p53 del 1-342

Liquid. In 100 mM KCl, 20 mM Tris-HCI, 1 mM DTT, 200 µM EDTA, 20% glycerol, pH 8.0. AVOID FREEZE/THAW CYCLES. Recombinant, human p53 (amino acids 1-342) expressed in S. frugiperda insect cells using a baculovirus expression system. Expressed as a truncated protein with deletion of the C-terminal 51 amino acids, including the entire basic domain and part of the tetramerization domain. The tetramerization domain of p53 plays an important role in cell cycle. Disruption or loss of oligomerization function is associated with loss of cell cycle arrest. This mutant protein can be used as a unique tool to study specific function of p53 related to the C-terminus. Activity: 1 unit/ng protein. One unit is sufficient for a gel mobility shift assay in a 20 µl reaction; 50 units are sufficient for reconstituted transcription assay and 100 units are sufficient for a protein-protein interaction assay. Purity: ≥95% by SDS-PAGE. Contaminants: DNase, RNase, and protease activity: none detected.

Ref.: Waterman, M.J., et al. 1996. Cancer Res. 56, 158. Ishioka, C., et al. 1995. Oncogene 10, 1485. Pellegata, N.S., et al. 1995. Oncogene 11, 337. el-Deiry, W.S., et al. 1992. Nat. Genet. 1, 45. Hupp, T.R., et al. 1992. Cell 71, 875. Hollstein, M., et al. 1991. Science 253, 49.