Anti-Human ACAD8 Antibody Pair

Product Description: Acyl-CoA dehydrogenase family member 8 (ACAD8) plays a critical role in the catabolism of the branched-chain amino acid valine. Structurally, ACAD8 functions as a homotetramer composed of an NH2-terminal alpha-helical domain, a medial beta-strand domain, and a C-terminal alpha-helical domain, consistent with other members of the acyl-CoA dehydrogenase family. The enzyme catalyzes the third step of valine breakdown by converting isobutyryl-CoA into methylacrylyl-CoA, contributing to cellular energy production through amino acid metabolism. Pathogenic mutations in ACAD8 cause isobutyryl-CoA dehydrogenase deficiency, a rare metabolic disorder that impairs valine catabolism. While most patients remain asymptomatic, some children with the deficiency may develop complications such as dilated cardiomyopathy and transient metabolic disturbances. Diagnosis often occurs via newborn screening, detecting elevated C4-carnitine levels indicative of disrupted valine metabolism and reduced enzyme activity. Protein Function: Isobutyryl-CoA dehydrogenase which catalyzes the conversion of 2-methylpropanoyl-CoA to (2E)-2-methylpropenoyl-CoA in the valine catabolic pathway (PubMed:11013134, PubMed:12359132, PubMed:16857760). To a lesser extent, also able to catalyze the oxidation of (2S)-2-methylbutanoyl-CoA (PubMed:11013134, PubMed:12359132) [The Uniprot Consortium]