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FITC - anti human CD79a - Clone HM57

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產(chǎn)品名稱: FITC - anti human CD79a - Clone HM57
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FITC - anti human CD79a - Clone HM57


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FITC - anti Human CD79a - HM57

Reference Size Price Quantity Add to cart
79AF-100T 100 test
210,00 € tax excl.

Product Description

  • HM57
  • IgG1
  • FCM
  • FITC
  • Please refer to the Certificate of Analysis for the lot-specific concentration.
  • Synthetic peptide corresponding to 202-216 amino acid sequence of human mb-1.
  • Human
  • The reagent is provided in aqueous buffered solution containing protein stabilizer, and ≤0.09% sodium azide (NaN3)
  • RUO
  • CD79a, clone HM57, is a mAb intended for the identification of B lymphocytes. This reagent is effective for direct iIF staining of human tissue for FCM analysis using ≤1 μg/106 cells.
CD79a View larger
  • CD79a
  • CD79a

This antibody reacts with the CD79a-antigen. CD79a associates with CD79b to form part of the B-cell receptor complex. It has been suggested that CD79a may play a role in mediating the transport of IgM to the cell surface. This antibody has been found to react on permeabilized A20 cells (mouse B cell line). CD79a (Ig alpha, MB1) forms disulfide-linked heterodimer with CD79b (Ig beta). They both are transmembrane proteins with extended cytoplasmic domains containing immunoreceptor tyrosine activation motives (ITAMs), and together with cell surface immunoglobulin they constitute B-cell antigen-specific receptor (BCR). CD79a and b are the first components of BCR that are expressed developmentally. They appear on pro-B cells in association with the endoplasmic reticulum chaperone calnexin. Subsequently, in pre-B cells, CD79 heterodimer is associated with lambda5-VpreB surrogate immunoglobulin and later with antigen-specific surface immunoglobulins. At the plasma cell stage, CD79a is present as an intracellular component. CD79a/b complex interacts with Src-family tyrosine kinase Lyn, which phosphorylates its cytoplasmic ITAM motives to form docking sites for downstream signaling.
  • Mb-1, Ig?
  • 973
  • 47 kDa
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