ACADL-Specific Recombinant Rabbit mAb

ACADL, a homotetrameric flavoenzyme localized in the mitochondrial matrix, with each subunit containing one FAD cofactor. Its canonical function is to catalyze the first step of fatty acid β-oxidation, dehydrogenating long-chain acyl-CoAs to the corresponding 2,3-enoyl-CoAs and transferring electrons to electron-transferring flavoprotein (ETF) for entry into the respiratory chain. However, recent crystallographic studies have revealed that its substrate-binding cavity is exceptionally large, accommodating not only long- and medium-chain fatty acids but also bulky branched-chain substrates such as intermediates in bile acid synthesis. This suggests that its physiological roles may extend beyond conventional fatty acid oxidation, and it has been proposed that LCAD, together with ACAD10 and ACAD11, forms a distinct eukaryotic ACAD subfamily. Although homozygous LCAD deficiency is extremely rare in humans, mouse model studies indicate that its deficiency is associated with pathological conditions including cardiomyopathy, hepatic steatosis, and hypoglycemia, and the gene's function has also been linked to sudden infant death syndrome.