Anti-Acetyl CoA Carboxylase 1 Antibody, clone 7H4.2 clone 7H4.2, from mouse

Acetyl-CoA carboxylase 1 (UniProt: Q13085; also known as ACC1, ACC-alpha) is encoded by the ACACA (also known as ACAC, ACC1, ACCA) gene (Gene ID: 31) in human. It catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. ACC1 is a multi-subunit, biotin-dependent enzyme that catalyzes carboxylation of acetyl-CoA to produce malonyl-CoA through its two catalytic activities, biotin carboxylase (BC) and carboxyltransferase (CT). The activity of ACC can be controlled at the transcriptional level as well as by small molecule modulators and covalent modification. Two isoforms fof ACC have been reported, alpha and beta that are encoded by two different genes. ACC-alpha is highly enriched in lipogenic tissues. ACC1 levels are regulated under long term control at the transcriptional and translational levels and under short term regulation by the phosphorylation/dephosphorylation of targeted serine residues and by allosteric transformation by citrate or palmitoyl-CoA. ACC1 activity is inhibited upon phosphorylation, which occurs when glucagon or epinephrine binds to the receptors or when the energy status of the cell is low, leading to the activation of the AMP-activated protein kinase. The presence of fatty acids inhibits the activities of ACC1. ACC is considered as an important target in the design of new anti-obesity drugs.