Acetylated Lysine (monoclonal, clone 7F8)

Protein G purified IgG2B in PBS, pH 7,4 with 0,09 % sodium azide and 50 % glycerol at concentration 1 mg/mlantibody detects Proteins containing acetylated lysine residues in ELISA and WBs, Does not detect non-acetylated lysine residues,1 µg of this antibody is sufficient to detect acetylated chicken erythrocyte histones (sodium butyrate-treated) using 20 µg total protein and ECL detection system

Post-translational modification of proteins plays a key role in the regulation and function of many known biological processes. Proteins can undergo post-translational modifications in a number of different ways, and a common post-transcriptional modification of lysine involves acetylation (1). The four core histones (H2A, H2B, H3, and H4) contain lysine that is acetylated by histone acetyltransferases (HATs) and deacetylated by histone deacetylation (hdac) (2). Reversible lysine acetylation and deacetylation after protein translation have been identified as an emerging intracellular signaling mechanism that plays a key role in regulating gene transcription, cell cycle progression, apoptosis, DNA repair, and cytoskeletal organization (3).