a, 6, s, y, or p. Furtlielmore, heavy chains of various subclasscs (such as the 1gG subclasses of heavy chains) are responsible for different effector functions and thus, by choosing the desired heavy clraili consta~~retg ion, proteins with desired effector fu~lctio~l call bc produced. Excmplaly lica\ry chain constant rcgions arc ganilna 1 (IgGI), gamma 2 (IgG2) and gdnn~~3 a(l gG3), or hybrids thcrcof. A "constant domain" is a domain in an antibody the scqucncc of which is highly si~nilarin antibodies/antibodies of the same type, e.g., 1gG or 1gM or 1gE. A constant rcgioti of an antibody gc~icrally comprises a plurality of constant dotnains, c.g., the constant region of y, a or 6 hcavy chaitl comprises two constant domains. As uscd herein, the term "specifically binds" shall be taken to rncan an immunoglobulin or antibody by which is meant that the binding interaction betweell an i~n~nnt~oglobourl ia~nt~ib ody and IL-3Ra chdi11 is dcpcndcnt on the presence of the antigenic determinant or epitope of an IL-3Ra chain bour~d by the immunoglobulin or antibody. Accordingly, thc immunoglobuli~~o r antibody prcfcrelitially binds or recognizes an IL-3Ra chain antigenic determinant or cpitopc even when prcscnt in a mixture of otllcr molecules or organisms. In one cxa~nplc, tlic immnunoglobulin or antibody reacts or associates Inore frequently, rnorc rapidly, with grcatcr du~;itiosa nd/or with greater affinity with IL-3Ra or cell expressing same than it does with alternative antigens or cells. It is also undcrstood by reading this definition that, for example, at1 immu~loglobnlio~r~ antibody specifically binds to IL-3Ra may or may not specifically bind to asecond antigen. As such, "specific binding" does not necessarily require exclusive binding or non-detectable binding of another antigen. The term "specifically binds" is used intclrhdngcably with "selectively binds" hercin. Generally, refcrcncc hcrcin to binding mcans spccilic binding, afid C I K ~ tcnn shall bc undcrstood to providc explicit support for the othcr tenn. ". 111 one example, "specific binding" to with 11.-3Ra or ccll cxprcssing samc, mcans that tlic immunoglobulin or antibody binds to thc with IL-3Rtx or ccll cxprcssing samc with an equilibrium constant (I<,)) of lOOnM or less, such as 50nM or Icss, for cxamplc 20nM or less, such as, InM or Icss, e.g., 0.8nM or less. 'Thc tcrm "EU numbcring system of Kabat" will be understood to meim the numbcring of an antibody heavy chain is according to the EU index as taugl~t in Kabat el ( I / . , 1991, Scqucnccs of l'rotcins of l~n~nnnologicaInl tcrcst, 5th Ed., United States Public Hcalth Scrvicc, National I~lstitutcso f Hcalth, Bcthcsda. Thc Ell indcx is bascd on thc rcsiduc numbcring of the human IgG1 EU antibody. As nsed hercin, tlic term "IL-3Ra-mctliatcd condition" will be understood to Incall a condition associatcd with or causcd by cxccssive IL-3Rn cxprcssion andlor an cxccssivc ninnbcr of' IL-3Ra cxprcssing cclls in a tnammal, sncll as cancer cells (c.g., Icukcmic cells) andlor immune cells (e.g., plasniacytoid dcrrdritic cells). As uscd hcrcin, the term "myelodysplastic syndrome" or "MDS" will bc understood to refer to a diverse colleclion of hcmatologicdl ~nedical conditior~s that involve ineffective productio~i (or dysplasia) of the myeloid class of blood cclls. Subjects with MDS often dcvelop sevcrc aacmia and can rcquire frequent blood transfusions. In many cascs, as MDS progrcsscs thc subjcct dcvclops cytopcnias (low blood counts) due to progrcssivc bone ~i~asrofwai lure. In about one third of patients with MDS, thc diseasc transforms illto acutc myelogc~cnous lcukemia (AML). 'The MDS can bc diagnosed or classified to various systems, including thc Frcnch-Amcl.ican-British Classification Systcnl (Bcnnctt el (11.. B,: J. Hnen.n,cllol. 33: 451-458, 1976), Tlic Intcr~~ationaPlr og~iosticS coring Systeiii (Grecnberg et nl., Blood 89: 2079-88, 1997) or a system published by tlie World Health Orga~?ization. As used liercin, thc tcrrn "treatme~it" refers to cli~~icailn tervention designed to alter tlic liatural course of thc individual or cell being treated during the course of cli~iicalp athology. Desilablc effects of treatmcnt ilicludc dccrcasing the rate of discasc progression, ameliorating or palliating thc discasc statc, and remissio~l or imptaved prognosis. An individual is successfully "lreated", for cxamplc, if one or more symptoms associated with a discasc are mitigated or eliminated. As used hcrcin, the term "prevention" includcs providing propliylaxis with respect to occurrence or rccurrcncc of a discase in an individual. An i~~divitlual may be predisposed to or at risk of developing thc disease or disease relapse but has not yet been diagnosed with tl~cd isease or the sclapse. As used lierein, a mammal "at risk" ofdcveloping a disease or condition or relapsc thcwof or rclapsi~igm ay or may not have detcctable diseasc or symptoms of discaqe, and may or may not l~aved isplaycd detectable disease or syrnptoliis of discasc prior to thc trcattilcnt according to thc prcscnt disclosurc. "At risk" dc~iotcs that a niammr~l has onc or marc risk factors, which are rncasurablc paramcters that correlate with dcvclopmcnt of tlic disease or condition, as known in thc art andlor described lierein. AII "cffcctive amount" rcfcrs to at Icast an amount cffcctivc, at dosagcs and for periods of tinle ncccssary, to achicve ll~c dcsirc(l therapeutic or prophylactic result. An cffcctivc alnoulit call bc provided in one or niorc adniinistrations. In some examples of tlie prcscnt disclosurc, the term "effcctive amount" is meant an a~iiount ncccssary lo cffcct trcattnclit of a diseasc or condition as licrcinbcforc dcscribcd. Thc cffcctivc aliioulit niay vary according to tlic tliscasc or condition to be treated and also according to thc weight, age, racial background, scx, health andlor 1)hysical condition and othcr factors rclcvdnt to t11c ~namrnabl cir~gtw ated. Typically, tl~cc ikctivc amount will fall within a relatively broad range (e.g, a "dosagc" railye) tllat can bc dctcrmincd tl~rol~grho utine lrial and experitneatation by a medical practitioner. The cffcctivc arnoulit can bc adniinistcrcd ia a single dose or in a dose rcpeatcd once or scveml tinies over a treatment period. A "thetapentically effective amount" is at least the ~niiiimu~cioin centration required to effect a measurable improvement of a particular disorder (e.g., SLE). A therapeutically cffcctive amount herein may vaty accordiag to factors such as tlic discasc state, agc, scx, and wciglit of tlic patient, and tlic ability of thc immutiogiobulin or antibody to elicit a desired rcsponsc in thc individual. A therapeutically effective amount is also one in which any toxic or detrimental effects of the itnmu~~oglobuloi~r ia lltibody are outweighed by the tl~erapeutically bcacficial cffccts. A "pluphylactically effective amount" refers to an amount effective, at tlie dosages and for periods of timc necessaly, to achicvc the desired prophylactic result. Typically but not necessarily, since a prophylactic dose is used in mammals prior to or at an earlier stage of diseasc, a prophylactically effective amount may bc less than a tlierapeutically eKcctive amount. Reference herein to "the number of NK cells in the mammal" will bc ul~de~stootod ir~cludeth c number of NK cells in a sample %om a malnlnal and not to require determining thc total number oS NK cells in a mammal. This ~iumbcr can be expressed as, for cxamplc, cells per mL or dL or as a percentage of tlie ~lu~nboefr c ells froni a sample taken at a different point in time from the mammal. For the pulposes of nome~iclatureo nly and not limitatioo, tlie a~niiioa cid sequcncc of an IL-3Ra chain is taught in Gent ID Accession Number 3553 andlor in SEQ ID NO: 1. The "mammal" treated according to tlie present disclosurc may be a mammal, such as a non-Iiuman pri~i~atoer a human. In one example, tlie mammal is a liuma~i. 