PCAF Histone Acetyltransferase (human, recombinant)

p300/(CREB binding protein) associated factor (PCAF) belongs to the GCN5/PCAF family of nuclear histone acetyltransferases (HATs). Gcn5/PCAF proteins contain a ~160 residue HAT domain and a conserved bromodomain directly C-terminal to the HAT domain, which has been shown recently to be an acetyl-lysine targeting motif. PCAF acetylates specific lysines on the N-terminal tails of Histones H3 & H4 and on the transcriptional activators MyoD, E2F1, and p53. Recently, PCAF was also shown to acetylate PTEN on lysine residues K125 & K128 within the catalytic cleft thus inactivating the enzyme. In many, but not all of these cases, acetylation has been shown to enhance the DNA binding affinity of the affected protein. Although the recombinant HAT proteins will acetylate free histones, nucleosomal acetylation only occurs in the context of the in vivo HAT complex. Cayman's PCAF preparation contains 165 amino acids from the HAT activity domain of human PCAF fused to GST at the N-terminus. Enzyme activity was determined using a fluorescent HAT assay and is comparable to that found in the literature.Synonyms: HAT, p300/(CREB binding protein) Associated Factor. Purity: >80% estimated by SDS-PAGE. Source: Active recombinant GST-tagged protein purified from E. coli. Amino Acids: 492-656 (partial protein). MW: ~40 kDa. Formulation: (Request formulation change), 50 mM HEPES, pH 8, with 150 mM NaCl, 1 mM EDTA, and 20% glycerol.