• Nature
  • Source
  • Amino Acid Sequence
    • Accession
    • Species
    • Molecular weight
      385 kDa


Our Abpromise guarantee covers the use of ab170086 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Biological activity
    No reaction by IEP with antiserum to Human Albumin, IgD, IgE, IgG, IgM and Lactoferrin.
  • Applications


  • Purity
    >95% by SDS-PAGE .

  • Form
  • Additional notes
    ab170086 is prepared from colostrum shown to be non reactive for HbsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.No reaction by IEP with antiserum to Human Albumin, IgD, IgE, IgG, IgM and Lactoferrin.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 7.40
    Constituents: 0.28% Sodium phosphate, 0.88% Sodium chloride

General Info

  • Alternative names
    • B lymphocyte-specific MB1 protein
    • B-cell antigen receptor complex-associated protein alpha chain
    • CD 79a
    • CD79a
    • CD79A antigen
    • CD79a antigen (immunoglobulin-associated alpha)
    • CD79a molecule, immunoglobulin-associated alpha
    • CD79A_HUMAN
    • Ig alpha
    • Ig-alpha
    • IGA
    • IgM-alpha
    • Immunoglobulin-associated alpha
    • Ly54
    • MB-1 membrane glycoprotein
    • MB1
    • Membrane-bound immunoglobulin-associated protein
    • Surface IgM-associated protein
    see all
  • Function
    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.
  • Tissue specificity
  • Involvement in disease
    Defects in CD79A are the cause of agammaglobulinemia type 3 (AGM3) [MIM:613501]. It is a primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life. Note=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.
  • Sequence similarities
    Contains 1 Ig-like C2-type (immunoglobulin-like) domain.
    Contains 1 ITAM domain.
  • Post-translational
    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.
  • Cellular localization
    Cell membrane. 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.
  • Information by UniProt


  • SDS-PAGE analysis of ab170086.

    Lane 1: 5 µg ab170086, reduced
    Lane 2: 10 µg ab170086, reduced
    Lane 3: 20 µg ab170086, reduced
    Lane 4: Molecular weight markers
    Lane 5: 5 µg ab170086, non-reduced
    Lane 6: 10 µg ab170086, non-reduced
    Lane 7: 20 µg ab170086, non-reduced


ab170086 has not yet been referenced specifically in any publications.

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