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Render Timestamp: 2024-09-26T10:34:44.714Z
Commit: 60a5021c3a47fc24d1656fb463e2c3c41a1ad145
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464
  1. Products /
  2. Primary Antibodies /
  3. Hck Antibody

Hck Antibody #4352

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  • WB
This product is discontinued

Inquiry Info. # 4352

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    Supporting Data

    REACTIVITY H M Mk
    SENSITIVITY Endogenous
    MW (kDa) 61
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    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

    Hck Antibody detects endogenous levels of total Hck protein. This antibody does not cross-react with family members Src, Lyn and Fyn.

    Species Reactivity:

    Human, Mouse, Monkey

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to amino-terminal residues of human Hck. Antibodies are purified by protein A and peptide affinity chromatography

    Background

    The hematopoietic cell kinase (Hck) is a Src family protein tyrosine kinase that is prominently expressed in lymphoid and myeloid lineages of hematopoiesis (1). The Hck kinase participates in transduction of a variety of extracellular signals that affect cellular processes, including cell proliferation, differentiation, and migration. Hck protein structure includes a relatively divergent amino-terminal "unique" domain that is subject to post-translational lipid modifications and targets Hck to the plasma membrane. Src homology 3 (SH3) and 2 (SH2) domains, and a tyrosine kinase catalytic domain are adjacent to the "unique" domain. Research studies indicate that phosphorylation of conserved tyrosine residues positively and negatively regulate Hck catalytic activity. Phosphorylation of Hck at the conserved, carboxy-terminal Tyr499 by protein kinase Csk promotes an interaction between the phosphorylated tyrosine and the SH2 domain, rendering Hck inactive. Disruption of this interaction through dephosphorylation, the replacement of the Tyr522 with phenylalanine, or carboxy-terminal truncation mutations, results in constitutive activation of Hck. Autophosphorylation of Tyr411 within the kinase domain positively regulates Hck catalytic activity. Thus, the activation of Hck requires both disruption of the regulatory tyrosine-SH2 domain interaction and autophosphorylation of the regulatory tyrosine residue within the kinase domain (2,3). The dysfunction or dysregulation of Hck may contribute to the pathogenesis of some human forms of leukemia (4).

    Database Links

    UniProt ID: P08631


    Entrez-Gene Id: 3055


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