'The term "sequence identity" is uscd licrein in its broadest scnsc to include tlic number of cxact nuclcotidc or an~ino acid matclics having regard to an al)propriate aligome~itu sing a sta~idarda lgorithm, liaving irgard to tlic extent tliat sequences arc identical ovcr a window of comparison. Scqucncc identity may be detenni~ied by alignment of cornpared sequenccs using computerised implcmcntations of algorithms (,Gcncworks program by lntclligcnctics; GAP, BESTFIT, FASTA, and TFASI'A in tlic Wisconsin Gcnctics Software Package Release 7.0, Gcnctics Cornputcr Group, 575 Scicncc Drivc Madison, WI, USA, incolporatcd herein by rcfclcnce) or by itispection and thc bcst aligllmi~it (i.e., resulting in the higlicst pcrccntagc liomolo~y ovcr thc comparison window) gcncratcd by any of tlic various mctliods sclcctcd. Rcfcrcncc illso m;ay bc ll~adcto the BLAST fanlily of programs as for cxamplc disclosed by Altschol el nl., 1907, Nucl. Acids Rcs. 25 3389. A dctailcd discussion of sequencc analysis can be Sound in Unit 19.3 oC CIJIcptidc component thereof. DNA includes genomic DNA and cDNA. RNA i~~cludes 5 mlWA and cllNA. Nuclcic acids 11~aayl so bc DNA-RNA hybrids. A nuclcic acid comprises a tlucleotide scquencc which typically i~lcludcs nucleotidcs that comprise an A, G, C, T or U basc. However, nucleotide scqoctlces lnay include other bases such as inosine, methylycytosine, methylinosinc, methyladet~osine andior thiouridinc, although without limitatioll thcrcto. 10 "Hybridize and Hybridization" is used l~crcint o de~loteth c pairing of a1 least partly compleme~lta~y~ iucleotidc seqnenccs to produce a DNA-DNA, RNA-RNA or DNA-RNA hybrid. Hybrid scquc~tccsc omprising co~nplcmcntary ~lucleotides equences occur through basc-pairing between complemcntaly purines and 11yrimidincs as are well known in thc art. 15 In this regard, it will be apprcciated that modified purincs (for example, inosine, methylinosine and mcthyladcnosi~ie) and modified pyrimidines (tliiouridine and methylcytosine) may also engage in base pairing. "St~.itlge~lcy"a s uscd herein, rcfcrs to temperdturc and ionic strength conditions, and presence or abse~lceo f celtai~o~rg anic solvc~itsa ~ldiord etergents 20 during hybridisation. The higher thc stringency, the higl~er will bc the required level of complcmc~~tat~hietytw cco hybridizitlg ~luclcotidesc qucnces. "I-ligh stringency condilions" dcsignalcs thosc co~lditio~ulstl der whiclt olliy nuclcic acid Ilaving a higll frcqucncy of con~plcmcntaryb ascs will hybridize. Rcfcrcncc herein to high stringency conditions include and 25 cncornpass:- (i) from at least about 31'% vlv to at least about SO'% v/v formamidc and frotn at lcast about 0.01 M to at lcast itbout 0.15 M salt for llybridisatio~l at 42"C, a~ltl at lcasl about 0.01 M to at least about 0.15 M salt for washing at 42'C; (ii) 1%) BSA, 1 mM EDTA, 0.5 M. NaHl'Oo (pl-l 7.2), 7% SDS for hybridization at 6S°C, and (A) 0.1 x SSC, 0.1% SDS; or (b) 0.5% BSA, lmM EDTA, 40 mM NaHP04 (pH 7.2), 1% SDS for waslling et w tctnpcratule in excess of 6S°C for about onc hour; and 35 (iii) 0.2 x SSC, 0.1'%, SDS Ibr washing at or abovc OXUC fir about 20 minutcs. h~ gcncral, washing is carried out at T,, = 69.3 t 0.41 (C i-C ) % -12°C. h~ gcncral, the T,,, of a duplex DNA decreases by about 1°C with cvcry increase of 1% in the tlu~nbero f mismatched bases. 40 Notwithstanding the above, stritige~ltc onditions are known in the art, sl~cll as describcd in Chapters 2.9 and 2.10 of. Ausubel et a/., CURRENT PROTOCOLS lN MOLECULAR BIOLOGY John Wiley & Sons, Inc. 1995-2009 An "cx~~rcssiovnc ctor" may bc citlicr a sclf-replicating cxtra-cli~omoso~iial vector such as a plabmid, or a vcctor that integrates illto a host gcnome. l~nrnunoelobulins 5 Suitably, an imniunoglobuliti or antibody of thc disclosurc sclcctivcly binds IL-3Ra chain, by which is meant that the binding inte~action betweell the immunoglobulin or antibody atid IL-3Ra chain is dcpe~ident on the prescnce of the antigcnic determinant or epitope of an IL-3Ra chain bound by the immunoglobulin. Accordingly, tlic immunoglobulin 01. antibody prcfercntially 10 binds or rccognizes an IL-3Ra cliain antigcnic deteniiinant or cpitope cvc11 when present in a mixture of othcr molcculcs or organisms. A~ilibodies In one example, an immu~ioglobuli~asi described 11crcin according to any 15 example is an antibody, c.g., comprising CDRs andlor one or more variable regions described hcrein. Suitably, the immunoglobulin is a humanized, chimeric or human antibody that comprises light and lieavy chain CDR 1, 2 and 3 amino acid scqucnces according to SEQ ID NOS: 2-7 respcctivcly. In one example, thc antibody 20 co~iiprisca lleavy chain variable region amino acid sequence according to SEQ ID NO: 9 and a liglit chain variablc region amino acid sequence according to SEQ ID NO: 8. In onc example, the antibody compriscs a lieavy chaiti amino acid scqucncc according lo SEQ ID NO: 10, SEQ ID NO: 1 1 or SEQ ID NO: 12 and a liglit chain a~iii~aicoi d sequclicc according to SEQ 1D NO: 13. 25 In onc cxamplc, the antibody is a rccombinat~t antibody. Methods for produci~iga ntibodies comprising CDRs andlor va~iablcr cgions dcscribed lierein will bc apparent to thc skillcd artisan kbascd on tlic disclosurc herein andlor documents referred to Iicrcin. In onc examplc, an antibody of tlie disclosurc compriscs a VII andlor a \'I. 30 comprising CDRs as sct Forth liercin and FRs from a human sntibody. Optionally, thc FRs comprise one or marc atnillo acid substitutio~is, c.g., 2 or morc or 3 or niorc or 4 or morc of 5 or morc or 10 or morc or 15 or morc. 111 onc example, tlie FRs comprise no morc illan 30 a~iiino acid substitutions, e.g., no more than 20 amino acid substitutio~~cos ~nparedto tlic Iiuma~iF Rs. 35 111 one examplc, an antibody of tlic disclosure co~iipriscsa VII a~idlora \'I, co~iiprisingC Dlls as sct forth I~aoinan ti FRs Tram a lion-lluman primate aotibociy, i.c., thc antibody is Synhumanized, e.g., as described in WO2007i019620. I11 one example, an antibody of the disclosure is a con~positea ntibody, e.g., as described in WO200(,1082406. 