Anti-Mono/Di/Tri-Methyl-Histone H3 (Lys79) Rabbit mAb
Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone
code”. The PTMs on histone including acetylation, methylation, phosphorylation and novel acylations directly affect the accessibility of
chromatin to transcription factors and other epigenetic regulators, altering genome stability, gene transcription, etc. Histone methylation occurs
primarily at lysine and arginine residues on the amino terminal of core histones. Methylation of histones can either increase or decrease
transcription of genes, depending on which amino acids (Lys or Arg) in the histones are methylated and how many methyl groups are attached
(mono-, di-,tri-methylation on Lys, mono-di-symmetric/asymmetric methylation on Arg).Mostly, lysine methylation occurs primarily on histone
H3 Lys4, 9, 27, 36, 79 and H4 Lys20, while Arginine methylation occurs primarily on histone H3 Arg2, 8, 17, 26 and H4 Arg3. Histone
methylases (HMTs) and histone demethylases (HDMs) are major regulating factors._x000D_
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Reference:
PTM-7435
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