|Calculated MW||H=50,40;M=49;R=49 KDa|
|Other Names||Histone acetyltransferase type B catalytic subunit, Histone acetyltransferase 1, HAT1, KAT1|
|Target/Specificity||This KAT1 (HAT1) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 389-419 amino acids from the C-terminal region of human KAT1 (HAT1).|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||KAT1 (HAT1) Antibody (C-term) is for research use only and 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.|
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).