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| Product Name | Recombinant Human Very long-chain acyl-CoA synthetase |
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| Description | 283-620aa; Cytoplasmic Domain. MW: 54.8kD. Purity >90% as determined by SDS-PAGE. Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precurors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Does not utilize C24 bile acids a |
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| Size | 0.01 mg (Yeast), 0.01 mg (E-Coli), 0.05 mg (Yeast), 0.05 mg (E-Coli), 0.1 mg (E-Coli) |
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| Concentration | n/a |
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| Applications | n/a |
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| Other Names | [Fatty acid transport protein 2; FATP-2; Fatty-acid-coenzyme A ligase, very long-chain 1; Long-chain-fatty-acid-CoA ligase (EC:6.2.1.3); Solute carrier family 27 member 2; THCA-CoA ligase; Very long-chain-fatty-acid-CoA ligase] |
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| Gene, Accession, CAS # | SLC27A2, Gene ID: 11001, Accession: NP_001153101.1 |
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| Catalog # | MBS1032322 |
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| Order / More Info | Recombinant Human Very long-chain acyl-CoA synthetase from MYBIOSOURCE INC. |
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| Product Specific References | Molecular cloning of a possible human homolog of the rat very-long-chain acyl-CoA synthetase cDNA and its chromosomal localization.Uchiyama A., Aoyama T., Kamijo K., Wakui K., Fukushima Y., Shimozawa N., Suzuki Y., Kondo N., Orii T., Hashimoto T. Human very-long-chain acyl-CoA synthetasecloning, topography, and relevance to branched-chain fatty acid metabolism.Steinberg S.J., Wang S.J., Kim D.G., Mihalik S.J., Watkins P.A.Biochem. Biophys. Res. Commun. 257:615-621(1999) Complete sequencing and c |
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