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.

The Abbkine Acetyl Lysine Mouse Monoclonal Antibody was affinity-purified from mouse ascites by affinity-chromatography using epitope-specific immunogen and detects endogenous Acetyl Lysine protein. The antibody has been validaed in WB, IHC-P and reacts with all samples.

Abbkine supplies below price/size: $100/30μl, $220/100μl, $360/200μl of Mouse Anti-Acetyl Lysine Monoclonal Antibody at https://www.abbkine.com/product/acetyl-lysine-monoclonal-antibody-abm40200.

Abbkine Scientific Co., Ltd. was founded by a number of scientists and marketing experts in the field of life science in California in 2012. With growing demands from Asia Pacific, it move its headquarters to China. Combining cutting edge technology from United States with China's manufacturing engineering and cost advantages, we aim to provide innovative, high quality assay kits, recombinant proteins, antibodies and other research tools to accelerate life science fundamental research, drug discovery, etc.