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Human Isovaleryl-CoA dehydrogenase / IVD Protein (aa 30-423, His Tag)

ACAD2

Catalog Number P14206-H07B
Organism Species Human
Host Baculovirus-Insect Cells
Synonyms ACAD2
Molecular Weight The recombinant human IVD consists of 412 amino acids and has a calculated molecular mass of 45.3 kDa. The recombinant protein migrates as an approximately 43 kDa band in SDS-PAGE under reducing conditions.
predicted N His
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human IVD (AAH17202.1) (His30-His423) was fused with a polyhistide tag at the N-terminus.
Bio-activity
Research Area Neuroscience |Neurotransmitter |Amino Acids
Formulation Lyophilized from sterile 50mM Tris, 100mM Nacl, pH 8.0, 10% glycerol
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Isovaleryl-CoA dehydrogenase, also known as IVD, plays an essential role in processing proteins obtained from the diet. The body breaks down proteins from food into smaller parts called amino acids. Amino acids can be further processed to provide energy for growth and development. Isovaleryl-CoA dehydrogenase helps process a particular amino acid called leucine. Specifically, isovaleryl-CoA dehydrogenase is responsible for the third step in the breakdown of leucine. This step is a chemical reaction that converts a molecule called isovaleryl-CoA to another molecule, 3-methylcrotonyl-CoA. Additional chemical reactions convert 3-methylcrotonyl-CoA into molecules that are used for energy.
Reference
  • BACHHAWAT BK, et al. (1956) Enzymatic carboxylation of beta-hydroxyisovaleryl coenzyme A. J Biol Chem. 219(2):539-50.
  • Ikeda Y, et al. (1983) Purification and characterization of isovaleryl coenzyme A dehydrogenase from rat liver mitochondria. J Biol Chem. 258(2):1077-85.
  • Tanaka K, et al. (1966) Enzymatic carboxylation of beta-hydroxyisovaleryl coenzyme A. J Biol Chem. 219(2):539-50.