40 One exemplary antibody of tlie disclosure is a Iiuma~~izcadn tibody, e.g., as defined herein. Exempla~y humaliized antibodies are dcscribed herein. In one example, tlie liumd~iizeda ntibody has been affinity matured. In o~icx atnple, thc Iiumanizcd antibody cotnpsiscs: (i) a VL comprisi~ig: a) a CDR I cotnprisi~lga scquencc set fottli in SEQ ID NO: 2 (or cncoclcd by a sequence set forth in SEQ ID NO: 14); 5 b) a CDR2 co~nprisinga scqucncc sct fo~tliin SEQ ID NO: 3(or c~lcodcd by a sequelice sct fortli it1 SEQ ID NO: 15); a~id c) a CDR3 co~nptisi~alg s equence set forth in SEQ ID NO: 4 (or encodcd by a sequence set fo~ihin SEQ ID NO: 16); and (ii) a VII comprising: 10 d) a CDRl comprisi~iga sequcncc sct forth in SEQ ID NO: 5 (or c~icodcd by a scquc~iccs ct fortli in SEQ ID NO: 17); c) a CDR2 cornptising a sequc~iccsc t forth it1 SEQ ID NO: 6 (or cncoded by a sequence set forth in SEQ ID NO: 18); and f) a CDR3 comprisi~ig a scquence set fortli in SEQ ID NO: 7 (or 15 encoded by a sequence set fortli in SEQ ID NO: 19). Tliose skilled in tlie att will appreciate that irnmutloglobuli~~osr antibodies of thc disclosure may include modificatio~lsth at introduce scqucnces not nalumlly found in humans, for cxamplc to incwase affinity or cffcctor function. Thc disclosure also provides variants of the immunoglobuliri or alltibody of 20 thc disclosure. Suitably, variants have at least 80%, X5%, 90%, 91%, 92%, 03%, 94%, 95%, 96%, 97%, 98% or 99% sequence idcntity with any of the amino acid sequences sci ford1 in SEQ ID NOS:2-13. For cxamplc, it is understood in tlic ali that so~iic atiiino acids nlay bc substituted or deletctl without advcrscly or significnnlly affecting tlie IL-3Ra 25 specificity andlor effcctor function of the immunoglobulin or antibody (c.g. co~iservatives ubstitutions). Dcsivativcs of antibodies or i~n~nu~ioglobulincos ntcmplatcd by tbc disclosi~lri nclude, but are not limitcd to, modification to a~iii~alcoi d side chains, incorpovation of unnntural amino acids andlor their desivativcs dusing peptide or 30 polypeptide sy~ithcsisa nd thc use ofcrosslinltcn. Exctnpla~-yaa litibodics and antigen bindit~gf ragments tlicrcof of tlic prcsait disclosorc aar dcscribcd in Table 1. Table 1: Excniplary aatibodics and a~itigcnb inding fragments thcrcof Namc / Hcavy Chain SEQ ID I Light Chain SEQ ID NOT 2 Hcavy chain constant icgion is afucosylatcd CSL362B CSL362X1 CSL362X2 5 A~~tibodFvra emcnts Single-Domctin Anlibodies In some examplcs, an antigc~b~in ding fragment of an alltibody of the disclosure is or co~nprises a single--domain antibody (which is used i~~tcrchangcablwyi th thc tcr~n" domain antibody" or "dAb"). A singlcilomain 10 antibody is a singlc polypeptide chain comprising all or a po1lio11 of the heavy chain variable domain of an antibody. Dicil)odies, Trirrbodie,~, Te/r.cthodies In some cxamplcs, an antigc!~ binding kagrnmt of thc disclosurc is or I5 comprises a diabody, triabody, tctrabody or higher order protci~c~o1 11l>1cxs ue11 as tliosc described in W0981044001 andlor WO941007921. For examplc, a diabody is a protein coml~risingtw o associated polypeptide chains, cach polypcptidc chain comprising tlic structure VL-X-VII or VII-X-V~~ wherein X is a linkcr comprising insuMicie~irt esidues to pcrmit the Vu trnd V1, in a 20 single polypcptidc chain to associate (or form an Fv) or is absent, and wherein the VIIo f one polypcptidc chain binds to a VI. of the orl~erp olypc])tidc chain to form an antigen binding sitc, i.c., to form a Fv ~nolcculcc apable of specifically billding to one or more antigens. The V ~ a n Vd IIc an be the salnc in cacl~p olypeptide chain or the VI. and Vli can bc diffclc~~int each polypcptide chain so as to form a 25 bispccific diabody (i.c., comprising two Fvs having different specificity). A diabody, triabody, tctrabody, ctc capable of inducing effector activity can bc prodt~ccdu sing an aotigc~b~in ding d o ~ n ~caipta~b le of bit~tfintgo IL-3Rn and an antigen binding domain capable of binding to a ccll surfacc molecule on an irnmune ccll, c.g., a T cell (e.g., CD3). 30 Single Chain FV (scFv) Fr.ngnlen/s The skillcd artisan will be aware that scFvs comprise V Ia~nd VIAre giotis in a single polypeptide chain and a polypcptide linker between the VH and VL which enables the scFv to form thc desired structure for antigen binding (LC., for the VH 35 and V1.of the single polypeptide chait~to associate with one allother to for~na Fv). ' Variablc region sequencc only. 1 o2 I I 12 13 -. 13 13 For cxamplc, thc linkcr compriscs in cxccss of 12 amino acid rcsiducs with ( G l ~ ~ S cbrc)in~g onc of the marc favorcd linlcers for a scFv. The present disclosure also contcmplatcs a disulfidc stabilized Fv (or diFv or dsFv), in which a single cysteine rcsidue is introduced into a FK of VII and a FK 5 of VI, and tl~cy stcinc rcsiducs linkcd by a disulfidc bond to yicld a stablc Fv. Alternatively, or in addition, the present disclosure elicotnpasses a ditneric scFv, i.e., a protcin comprising two scFv tnolecl~les linkcd by a non-covalcnt or covalent linkagc, e.8.. by a lcucinc zipper domain (e.g., derivcd from Fos or Jun). Altcmativcly, two scFvs ale linked by a peptidc linker of sufficiez~t imgth to 10 permit both scFvs to form and to bind to an antigcn, e.g., as described in US20060263367. Thc present disclosnre also contemplates a dimeric scFv capablc of inducing cffector activity. For cxample, one scFv binds to IL-3Rn and compriscs CDRs at~dlorv ariablc regions dcscribcd hcrcitl and another scFv binds to a ccll 15 sllrface molec~~olen an immunc cell, e.g., a T cell (e.g., CD3 or CD19). In one example, the dimcric protein is a combination of a dAb and a scFv. Examplcs of bispecific antibody fiagmcnts capable of il~duci~cigff ector function are described, for examplc, in US7235641. 20 Other Antibodies flolid Antibodj Fr(~gr?~eol~rs Thc prcsent disclosurc also contcmplatcs othcr antibodies and alltibody fragments, such as: (i) "kcy and holc" bispccificprotcins as described in US5,73 1,168; (ii) 11cteroco1;jugate proteins, c.g., as dcscribcd in US4,676,')80; 25 (iii) hetemco~~jogatper oteins produced using a che~nicalc ross-linkcr, c.g., as described in US4,676,980; and (iv) Fab, (c.g., as dcscribcd in E1'19930302894). Constant R 'L ~~10'1 1s 30 'The prescnt disclosure encompasses immunoglobulins and antibodies and antigen binding fragments comprising a constant region of an antibody andlor a Fc rcg~ono f an antibody. Sequences of constant rcgions andlor Fc regions useful for producing thc i~n~nonoglobul~liasn, tibodies or antigcn binding fragments of thc prcscnt 35 disclosure may bc obtairlcd from a nutnher of diffe~enst ourccs. In some examples, tl~cc onsta~~retg ion, Fc or portion thereof of the i~~imu~~oglobau~lil~ibi,o dyo r antigen binding fragment is derived from a hornan aitibody. The collstant rcgion, Fc or portion thereof may be derived from any antibody class, including IgA, IgM, IgG, IgD, Ig.4 and IgE, and ally antibody