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Human CROT Protein (474 Leu/Val, His Tag)

COT

Catalog Number P11015-H08B
Organism Species Human
Host Baculovirus-Insect Cells
Synonyms COT
Molecular Weight The recombinant human CROT consists of 623 amino acids and predicts a molecular mass of 71.5 kDa. The apparent molecular mass of rhCROT is approximately 65 kDa in SDS-PAGE under reducing conditions.
predicted N Met 1
SDS-PAGE
Purity > 93 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human CROT (Q9UKG9) (Met 1-Leu 612, 474 Leu/Val) was fused with a polyhistidine tag at the C-terminus.
Bio-activity
Research Area Cancer |Cancer Metabolism |Metabolic signaling |Metabolism of lipids and lipoprotein
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 Carnitine octanoyltransferase (CROT or COT), also known as octanoyl-CoA: L-carnitine O-octanoyltransferase, medium-chain/long-chain carnitine acyltransferase, and carnitine medium-chain acyltransferase, is a carnitine acyltransferase belonging to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups that catalyzes the reversible transfer of fatty acyl groups between CoA and carnitine. Carnitine octanoyltransferase (CROT or COT) facilitate the transport of medium- and long-chain fatty acids through the peroxisomal and mitochondrial membranes. It is physiologically inhibited by malonyl-CoA. COT also has functions in efficiently converting one of the end products of the peroxisomal beta-oxidation of pristanic acid, 4, 8-dimethylnonanoyl-CoA, to its corresponding carnitine ester. 
Reference
  • Ferdinandusse S, et al. (1999) Molecular cloning and expression of human carnitine octanoyltransferase: evidence for its role in the peroxisomal beta-oxidation of branched-chain fatty acids. Biochem Biophys Res Commun. 263 (1): 213-8.
  • Feike R, et al. (2000) Genomics of the Human Carnitine Acyltransferase Genes. Molecular Genetics and Metabolism. 71 (1-2): 139-53.
  • Montserrat Morillas, et al. (2002) Structural Model of a Malonyl-CoA-binding Site of Carnitine Octanoyltransferase and Carnitine Palmitoyltransferase I. The Journal of Biological Chemistry, 277: 11473-80.