05646
Alcohol Dehydrogenase from equine liver
crystalline suspension in 20 mM potassium phosphate buffer, ~2 U/mg protein (~10 mg/ml)
别名:
ADH, Alcohol Dehydrogenase from horse liver, Alcohol:NAD+ oxidoreductase, HLADH
form
suspension
quality
crystalline suspension in 20 mM potassium phosphate buffer
specific activity
~2 U/mg protein (~10 mg/ml)
mol wt
Mr ~80,000
storage temp.
2-8°C
Application
Alcohol dehydrogenase breaks down potentially toxic alcohols and is involved in the biosynthesis of various metabolites. Alcohol dehydrogenase is used to study its role in alcoholism and cancer . Alcohol dehydrogenase, from horse liver, has been used to prepare proteins in order to study the specificity of retinol dehydrogenases .
Biochem/physiol Actions
Alcohol dehydrogenase facilitates the interconversion between alcohols and aldehydes or ketones. In yeast and bacteria, alcohol dehydrogenase is involved in fermentation. Genetic mutations in the alcohol dehydrogenase gene cluster many increase the risk of developing gastric cancer .
Other Notes
Sales restrictions may apply
1 U corresponds to the amount of enzyme which oxidizes 1 μmol ethanol per minute at pH 8.8 and 25 °C
法规信息
新产品
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Françoise Haeseleer et al.
The Journal of biological chemistry, 277(47), 45537-45546 (2002-09-13)
Retinoids are chromophores involved in vision, transcriptional regulation, and cellular differentiation. Members of the short chain alcohol dehydrogenase/reductase superfamily catalyze the transformation of retinol to retinal. Here, we describe the identification and properties of three enzymes from a novel subfamily
Eric J Duell et al.
Carcinogenesis, 33(2), 361-367 (2011-12-07)
Studies that have examined the association between alcohol consumption and gastric cancer (GC) risk have been inconsistent. We conducted an investigation of 29 genetic variants in alcohol metabolism loci (alcohol dehydrogenase, ADH1 gene cluster: ADH1A, ADH1B and ADH1C; ADH7 and
Liron Amir et al.
Journal of the American Chemical Society, 135(1), 70-73 (2012-12-13)
The generation of a current through interaction between bacteria and electrodes has been explored by various methods. We demonstrate the attachment of living bacteria through a surface displayed redox enzyme, alcohol dehydrogenase II. The unnatural amino acid para-azido-L-phenylalanine was incorporated
Baek-Rock Oh et al.
Journal of industrial microbiology & biotechnology, 40(2), 227-233 (2013-01-09)
Transcriptome analysis of a K. pneumoniae GEM167 mutant strain derived by irradiation with gamma rays, which exhibited high-level production of ethanol from glycerol, showed that the mutant expressed AdhE at a high level. Ethanol production decreased significantly, from 8.8 to
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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