Based on our superior High-Affi™ technology, Creative Biolabs provides pan acetylation and site-specific acetylation antibodies, which are valuable tools to detect, validate, and quantify protein acetylation.
Acetylation is one of the common post-translational modifications in cells. This chemical reaction is usually added an acetyl chemical group (CH3C=O, sometimes abbreviated in chemical structures as Ac) supplied by acetylcoenzyme A either on various amino N-terminal residues or the ε-amino group of lysine residues.
N-terminal acetylation is evolutionarily conserved modification that occurs not only on the bulk of eukaryotic proteins and regulatory peptides but also on the part of prokaryotic proteins. It is catalyzed by various N-terminal acetyltransferases (NATs), and the modification process is considered to be irreversible. Although around 80-90% proteins generate N-terminal acetylation, and several molecular processes have been described, the whole concepts of its physiological role are still unknown. Existing studies show that N-terminal acetylation can affect protein folding, subcellular localization, protein-protein interactions, and manifold cell functions.
In contrast to N-terminal acetylation, lysine acetylation is reversible and tightly regulated post-translational modification. It can occur at different positions on a variety of proteins. Histone (H2A, H2B, H3, and H4) acetylation of lysine residues within proteins is an important mechanism for chromatin decondensation and plays a central role in the regulation of chromatin structure, function, and dynamics. In addition to modifying on histone lysines, acetylation also takes place on transcription factors, molecular chaperones, effector proteins, and cytoskeletal proteins. With the dynamic regulating by lysine acetyltransferases (KATs) and lysine deacetylases (KDACs), lysine acetylation can influence several cellular pathways, like metabolic regulation, energy homeostasis, and gene expression. For instance, the acetylation of p53 is indispensable for its activation. The acetylation level of p53 will significantly increase when cell undergo stress and cause the suppression of cell growth. Dysfunctions in protein acetylation are associated with a variety of common diseases including cancer, diabetes mellitus, neurodegenerative diseases, and autoimmunity. Therefore, the acetylation regulation on human diseases related proteins has a potential for the development of therapy.
As one of the major PTMs, acetylation can make cross-talk with phosphorylation, glycosylation, methylation, ubiquitination and other modifications to regulate cellular processes together.
Creative Biolabs has developed a highly specific and high-quality antibody set for acetylation sites. Antibodies are produced by phage display platform with a synthetic acetylated amino acid (e.g. lysine) containing peptide. Acetyl-specific antibodies purified by protein A and peptide affinity chromatography with multiple applications will be delivered to customers.
In addition to the acetylation-specific antibody, Creative Biolabs also provides a comprehensive list of PTM-specific antibody production services of your choice.