p53 was identified as a tumor suppressor by showing that this protein has the ability to block transformation and to inhibit tumor cell growth. In addition, p53 is a transcription factor capable of regulating the expression of a subset of downstream genes (1-5). Mutation of two specific N-terminal residues in p53 (residues Leu22 and Trp23) impairs the ability of p53 to transactivate (6) and has been correlated with its ability to bind TAFII40 and TAFII60 (or TAFII31 and TAFII70) (7, 8) suggesting that one or both of these interactions is important for activation. Mutation of residues 22 and 23 to Ala does not affect binding to TBP (6), although mutation of these residues to charged amino acids has been reported to disrupt the p53-TBP interaction (9). Different mutations in p53 gene have been characterized in a variety of human cancers (10). Loss or mutation of p53 function is highly correlated with tumorigenesis.

GST-p53 is isolated from a strain of E. coli that contains the coding sequence of wild type human p53 (full length) under the control of a T7 promoter.

GST-p53 can be used for protein-protein interaction assay. The fusion protein is immunoreactive with the human p53-specific monoclonal antibody 1801.

The purified protein is greater than 95% homogeneous based on SDS-PAGE analysis.
1x dilution buffer A: 20 mM Tris-Cl (pH 8.0), 20% Glycerol, 100 mM KCl, 1 mM DTT and 0.2 mM EDTA

References:
1. Finlay, C. et al., (1989) Cell 57, 1083-1093
2. Michalovitz, D. et al., (1990) Cell 62, 671-680
3. Baker, S. et al., (1990) Science 249, 912-915
4. Fields, S. et.al., (1990) Science 249, 1046-1049
5. Raycroft, L. et al., (1990) Science 249, 1049-1051
6. Lin,J., et al., (1994) Genes Dev 8, 1235-1246
7. Thut,C., et al., (1995) Science, 267, 100-104
8. Chang,J., et al., (1995) J. Biol. Chem 270, 25014-25019
9. Hollstein, M. et al., (1991) Science 253, 49-53
10. Bennett, W. et al., (1992) Chest 101, 19S-20S

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