Render Target: STATIC
Render Timestamp: 2024-12-20T11:35:54.786Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-08-01 15:32:46.901
Product last modified at: 2024-10-15T13:15:08.603Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Claspin Antibody #2800

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 220
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    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

    Claspin Antibody detects endogenous levels of total claspin protein.

    Species Reactivity:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to amino acids near the carboxy terminus of human claspin. Antibodies are purified by peptide affinity chromatography.

    Background

    Originally identified in Xenopus (1), and later in human cells (2), claspin is a mediator of Chk1 signal transduction at the replication checkpoint and in response to DNA damage. Expression of claspin is cell cycle-regulated, with protein levels peaking at the S/G2 phase (2). Expression is negatively regulated by both proteosome- and caspase-mediated degradation (3), and stabilized by activation of Chk1 (4). Claspin is a chromatin-bound protein, and has been shown to interact with the PNCA complex in the absence of DNA damage (5). Following checkpoint activation it remains chromatin-bound but is released from the PCNA complex and is phosphorylated in an ATR-dependent manner. Phosphorylated claspin interacts with several components of the DNA damage response including BRCA1 (6) and Chk1 (7), leading to ATR-dependent phosphorylation on each of these proteins. Phosphorylated Rad17 has also been shown to bind to and regulate the phosphorylation of claspin (8). It has been proposed that claspin behaves as a tumor suppressor in come cases since down-regulation promotes apoptosis following genotoxic stress (2). Conversely, claspin seems to behave as an oncogene in other instances since overexpression promotes cellular proliferation (6). Upregulated claspin has been suggested to be a sensitive marker of abnormally proliferating cells (9).
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