Render Target: SSR
Render Timestamp: 2024-10-24T19:46:46.052Z
Commit: 56767fe525c928647c8401233a175d0d607d385d
XML generation date: 2024-08-01 15:30:22.258
Product last modified at: 2024-08-29T11:45:07.657Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-BAP1 (Ser592) Antibody #9373

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 95
    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 1:50

    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-BAP1 (Ser592) Antibody detects endogenous levels of BAP1 only when phosphorylated at Ser592.

    Species Reactivity:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser592 of human BAP1.

    Background

    BAP1 (BRCA1-Associated Protein 1) was originally identified as a BRCA1 associated, nuclear localized ubiquitin hydrolase that suppresses cell growth (1). The protein belongs to the UCH family of deubiquitinases, with a UCH domain in its N-terminal segment and a BRCA1 interaction domain as well as a nuclear localization signal in its C-terminal segment (1). Frequent gene locus rearrangement, deletion and null mutation of BAP1 have been found in lung and breast cancers (1,2). Mutation analysis in vivo in cancer cell line survival and in animal tumorigenesis indicate that both the deubiquitinase activity and the nuclear localization signal are required for BAP1 function as a tumor suppressor (3). BAP1 does not have direct deubiquitination activity towards the autoubiquitinyled BRCA1/BARD1 E3 complex (4), but its interaction with BARD1 inhibits BRCA1/BARD1 E3 activity by interfering with the compex dimerization process (5). In addition to its interaction with BRCA1/BARD1, BAP1 has also been shown to interact with and deubiquitinylate HCF-1, thereby controlling its stability (6).
    Phosphorylation of Ser592 on BAP1 was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC-MS/MS platform for phosphorylation site discovery (7).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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