isotypc, including IgG1, IgG2, IgG3 and 40 lgG4. In one example, the consta~itr egion or Fc is human isotype IgG1 or 11i11nan isotype IgG2 or liu~na~is?o type IgG3 or a hybrid of any ofthe foregoing. In onc cxamplc, thc constant rcgion or Fc rcgioti is capablc of i~iduci~aign cffcctor fi~tictio~iF. or example, the constalit region or Fc region is a human lgGl or lgG3 Fc region. In aootlier example, the constant rcgion or Fc region is a hybrid of an lgG1 aud an lgG2 constant region or Fc region or a hybrid of at1 IgGI atid an IgG3 consta~~retg ion or Fc rcgion or a Iiybrid of an lgG2 and an lgG3 co~~statrict gion or Fc region. Exempla~yh ybrids of liu~iia~Igi Gl and IgG2 co~~stare~giito n or Fc regions are described in Chappel el nl., Proc. Natl Acc~rlS. ci. USA, 88: 9036-9040, 1991. Methods for determining whether or not a Fc region can inducc cffcctor function will be apparctlt to thc skillcd artisan and/or described 11crci11. Effector Function Suitably, an anti-1L-3Rn immu~ioglobulin, antibody or a11tige11 binding fragment of tlie disclosurc has or displays an effector fu~iction that facilitates or enables at least partial depletion, substantial depletion or elimination of IL-3Ra'. cells. Such an cffcctor function may be enhanced binding affinity to Fc receptors, antibody-dependent cell-mediated cytotoxicity (ADCC), antibody-dcpcndent cell mcdiated phagocytosis (ADCP) a~idlor complemc~it dependent cytotoxicity (CDC). As will bc apparent to the skilled artisan based 011 the description herein, somc examplcs of the prescnt disclosurc include an itnmunoglobulin, antibody or antigen billding fkagmctit capable of inducing cffcctor function. For tlic IgG class of aatibodics, thcsc cffcctoi' fu~ictio~aisr c govcrncd by ellgagement of the Fc rcgion with a family of rcceptors rcfcrrcd to as the Fcy receptors ((FcyRs) which are expressed on a variety of irnrnuue cells and/or wit11 con~plement, c.g., Clq, for ma ti or^ of the FclFcyR complex recruits these cclls to sitcs of boi~tid antigen, typically resulting in signaling a~id subscquc~it immuuc responses. Mctliods for optimizing the binding alfinity of the FcyRs to the antibody Fc rcgio~iin ordcr to eohancc the cffcctor functions, in particular to alter the ADCC andlor CDC activity rclative to tlie "[)arc~~tF"c region, arc known to persons skillcd in thc art. Thcsc mcthods can includc ~nodificatioo~f~ t l~cF c rcgion of thc alltibody to cl~lla~~itsc cin tcractiot~w ith relcva~~Ftc rcccptors and increase its potential to facilitate ADCC and ADCP. ]i,nl~a~~cemien ~A~DtsC C activity havc also been dcscribed followi~ig thc modification of the oligosaccharide covalently attached to lgGl a~itibodicsa t the conserved As11297 in thc Fc regio~i. I11 this regard, it will be appreciated that in some lion-limiting examples, enhancing effector function such as ADCC may be achieved by moditicatio~io f an immunoglobulir~ or antibody which has a normally glycosylated wild-typc constant domain, i~icludi~al~tegr atio~o~r removal of glycosylatiol~( see for example W000161739) andlor ami~io acid sequence mutations (sce for examplc W02008036688). 111 onc cxamplc, thc irnmunoglobulin, antibody or antigci~b indiiig fraglncnt binds to IL-3Ra in such a manner that it is calsable of inducing an effector function, such as, ADCC. I11 one exatnple, the i~ntniuioglobulin,a ntibody or alrtiget~b inding ftaglnent binds to an cpitopc w i t l ~ IiL~-~3R a that permits it to inducc all cffcclor functior~, such as ADCC. In another example, the irnmunoglobulin, antibody or antigen binding fragment is capable of binding to IZ.-3Ra on a cell in a mammal to thcrcby inducc an effector futlction, such as ADCC. For example, thc inimunoglobulin, atitibody or antigc~l binding frag~ne~~t remains bound to IL-3Ra on the surface of a cell for a time suff~ciieto indnce an cffector fuoction, such as ADCC. For example, tllc irnn~unoglobulin or antibody is not ititcr~ializcdt oo quickly to permit ADCC to be induced. Alten~atively, or in addition, tl~c immunoglob~ilin, antibody or antigen binding hgrncl~tis bonntl to tlie IL-3Ra on the surface of the cell in a manner pe~mittinga n immune effector cell to bind to a constant region or Fc legion in the immunoglobulin, antibody or antigen binding fragment and induce an effcctor function, such as ADCC. For example, thc Fc region of thc immunoglobulin, antibody or antigen binding fragment is exposed in such a lnanucr wlicn the im~nunoglobulin, antibody or antigen binding fragment is bound to tlic JL-3Rn that is capablc of interacting with a Fc receptor (e.g., a FcyR) on an immune effcctor ccll. In tlte context of the present disclosure, thc tcrm "irnmane ei'fcclor ccll" shall bc understood to Incall ally ccll that cxpresscs a Fc rcccptor and that is calsablc of killing a ccll to which it is bound by ADCC or ADCP. In onc cxample, tlie immune effector cell is aNK ccll. Each of tlie above paragraphs rclating lo effector functions of an immunoglobulin, antibody or antigcn binding fragmcfit shall bc taken to apply mutntis nlutcmdis to inducing CDC. For cxamplc, the itnmu~~oglobulina,~ tibody or antigcn binding fragmcnt is bound to tl~cIL -3Rn on tl~csu rface of thc cell in a rnarnier pcrrnitting complement component Clq to bind to zt constant rcgion or Fc rcgion in tlie itnmunoglobulin, antibody or antigcn binding fragment and ir~ducc CDC. 111 one cxatnplc, the im~~ii~~~ogloabllutilbio~diy, or antigeo binding fragmcnt is capable of inducing an cnllanced levcl of cffcctor functios. In one example, the lcvcl or cffector f~~nctioinn duced by thc consVant rcgion or Fc region is e~~lia~icreeldat ivc to a wild-type constant region or PC rcgion of an IgGl antibody or a wild-type constant region or Fc region of an lgG3 antibody. In another example, the constant region or Fc region is modified to increase the level of effector functio~i it is capablc of inducing compared to the constant region or Fc rcgion without tlic modification. Such ~nodifications call be at the amino acid lcvcl and/or thc secondary structural lcvcl andlor thc tcrtialy structi~ral level andlor to the glycosylation of the co~~stalreitg ion or Fc rcgion. The skilled addressee will appreciate that grcatcr cffector function may be manifested in any of a number of ways, for example as a greater level of effect, a morc sustait~cdc ffcct or a fastcr ratc of cffcct. For example, the anti-IL3Ru imtnunoglobulin, antibody or antigen binding fiagnent has or displays an effector function that includes antibody-dependent cell-mediated cytotoxicity (ADCC). In one examl~le,t hc constant rcgioti or Fc region comprises onc or marc amino acid modificatioss that iticrcasc its ability to induce c~~l~ancceffdc ctor function. In one cxarnple, the constant region or Fc region binds with greatcr affinity to onc or morc FcyRs. In one example, the constant region or Fc region has an affinity for an FcyR that is more than I-fold greater than that of a wild-type constant region or Fc region or more thari 5-fold greater tlran tlirrt