MOUSE ANTI HUMAN CD79a

CD79a

Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant

Recognises an epitope within the cytoplasmic domain of CD79a. CD79a also known as mb-1 is a 45kD protein that is expressed by B lymphocytes during differentiation from early pre-B cell stage through to plasma cells. The CD79a molecule associates with CD79b (B29) to form a heterodimer that is non-covalently linked to surface immunoglobulin forming the B-cell receptor (BCR) complex. The CD79a/CD79b heterodimers are also necessary for intracellular signalling following antigen-binding to surface immunoglobulin. Clone HM57 has been reported to work in western blotting applications. Recommended Negative Controls: MOUSE IgG1 NEGATIVE CONTROLRecommended Secondary Antibodies: Rabbit Anti Mouse IgGGoat Anti Mouse IgGGoat Anti Mouse IgG (H/L)Goat Anti Mouse IgG IgA IgMHuCAL Anti Mouse IgG1Goat Anti Mouse IgG (Fc)Sheep Anti Mouse IgG (H/L)

Following antigen binding the BCR has been shown to translocate from detergent-soluble regions of the cell membrane to lipid rafts although signal transduction through the complex can also occur outside lipid rafts By similarity. Tissue specificityB-cells. Post-translational modificationPhosphorylated on tyrosine serine and threonine residues upon B-cell activation. Phosphorylation of tyrosine residues by Src-family kinases is an early and essential feature of the BCR signaling cascade. The phosphorylated tyrosines serve as docking sites for SH2-domain containing kinases leading to their activation which in turn leads to phosphorylation of downstream targets. Phosphorylation of serine and threonine residues may prevent subsequent tyrosine phosphorylation. Ref. 16Involvement in diseaseDefects in CD79A are a cause of non-Bruton type agammaglobulinemia [MIM:601495]. Agammaglobulinemia is an immunodeficiency disease which results in developmental defects in the maturation pathway of B-cells. Two different mutations one at the splice donor site of intron 2 and the other at the splice acceptor site for exon 3 have been identified. Both mutations give rise to a truncated protein. Ref. 15Ref. 17Sequence similaritiesContains 1 Ig-like C2-type (immunoglobulin-like) domain. Contains 1 ITAM domain. [1] \" Human interferon consensus sequence binding protein is a negative regulator of enhancer elements common to interferon-inducible genes. \" Weisz A. Marx P. Sharf R. Appella E. Driggers P. H. Ozato K. Levi B. -Z. J. Biol. Chem. 267:25589-25596(1992) [PubMed: 1460054] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung and Monocyte. [2] Schmidt M. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databasesCited for: SEQUENCE REVISION. [3] \" The status quality and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). \" The MGC Project TeamGenome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. [4] \" Interaction between interferon consensus sequence-binding protein and COP9/signalosome subunit CSN2 (Trip15). A possible link between interferon regulatory factor signaling and the COP9/signalosome. \" Cohen H. Azriel A. Cohen T. Meraro D. Hashmueli S. Bech-Otschir D. Kraft R. Dubiel W. Levi B. Z. J. Biol. Chem. 275:39081-39089(2000) [PubMed: 10991940] [Abstract]Cited for: INTERACTION WITH COPS2. [5] \" The consensus coding sequences of human breast and colorectal cancers. \" Sjoeblom T. Jones S. Wood L. D. Parsons D. W. Lin J. Barber T. D. Mandelker D. Leary R. J. Ptak J. Silliman N. Szabo S. Buckhaults P. Farrell C. Meeh P. Markowitz S. D. Willis J. Dawson D. Willson J. K. V. Gazdar A. F. Hartigan J. Wu L. Liu C. Parmigiani G. Park B. H. Bachman K. E. Papadopoulos N. Vogelstein B. Kinzler K. W. Velculescu V. E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract]Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-81 AND THR-197.