p53 (pS46) Mouse anti-Human, Unlabeled, Clone: I117-1091, BD

Description

The p53 protein is critical to regulation of normal cell growth and is a suppressor of tumor cell proliferation. Inactivation of p53 by a number of mechanisms, such as missense mutations or interaction with oncogenic viral or cellular proteins, can result in tumor progression. Mutations and/or allelic loss of the p53 gene are associated with a wide variety of human tumors. Known to have a role in transcriptional regulation, p53 suppresses various promoters containing TATA elements in an apparently sequence-independent fashion. p53 also binds to DNA in a sequence-specific manner via recognition of a 20-bp consensus-binding site. This interaction stimulates the expression of genes downstream of the p53 binding site. A number of genes that contain p53-binding sites have been identified, including MDM2, GADD45, and muscle creatine kinase. MDM2 mediates feedback inhibition of p53, which is prevented by phosphorylations of p53 amino-terminal serines and threonines. UV radiation-induced phosphorylation of Serine 46 (S46) is mediated by homeodomain-interacting protein kinase-2 (HIPK2) and is involved in the promotion of apoptosis. Other stress stimuli mediate S46 phosphorylation in p53 via as yet unidentified kinase(s). The I117-1091 mAb recognizes p53 phosphorylated at S46.

Immunohistochemistry, Western Blotting