Recombinant Human Alcohol Dehydrogenase protein is a Human Full Length protein, in the 1 to 375 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Alcohol dehydrogenase (PubMed:2738060). Oxidizes primary as well as secondary alcohols. Ethanol is a very poor substrate (PubMed:2738060).
ADH1, ADH1A, Alcohol dehydrogenase 1A, Alcohol dehydrogenase subunit alpha
Recombinant Human Alcohol Dehydrogenase protein is a Human Full Length protein, in the 1 to 375 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab123147 was purified using conventional chromatography.
Alcohol dehydrogenase (PubMed:2738060). Oxidizes primary as well as secondary alcohols. Ethanol is a very poor substrate (PubMed:2738060).
Belongs to the zinc-containing alcohol dehydrogenase family.
Alcohol dehydrogenase (ADH) also known as aldehyde reductase is an enzyme that catalyzes the conversion of alcohols to aldehydes while reducing NAD+ to NADH. This enzyme's structure comprises approximately 40 kDa per subunit and it typically functions as a dimer. ADH is predominantly expressed in the liver where it plays a major role in alcohol metabolism. However its presence is also noted in other tissues such as the stomach lining and kidneys. The enzyme's activities are significant enough to be measured through various assays including ADH assay and alcohol dehydrogenase test highlighting its enzymatic kinetics.
Alcohol dehydrogenase's role extends beyond simple alcohol metabolism. It participates in the body's detoxification processes. This enzyme is not part of a larger complex but can function alongside other dehydrogenases involved in metabolic processes. ADH's activity helps in managing blood alcohol levels by converting ethanol to acetaldehyde which is further processed by aldehyde dehydrogenase to acetate. The balance and efficiency of these reactions determine the rate and capacity of alcohol clearance from the body.
Alcohol dehydrogenase significantly contributes to the alcohol metabolism pathway and the retinol metabolism pathway. It plays a role in converting retinol to retinal which is important for vision and cell growth. In these pathways ADH works closely with aldehyde dehydrogenase to ensure the continuation of the metabolic processes in the human body. The enzyme's function is also connected to the smooth operation of the cytochrome P450 system in the liver for comprehensive detoxification.
The activity of alcohol dehydrogenase links closely to conditions like alcoholism and liver disease. Variations in ADH enzyme activity can affect an individual's susceptibility to alcohol use disorder due to differences in alcohol metabolism rates. Additionally high acetaldehyde levels a product of the alcohol dehydrogenase reaction can contribute to liver damage leading to cirrhosis. This enzyme's relationship to aldehyde dehydrogenase is critical as the failure in converting acetaldehyde can exacerbate the toxic effects and contribute further to these disorders.
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15% SDS PAGE, 3 µg of ab123147 loaded.
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