The antibody detects endogenous level of Chk2 only when phosphorylated at serine 516.
Purification
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography usingepitope-specific phosphopeptide. The antibody against non-phosphopeptide was removedby chromatogramphy using non-phosphopeptide corresponding to the phosphorylation site.
Immunogen
Peptide sequence around phosphorylation site of pSer516 (Q-P-S (p) -T-S) derived from Human Chk2. Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates.
In response to DNA damage and replication blocks, cell cycle progression is halted through the control of critical cell cycle regulators. The protein encoded by Chk2 gene is a cell cycle checkpoint regulator and putative tumor suppressor. It contains a forkhead-associated protein interaction domain essential for activation in response to DNA damage and is rapidly phosphorylated in response to replication blocks and DNA damage. When activated, the encoded protein is known to inhibit CDC25C phosphatase, preventing entry into mitosis, and has been shown to stabilize the tumor suppressor protein p53, leading to cell cycle arrest in G1. In addition, this protein interacts with and phosphorylates BRCA1, allowing BRCA1 to restore survival after DNA damage. Mutations in this gene have been linked with Li-Fraumeni syndrome, a highly penetrant familial cancer phenotype usually associated with inherited mutations in TP53. Also, mutations in this gene are thought to confer a predisposition to sarcomas, breast cancer, and brain tumors. This nuclear protein is a member of the CDS1 subfamily of serine/threonine protein kinases. Three transcript variants encoding different isoforms have been found for this gene.