CBP (catalytic domain) human recombinant

Although originally termed histone acetyltransferases (HATs) for their lysine acetylation activity on histone N-terminal tails, p300 and its paralogue, CBP, have been shown to acetylate a variety of non-histone proteins including p53, DNA polymerase ß and nuclear import factors. p300/CBP acetylations play regulatory roles in transcription, DNA repair and replication, the cell cycle, p53 turnover, and nuclear import. In addition to functions which overlap with those of CBP, p300 has a number of unique functions, including a role in the induction of p21Waf1/Cip1 cell cycle inhibitor.

Source:
Catalytic domain (residues 1319-1710) of human CBP histone acetyltransferase

[Varies with lot. For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.] XXX 250 pmol/min/µg assayed as production of CoA-SH from AcCoA in the presence of a peptide comprising human p53 residues 368-386. CoA-SH is determined colorimetrically by reaction with DTNB (5,5′-Dithiobis (2-nitrobenzoic acid).

Acetyltransferase assays

CBP (catalytic domain) human recombinant protein expressed in E. Coli.

Format: Purified

In liquid containing 50 mM Tris/HCl, pH 8.0, 0.1 mM EDTA, 10% glycerol. Frozen solution.

Stable for 12 months at -80°C from date of receipt. Avoid multiple freeze/thaw cycles.

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