p300-Ch1 [302-531]

Human p300 and CBP (CREB binding protein) are highly related transcriptional coactivators. Both proteins have been identified through protein interaction assays (1-3). In addition to interacting with a variety of cellular factors and onco-proteins, loss of the wild type CBP alleles in isolated tumors suggests that CBP/p300 might serve as tumor suppressors (4). The ability of p300 to acetylate many transcription factors, including p53, E2F, TFIIE, and TFIIF etc. demonstrated a novel mechanism of targeted p300 regulation of gene expression (5-7).
p300-Ch1 was expressed in a bacterial system and purified by affinity and FPLC chromatography.
Recombinant p300-Ch1 can be used for: 1) protein-protein interaction assay; 2) in vitro transcription assay; 3) in vitro acetylation assay; and 4) cell growth assay. For Research Use Only.
The purified recombinant protein is greater than 95% homogeneous based on SDS-PAGE analysis.
1 unit equals 1 nanogram of purified protein. 1-5 units are sufficient for a gel mobility shift assay in a 20µl reaction; 50-100 units are sufficient for reconstituted transcription assay and 100-200 units are sufficient for a protein-protein interaction assay or an acetylation assay.
variable in different lots
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. Stein, RW. et al., (1990) J. Virol. 64, 4421-4427
2. Chrivia, JC. et al., (1993) Nature 365, 855-859
3. Eckner, R. et al., (1994) Genes & Dev. 8, 869-884
4. Kung, AL. et al., (2000) Genes & Dev. 14, 272-277
5. Imhof, A. et al., (1997) Curr. Biol. 7, 689-692
6. Gu, W. et al., (1997) Cell 90, 595-606
7. Martinez-Balbas, MA. et al., (2000) EMBO J. 19, 662-671