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Lysine acetylation is an evolutionarily conserved posttranslational modification that is found in prokaryotes and eukaryotes at histone and non-histone protein sites. Transfer of an acetyl group from acetyl-coenzyme A (acetyl-CoA) to the amino side chain of lysine is catalyzed by lysine acetyltransferases (KATs), including 13 canonical KATs from the GCN5, p300, and MYST families. Acetyl lysine removal is catalyzed by two major groups of lysine deacetylases (KDACs), the zinc-dependent histone deacetylases (HDACs) and the NAD⁺-dependent sirtuin deacetylases. Histone acetylation is associated with active gene transcription, and dysregulation of histone acetylation is associated with various diseases including cancer, Huntington''s and Alzheimer''s diseases, and amyotrophic lateral sclerosis (ALS). Non-histone protein acetylation is linked to various cellular processes including autophagy, DNA replication, lipid storage, mitochondrial fission and fusion, and protein synthesis, among others. Cayman''s Acetyl Lysine Monoclonal Antibody (Clone 7F8) can be used for ELISA, immunocytochemistry (ICC), and Western blot applications.