p53 Antibody (BP 53.12): sc-81168

p53 Antibody (BP 53.12) is an IgG2a kappa light chain mouse monoclonal antibody, raised against the N-terminus of p53 of human origin, is an important tool used to detect and study the p53 protein within cells and tissues. This p53 mouse antibody (BP 53.12) specifically binds to p53, allowing researchers to examine its expression levels and localization through techniques such as ELISA, immunohistochemistry, western blotting, and immunofluorescence microscopy in human samples. Notably, it enables detection of both wild type and mutant p53 under denaturing and non-denaturing conditions. By utilizing the anti-p53 antibody (BP 53.12), scientists can investigate alterations in p53 that are common in various cancers, many of which involve mutations or dysregulation of this protein. Encoded by the TP53 gene, p53 protein is a fundamental tumor suppressor in human cells, acting as a transcription factor, p53 regulates genes that control vital cellular processes such as DNA repair, cell cycle arrest, programmed cell death, and senescence. When cells experience stress or DNA damage, p53 becomes activated and can pause the cell cycle at checkpoints like G1/S or G2/M, providing an opportunity for DNA repair mechanisms to fix the damage. If the damage is irreparable, p53 can initiate apoptosis to prevent the propagation of cells with genetic abnormalities, thereby inhibiting tumor development. Studying p53 with the help of p53 monoclonal antibody (BP 53.12) enhances our understanding of tumor suppression mechanisms and aids in the development of potential therapeutic strategies targeting the p53 pathway.

Alexa Fluor^® is a trademark of Molecular Probes Inc., OR., USA

LI-COR^® and Odyssey^® are registered trademarks of LI-COR Biosciences

p53 Antibody (BP 53.12) References:

1. Phosphorylation of Ser-20 mediates stabilization of human p53 in response to DNA damage.  |  Chehab, NH., et al. 1999. Proc Natl Acad Sci U S A. 96: 13777-82. PMID: 10570149
2. Post-translational modification of p53 protein in response to ionizing radiation analyzed by mass spectrometry.  |  Abraham, J., et al. 2000. J Mol Biol. 295: 853-64. PMID: 10656795
3. Nuclear accumulation of p53 protein and apoptosis induced by various anticancer agents, u.v.-irradiation and heat shock in primary normal human skin fibroblasts.  |  Chikayama, S., et al. 2000. Int J Oncol. 16: 1117-24. PMID: 10811983
4. Stabilization of alanine substituted p53 protein at Ser15, Thr18, and Ser20 in response to ionizing radiation.  |  Yamauchi, M., et al. 2004. Biochem Biophys Res Commun. 323: 906-11. PMID: 15381086
5. Essential role of p53 in silica-induced apoptosis.  |  Wang, L., et al. 2005. Am J Physiol Lung Cell Mol Physiol. 288: L488-96. PMID: 15557088
6. Expression of mutant p53 proteins in lung cancer correlates with the class of p53 gene mutation.  |  Bodner, SM., et al. 1992. Oncogene. 7: 743-9. PMID: 1565469
7. Label-free electrochemical detection of the p53 core domain protein on its antibody immobilized electrode.  |  Yeo, J., et al. 2009. Anal Chem. 81: 4770-7. PMID: 19435284
8. Structure and stability insights into tumour suppressor p53 evolutionary related proteins.  |  Pagano, B., et al. 2013. PLoS One. 8: e76014. PMID: 24124530
9. Multiple p53 protein isoforms and formation of oligomeric complexes with heat shock proteins Hsp70 and Hsp90 in the human mammary tumor, T47D, cell line.  |  Selkirk, JK., et al. 1994. Appl Theor Electrophor. 4: 11-8. PMID: 7811761
10. Therapeutic targeting of the p53 tumor suppressor gene.  |  Beaudry, GA., et al. 1996. Curr Opin Biotechnol. 7: 592-600. PMID: 8939636

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