Acetyl Lys proteins Polyclonal Antibody

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.