p300 (C1135-2414)

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 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 C-terminus of p300 contains a histone acetyltransferase (HAT) domain expanded from residues 1195 to 1673, an activation domain (residues 1763-1812) that interacts with many transcription factors and an SRC-1 domain further down stream of the activation domain. P300 is able to acetylate histones and many other transcription factors, including p53 (Cat#P2001), E2F (Cat#1031), TFIIE (Cat#P1007), and TFIIF (Cat#P1010) etc. implicating diverse roles of p300 in gene regulation (5-8).
The C-terminus of Flag tagged p300 (residues 1135-2414) was expressed in a baculovirus system and purified by affinity and FPLC chromatography.
Recombinant p300 (C-terminus) can be used for: 1) protein-protein interaction assay; 2) in vitro transcription assay; 3) in vitro acetylation assay; and 4) cell growth assay.
Purified protein is greater than 95% homogeneous based on SDS-PAGE analysis.
1 unit equals 1 nanogram of purified protein. 50 units are required for a reconstituted transcription assay and 100 units are required for a protein-protein interaction 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. Ogryzko, V.V. et al., (1996) Cell 87, 953-959
5. Kung, AL. et al., (2000) Genes Dev. 14, 272-277
6. Imhof, A. et al., (1997) Curr. Biol. 7, 689-692
7. Gu, W. et al., (1997) Cell 90, 595-606
8. Martinez-Balbas, MA. et al., (2000) EMBO J. 19, 662-671