Active, pure human recombinant enzyme
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PCAF Histone Acetyltransferase (human, recombinant)

Item No. 10009115

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
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
Shipping & Storage Information
Storage
-80°C
Shipping
Wet ice in continental US; may vary elsewhere
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    100 µg

    $541

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    Product Description

    p300/(CREB binding protein) associated factor (PCAF) belongs to the GCN5/PCAF family of nuclear histone acetyltransferases (HATs).1 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.1,2 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.3 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.4 Enzyme activity was determined using a fluorescent HAT assay and is comparable to that found in the literature.5

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Marmorstein, R. Structure and function of histone acetyltransferases. Cell. Mol. Life Sci. 58(5-6), 693-703 (2001).

    2. Carrozza, M.J., Utley, R.T., Workman, J.L., et al. The diverse functions of histone acetyltransferase complexes. Trends Genet. 19(6), 321-327 (2003).

    3. Okumura, K., Mendoza, M., Bachoo, R.M., et al. PCAF modulates PTEN activity. The Journal of Biological Chemisty 281, 26562-26568 (2006).

    4. Clements, A., Rojas, J.R., Trievel, R.C., et al. Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A. EMBO J. 18(13), 3521-3532 (1999).

    5. Trievel, R.C., Li, F.Y., and Marmorstein, R. Application of a fluorescent histone acetyltransferase assay to probe the substrate specificity of the human p300/CBP-associated factor. Anal. Biochem. 287, 319-328 (2000).