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pCAF Histone Acetyltransferase

Cayman Chemical Item Number 10009115

HAT; p300/(CREB binding protein) Associated Factor

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Description

Source: active recombinant GST-tagged protein purified from E. coli · Mr: ~40 kDa · 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

1 Marmorstein, R. Structure and function of histone acetyltransferases. Cell Mol Life Sci 58 693-703 (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. J Biol Chem 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., 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).

Synonyms
  • HAT
  • p300/(CREB binding protein) Associated Factor
Formulation A solution in 50 mM sodium phosphate, pH 7.2, containing 100 mM sodium chloride, 1 mM EDTA, and 20% glycerol
Purity ≥95%
Stability 6 months
Storage -80°C
Shipping Wet ice in continental US; may vary elsewhere

Background Reading

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

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).

Okumura, K., Mendoza, M., Bachoo, R.M., et al. PCAF modulates PTEN activity. J Biol Chem 281 26562-26568 (2006).

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).

Trievel, R.C., Li, F., 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).

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Size Price Quantity Subtotal
25 µg $112.00 $0.00
50 µg $213.00 $0.00
100 µg $403.00 $0.00
Bulk Contact
Cart Total $0.00

This product is available in custom sizes and/or larger quantities.

Please contact our Sales Department for a quote or to purchase.

Pricing updated 2012-05-25. Prices are subject to change without notice.

To ask for assistance with one of our products please contact a Technical Support Scientist.

Warning This product is not for human or veterinary use.

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