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Enzymes for Research, Diagnostic and Industrial Use

Alcohol dehydrogenase from E. coli, Recombinant

Cat No.
NATE-0803
Description
Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+.
Abbr
ADH, Recombinant (E. coli)
Alias
ADH
Source
E. coli
Applications
High purity recombinant Alcohol dehydrogenase (E. coli) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
Form
In 3.2 M ammonium sulphate
Enzyme Commission Number
EC 1.1.1.1
Activity
6.7 U/mg protein at pH 8.5 and 25°C.
CAS No.
9031-72-5
Molecular Weight
~ 38,642 Da
Isoelectric point
~ 6.6
Unit Definition
One Unit of alcohol dehydrogenase is defined as the amount of enzyme required to produce one µmole of NADH from NAD+.
Optimum pH
8.5
Optimum temperature
25°C
Storage
Store at 4°C. Do not store the enzyme in presence of sodium azide.
Preparation Instructions
For assay, this enzyme should be diluted in 1 mg/ml BSA. Swirl to mix the enzyme suspension immediately prior to use.
Synonyms
aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1
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