| Product Name |
p-Claspin Antibody (Ser 945) |
| Antibody Type |
Primary Antibodies |
| Antigen Alias |
recommended for detection of Ser 945 phosphorylated Claspin of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian |
| Modification |
Phosphoralated |
| Modification Notes |
Claspin is a large acidic protein that undergoes phosphorylation and binds to Chk1 in the presence of checkpoint-inducing DNA templates in Xenopus egg extracts. Serine 864, Serine 895 and Threonine 906 undergo phosphorylation during the DNA replication checkpoint response. Phosphorylation of Threonine 906 creates a docking site for Plx1, the Xenopus Polo-like kinase. This interaction promotes the phosphorylation of Claspin on a nearby Serine 934 by Plx1. Phosphorylation of Claspin at Threonine 916 and Serine 945 is required for the DNA-dependent binding of Claspin to Chk1. A mutant of Claspin containing substitutions at positions 864 and 895 cannot bind to Chk1 and is unable to mediate its activation. Claspin, ATR, and Rad17 may collaborate in checkpoint regulation by detecting different aspects of a DNA replication fork. Down-regulation of Claspin augments the premature chromatin condensation induced by hydroxyurea, inhibits the UV-induced reduction of DNA synthesis, and decreases cell survival. ATR can regulate Claspin phosphorylation in response to DNA damage and replication stress, resulting in recruitment and phosphorylation of BRCA1. |