Acetyl-Histone H2A (Lys15) Primary Antibody

In eukaryotes, DNA is wrapped around histone octamers to form the basic unit of chromatin structure. The nucleosome, made up of DNA wound around eight core histone proteins (two each of H2A, H2B, H3 and H4), is the primary building block of chromatin. Two molecules of each of the four core histones (H2A, H2B, H3 and H4) form the octamer, which is comprised of two H2A-H2B dimers and two H3-H4 dimers, creating two nearly symmetrical halves by tertiary structure. The amino-terminal tails of core histones undergo various post-translational modifications, including acetylation, phosphorylation, methylation and ubiquitination. These modifications occur in response to various stimuli and have a direct effect on the accessibility of chromatin to transcription factors and, therefore, on gene expression. In most species, histone H2B is primarily acetylated at Lys5, 12, 15 and 20. Histone H3 is primarily acetylated at Lys9, 14, 18, 23, 27 and 56. Acetylation of H3 at Lys9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms. Histone H4 may also be acetylated at Lys5, 8, 12 and 16, and the involvement of acetylated H4 with Histones H2A, H2B and H3 suggests that acetylated histones may be involved in dynamic chromatin remodeling.