53BP1 Polyclonal Antibody

Gel pack with blue ice.

The p53 binding proteins 53BP1 and 53BP2 (Bbp) bind to the central DNA-binding domain of wild type p53, but do not bind mutant p53. The central DNA-binding domain of p53 is required for site-specific DNA binding and is frequently mutated in malignant tumors. Binding of 53BP1 to the L3 loop of p53 and of 53BP2 to the L2 loop of p53 confirms that the loop is dependent on p53 conformation. Site-specific binding also suggests that 53BP1 and 53BP2 are involved in p53-mediated tumor suppression. 53BP1 was isolated from H258 cells and is expressed in Jurkat cells in both the cytoplasm and the nucleus. The N-terminus of 53BP2 is localized to the cytoplasm, while the C-terminus might be localized in the nucleus. 53BP1 promotes cell proliferation by binding to p202, whereas 53BP2 induces cell death by binding to Bcl2 and NFkB p65.

Synthesized peptide derived from human 53BP1 around the non-phosphorylation site of S6

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen

53BP1 Polyclonal Antibody detects endogenous levels of 53BP1 protein.