Tumor Protein P53 (TP53) antibody
|Synonyms||p53, LFS1, TRP53, FLJ92943, P53, Trp53, MGC112612, brp53, drp53, fb40d06, wu:fb40d06, zgc:111919, TP53, bbl, bfy, bhy, p44, Tp53, tp53|
|Clonality||Monoclonal (PAb 1801)|
Alternatives Immunohistochemistry (Formalin-fixed Sections) (IHC (f)), Western Blotting (WB), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (Frozen Sections) (IHC (fro))
|9 references available|
|Quantity||0.25 mg (0.5 mg/ml) (Variants)|
|Price||Product not available in this region.|
|Immunogen||Recombinant fusion protein|
|Description||The gene for the nuclear phosphoprotein p53 is the most commonly mutated gene yet identified in human cancers. Missense mutations occur in tumors of the colon, lung, breast, ovary, bladder and several other organs. The mutant p53 is over-expressed in a variety of transformed cells and it forms specific complexes with several viral oncogenes including SV40 large T, E1B from adenovirus and E6 from human papilloma virus. Recent data suggest that wild type p53 plays a role as a checkpoint protein for DNA damage during the S-phase of the cell cycle. However, it is still unclear whether point mutated forms of p53 are simple null mutants and/or dominant negatively acting proteins. p53 migrates at a reduced molecular weight of 53 kDa. Clone PAb 1801 recognizes an epitope between amino acids 32-79 in the N-terminal domain of human wild type and mutant p53 antibody. It does not cross-react with p53 from other species. A truncated recombinant human p53 fusion protein was used as immunogen.|
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
|Molecular Weight||53 kDa|
|Application Notes||Applications include western blot analysis (1-2 µg/ml), immunoprecipitation (1-2 µg/1 x 10^6 cells), immunofluorescence microscopy of cultured cells, immunohistochemistry of frozen (5-20 µg/ml), and antigen-unmasked paraffin-embedded tissue sections (5-20 µg/ml). Positive control cell lines include SK-BR-3 human breast carcinoma cells (ATCC HTB-30), and A431 human vulval carcinoma cells (ATCC CRL-1555). COS-7 SV40 transformed monkey kidney cells (ATCC CRL-1651) or another SV40-transformed cell line are also useful as positive controls for detecting p53. MCF-7 human breast carcinoma cells (ATCC HTB-22) are suggested as a negative control. Positive immunostaining is seen in a high proportion of breast and colon carcinomas. p53 staining is not typically detected in normal skin, brain, kidney, lung, stomach or breast tissue.|
|Purification||Purified from tissue culture supernatant or ascites by affinity chromatography.|
|Buffer||Aqueous buffered solution.|
|Preservative||0.09% Sodium azide.|
|Storage||Store undiluted at 4°C.|
|Research Area||Cancer, Cell Cycle, Transcription Factors, DNA/RNA, Apoptosis/Necrosis|
|Restrictions||For Research Use only|
|Anti-human p53. Formalin-fixed, paraffin-embedded tissue section of breast carcinoma stained for p53 (clone PAb 1801, ABIN967422) using a DAB chromogen and Hematoxylin counterstain.|
Vojtĕsek, Bártek, Midgley et al.: "An immunochemical analysis of the human nuclear phosphoprotein p53. New monoclonal antibodies and epitope mapping using recombinant p53." in: Journal of immunological methods, Vol. 151, Issue 1-2, pp. 237-44, 1992 (PubMed).
Said, Barrera, Shintaku et al.: "Immunohistochemical analysis of p53 expression in malignant lymphomas." in: The American journal of pathology, Vol. 141, Issue 6, pp. 1343-8, 1993 (PubMed).
Walker, Dearing, Lane et al.: "Expression of p53 protein in infiltrating and in-situ breast carcinomas." in: The Journal of pathology, Vol. 165, Issue 3, pp. 203-11, 1992 (PubMed).
Porter, Gown, Kramp et al.: "Widespread p53 overexpression in human malignant tumors. An immunohistochemical study using methacarn-fixed, embedded tissue." in: The American journal of pathology, Vol. 140, Issue 1, pp. 145-53, 1992 (PubMed).
Baker, Markowitz, Fearon et al.: "Suppression of human colorectal carcinoma cell growth by wild-type p53." in: Science (New York, N.Y.), Vol. 249, Issue 4971, pp. 912-5, 1990 (PubMed).
Vogelstein: "Cancer. A deadly inheritance." in: Nature, Vol. 348, Issue 6303, pp. 681-2, 1991 (PubMed).
Banks, Matlashewski, Crawford: "Isolation of human-p53-specific monoclonal antibodies and their use in the studies of human p53 expression." in: European journal of biochemistry / FEBS, Vol. 159, Issue 3, pp. 529-34, 1986 (PubMed).
Legros, Lacabanne, dAgay et al.: "Production of human p53 specific monoclonal antibodies and their use in immunohistochemical studies of tumor cells." in: Bulletin du cancer, Vol. 80, Issue 2, pp. 102-10, 1994 (PubMed).
Jacquemier, Molès, Penault-Llorca et al.: "p53 immunohistochemical analysis in breast cancer with four monoclonal antibodies: comparison of staining and PCR-SSCP results." in: British journal of cancer, Vol. 69, Issue 5, pp. 846-52, 1994 (PubMed).