of a wild-type constant region or Fc region or between 5-fold and 300-fold greater tban that of a wild-type constant region or Fc region. In one example, the co~istar~e~gito n or Fc rcgio~l compriscs at least onc amino acid substitution at a position sclectcd from tlic group colisisting of 230, 233, 234, 235, 239, 240, 243, 264, 266, 272, 274, 275, 276, 278, 302, 318, 324, 325, 326, 328, 330, 332, and 335, numbercd according to tlic EU indcx of Kabat. In onc cxatnplc, the constant region or Fc region comprise at lcast ot~c amino acid substitution sclectcd fium thc group consisting of: P230A, E233D, L234E, L234Y, L2341, L235D, L235S, L235Y, L2351, S239D, S239E, S239N, S239Q, S239T, V2401, V240M, F243L, V2641, V264T, V264Y, V2661, E272Y, K274T, K274E, K274R, K274L, K274Y, F275W, N276L, Y278T, V3021, E318R, S324D, S3241, S324V, N325T, K3261, K326T, L32XM, 1.3281, L328Q, L328D, IL128V, L328T, A330Y, A330L, A3301, I332D, 1332E, I332N, 13320, T335D, T3351<, and T335Y, numbcrcd according to thc EU indcx of Kdbat. In o~ic example, the constant region or Fc region compriscs amino acid sobstitutions sclccted frotn tile group consisting of V2641, F243LiV2641, L328M, 1332E, L328M/I332E, V264V1332E, S298A/1332E, S239E/1332E, S239Q/1332E, S239E, A330Y, 13321), L3281/1332E, L328Q/1332E, V264T, V2401, V2661, S239D, S239D/I332D, S239DA332E, S239D/1332N, S239D/1332Q, S239E/1332D, S239E/1332N, S239E/J332Q, S239N/1332D, S239NiI332E, S239Q/1332D, A330Y11332I5, V261l/A330Y/1332E2 A330L/1332E, V264VA330L/1332E, L234E, L234Y, L2341, L235D, L235S, L235Y, L2351, S239'1', V240M, V264Y, A3301, N325T, I2328D/1332E, L328V/1332E, L328T/1332E, L328111332E, S239E/V2641/1332E, S239Q/V2641/1332E, S239EN264VA330Y/1332E, S239D/A330YII332E, S239N/A330Y/I332E, S239D/A330Li1332E, S239N/A330L/1332E, V2641/S298A/1332E, S239D/S298A/1332E, S239N/S298A/1332E, S239D/V2641/1332E, S239D/V2641/S298A/1332E, S239D/V2641/A330L/I332E, S239D/1332E/A3301, P230.4, P230A/E233D/I332E, E272Y, K274T, K274E, K274R, K274L, K274Y, F275W, N276L, Y278T, V3021, E318R, S324D, S3241, S324V, K3261, K326T, T335D, T335R, T335Y, V2401iV2661, S239DiA330Y/1332E/L2341, S239DIA330Y/I332E!L235D, S239D/A330Y/1332EN2401, S239DiA330Yi1332EIV264T. S239DIA330Y/1332E/K326E, and S239DiA330Y/1332E/K326T, numbcrcd according to thc EU indcx of Kabat. In another example, the constant region or Fc region binds to FcyRIlIa morc efficiently than to FcyRllb. For example, the collstant region or Fc rcgio~i comprises at least onc amino acid substitutio~i at a position selected from thc group consisting of: 234, 235, 239, 240, 264, 296, 330, and 1332, numbered accordi~lg to the EU index of Kabat. In onc examplc, thc coilstant region or Fc region comprises at least one amino acid si~bstitutio~sel lected fiom the group consisting of: L234Y, L2341, L2351, S239D, S239E, S239N, S239Q, V240A, V240M, V2641, V264Y, Y296Q, A330L, A330Y, A3301, 1332D, and 1332E, numbcrcd according Lo the EU indcx of Kabat. For example, the constant scgion or Fc region co~nprises amino acid substitr~tions selected from the group consisting of: 1332E, V2641/1332E, S239E!l332E, S239Q!1332E, Y296Q, A330L, A330Y, I332D, S239D, S239D/1332E, A330Y/1332E, V2641/A330Y/I332E, A330Li1332E, \~264YA330L!1332E, L234Y, L2341, L2351, V240A, V240M, V264Y, A3301, S239D/A3301.J1332E, S239D/S298A/1332E, S239NIS298Ai1332E. S2391liV2641!1332E, S239D/V2(i4YS298Ail332E, and S239DIV264I/A3301/1332E, numbcrcd according to thc T:U indcx of Kabat. In a Further cxamplc, Ll~e constant region or Fc regio~l induces ADCC at a lcvcl grcatcr than that mcdiatcd by a wild-typc co~lsla~rletg ion or Fc rcgion. For cxamplc, tl~ec onsta~ltr egion or Fc rcgio~li nduccs ADCC at a level that is morc than 5-fold or between 5-fold and 1000-fold gwater than that intluccd by a wild-type constant region or Fc rcgiot~. In one example, the coustdnt region or I'c rcgion compriscs at lcast onc amino acid substitutio~l at a position sclcctcd from thc group co~lsisti~logf: 230, 233, 234, 235, 239, 240, 243, 264, 266, 272, 274, 275, 276, 278, 302, 318, 324, 325, 326, 328, 330, 332, and 335, ~iumbcrcd according to the Ell index of Kabat. In onc example, the constatlt region or Fc rcgion comprises at lcast onc amino acid sub~titi~tiosc~le~cstc d from tllc gmup consisting of: P230A, E233D, L234E, 1.234Y, L2341, L235D, L235S, L235Y, L2351, S239U, S239E, S239N, S239Q, S239T, V2401, V240M, F243L., V2641, V264T, V264Y, V2661, E272Y, 1<274T, 1<274E, 1<274R, K2741., K274Y, F275W, N27hl., Y27HT, V3021, E3181<, S324D, S3241, S324V, N325T, K3261, K326'1', L328M, L3281, L328Q, L328D, L328V, 1.328T, A330Y, A330L, A3301, I332D, I332E, 1332N, I332Q, T335D, T335R, and T335Y, numbered according to the EU index of Kabat. In one example, the consldnt region or Fc region comprises amino acid substitutions selected from the youp consistitig of: V2641, F243LlV2641, L328M, 1332E, l..32HM/1332E, V2641/1332E, S298A/1332E, S239E/l332E, S239Q/I332E, S239E, A330Y, I332D, L3281/1332E, L328QA332E, V264T, V2401, V2661, S239D, S239D/I332D, S239D/1332E, S239D/1332N, S239D/I332Q, S239E/1332D, S239E/1332N, S239E/1332Q, S239NlI332D, S239N/1332E, S239Q/1332D, A330Y/1332E, V2641/A330Y/I332E, A330L/I332E, V264I/A330L/1332E, L234E, L234Y, L2341, L235D, L235S, L235Y, 1-2351, S239T, V240M, V264Y, A3301, N325'l', L3280/1332E, L328V/1332E, L3281'/1332E, L328111332E, S239EN2641/1332E, S239Q/V264IiI332E, S239E/V264I/A330Y/1332E, S239DIA330Y/1332E, S239N/A330Y/I332E, S239D/A330U1332E, S239N/A330L/1332E, V264IIS298A/1332E, S239D/S29XA/1332E, S239N/S29XA/T332E, S239DN264111332E. S239D/V264VS298A/1332E, S239D/V2641/A330L/1332E, S239D/1332E/A3301, P230A, P230AiE233D/1332E, E272Y, K2741', K2745, K274R, K274L, K274Y, F275W, N276L, Y278T, V3021, E31XR, S324D, S3241, S324V, K3261, K326T, T335D, T335R, T335Y, V2401N2661, S239D/A33OY/1332E/L2341, S239D/A330Y/1332E/L235D, S239D/A33OY/1332E/V2401, S239DiA330Y/1332E/V264T, S239D/A330Y/1332E/K326E, and S239D/A330Y/I332E/K326T, ~iumbereda ccording to thc EU i~~doefx K abat. In o11c cxample, the constant region or Fc region compriscs the following amino acid substitutiolis S239D/1332E, numbcrcd according to the EU index of Kabat. This constant region or Fc region has about 14 fold i~lcrcasein affinity for FcyRIPa co~npared to a wild-type constant region or Fc region and about 3.3 i~lcrcascda bility to induce ADCC coniparcd to a wild-typc constant rcgion or Fc region. In one example, the constant region comprises a sequcncc set forth bctwec~i rcsiducs 121-450 (inclusivc) of SEQ 11) NO: I l . In onc cxamplc, thc Fc region conip~.iscsa scqucncc sct fo~tlbl ctwccn rcsiducs 234-450 of SEQ ID NO: 11. In one examplc, tlie constalit region or Fc mgioo compl.iscs the following amino acid substitutio~ls S239D/A330L/1332E, numbered according to the EIJ index of Kabat. 'This constant icgion or Fc rcgion has about 138 fold itlcrcdsc in affinity for FcyRIlla cornparcd to a wild-type constant rcgio~o~r I'c region 811d about 323 incrcascd ability to inducc ADCC compared to a wild-type co~lstal~t region or Fc rcgion. 