ACAD8 Human

ACAD8 is a mitochondrial enzyme that is involved in the catabolism of the branched-chain amino acid valine. It specifically catalyzes the conversion of 2-methylpropanoyl-CoA to (2E)-2-methylpropenoyl-CoA in the valine catabolic pathway . To a lesser extent, it can also catalyze the oxidation of (2S)-2-methylbutanoyl-CoA .

The human recombinant form of ACAD8 is produced in Escherichia coli and is a single, non-glycosylated polypeptide chain containing 416 amino acids (23-415) with a molecular mass of 45.1 kDa . It is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques .

• Source: Escherichia coli
• Molecular Mass: 45.1 kDa
• Amino Acid Sequence: Contains 416 amino acids (23-415)
• Purity: Greater than 95% as determined by SDS-PAGE
• Formulation: The ACAD8 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT, and 30% glycerol

ACAD8 should be stored at 4°C if the entire vial will be used within 2-4 weeks. For longer periods, it should be stored frozen at -20°C. For long-term storage, it is recommended to add a carrier protein (0.1% HSA or BSA) and avoid multiple freeze-thaw cycles .

Defects in the ACAD8 gene are associated with isobutyryl-CoA dehydrogenase deficiency, a metabolic disorder that affects the catabolism of valine . This deficiency can lead to a buildup of isobutyryl-CoA and related metabolites, which can cause various clinical symptoms.

The human recombinant form of ACAD8 is used in various research applications to study its role in fatty acid and amino acid metabolism. It is also used to investigate the molecular mechanisms underlying isobutyryl-CoA dehydrogenase deficiency and to develop potential therapeutic interventions.