Merck, 07-329, Anti-acetyl-Histone H4 (Lys16) Antibody

Histone H4, Acetylated on Lysine 16 (UniProt: P62805; also known as H4K16Ac, Histone H4 (acetyl K16), H4 histone family, member A, H4a) is encoded by the HIST1H4A (also known as H4/J, HIST1H4F, HIST1H4L, H4FN, H4FA, H4FH, HIST1H4H, H4F2, H4FM, H4/A, H4FK, H4FG, HIST2H4, HIST1H4I, H4/N, HIST1H4B) gene (Gene ID: 121504, 554313, 8294, 8359, 8360, 8361, 8362, 8363, 8364, 8365, 8366, 8367, 8368, 8370) in human. Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. Histone modifications regulate DNA transcription, repair, recombination, and replication. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which DNA is wrapped in repeating units, called nucleosomes, which limits DNA accessibility to the cellular machineries, which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Histone H4 features a main globular domain and a long N terminal tail H4 is involved with the structure of the nucleosomes of the ′beads on a string′ structure. Histone H4 are known to be acetylated on Lysine 5, 8, 12, and 16. Acetylations are important for the regulation of histone deposition, transcriptional activation, DNA replication and repair. Hyper-acetylation of the histone tails is shown to neutralize positive charge and weakens histone-DNA and nucleosome-nucleosome interactions that destabilizes chromatin structure and increases the accessibility of DNA to various DNA-binding proteins. Chromosomal aberrations involving histone H4 is a cause of B-cell non-Hodgkin lymphomas.