111 onc example, tlie consta~itr cgio~c~ot nprises a scquencc sct for111 bctwccn rcsidues 121-450 (inclusivc) of SEQ ID NO: 12. In o~ic cxamplc, thc Ec rcgion compriscs a scqucncc sct forth betwcc~rc~s iducs 234-450 of SEQ ID NO: 12. Additiot~al amino acid substitutions that incrcasc ability of a Fc rcgion to induce effector function are known in thc art a~ldlor dcsclibcd, for examplc, in US6737056 or US7317091. In one examplc, thc glycosylation of the constant rcgio~i or Fc region is altered to increase its ability to induce eoha~iced effector function. Ill this regard, native antibodies produced by mammalia~i cells typically comprise a branched, biantennary oligosacchaside that is generally attaclied by ail N-linkage to As11297 of tlie C1.12 domain of the constant region or Fc region. The oligosaccharidc may include various carbohydrates, e.g., mannose, N-acetyl glucosaminc (GlcNAc), galactosc, and sialic acid, as wcll as a fucosc attachcd to a GlcNAc in thc "stcm" of the bia~itc~inaroyl igosaccharide structure. I11 some cxamplcs, constant regions or Fc rcgioos according to tlie present disclosure comprise a carbohydrate structure that lacks fucose attached (directly or indirectly) to at) Fc rcgioti, i.e., the Fc rcgion is "afucosylatcd". Such varia~itsti ray havc an improvcd ability to itiducc ADCC. Methods for producing afucosyhtcd a~itibodics includc, cxprcssing thc i~nmu~ioglobulin or alltibody in a cell line ilicapablc of expressing a-l,6-fucosyltmsfe~ase (FUTX) (e.g., as described in Yurnane-Olisuki el nl., Bio/ccs simplex gD signal). Exemplary prornotcrs active in n ~ a ~ ~ i ~ ncacllilsa ~inic ludc cytomcgalovirus immedifktc ci~rly promotcr (CMV-IE), human clongntion factor I-a promotcr (EFI), small nuclear RNA promoters (Ula and Ulb), a-myosin licavy chain promoter, Simian virus 40 promoter (SV40), Rous sarcoma virus promoter (RSV), Adcnovirus major late promotcr, b-actin promotcr; hybrid regulatory clcnlc~it comprising a CMV enhancer1 I)-actin promoter or an i~~i~nunoglobuolri na ntibody promoter or active fndgment thereof. Examples of useful mammalian host cell lines are monkey kidney CV1 line transformed by SV40 (COS-7, ATCC CRL 1651); liu~nale~~ nb~yonkicid ncy line (293 or 293 cclls subcloned for growtli in suspension culture; baby hamster kidney cclls (BHK, ATCC CCL 10); or Chincsc ht~mslero viay cells (CHO). Typical promoters suitable for expression ill yeast cells such as for cxample a yeas1 cell selected from the goup comprising I'ichic~ r)n.stori.~S, ~lclcchuroa7j'ces cc!rc?vi,tiiie antl S. ponibe, i~rclode, but are 1101 linrilcd to, the ADHI ])romotcr, the GAL1 promoter, the GAL4 promoter, the CUP1 promoter, the pH05 promoter, the nntr promoter, the RPRl promoter, or the TEFI promoter. Means for introducing the isolated nucleic acid or cxprcssion construct comprising same into a cell for expression are known to those skilled in the art. The technique used for a given cell depends on the known successful techniques. Means for introducing recombinant DNA into cells include ~nicroinjection, tratisfcction ~nediatcd by DEAE-dcxtrai, ttransfcction mcdiatcd by liposonics such as by using lipofectamine (Gibco, MD, USA) andlor ccllfectin (Gibco, MD, USA), PEG-mediated DNA uptake, electroportation and microphrticle bombardment sucll as by using DNA-coated tungsten or gold particles (Agracetus 5 Inc., WI, USA) amongst othcrs. Tlle Ilost cells uscd to produce the itnmu~ioglobuliti or antibody nray be culturcd in a varicty of media, depending on tlie cell type used. Coni~nerc?ally available media such as I-lam's F10 (Sigma), Minimal Essential Medium ((MEM), (Sigma), RPMI-1640 (Sigma), and Dulbecco's Modified Eagle's Medium 10 ((DMEM), Sigma) are suitable for culturing mammalian cells. Media for culturing other cell types discussed hcreiti are known in the art. Isolation of Protcins .Methods for purifying an irnrnunoglobulin or alltibody are known in the art 15 andlor described herein. Wherc an immut~oglobulin or antibody is sccretcd into the medium, supernatants from such expression systems can be filst concentrated using a commercially available protein co~icentration filter, for example, an Amicon or Millipore Pellicon ultrafiltratioll unit. A protease inhibitor such as PMSF may be 20 included in any of the foregoing steps to inliibit 1)roteolysis and antibiotics nlay be included to prevent the yowtli of adventitious contaminants. The immunoglobulin or antibody prepared From tlic cells can bc purified using, for cxample, ion cxchangc, liydroxyapatitc cl~romatogwpliy, hydrophobic interaction chromatography, gcl clcctropliorcsis, dialysis, affinity climmatography 25 (e.g., proteio A affinity chromatography or protein G clirou~atography), or ally combination of thc foregoing. Thcsc mcthods arc known in the art and described, for cxamplc in W090157134 or Ed IIarIow and David Lnnc (editors) Antibodies: A Laboratory Manual, Cold Spring Ilsrbour Labort~tory(, 1 988). Tllc skillcd artisan will also bc aware that an immunoglobulin or antibody 30 call bc modified to include a tag to facilitate purification or detection, e.g., a poly-llistidinc tag, c.g., a hcxa-histidinc tag, or a influenza virus hemtigglutini~i (HA) tag, or a Simian Virus 5 (V5) tag, or a FLAG tag, or a glutathione S-traasfcrasc (GST) tag. Thc resulting i~iimunoglobulin or inltibody is then purified using mctliods known in tllc art, such as, affinity purification. For 35 example, an imniunoglobulin or antibody comprising a hexa-his tag is poriiied by contacting a samplc comlxising tlie ininiunoglobuliil or ~ntibody with nickel-nitrilotriacetic acid (Ni-NTA) that specifically binds a hexa-his tag ini~nobilized on a solid or setni-solid support, washing the satnple to removc unbound immunoglobulin, and subsequently eluting thc bound immunoglobulin. 40 Alternatively, or in addition a ligand or antibody that binds to a tag is used it1 an affinity purification mcthod. 111 onc cxample, thc initnunoglobulin or aitibody also llas a proteasc clcavagc sitc, such as for Factor X, or Thrombin, which allow thc rclcvwnt protcasc to partially digcst the immuiloglobulin or antibody and thereby liberate the immunoglobulin or antibody from tile tag. The liberated antibody or imtnunoglobuli~l can then bc isolated from the fx~sion partner by subscqucnt 5 cl~romatographicsc pamtion. Assaying Activity of an Im~nu~~oglobulin lmmunoglobuli~~osr antibodics of the disclosure are readily screcned for biological activity, e.g., as described bclow. 