A2529
Alcohol dehydrogenase–Agarose from baker′s yeast (S. cerevisiae)
lyophilized powder
Synonym(s):
ADH, Alcohol:NAD+ oxidoreductase
form
lyophilized powder
contains
citrate as stabilizer
lactose as stabilizer
storage temp.
−20°C
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Application
Alcohol dehydrogenase may be used to synthesize enantiomerically pure stereoisomers of chiral alcohols. It may be used to study ethanol fuel cells, alcoholism and drug dependence . Product A2529 is from S. Cerevisiae and is an insoluble enzyme with endless applications.
Biochem/physiol Actions
Sigma insoluble enzymes are produced by reacting a soluble enzyme with an inert base. This produces an insoluble compound with the activity of the original enzyme. Alcohol dehydrogenase has broad substrate specificity for alcohols, ketones and acetaldehyde.
Other Notes
One unit will convert 1.0 μmole of ethanol to acetaldehyde per min at pH 8.8 at 25 °C.
Storage Class Code
13 - Non Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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L S al-Kassim et al.
Biochemistry and cell biology = Biochimie et biologie cellulaire, 68(6), 907-913 (1990-06-01)
Alcohol dehydrogenase has been purified from the cell-free preparation of Thermoanaerobium brockii to homogeneity, employing combined DEAE, Sephadex, and affinity chromatographic procedures. The enzyme is tetrameric having subunit molecular weight of 40.4 x 10(3). The purified alcohol dehydrogenase is capable
Kate M Ehrensberger et al.
The Journal of biological chemistry, 288(2), 759-769 (2012-12-12)
In yeast, Adh1 (alcohol dehydrogenase 1) is an abundant zinc-binding protein that is required for the conversion of acetaldehyde to ethanol. Through transcriptome profiling of the Schizosaccharomyces pombe genome, we identified a natural antisense transcript at the adh1 locus that
Xingxing Diao et al.
Drug metabolism and disposition: the biological fate of chemicals, 41(2), 430-444 (2012-11-22)
3-n-Butylphthalide (NBP) is a cardiovascular drug currently used for the treatment of cerebral ischemia. The present study aims to investigate the metabolism, pharmacokinetics, and excretion of NBP in humans and identify the enzymes responsible for the formation of major metabolites.
Nathan C Contino et al.
Journal of the American Society for Mass Spectrometry, 24(1), 101-108 (2012-12-01)
Charge detection mass spectrometry (CDMS) measurements have been performed for cytochrome c and alcohol dehydrogenase (ADH) monomer using a modified cone trap incorporating a cryogenically cooled JFET. Cooling the JFET increases its transconductance and lowers thermal noise, improving the signal
Shuo Zhou et al.
Biotechnology letters, 35(3), 359-365 (2012-11-20)
The gene encoding a novel short-chain alcohol dehydrogenase in the thermophilic bacterium, Carboxydothermus hydrogenoformans, was identified and overexpressed in Escherichia coli. The enzyme was thermally stable and displayed the highest activity at 70 °C and pH 6.0. It preferred NAD(H) over
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