Render Target: STATIC
Render Timestamp: 2024-12-20T12:04:23.968Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-30 01:55:36.715
Product last modified at: 2024-09-30T08:01:41.451Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

PTP-PEST (AG10) Mouse mAb #4864

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 110 to 125
    Source/Isotype Mouse IgG1
    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, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    PTP-PEST (AG10) Mouse mAb detects endogenous levels of total PTP-PEST protein. This antibody does not cross-react with other protein tyrosine phosphatases.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with human PTP-PEST recombinant protein. The antibody recognizes an epitope within the amino-terminal 305 residues.

    Background

    PTP-PEST is a ubiquitously expressed cytosolic protein tyrosine phosphatase with multiple proline-rich regions that appear to be the docking sites for PTP-PEST binding partners or substrates (1). PTP-PEST regulates fibroblast adhesion, migration, and cytokinesis through its association with and dephosphorylation of p130 Cas, paxillin, PSTPIP1, WASP, and other adhesion molecules (1-5). By modulating phosphorylation states of Shc, Pyk2, Fak, and WASP, PTP-PEST negatively regulates lymphocyte activation (1,6). In mammary epithelial cells, EGF facilitates the dephosphorylation of Jak2 by PTP-PEST, thereby interfering with lactogenic hormone PRL signaling (7). PTP-PEST dephosphorylates c-Abl as well, which affects the phosphorylation states of PTP-PEST substrates such as paxillin, p130 Cas, Crk, and PSTPIP1 (8).
    PTP-PEST regulates adhesion and motility of cultured epithelial cells through modulation of Rho GTPase activity (9), and is required for integrin-mediated endothelial cell adhesion and migration (10).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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