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Safety Data Sheet (SDS) Purified Anti-mouse CD79a Igalpha Antibody     Product Data Sheet (PDF)    
Purified Anti-mouse CD79a (Igα) Antibody
1265510 500 µg $245.00       
Clone: F11-172
Isotype: Armenian Hamster IgG
Reactivity: Mouse
Formulation: Phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide.
Preparation: The antibody was purified by affinity chromatography.
Concentration: 0.5 mg/ml
Storage & Handling: The antibody solution should be stored undiluted between 2°C and 8°C.

ICFC - Quality tested
IP - Reported in the literature

Recommended Usage:

Each lot of this antibody is quality control tested by intracellular immunofluorescent staining with flow cytometric analysis. For flow cytometric staining, the suggested use of this reagent is ≤0.25 µg per million cells in 100 µl volume. It is recommended that the reagent be titrated for optimal performance for each application.

Application References:

1. Kraus M, et al. 2001. J. Exp. Med. 194:455


Mouse CD79a (Ig α chain) is a 47 kD type I integral membrane protein, known as mb-1 or Ig α. It forms a heterodimer with CD79b (Ig β chain). The CD79a and CD79b heterodimers are associated with surface IgM to form the B-cell receptor (BCR) that is necessary for signal transduction via the BCR in mature B cells. CD79a may play a role in mediating the transport of IgM to the cell surface. Clone F11-172 antibody recognizes the 47 kD membrane glycoprotein present on B lymphocytes.

Other Names: Mb-1, Igα
Structure: A 47 kD membrane glycoprotein which associates with CD79b to form part of B-cell receptor complex.
Distribution: CD79a is expressed on B cells at various differentiation stages, from pre-B cell to plasma cells. It is expressed probably before expression of cytoplasmic µu chain.
Function: Mediating the transport of IgM to the cell surface.
Ligand Receptor: CD79a/CD79b heterodimers are associated with surface IgM to form B cell receptor complex (BCR) to recognize specific antigen.
Antigen References:

1. Schamel W, et al. 2000. Immunity 13:5
2. Taddie JA, et al. 1994. J. Biol. Chem. 269:13529