Render Target: STATIC
Render Timestamp: 2024-12-20T11:52:52.422Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-08-01 15:27:19.766
Product last modified at: 2024-12-06T14:30:10.685Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

PTPRF/LAR Antibody #17164

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 150, 213
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:200

    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

    PTPRF/LAR Antibody recognizes endogenous levels of total PTPRF/LAR protein. This antibody detects the E-subunit of the processed PTPRF/LAR protein.

    Species Reactivity:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala1109 within the extracellular domain of human PTPRF/LAR protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Receptor type protein tyrosine phosphatase F (PTPRF, LAR) is a transmembrane PTP that helps to regulate insulin signaling, cell proliferation and cell migration. The PTPRF protein is composed of an extracellular segment that contains several Ig-like and fibronectin (Fn-III) domains, a transmembrane region and a pair of cytoplasmic phosphatase domains (1,2). Functional studies reveal that the membrane-associated D1 phosphatase domain is responsible for substrate dephosphorylation, while the D2 domain is important for substrate specificity (3). PTPRF negatively regulates insulin signaling through dephosphorylation of insulin receptor and insulin receptor substrate (4). This phosphatase activates the pro-apoptotic DAPK serine/threonine kinase by removing a phosphate at Tyr491/492, while the kinase Src replaces the phosphate to inactivate DAPK at the same time it down regulates PTPRF expression (5). PTPRF is commonly found at focal adhesions where it interacts with liprin, which localizes the phosphatase to the membrane, and the Rac/Rho family GTPase Trio (6). Localization of PTPRF at adherens junctions results in PTPRF modification of β-catenin, which inhibits cell migration by limiting the amount of available cytosolic β-catenin (7).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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