Anti-p53 Antibody, aa 211-220, clone240

p53 was discovered in 1979 as a cellular protein associating with the transforming protein of SV40 tumor virus. Since then, many different biochemical functions have been attributed to the 53 kD phosphoprotein. Experimental evidence has suggested that p53 acts as a negative regulator of cell growth in normal cells (Finlay, 1989). Thus, the inactivation or mutation of p53 may be an essential step in the development of malignancy (Lane and Benchmol, 1990). Wild-type p53 levels in normal cells and tissues were found to be very low. Mutant p53 polypeptide, however, is often found to be present at high concentrations in mammalian tumors and tumor cell lines. For example, in an immuno-histochemistry study 40% of human breast cancer showed elevated levels of mutant p53 in the cell nucleus. Mutations of the p53 protein have some characteristic features:

a) Most of them are missense point mutations giving rise to an altered protein function.

b) Many -but not all- mutant p53 proteins exhibit a common mutant structure, which can be recognized by monoclonal antibodies specific for p53 in the mutant conformation.

Epitope: aa 211-220

Murine p53-beta galactosidase fusion protein expressed in E. coli.

Detect p53 with Anti-p53 Antibody, aa 211-220, clone240 (Mouse Monoclonal Antibody), that has been shown to work in IP, WB & IHC.

Detection of p53 oncogene protein

Detection of mutant p53

Prevalence of detection using CBL 404

-50% colon carcinoma sections positive (30 samples)

-70% lung carcinoma sections positive (50 samples)

-30% carcinoma breast samples positive (50 samples)

Normal and pre-malignant tissues negative

Reacts on methacarn fixed tissue

Optimal working dilutions must be determined by the end user.

Research Category
Epigenetics & Nuclear Function

Research Sub Category
Transcription Factors

PAb 240 recognizes an epitope of p53 tumor suppressor protein between amino acids 211 and 220 (Gannon, 1990; Legros, 1994) in human, mouse, rat, hamster, monkey, cow and chicken. Assaying native samples (immunoprecipitation, ELISA) the PAb 240 detects only the mutant forms of p53 (Gannon, 1990; Said, 1994). In methods using denatured samples [Western blot analysis (Gannon, 1990) and immunohistochemistry of frozen tissue sections (Said, 1994; Bartek, 1991; Walker, 1991)], the PAb 240 recognizes both mutant and denatured wild-type p53.

Format: Purified

Purified mouse monoclonal in buffer containing 0.1M Tris-glycine (pH 7.4), 0.15M NaCl, with 0.05% sodium azide. We recommend that each laboratory determine an optimum working titre for use in its particular application.

For use within 1 month of purchase store at +4°C, for long term storage aliquot antibody into small volumes and store at -20°C.

Replaces: 04-1083

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