Render Target: STATIC
Render Timestamp: 2024-10-31T10:48:34.071Z
Commit: 23cb9f61fe67e1e9093fd644a533c4ff516a6463
XML generation date: 2024-08-01 15:23:26.077
Product last modified at: 2024-06-27T13:36:33.875Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-PTPα (Tyr789) Antibody #4481

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 145
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50

    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-PTPα (Tyr789) Antibody detects endogenous levels of PTPα only when phosphorylated at Tyr789. This antibody does not cross-react with other phosphorylated receptor tyrosine phosphatases.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr789 of human PTPα. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    PTPα (PTPRA) is a transmembrane receptor tyrosine phosphatase implicated in the regulation of Src family kinases during the G2 to mitosis entry point. Two identified splice variants differ in the size of the extracellular region; the shorter form appears to be ubiquitously expressed while the larger protein is more limited in distribution (1). The cytoplasmic region of PTPα contains two putative catalytic domains. One phosphatase domain (D1) exhibits catalytic activity while the other (D2) may regulate phosphatase activity by allowing receptor dimer formation (2,3). PTPα is a physiological regulator of Src and Src family kinases (4). Constitutive phosphorylation of the carboxy-terminal Tyr789 of PTPα is essential for dephosphorylation of Src at Tyr527. Phosphorylation of PTPα at this residue also allows binding of the Grb2 inhibitor, restricting PTPα activation of Src (5,6). PKC-mediated phosphorylation of the PTP at Ser180 and Ser204 also increases PTPα phosphatase activity (7).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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