Anti-p53 acetyl-K382 antibody, monoclonal (2B7E4)

Product#: 71-133
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Anti-p53 acetyl-K382 antibody, monoclonal (2B7E4)

General Information

Cat. No. 71-133
Size :100 ug
Antigen Species Human
Host Species Rabbit
Isotype Mouse IgG1 (κ)
Immunogen Synthetic peptide containing acetyl-Lys382 of human p53
Reactivity Reacts with human p53 acetylated at Lys382. Other species have not been tested.
  1. Western blotting (~1 ug/ml)
  2. Other applications have not been tested.
Storage Sent at 4℃ or -20℃. Upon arrival, briefly centrifuge and store at -20℃
Form Purified IgG 1mg/ml in PBS (pH 7.4), 50% glycerol, sterilized by filtration
Data Link UniProtKB/Swiss-Prot P04637 (P53_HUMAN)


p53 mutants are found in more than half of human cancers and are considered as the most important human cancer related gene. p53 is detected at 53kD position by electrophoresis and is composed of 393 amino acids. In the unstressed normal cells, the p53 level is low and it is inactive. However, with stress, especially with DNA damage, it is activated to promote arrest of cell cycle and repair of DNA damage, or induction of apoptosis. The functions and stability of p53 are regulated by phosphorylation of serine and threonine, and acetylation of lysine at various sites in the molecule. Acetylation of lysine 382 (acetyl-K382) of p53 occurs after DNA damage and is catalyzed by the p300/CBP acetyltransferase, which stabilizes p53 proten (ref 1).


p53 protein was first described in 1979 and ten years later identified as a tumor suppressor protein. It is approximately 53 kDa and contains 393 amino acids that comprise several functional domains. It consists of an acidic N-terminus with a transactivation domain, a hydrophobic central DNA-binding core and a basic C-terminus with regulatory and oligomerisation domains. Upon sources of cellular stress such as damaged DNA, p53 protein is stabilized and activated via post-transcriptional mechanisms, and this leads to cell cycle arrest and DNA repair or apoptosis. 

As just described, activation of p53-mediated transcription is a critical cellular response to DNA damage. p53 stability and sitespecific DNA-binding activity and, therefore, transcriptional activity, are modulated by post-translational modifications including phosphorylation and acetylation. p53 is phosphorylated at several serine residues within its amino- and carboxy-terminal domains and is also acetylated at lysines within the carboxy-terminal portion of the molecule.


Fig.1 Identification of p53 protein, whose Lys382 is acetylated, by Western blotting with 2B7E4 antibody.

MCF7 cells in culture were treated with actinomycin D at 5 nM for the indicated periods and the cell extracts were analyzed by Western blotting with anti-p53 acetyl-K382 antibody (2B7E4) and omnipotent anti-p53 antibody (DO-1). Acetylation of p53 at K382 was induced by the DNA damaging treatment.


  1. Bode, A. M., et al., "Post-translational modification of p53 in tumorigenesis.", Nat. Rev. Cancer, 4 (10), 793-805 (2004). PMID:15510160]
  2. Serpi, R., et al., Pharmacol. Toxicol., 92 (5), 242-245 (2003). [PMID : 12753412]
  3. Brazdova, M., et al., Nucleic Acids Res., 30 (22), 4966-4974 (2002). [PMID : 12434001]
  4. Shieh, S. Y., et al., Genes Dev., 14 (3), 289-300 (2000). [PMID : 10673501]
  5. Sakaguchi, K., et al., Genes Dev., 12 (18), 2831-2841 (1998). [PMID : 9744860]

Aliases for TP53 Gene

  • Tumor Protein P53 2 3 5
  • P53 2 3 4
  • Cellular Tumor Antigen P53 3 4
  • Phosphoprotein P53 3 4
  • Antigen NY-CO-13 3 4
  • LFS1 2 3
  • Transformation-Related Protein 53 3
  • Mutant Tumor Protein 53 3
  • Li-Fraumeni Syndrome 2
  • P53 Tumor Suppressor 3
  • Tumor Suppressor P53 4
  • Tumor Supressor P53 3
  • Tumor Protein 53 3
  • BMFS5 3
  • TRP53 3
  • BCC7 3
  • TP53 5

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