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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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
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
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
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
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
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