BATF ELISA Kits

Bile acid-CoA:amino acid N-acyltransferase (BAT, also known as BACAT) catalyzes the conjugation of bile acids to glycine and taurine for excretion into bile. The protein encoded by this gene is a liver enzyme that catalyzes the transfer of C24 bile acids from the acyl-CoA thioester to either glycine or taurine, the second step in the formation of bile acid-amino acid conjugates. The bile acid conjugates then act as a detergent in the gastrointestinal tract, which enhances lipid and fat-soluble vitamin absorption. Defects in this gene are a cause of familial hypercholanemia (FHCA). Tissue expression studies showed strong expression of BAT in liver, gallbladder, and the proximal and distal intestine. However, BAT is also expressed in a variety of tissues unrelated to bile acid formation and transport, suggesting important functions also in the regulation of intracellular levels of very long-chain fatty acids. Green fluorescent protein localization experiments in human skin fibroblasts showed that the hBACAT enzyme is mainly cytosolic. The cytosolic BAT enzyme may play important roles in protection against toxicity by accumulation of unconjugated bile acids and non-esterified very long-chain fatty acids.

Cholate-CoA ligase (CCL) and bile acid-CoA: amino acid N-acyltransferase (BAT) sequentially mediate bile-acid amidation. A study assessed potential clinical utility of immunostaining of liver for CCL and BAT. A study used commercially available antibodies against BAT and CCL, a study immunostained liver from an infant with jaundice, deficiency of amidated bile acids and transcription-terminating mutation in BAAT. CCL was normally expressed and BAT expression was not detected. Therefore, the study shows that immunostaining may facilitate diagnosis in bile-acid amidation defects.