Gcn5 and PCAF are highly homologous members of the Gcn5-related N-acetyltransferase (GNAT) superfamily of N-acetyltransferases involved in histone acetylation.1 Gcn5 and PCAF contain a highly conserved central core with divergent N- and C-terminal ends.2 Gcn5/PCAF are enzymatic subunits that exist in a mutually exclusive manner as part of the mammalian SAGA and ATAC complexes.3,4 Recombinant Gcn5 preferentially acetylates lysine 14 on histone H3 in vitro. Recombinant Gcn5 alone is unable to acetylate nucleosomal core histone substrates. Acetylation of the nucleosomal histones requires that Gcn5 be a part of either the multisubunit SAGA or ATAC protein complexes.5 The multisubunit Gcn5/PCAF-containing complexes have a broad substrate specificity, including H3K9, H3K18, H4K8, and H4K16, as well as additional sites on histone H2B.3Technical InformationSynonymsGeneral control of amino acid synthesis protein 5-like 2KAT2ALysine acetyltransferase 2ASTAF97Purity50 % (estimated by SDS-PAGE)Sourceactive recombinant N-terminal His-tagged protein expressed in Sf21 cellsAmino Acids2-837 (full-length)MW96.3 kDaFormulation50 mM Tris-HCl, pH 8.0, containing 150 mM sodium chloride and 20% glycerolUniProt Accession Q92830