Anti-p53 [Pab DO-1]
Invented by David Lane at University of Dundee
Catalogue Number | 153402 |
Applications | IHC IP WB |
Antigen/Gene or Protein Targets | Human TP53 / p53 |
Synonyms | p53 |
Reactivity | Human |
Relevance |
Monoclonal antibody which binds mutant and unfolded p53. Background and Research Application Anti-p53 binds p53 protein, a crucial tumour suppressor protein implicated in over 50% of cancers. p53 is a stress-regulated transcription factor that regulates cell cycle arrest and was first identified as an SV40 large T antigen-binding protein. p53 is involved in many mechanisms of anti-cancer function, and plays a role in apoptosis, genomic stability, cell cycle regulation and inhibition of angiogenesis. p53 is known as the guardian of the genome as it functions to prevent gene mutation. Mutants of p53 which frequently occur in human cancers fail to recognise their DNA binding site, leading to the loss of tumour suppressor activity. p53 is typically found in low levels in healthy cells due to its short half-life, however in disease states it is expressed in high amounts due to somatic mutations and believed to contribute to transformation and malignancy. p53 mutations are found in over 50% of cancers with germline mutations, offering a predisposition to inherited cancer susceptibility syndrome. Understanding the functions of mutant p53 can help in the development of new therapeutic approaches that may be useful in a broad range of cancer types. Nine isoforms of human p53 are produced by alternative splicing and promotor usage, the epitope recognized by clone DO-11 is present in all isoforms. Anti-p53 (DO-11) defines a cryptic epitope exposed in unfolded/ denatured p53 and recognises mutant forms of p53. |
Host | Mouse |
Immunogen | Recombinant human p53 |
Immunogen UniProt ID | P04637 |
Positive Control | Colon or breast carcinoma tissue |
Subclass | IgG1 |
Molecular Weight (kDa) | 53 |
Notes |
Production Details Purified using multi-step affinity chromatography with protein A. Storage Conditions Store at -20 degrees frozen. Avoid repeated freeze/thaw cycles. Points of Interest Anti-p53 (DO-11) binds to an epitope in the central region of p53, between amino acids 181-190. This antibody has been used successfully for detection of p53 by western blotting (Wei et al. 2012). Concentration 1mg/ml as standard |
Research Area | Apoptosis and Programmed Cell Death, Cancer, Cell Cycle, Immunology |
Wei et al. 2012. Proc Natl Acad Sci U S A. 109(38):E2543-50. PMID: 22927405.
Pathogenic bacterium Helicobacter pylori alters the expression profile of p53 protein isoforms and p53 response to cellular stresses.
Europe PMC ID: 22927405
Warnock et al. 2011. Cancer Biol Ther. 12(12):1059-68. PMID: 22157150.
Aurora A mediates cross-talk between N- and C-terminal post-translational modifications of p53.
Europe PMC ID: 22157150
Coomber et al. 2001. Clin Cancer Res. 7(9):2802-8. PMID: 11555596.
Isolation of human antibodies against the central DNA binding domain of p53 from an individual with colorectal cancer using antibody phage display.
Europe PMC ID: 11555596
Palecek et al. 2001. Eur J Biochem. 268(3):573-81. PMID: 11168396.
Binding of p53 and its core domain to supercoiled DNA.
Europe PMC ID: 11168396
Wei et al. 2012. Proc Natl Acad Sci U S A. 109(38):E2543-50. PMID: 22927405.
Pathogenic bacterium Helicobacter pylori alters the expression profile of p53 protein isoforms and p53 response to cellular stresses.
Warnock et al. 2011. Cancer Biol Ther. 12(12):1059-68. PMID: 22157150.
Aurora A mediates cross-talk between N- and C-terminal post-translational modifications of p53.
Coomber et al. 2001. Clin Cancer Res. 7(9):2802-8. PMID: 11555596.
Isolation of human antibodies against the central DNA binding domain of p53 from an individual with colorectal cancer using antibody phage display.
Palecek et al. 2001. Eur J Biochem. 268(3):573-81. PMID: 11168396.
Binding of p53 and its core domain to supercoiled DNA.