Proteins are reversibly and dynamically acetylated on the epsilon-amino group of lysine by acetyltransferases and deacetylated by deacetylases. This post-translational modification can regulate protein function (interactions with other proteins and DNA binding). Histones and transcription factors (PCAF, p53, p300, etc) appear to be the major targets of acetytransferases. Acetylation is usually associated with chromatin remodeling and transcriptional activation, although in some cases (telomeres) it is associated with gene silencing. The 15G10 antibody recognizes acetylated lysine residues on proteins.