Acetylation of lysine is an important reversible modification. The activities of some proteins are controlled by acetylation of lysine. Histone acetyltransferases (HATs) acetylate the conserved amino-terminal domains of the four core histones (H2A, H2B, H3 and H4) that contain lysine residues. Histone deacetylases (HDACs) remove the acetyl group from the same residue. Acetylation/deacetylation of histones results in cell signaling processes that include gene activity, cell growth, differentiation and apoptosis. In cancer and polyglutamine diseases, the regulation of protein acetylation/deacetylation is impaired. Numerous anti-cancer drugs target HDACs.
This antibody is an affinity purified rabbit polyclonal that recognizes the acetylated form of lysine. Acetylated histone, acetylated BSA, and acetylated MBP have been tested with no reaction to the non-acetylated proteins. KLH-acetylated lysine is used as the antigen, and the antibody is affinity-purified using immobilized acetylated lysine. The affinity-purified antibody is conjugated to horseradish peroxidase (HRP) via reductive amination with 2/1 molar ratio of HRP/antibody. The concentration is 250 åµg/ml.
Reported to be effective for ELISA, immunoblotting, and immunoprecipitation.
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