10 Bindi~A~ss ays One fo~mo fsucll a11 assay is an antigel] bindingassay, c.g., as described in Scopes (117: Protein purification: principles and practicc, Third Edition, Spriilger Verlag, 1994). Such a mcthod ge~lerally i~lvolves labcling the immunoglobulin 15 or antibody aild contacting it with itnnlobilized antigen. Following washing to removc non-spccific bound protein, the amount of label and, as a consequence, bound protein is detected. Of coursc, the immunoglobulin or antibody call lbc immobilized and the antigen labclcd. I'anning-typc assays, e.g., as dcscribcd or exemplificd herein call also be used. 20 Dctcrmininrr. Neutralization In somc cxatnplcs of tllc prcscm disclosure, arr immunoglobulin or antibody is cal~ablco f neutralizing IL-3 signaling. Va~.ious assays arc known in the art for asscssi~lg thc ability of an 25 immunoglobulin to neutralize signaling of a ligand through a receptor. In one cxamplc, the immunoglobulin or alltibody rcduces or prevents IL-3 binding to thc 3Rn chain andlor a hctcrodimcr oflL-31scsencc of an initnunoglobulin or alltibody and an i~iduccro f tliosc cclls that occurs in a disease or condition (c.g., CpG oligonucleotides andlor immunc coniplcxes). 'l'lic efficacy of tlie immunoglobulin or antibody in treating the disease or condition is tlicn asscssed, c.g., by determiniiig tlie level oflFNa sccrctcd into cell culturc mcdium using a11 ELISA. Altc~wativcly or in addition tl~c lcvcl of histaniine sccmtioa or 1L-4, IL-0 andlor 1L-I3 secretion is assessed. A reduction in tlic lcvcl of any of these cytoki~~ccso mpared to it1 tlic abscncc of immunoglobulin or antibody (or in tlic preseiice of an isotypc control immunoglobulin or antibody) indicates that the immunoglobulin or alltibody is suitable for trcating tlic discasc or condition. Altclnativcly, or in addition, tllc lcvcl of ccll dcatli is assessed. An increase in cell death is i~~dicativocf an i~n~nu~ioglobuolri nan tibody suitable for treating thc disease or conditioci. lri i'ii~o Assyj~.s hi one example, tlie efficacy of a11 iin~nu~loglobulitno lrcat a disease or condition is assessed using an in vivo assay. hi one example, a xcnotra~ispla~itatiomno del of a cancer is used to assess therapeutic efficacy. For example, NODISCID mice are irradiated and optioi~ally treated with anti-CD122 antibody to deplete NK cells. Hurna~i leukemic cells (e.g., acute myeloid leukemia cells) and mouse or human bone marrow stem cells arc adnii~listcrcdt o thc micc. Followi~igc cll cngraftmcnt, a tcst immunoglobulin or antibody is administcrcd lo thc micc and the level of Icukemic cclls in circulation andlor bone marrow a~tdiorly rnpll nodes is assessed. A reduction in the number of lcukcmic cells in circulatioti andlor bone marrow and/or Lympli nodcs in tlic prcsclicc of tllc alltibody or immunoglobulia comyarcd to in thc absencc of tllc aritibody or immunoglobulin itidicates therapeutic efficacy. In another example, the immunoglobulin or atitibody is adminisicred to a non-human animal (e.g., a oon-human primate) and tlic number/level of immune cells, e.g., pDCs and/or basopl~ils, in circulation is assessed. An irnmu~loglobulio~r ~a ntibody that reduces the numbedlevel of immune cclls, c.g., pDCs and/or basophils compared to p~iorto administration andlor ill a control mammal to which thc in?munoglobulin or antibody has not bccn administercd is considcrcd suitable for treating the disease or condition. In arlotller example, the level of a cytokine, such as lFNa is detected in the circulatioti of a mammal, e.g., using ail ELISA. An immunoglobulin or alltibody that reduces the level of the cytokinc compared to the level prior to admitlist~atio~~ andior in a control mammal to which tlie immu~ioglobulin or antibody has not been administered is cotlsidered suitable for treating the discase or condition. Since cytokines such as IFNO. are considered to play a mle in solnc diseasesiconditio~is, e.g., lupus, an immunoglobulin or alltibody that rcduccs IFNn production is considered to be suitable for treating such conditions. Co~nposilions Suitably, in coml~ositionso r methods for ndmiaistratiotr of tlie anti-1L-3Rtx. imtnunoglobulin or antibody to a mammal, the immu~ioglobuli~oir antibody is cornbi~icdw ith a pharmaceutically acceptable carrier, dilue~ita ~idlore xcipie~it,a s is undcrstood in thc art. Accosdingly, one cxatnplc of thc prcscnt disclosusc providcs a pharmaceutical composition co~iiprisi~lgtli e immunoglobulin or antibody of tile disclosure combincd with a pharmaceutically acceptable carriel; diluetlt atidior excipicnt. I11 another example, tlic disclosure provides a ltit cotliprisi~lga plsannaccutically acccptablc carricr, dilucnt atldlor cxcipicnt suitablc for combining or ~iiixing with thc i~ii~ii~tnoglobuolir~ ia ntibody prior to administration to the mammal. I11 tliis example, the kit nay further comprisc instructions for use. In general terms, by "carrier, dilucnt or cxcipicnt" is lncatlt a solid or liquid filler, bi~~detrl,il uent, encapsulating substance, crnolsificr, wctting aycllt, solvent, sospendittg agent, coating or lubrica~it hat may be safcly ad~ninistercdt o any mammal, e.g., a huma~lD. epeading upon the particular routc of administration, a variety of acceptable carriers, diluents or excipients, know11 in thc art may be used, as for example described in Remi~igton's Pharmaceutical Scie~lces (Mack Publishing Co. N.J. USA, 1991). By way of exarnple only, the carriers, diluetits 01. cxcipie~lls may be sclcctcd fiom a group including sugars (c.g. sucrosc, maltosc, trchalosc, glucose), starches, ccllnlosc and its dcrivativcs, malt, gelatinc, talc, calci~i~surr lphatc, oils inclusive of vcgctablc oils, synthctic oil5 and synthct~c mono- or di-glycerides, lowcr alcohols, polyols, alginic acid, phosphate buffcred bolutions, lubricants such 5 as sodium or n~agncsiunl stcaratc, isotonic salinc and pyrogcn-ficc watcr. For cxanplc, the carricr, dilucnt or cxcipicnt is colnpatiblc with, or suitable for, parentera1 administration. Parenteral administration includes any route of administration that is not through the alimentary canal. Non-limiting examples of parcnte~al admillistration include injection, infi~sion and the like. By way of 10 example, ad~ninistratio~b~y injection includes int~-nvenous, intra-arterial, intlamoscular and subcutaneous injection. Also contemplated is dclivcry by a dcpot or slow-rcleasc formulation which may bc dclivercd intradcr~nally, intramuscularly and subcutaneously, for cxample. 15 Combinatio~T~h erapies h~ one cxarnplc, thc immunoglobulin or antibody of the disclosure is administered in combi~~atiowni th another compound or therapeutic treatment useful for treating a disease or condition. In onc example, the imtnunoglobulin or antibody is ad~ninistcrcdp rior to, 20 c.g., one month or one fortnight or one week prior to radiation thcrapy, c.g., for the treatment of canccr, such as a Lcmiltologic canccr, such as leukemia. 