Render Target: STATIC
Render Timestamp: 2024-11-01T09:57:13.334Z
Commit: 23cb9f61fe67e1e9093fd644a533c4ff516a6463
XML generation date: 2024-08-01 15:27:21.737
Product last modified at: 2024-10-14T21:15:08.951Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-Bcr (Tyr177) Antibody #3901

Filter:
  • WB
  • F

    Supporting Data

    REACTIVITY H M
    SENSITIVITY Endogenous
    MW (kDa) 160 (Bcr); 210 (Bcr-Abl)
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    • F-Flow Cytometry 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Flow Cytometry (Fixed/Permeabilized) 1:100

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-Bcr (Tyr177) Antibody detects endogenous levels of Bcr and Bcr-Abl only when phosphorylated at tyrosine 177.

    Species Reactivity:

    Human, Mouse

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr177 of human Bcr. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    The Bcr gene was orginally identified by its presence in the chimeric Bcr-Abl oncogene (1). The amino-terminal region of Bcr contains an oligomerization domain, a serine/threonine kinase domain, and a region that binds SH2 domains. The middle of the protein has a PH domain and a region of sequence similarity to the guanine nucleotide exchange factors for the Rho family of GTP binding proteins. The carboxy-terminal region may be involved in a GTPase activating function for the small GTP-binding protein Rac (2,3). The function of wild type Bcr in cells remains unclear. PDGF receptor may use Bcr as a downstream signaling mediator (4). Research studies have shown that the Bcr-Abl fusion results in production of a constitutively active tyrosine kinase, which causes chronic myelogenous leukemia (CML) (5). Tyr177 of Bcr is phosphorylated in the Bcr-Abl fusion protein, which plays an important role in transforming the activity of Bcr-Abl (6). Phosphorylated Tyr177 provides a docking site for Gab2 and GRB2 (7,8).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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