Purified recombinant Human CD79A

This recombinant monoclonal antibody can detects endogenous levels of CD79A protein.

CD79A IGA MB1

B-cell antigen receptor complex-associated protein alpha chain (Ig-alpha) (MB-1 membrane glycoprotein) (Membrane-bound immunoglobulin-associated protein) (Surface IgM-associated protein) (CD antigen CD79a)

B lymphocyte-specific MB1 protein antibody ;
B-cell antigen receptor complex-associated protein alpha chain antibody ;
CD 79a antibody ;
CD79a antibody ;
CD79a antigen ;
immunoglobulin-associated alpha ;
antibody ;
CD79A antigen antibody ;
CD79a molecule ;
immunoglobulin-associated alpha antibody ;
CD79A_HUMAN antibody ;
Ig alpha antibody ;
Ig-alpha antibody ;
IGA antibody ;
IgM-alpha antibody ;
Immunoglobulin-associated alpha antibody ;
Ly54 antibody ;
MB-1 membrane glycoprotein antibody ;
MB1 antibody ;
Membrane-bound immunoglobulin-associated protein antibody ;
Surface IgM-associated protein antibody ;
CD79A nanobody ;

The B lymphocyte antigen receptor is a multimeric complex that includes the antigen-specific component, surface immunoglobulin (Ig). Surface Ig non-covalently associates with two other proteins, Ig-alpha and Ig-beta, which are necessary for expression and function of the B-cell antigen receptor.This gene encodes the Ig-alpha protein of the B-cell antigen component. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jul 2008]

Disease:Defects 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.,Required in cooperation with CD79B for initiation of the signal transduction cascade activated by binding of antigen to the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Also required for BCR surface expression and for efficient differentiation of pro- and pre-B-cells. Stimulates SYK autophosphorylation and activation. Binds to BLNK, bringing BLNK into proximity with SYK and allowing SYK to phosphorylate BLNK. Also interacts with and increases activity of some Src-family tyrosine kinases. Represses BCR signaling during development of immature B cells.,online information:CD79A mutation db,PTM:Phosphorylated 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.,similarity:Contains 1 Ig-like C2-type (immunoglobulin-like) domain.,similarity:Contains 1 ITAM domain.,subcellular location: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.,subunit:Heterodimer of alpha and beta chains; disulfide-linked. Part of the B-cell antigen receptor complex where the alpha/beta chain heterodimer is non-covalently associated with an antigen-specific membrane-bound surface immunoglobulin of two heavy chains and two light chains. Interacts through its phosphorylated ITAM domain with the SH2 domains of SYK which stimulates SYK autophosphorylation and activation. Also interacts, when phosphorylated on Tyr-210, with the SH2 domain of BLNK/SLP65, bringing BLNK into proximity with SYK and allowing SYK to phosphorylate BLNK which is necessary for trafficking of the BCR to late endosomes. Interacts with Src-family tyrosine kinases including FYN and LYN, increasing their activity.,tissue specificity:B-cells.,

Cell membrane; Single-pass type I membrane protein. 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. .

Detected on marginal zone and germinal center B cells in lymph nodes (PubMed:24631). Detected on blood B cells (at protein level) (PubMed:24631, PubMed:1667271).