CROT Protein (His Tag)

Carnitine O-octanoyltransferase Protein Datasheet

CROT Protein Product Information

• Synonym: COT
• 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.
• Source: Human
• Expression Host: Baculovirus-Insect cells

CROT Protein QC Testing

• Purity: > 93% as determined by SDS-PAGE.
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Met 1
• Molecular Mass: 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.
• Formulation: Lyophilized from 0.2μm filtered solution of 50mM Tris, 100mM NaCl, pH 8.0, 10%glycerol
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: CROT protein

CROT Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

CROT Protein Description

Carnitine octanoyltransferase (CROT or COT) is a carnitine acyltransferase 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.

References

1. Ferdinandusse S. et al., 1999, Biochem Biophys Res Commun. 263 (1): 213-8.
2. Feike R. et al., 2000, Molecular Genetics and Metabolism. 71 (1-2):1 39-53.
3. Montserrat Morillas. et al., 2002, The Journal of Biological Chemistry. 277: 11473-80.