Anti-p53 [Pab DO-2]
Invented by David Lane at University of Dundee
Anti-p53 [Pab DO-1]
Invented by David Lane from Karolinska Institutet
Invented at University of Dundee
- Datasheet
- References (21)
- Inventor Info
Info
| Catalogue Number | 151147 |
| Applications | ChIP IHC IF IP WB |
| Antigen/Gene or Protein Targets | p53 (N terminus) |
| Synonyms | P53, Trp53, pantropic |
| Reactivity | Human |
| Relevance |
Anti p53 monoclonal antibody used to analyse and detect ‘the most mutated gene in cancer’ p53 and its protein interactions, enabling identification of transformed cell lines. 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. Anti-p53 antibody can be used on frozen sections as well as methacarn or formol saline fixed paraffin sections. This antibody was created by David Lane, who also discovered p53, to measure p53 in various analyses of different tissue samples. It can detect interactions of proteins with p53. |
| Host | Mouse |
| Immunogen | Recombinant human wild type p53 protein expressed in E.coli |
| Immunogen UniProt ID | P04637 |
| Positive Control | MDA-MB-231 cell line |
| Subclass | IgG2a |
| Molecular Weight (kDa) | 53 |
| Myeloma Used | Sp2/0-Ag14 |
| Recommended Growing Conditions | DMEM + 5% FCS |
| Strain | Balb/c |
| 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 Epitope maps between amino acid residues 11-25 of p53 of human origin Anti-p53 reacts very strongly with p53 in conventionally fixed and processed histological sections. It allows for analysis of p53 expression in human tumours, including IHC on paraffin-embedded specimens. Anti-p53 DO-1 can be biotinylated and used for detection of p53 as the labelled antibody, using Pab 421 as the solid-phase capture antibody. This antibody has specificity for a denaturation-resistant epitope at the N terminus of p5. Anti-p53 is useful tool for analysis of p53 expression in human tumours including immunohistochemistry on paraffin embedded specimens. Concentration 1mg/ml as standard Difference Between Clones All clones were created at the same time as anti-p53 DO-7, and all bind to p53 protein, confirmed via immunoblotting, immunoprecipitation and immunocytochemistry. DO1 secreted large amounts of an IgG2a antibody whilst DO2 and DO7 secreted large amounts of an IgG2b antibody. It is likely DO-2 recognises a denatured epitope. |
| Research Area | Apoptosis and Programmed Cell Death, Cancer, Cell Cycle, DNA Damage and Repair, Epigenetics & Nuclear Signalling |
Anti-p53 [DO-11]
Invented by Prof David Lane at University of Dundee
References: 21 entries
Choi et al. 2018. Proc Natl Acad Sci U S A. 115(42):10666-10671. PMID: 30266789.
Choi et al. 2018. Cell Death Dis. 9(6):633. PMID: 29795372.
Ghosh et al. 2018. Elife. 7:. PMID: 29474172.
SIRT6 interacts with TRF2 and promotes its degradation in response to DNA damage.
Europe PMC ID: 27923994
Rizzo et al. 2016. Nucleic Acids Res. :. PMID: 27923994.
WB
Targeting polo-like kinase 1 suppresses essential functions of alloreactive T cells.
Europe PMC ID: 26724940
Beckerman et al. 2016. Cell Cycle. :1-14. PMID: 27210019.
IF
Lysines in the tetramerization domain of p53 selectively modulate G1 arrest.
Europe PMC ID: 27210019
İlhan et al. 2016. J Vet Diagn Invest. :. PMID: 27016721.
Expression of p53 protein, Jaagsiekte sheep retrovirus matrix protein, and surfactant protein in the lungs of sheep with pulmonary adenomatosis.
Europe PMC ID: 27016721
Berges et al. 2016. Immunol Res. :. PMID: 26724940.
Kloet et al. 2015. Biochem J. 469(2):289-98. PMID: 25990325.
FOXO target gene CTDSP2 regulates cell cycle progression through Ras and p21(Cip1/Waf1).
Europe PMC ID: 25990325
Loughery et al. 2014. Nucleic Acids Res. 42(12):7666-80. PMID: 24928858.
ChIP WB
Critical role for p53-serine 15 phosphorylation in stimulating transactivation at p53-responsive promoters.
Europe PMC ID: 24928858
Llanos et al. 2001. Nat Cell Biol. 3(5):445-52. PMID: 11331871.
IF
Stabilization of p53 by p14ARF without relocation of MDM2 to the nucleolus.
Europe PMC ID: 11331871
Stephen et al. 1995. J Mol Biol. 248(1):58-78. PMID: 7537340.
Characterisation of epitopes on human p53 using phage-displayed peptide libraries: insights into antibody-peptide interactions.
Europe PMC ID: 7537340
Vojtĕsek et al. 1992. J Immunol Methods. 151(1-2):237-44. PMID: 1378473.
An immunochemical analysis of the human nuclear phosphoprotein p53. New monoclonal antibodies and epitope mapping using recombinant p53.
Europe PMC ID: 1378473
Add a reference
References: 21 entries
Choi et al. 2018. Proc Natl Acad Sci U S A. 115(42):10666-10671. PMID: 30266789.
Choi et al. 2018. Cell Death Dis. 9(6):633. PMID: 29795372.
Ghosh et al. 2018. Elife. 7:. PMID: 29474172.
SIRT6 interacts with TRF2 and promotes its degradation in response to DNA damage.
Rizzo et al. 2016. Nucleic Acids Res. :. PMID: 27923994.
WB
Targeting polo-like kinase 1 suppresses essential functions of alloreactive T cells.
Beckerman et al. 2016. Cell Cycle. :1-14. PMID: 27210019.
IF
Lysines in the tetramerization domain of p53 selectively modulate G1 arrest.
İlhan et al. 2016. J Vet Diagn Invest. :. PMID: 27016721.
Expression of p53 protein, Jaagsiekte sheep retrovirus matrix protein, and surfactant protein in the lungs of sheep with pulmonary adenomatosis.
Berges et al. 2016. Immunol Res. :. PMID: 26724940.
Kloet et al. 2015. Biochem J. 469(2):289-98. PMID: 25990325.
FOXO target gene CTDSP2 regulates cell cycle progression through Ras and p21(Cip1/Waf1).
Loughery et al. 2014. Nucleic Acids Res. 42(12):7666-80. PMID: 24928858.
ChIP WB
Critical role for p53-serine 15 phosphorylation in stimulating transactivation at p53-responsive promoters.
Llanos et al. 2001. Nat Cell Biol. 3(5):445-52. PMID: 11331871.
IF
Stabilization of p53 by p14ARF without relocation of MDM2 to the nucleolus.
Stephen et al. 1995. J Mol Biol. 248(1):58-78. PMID: 7537340.
Characterisation of epitopes on human p53 using phage-displayed peptide libraries: insights into antibody-peptide interactions.
Vojtĕsek et al. 1992. J Immunol Methods. 151(1-2):237-44. PMID: 1378473.
An immunochemical analysis of the human nuclear phosphoprotein p53. New monoclonal antibodies and epitope mapping using recombinant p53.
Add a reference
