p53, Human, Control Peptide (Tumor Suppressor Protein, Oncogene Protein)

A peptide surrounding the human p53, acetylated at Lys373, was coupled to KLH and injected into rabbits. Lysine373 is acetylated by p300. p53, the most frequent target of genetic alterations in human cancer, is one of the most widely studied tumor suppressor gene. The most important activities of p53 are its cellular growth arrest and induction of programmed cell death (apoptosis). Human p53 is a single polypeptide chain of 393aa. It has three well-defined functional domains: An N-terminal acidic transactivation domain (TAD), a central DNA-binding domain (DBD), and a C-terminal homo-oligomerization domain (OD). All three domains are important for interaction with target genes. A great majority of tumor-associated missense mutations occur within the DBD and the mutant protein fails to regulate p53 target genes. , Posttranslational modifications of p53 (phosphorylation and acetylation) have been implicated in its physiological role. p53 has at least 4 phosphorylation sites at the N-terminus with Ser15 as an important site in response to DNA damage and a target of the ATM and DNA PK proteins. There are three potential sites within the C-terminus of p53 that may affect its DNA-binding ability. p53 also serve as a substrate for various histone acetylases to enhance it transcriptional activity. Applications: ELISA:1:10K-1:100K using 50-100ng of control peptide/well.