Chromatin is the arrangement of DNA and proteins in which chromosomes are formed. Correspondingly, chromatin is formed from nucleosomes, which are comprised of a set of four histone proteins (H2A, H2B, H3, H4) wrapped with DNA. Chromatin is a very dynamic structure in which numerous post-translational modifications work together to activate or repress the availability of DNA to be copied, transcribed, or repaired. These marks decide which DNA will be open and commonly active (euchromatin) or tightly wound to prevent access and activation (heterochromatin). Common histone modifications include methylation of lysine and arginine, acetylation of lysine, phosphorylation of threonine and serine, and sumoylation, biotinylation, and ubiquitylation of lysine. Phosphorylation of threonine 3 (H3 pT3) is a known mitotic marker and modified by the Haspin/Thr3 enzyme, while acetylation of lysine 4 (H3K4ac) on histone 3 is associated with transcriptional activation by Esa1. Methylation that occurs on H3K4 concurrently with acetylation seems to act as an adjuster to the activation effects of acetylation. Shugoshin protein cannot bind to the centromere of active cells when H3K4 is acetylated, which reduces dimethylation, and thus slows meiosis and mitosis. Usually, H3K4Ac is a transitional modification, and will become further modified with methylation as transcription progresses, indicating complex transcriptional regulation. Anti-Histone H3 are ideal for researchers interested in Chromatin Modifiers, Chromatin Research, Histones and Modified Histones, and Epigenetics research.
H3.3B, H3 histone, family 3A, H3.3AH3F3H3F3B, histone H3.3, MGC87782, MGC87783, H3pT3/K4ac
Histone H3 [ac Lys4, p Thr3] affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with synthetic acetylated/phosphorylated peptide surrounding Lysine 4 and Threonine 3 of human Histone H3.