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| Product Name | Recombinant Human Alcohol dehydrogenase class 4 mu/sigma chain |
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| Description | 1-386aa; Full Length. MW: 45.6kD. Purity >90% as determined by SDS-PAGE. Could function in retinol oxidation for the synthesis of retinoic acid, a hormone important for cellular differentiation. Medium-chain (octanol) and aromatic (m-nitrobenzaldehyde) compounds are the best substrates. Ethanol is not a good substrate but at the high ethanol concentrations reached in the digestive tract, it plays a role in the ethanol oxidation and contributes to the first pass ethanol metabolism. |
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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 | [Alcohol dehydrogenase class IV mu/sigma chain; Gastric alcohol dehydrogenase; Retinol dehydrogenase] |
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| Gene, Accession, CAS # | ADH7, Gene ID: 131, Accession: NP_000664.2 |
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| Catalog # | MBS947896 |
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| Order / More Info | Recombinant Human Alcohol dehydrogenase class 4 mu/sigma chain from MYBIOSOURCE INC. |
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| Product Specific References | Alcohol dehydrogenase of class IV (sigma sigma-ADH) from human stomach. cDNA sequence and structure/function relationships.Farres J., Moreno A., Crosas B., Peralba J.M., Allali-Hassani A., Hjelmqvist L., Joernvall H., Pares X.Eur. J. Biochem. 224:549-557(1994) The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene.Satre M.A., Zgombic-Knight M., Duester G.J. Biol. Chem. 269:15606-15612(1994) Genomic structure and expression of the ADH7 |
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