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Acetyl Lysine Antibody
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These tails are subject to several publish-translational covalent modifications, including acetylation, phosphorylation, ubiquitination, sumoylation and methylation (reviewed in 1 ). Methylation been discovered on a variety of lysine residues in varied histones: K4 (utilizing the single-letter amino-acid code for lysine), K9, K27, K36 and K79 in histone H3, K20 in histone H4, K59 in the globular domain of histone H4 2 and K26 of histone H1B three Several proteins accountable for the methylation of specific residues have been characterised, and all but one of these accommodates a SET area