Purified Protein

The antibody detects endogenous Acetyl Lysine protein.

Monoclonal, Mouse

PBS, pH 7.4, containing 0.5%BSA, 0.02% sodium azide as Preservative and 50% Glycerol.

WB: 1:1000-2000 IHC: 1:200-500 IP 1:100-200. IF 1:50-200

The antibody was affinity-purified from mouse ascites by affinity-chromatography using epitope-specific immunogen.

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.

Acetyl Lysine

-20°C/1 year