p53 Antibody (BP 53.122): sc-73566

p53 Antibody (BP 53.122) is an IgG2a kappa light chain mouse monoclonal antibody raised against a recombinant protein corresponding to amino acids 16-25 of p53 of human origin. Reactive against all isoforms of p53, the p53 monoclonal antibody (BP 53.122) enables the study of p53′s localization, expression, and role in cancer by being employed in various assays such as western blotting, immunohistochemistry, immunofluorescence and ELISA in mouse, rat and human samples. The p53 protein, encoded by the TP53 gene, is a DNA-binding tumor suppressor that contains essential structural domains, including the oligomerization domain and transcription activation domain, which are crucial for its role in regulating cell fate. In response to stress signals such as DNA damage, p53 upregulates genes involved in growth arrest and apoptosis, influencing programmed cell death, cell differentiation, and cell cycle control mechanisms. Localized to the nucleus, p53 can be shuttled to the cytoplasm by MDM2, a key negative regulator and E3 ubiquitin ligase. MDM2 ubiquitinates p53 for proteasomal degradation, tightly regulating its activity. p53′s functionality is influenced by post-translational modifications such as phosphorylation and acetylation, which control its conformational state and DNA-binding activity. Mutations in the DNA-binding domain of p53, particularly within amino acids 110-286, compromise its ability to bind DNA effectively, leading to loss of tumor suppression and contributing to the progression of many human cancers. This region is a frequent target of mutations in cancers, disrupting the energetically favorable binding to cis elements necessary for gene regulation. Anti-p53 antibody (BP 53.122) provides valuable insights into p53’s cellular pathways and assists in identifying potential therapeutic targets aimed at restoring p53′s tumor-suppressing function.

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p53 Antibody (BP 53.122) References:

1. Increase in wild-type p53 stability and transactivational activity by the chemopreventive agent apigenin in keratinocytes.  |  McVean, M., et al. 2000. Carcinogenesis. 21: 633-9. PMID: 10753197
2. Mdm2 binding to a conformationally sensitive domain on p53 can be modulated by RNA.  |  Burch, LR., et al. 2000. FEBS Lett. 472: 93-8. PMID: 10781812
3. A role for p53 in base excision repair.  |  Zhou, J., et al. 2001. EMBO J. 20: 914-23. PMID: 11179235
4. Enhancement of p53 sequence-specific binding by DNA supercoiling.  |  Palecek, E., et al. 2004. Oncogene. 23: 2119-27. PMID: 14755248
5. A conformation hypothesis for the suppressor and promoter functions of p53 in cell growth control and in cancer.  |  Milner, J. 1991. Proc Biol Sci. 245: 139-45. PMID: 1682937
6. p53 represses autophagy in a cell cycle-dependent fashion.  |  Tasdemir, E., et al. 2008. Cell Cycle. 7: 3006-11. PMID: 18838865
7. Unraveling the Allosteric Mechanism of Four Cancer-related Mutations in the Disruption of p53-DNA Interaction.  |  Tang, Y., et al. 2021. J Phys Chem B. 125: 10138-10148. PMID: 34403252
8. Altering relative metal-binding affinities in multifunctional Metallochaperones for mutant p53 reactivation.  |  Kwan, K., et al. 2024. J Inorg Biochem. 251: 112433. PMID: 38043136
9. Dominance of wild-type p53-mediated transcriptional activation in breast epithelial cells.  |  Davis, P., et al. 1996. Oncogene. 13: 1315-22. PMID: 8808706
10. Identification of a novel p53 functional domain that is necessary for efficient growth suppression.  |  Walker, KK. and Levine, AJ. 1996. Proc Natl Acad Sci U S A. 93: 15335-40. PMID: 8986812

The preferred p53 antibody is p53 Antibody (DO-1): sc-126.