Synthesized acetyl-peptide derived from human acetylation Lys proteins.

Acetyl-Lys proteins Polyclonal Antibody detects endogenous levels of acetylated Lys proteins.

Acetylation of lysine , like phosphorylation of serine , threonine or tyrosine , is an important reversible modification controlling protein activity. The conserved amino-terminal domains of the four core histones (H2A , H2B , H3 , and H4) contain lysines that are acetylated by histone acetyltransferases (HATs) and deacetylated by histone deacetylases (HDACs) . Signaling resulting in acetylation/deacetylation of histones , transcription factors , and other proteins affects a diverse array of cellular processes including chromatin structure and gene activity , cell growth , differentiation , and apoptosis. Recent proteomic surveys suggest that acetylation of lysine residues may be a widespread and important form of posttranslational protein modification that affects thousands of proteins involved in control of cell cycle and metabolism , longevity , actin polymerization , and nuclear transport. The regulation of protein acetylation status is impaired in cancer and polyglutamine diseases , and HDACs have become promising targets for anti-cancer drugs currently in development.