Post-translational modifications of proteins play critical roles in the regulation and function of many known biological processes. Proteins can be post-translationally modified in many different ways, and a common posttranscriptional modification of Lysine involves acetylation (1). The conserved amino-terminal domains of the four core histones (H2A, H2B, H3 and H4) contain lysines that are acetylated by histone acetyltransferases (HATs) and deacetylated by histone deacetylases (HDACs) (2). Protein posttranslational reversible lysine Nε-acetylation and deacetylation have been recognized as an emerging intracellular signaling mechanism that plays critical roles in regulating gene transcription, cell-cycle progression, apoptosis, DNA repair, and cytoskeletal organization (3).

acetylated KLH

store at -20°C; avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.

AS15 3018 | anti-Acetylated Lysine, rabbit antibodiesAS10 707-100 | anti-Acetylated lysine (100 µl), mouse antibody AS15 3019 | anti-Acetylated Lysine, APL conjugated, rabbit antibodyAS15 3020 | anti-Acetylated Lysine, FITC conjugated, rabbit antibody

Secondary antibodies

protein G purified IgG2B in PBS, pH 7.4 with 0.09 % sodium azide and 50 % glycerol at concentration 1 mg/ml

antibody detects proteins containing acetylated lysine residues in ELISA and WBs. Does not detect non-acetylated lysine residues.