Acetylated-Lysine (Ac-K-100) MultiMab^®Rabbit Monoclonal Antibody mix (HRP Conjugate)#6952,Cell Signaling Technology (CST),6952

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) (1). 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 (2-6). Recent proteomic surveys suggest that acetylation of lysine residues may be a widespread and important form of post-translational protein modification that affects thousands of proteins involved in control of cell cycle and metabolism, longevity, actin polymerization, and nuclear transport (7,8). The regulation of protein acetylation status is impaired in cancer and polyglutamine diseases (9), and HDACs have become promising targets for anti-cancer drugs currently in development (10).Hassig, C.A. and Schreiber, S.L. (1997)Curr Opin Chem Biol1, 300-8.Allfrey, V.G. et al. (1964)Proc Natl Acad Sci USA51, 786-94.Liu, L. et al. (1999)Mol Cell Biol19, 1202-9.Boyes, J. et al. (1998)Nature396, 594-8.Polevoda, B. and Sherman, F. (2002)Genome Biol3, reviews 0006.Yoshida, M. et al. (2003)Prog Cell Cycle Res5, 269-78.Kim, S.C. et al. (2006)Mol Cell23, 607-18.Choudhary, C. et al. (2009)Science325, 834-40.Hughes, R.E. (2002)Curr Biol12, R141-3.Vigushin, D.M. and Coombes, R.C. (2004)Curr Cancer Drug Targets4, 205-18.