raised against an acetylated and phosphorylated Histone H3 peptide (amino acids 7-20, acetylated Lys 9 and phosphorylated Ser 10) corresponding to the N-terminus of Histone H3 of human origin
recommended for detection of Ser 10 and Lys 9 phosphorylated Histone H3 of mouse, rat, human, Drosophila, Xenopus and C. elegans origin by WB and IP; also reactive with additional species, including bovine
p-Ac-Histone H3 Background Information In eukaryotes, DNA is wrapped around histone octamers to form the basic unit of chromatin structure. The octamer is composed of Histone H2A, H2B, H3 and H4, and it associates with approximately 200 base pairs of DNA to form the nucleosome. The association of DNA with histones results in dense packing of chromatin, which restricts proteins involved in gene transcription from binding to DNA. p300 preferentially acetylates Histone H3 at Lysine 14 and 18 and Histone H4 at Lysine 5 and 8. Histone H4 may also be acetylated at Lysine 12 and 16, and the involvement of acetylated H4 with Histone H2A, H2B and H3 suggests that acetylated histones may be involved in dynamic chromatin remodeling. Phosphorylation of Histone H3 is involved in chromosome condensation during mitosis. Histone H3 phosphorylation correlates to the expression of immediate-early genes such as c-Jun, c-Fos and c-Myc. Research indicates that MSK1, a growth and stress activated kinase, also phosphorylates Histone H3 in vitro.