111 one uxarl~l~lLclr,e othcr cornpound ih a cl~crnotl~eracl~ony~ [~ounsdu,c 11 as ceboplatin, cisplatin, cyclopl~ospl~amidc,d occtaxal, doxorubicin, crlotinib, ctol)osidc, fluorouracil, irinotccan, mcthotrcxatc, paclitaxel, topotccan, vincristinc 25 or vinblastinc. In one examplc, the chemotherapy compound is selected fiom thc group consisting of mcthotrexatc, I-asparaginasc, vincristine, doxorubicin, danorubicin, cytarabinc, idarubicin, mitoxantronc, cyclopl~ospl~a~~fl~uiddacra, binc, chloramb~~caiul d co~nbinationsth crcoL In one example, the other compound is a cl~emotl~erdpcyo tnpouod used in 30 the trcat~ncnt of acute leukemia, sucll as, a compound selected from the group consisting of mcthotrcxatc, I-aspar:iginasc, vincristi~~dco, xorubicin, danorubicin, cytambinc, idarobici~l,m itoxantronc and combinations thcrcof. In onc cxnmplc, thc otl~ccr ompound is a chcmothcnrpy compound uscd in the twatmcnt of acute lympl~oblasticl eukcmia, such as, a compound sclccted fiom 35 thc group consisting of mcthotrcxatc, I-asl~araginasc, vincristinc, doxorubicin, danorubicio and combinations thcrcof. In a further example, the other cotnpound is a cl~emotherapy co~npound such as azacytidine. In one examplc, the other compound is a biologic useful for treating a 40 canccr, c.g., rituximab, trastuzumab, bcvacizumab, alemtuzumab, panitumumab, or cetuximab In one example, the othcr compound is an anti-inflamtnatory compound. Altcmativcly, or additionally, thc otllcr compou~~ids a11 immu~~osupprcssant. Alternatively, or additionally, the othcr compound is a corticosteroid, such as prcdnisone andlor prednisolone. Alternatively, or additionally, the other compou~ld is an antimalat-ial compound, such as l~ydroxycl~loroqui~or~ c chloroquininc. Altcmativcly, or additionally, thc othcr co~npou~~isd methotrexate. Altcmativcly, or additionally, the other cornpourtd is azathioprine. Alternatively, or additionally, the other compound is cyclopl~ospha~nide. Alternatively, or additiotlally, the other compound is mycophenolate mofetil. Altematively, or additionally, the other compound is an anti-CD20 alltibody (e.g., rituximab or ofatumumab). Alter~rativelyo, r additionally, the othcr compou~ldis an anti-CD22 antibody (e.g., cpratuzumab). Alternatively, or additionally, the othcr compound is an anti-TNF antibody (c.g., infliximab or adalimumab or golimumab). Altematively, or additionally, the other compound is a CTLA-4 antagonist (e.g., abatacept, CTLA4-lg). Alternatively, or additionally, the other compound is an anti-IL-6 a~~tibody. Alternatively, or additionally, thc other compound is a BLys antagonist, sucll as an anti-BLys antibody (e.g., belimumab). Dosages and Titning of Ad~ni~listration For the prevention or twatment of a disease or condition or relapse thereof, the appropriate dosage of an active agent (LC., an i~~l~llu~loglobour li~l antibody of the disclosure), will depend on the type of disease to be treatcd, the scvcrity and course of thc discasc, whctl~cr the immunoglobulin or antibody is administered for prcvcntive or thcra])cutic pu~l~oscpsr,e vious therapy, thc patient's clinical history and rcsponsc to thc im~nunoglobulin, and the discretion of the attending physician. The particular dosage regimen, i.e., dose, timing, and repetition, will dcpct~d on the particular individual and that individual's medical history as asscsscd by a physician. Typically, a clinician will administer an i~n~nu~loglobuut~lit~ial~ d osage is reachcd that achieves tl~ed esired result. Metl~ods of thc prcscnt disclosure arc uscf111 for treating, ameliorating or pwventing thc symptoms of diseases or conditions in a mammal, or for improving the prognosis o f a mammal. Mctl~odso f tllc prcscnt disclosurc arc also uscful for dclaying development of or prcvc~~tinlugp us in an individual at risk of dcvclopit~g lupus or a relapse thereof. For administration oftl~cim ~nunoglobulinso r antibodies described herein, tlor~nald osage anloutlts may valy froln about 101lglkgu p to about 100mglkg of an individual's body wcight or more per day. Exe~nplaryd osages at~dra nges tllcrcof are described herein. For repeated administrations over several days or longer, dcpe~ldi~l0g1 1 the severity of the disease or disorder to be treated, the treatment can be sustained until a desired suppression of symptoms is achieved. In sonle exatnples, the i~nmulloglobulino r antibody is administered at an initial (or loading) dose of between about 11ndkg to about 30mdkg, snch as from about lmglkg to about IOmglkg, or about 21nglkg or about 3mglkg or 41nykg or 5mgikg. Thc immunoglobulin or alltibody can thcli bc admi~iistcrcd at a mainte~la~icdeo se of between about 0.0001nigikg to about Imgkg, such as from about 0.0005mg/kg to about imgikg, for example, from about 0.001mgikg to about lmgikg, such as about O.Olmg/kg to about Imgikg, for examplc from about 0,Olmgkg to about O.lmgikg, sucli as about 0.02mglkg or 0.03nig/kg or O.041ngkg or 0.051ngikg. The maintenance doses luay be administcrcd every 7-30 days, such as, evc~y 10-15 days, for example, evcly 10 or 1 l or 12 or 13 or 14 or 15 days. In some cxamples, tlic inimu~ioglobuliti or antibody is administered at a dosc of bctwcc~i about 0.0001mgikg to about 50rng/kg, such as betweell about 0.0005mg/kg to about 50mg'kg, for example, between about 0.0Olmgikg to about 40rng/kg, for cxample, betwcer~ about 0.005mgikg to about 30mgikg, such as betweell about 0.Olmgikg to about 20mgikg. For example, the immunoglobulin is admitiistered at a dose of betwee11 about 0.0imgikg to about IOmgikg, sucli as from about 0.0lmgkg to about lingikg, such as about 0.02mgikg or 0.03mgikg or 0.04mgikg or 0.05mg/kg or 0.06mgikg or 0.07mgikg or 0.0Xmgikg or 0.09mgikg or 0.1mdkg or 0.2mgikg or 0.3mgikg or 0.4mgikg or O.5mgikg or 0.61ngkg or O.7mgikg or 0.8mgikg or 0.9mgikg (c.g., without a higher loading dose). In some cxamples, nulnerous doses are administered, c.g., evcry 7-30 days, such as, cvery 10-22 days, for example, cvery 10-15 days, for example, every 10 or 1 l or 12 or 13 or 14 or 15 or 16 or 17 or 18 or 19 or20or21 or 22 days. Fo~.cxamplc, tlic itnmunoglobulit~ or alltibody is administcrcd evcty 7 days or cvcry 14 days or cvc~y21 days. In some cx;iml)les, the immunoglobulin or antibody is administcrcd at a dose of between about Imgikg to about 30mg/kg, sucl~ as from about Imgikg to about lomgikg, or about 2mgikg or about 3mgikg or 4mgikg or Smgikg, or such as from about l0mg/kg to 30mg/kg, sucli as about lOmgikg or 15 mgikg or 201iig/kg or 25mg/kg (e.g., without a lowcr mdintcnancc dosc). la some cxamplcs, numerous doscs arc adtninistcrcd, e.g., cvcry 10-70 days, such as evcry 14-70 days, such as, cvery 14-60 days, for examplc, cvcry 14-50 tlays, such as cvcry 14-40 days, or cvcry 14-30 days. For cxarnplc thc doscs arc administcrcd cvcly 14 or 21 or 25 or 28 or 35 or 40 or 42 or 49 or 50 or 55 or 57 or 63 or 70 days. For example, the imtnunoglobuli~o~r antibody is administcrcd cvcry 21 days or every 28 days or eve~y3 5 days or cvcry 42 days or cvcry 49 days or cvery 56 tlays. 111 so~rlcc xamplcs, tlic itnmneoglobuli~io r antibody causcs or is associafcd with a rcductio~i of NK cells in a mammal following administration, e.g., within about 6 hours of administration. 111 some examples, a further dosc of thc immunoglobulin or antibody is administcrcd whcn thc ~iumbcr of NK cells in a ~natntnarl eturns to within 20% or 1O0/u or 5% or 1% of the number of NK cells ill the mammal prior to administration. 111 some cxamples, a furthcr dose of the immu~ioglobulin or antibody is a