p53, acetylated (Lys 320), Control Peptide (Tumor Suppressor Protein, Oncogene Protein)

Control Peptide for P1001-30N (antiserum). p53 is the most frequent target of genetic alterations in human cancer. It 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. Altering or inactivating p53 by mutation or reaction with oncogenes or viruses may cause depletion of p53, or conversion of p53 from a tumor suppressor gene to a transforming oncogene. The nuclear protein p53 is associated with cell transformation and proliferation, with definitive possibilities as a marker in malignant lymphoma progression. p53's role in the multistep process leading to cancer is still being investigated, with an emphasis on its relation and control over additional tumor suppressors. Expression correlates with poor prognosis in breast cancer. In colonic cancer p53 expression seen in 47% of tumors and 9% of colonomas. , The p53 tumor suppressor protein plays a major role in cellular response to DNA damage and other genomic aberrations. Activation of p53 can lead to either cell cycle arrest and DNA repair or apoptosis. p53 is phosphorylated at multiple sites in vivo and by several different protein kinases in vitro. DNA damage induces phosphorylation of p53 at Ser15 and Ser20 and leads to reduced interaction of p53 with its negative regulator, oncoprotein MDM2. MDM2 inhibits the accumulation of p53 by targeting it for ubiquitination and proteasomal degradation. p53 can apparently be phosphorylated by ATM, ATR and DNA-PK at Ser15 and Ser37, the phosphorylations impair the ability of MDM2 to bind p53, promoting both the accumulation and functional activation of p53 in response to DNA damage. Chk2 and Chk1 can phosphorylate p53 at Ser20, enhancing its tetramerization, stability and activity. p53 is phosphorylated at Ser392 in vivo and by CAK in vitro. Phosphorylation of p53 at Ser392 is altered in human tumors and has been reported to influence the growth suppressor function, DNA binding and transcriptional activation of p53. p53 is phosphorylated at Ser6 and Ser9 by ck1delta and ck1epsilon both in vitro and in vivo). Phosphorylation of p53 at Ser46 is important in regulating the ability of p53 to induce apoptosis. Applications: Suitable for use in ELISA, Antibody Blocking. Not suitable for use in Western Blot due to low molecular weight. Other applications not tested. Recommended Dilution: Antibody Blocking: 5-10ug per 1ul P1001-30N (antiserum)., ELISA: 50-100ng/well., Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4°C for short-term only. For long-term storage, aliquot and store at -20°C. Aliquots are stable for at least 6 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.