|Other Names||Histone acetyltransferase type B catalytic subunit, Histone acetyltransferase 1, HAT1, KAT1|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP1079b was selected from the C-term region of human HAT1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Acetylates soluble but not nucleosomal histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, acetylates histone H2A at 'Lys-5' (H2AK5ac). Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. May be involved in nucleosome assembly during DNA replication and repair as part of the histone H3.1 and H3.3 complexes. May play a role in DNA repair in response to free radical damage.|
|Cellular Location||Isoform A: Nucleus matrix.|
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Provided below are standard protocols that you may find useful for product applications.
Histone acetylation, particularly of histone H4, has been proposed to play an important role in replication-dependent nucleosome assembly. The HAT1 protein contains D, A, and B motifs, which are present in many N-acetyltransferases, including those that acetylate substrates other than histones. The HAT1 holoenzyme consists of 2 subunits: the catalytic 46-kD HAT1 and the accessory p46. The p46 subunit stimulated the activity of HAT1 and bound to core histones. The HAT1 holoenzyme acetylated newly synthesized but not nucleosomal histone H4 at lys5 and lys12, and, to a lesser extent, histone H2A at lys5. HAT1 and p46 polypeptides are located in the nucleus of S-phase cells. HAT1 may play a role in telomeric silencing.
Gronroos, E., et al., Mol. Cell 10(3):483-493 (2002).Makowski, A.M., et al., J. Biol. Chem. 276(47):43499-43502 (2001).Cheung, P., et al., Mol. Cell 5(6):905-915 (2000).Verreault, A., et al., Curr. Biol. 8(2):96-108 (1998).
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