Anti-CD79a Monoclonal Antibody

A disulphide-linked heterodimer, consisting of mb-1 (or CD79a) and B29 (or CD79b) polypeptides, is non-covalently associated with membrane-bound immunoglobulins on B cells. This complex of mb-1 and B29 polypeptides and immunoglobulin constitute the B cell Ag receptor. CD79a first appears at pre B cell stage, early in maturation, and persists until the plasma cell stage where it is found as an intracellular component. CD79a is found in the majority of acute leukemias of precursor B cell type, in B cell lines, B cell lymphomas, and in some myelomas. It is not present in myeloid or T cell lines. Anti-CD79a is generally used to complement anti-CD20 especially for mature B-cell lymphomas after treatment with Rituximab (anti-CD20) . This antibody will stain many of the same lymphomas as anti-CD20, but also is more likely to stain B-lymphoblastic lymphoma/leukemia than is anti-CD20. Anti-CD79a also stains more cases of plasma cell myeloma and occasionally some types of endothelial cells as well.

B-cell antigen receptor complex-associated protein alpha chain; Ig-alpha; MB-1 membrane glycoprotein; Membrane-bound immunoglobulin-associated protein; Surface IgM-associated protein; CD79a; CD79A; IGA, MB1

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. .

Antibody with azide - store at 2 to 8°C. Antibody without azide - store at -20 to -80°C. Antibody is stable for 24 months. Non-hazardous. No MSDS required.