Antiacetyllysine

Antiacetyllysine antibodies are antibodies raised against N-epsilon-acetyllysine, the acetylated form of the lysine side chain. They detect protein acetylation, a reversible post-translational modification that regulates protein function and interactions. Acetylation is catalyzed by lysine acetyltransferases (KATs) and removed by deacetylases such as histone deacetylases (HDACs) and sirtuins. While first studied in histones, acetylation occurs on many cellular proteins.

Antibodies are categorized as pan-acetyllysine, which recognize the acetylated lysine moiety across different sequence contexts, or site-specific, raised against peptides containing a particular acetylated lysine (for example histone H3K9ac). Pan antibodies are useful for global assessment of acetylation, whereas site-specific antibodies enable localization to a defined residue or protein. Specificity can vary, and cross-reactivity with nonacetylated lysine or other acyl-lysine forms can occur if validation is incomplete.

Common applications include Western blotting, immunoprecipitation, immunofluorescence, immunohistochemistry, ELISA, and chromatin immunoprecipitation (ChIP) to map histone acetylation. They can also be used to enrich acetylated peptides for mass spectrometry. Validation controls include deacetylase treatment, peptide competition assays, and use of appropriate isotype or species-specific controls.

Limitations of antiacetyllysine antibodies include varying affinity, context dependence, and potential cross-reactivity. Researchers should validate antibodies for their specific species, sample type, and assay, and use complementary methods to confirm acetylation changes.