Human/Mouse Acetyl-CoA Carboxylase  alpha /ACACA Alexa Fluor™ Plus 488‑conjugated Antibody

ACAC-A (Acetyl-CoA carboxylase alpha/1; also ACC-1 and biotin carboxylase) is a 260-265 kDa cytoplasmic, phosphorylated biotinyl-enzyme. It is widely expressed, and found to be concentrated in hepatocytes, adipocytes and lactating mammary epithelium. It is one of two gene products (ACAC-B/beta being the other) that catalyze the formation of malonyl-CoA from acetyl-CoA. The formation of malonyl-CoA by ACAC-A is a rate-limiting step in fatty acid synthesis; malonyl-CoA formed by ACAC-B acts as a regulator of CPT-1 during fatty acidoxidation. Human ACAC-A is 2346 amino acids (aa ) in length. It contains an N-terminal acetylated Met, one ATP-Grasp domain (aa 275-466) with an embedded biotin carboxylation domain (aa 117-618), a biotinyl-binding region (aa 752-818), and a carboxyltransferase domain (aa 1698-2194). There are at least 17 utilized phosphorylation sites, and two acetylated Lys. ACAC-A exists as either a dimer or higher-order oligomer. Multiple splice variants exist. One possesses an alternative start site at Met79, a second utilizes an alternative start site 37 aa upstream of the standard site, and a third (called PIII) shows a 17 aa substitution for aa 1-75. Over aa 1185-1352, human ACAC-A shares 95% aa identity with mouse ACAC-A, and 97% aa identity with both ovine and bovine ACAC-A.