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Biological Description
| Specificity | Alcohol Dehydrogenase Rabbit mAb detects endogenous levels of total alcohol dehydrogenase protein. |
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| Background | Alcohol dehydrogenase (ADH), is the constitutive enzyme which are a family of NAD(P)H-dependent oxidoreductases that catalyze the reversible conversion of alcohols to aldehydes or ketones, and vice versa. Structurally, ADHs typically exist as dimers or tetramers with a conserved zinc-binding catalytic domain and a Rossmann-fold domain for nucleotide (NAD⁺/NADP⁺) binding. They are widely expressed in microorganisms, plants, and animals, with multiple isoenzymes in humans showing tissue-specific expression, particularly in the liver where they play a central role in ethanol metabolism. Functionally, ADHs are essential for detoxification, energy metabolism, and biosynthesis of various compounds, and they are extensively exploited in biotechnology for the stereoselective synthesis of chiral alcohols. |
Usage Information
| Application | WB, IHC, IF | Dilution |
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| Reactivity | Human, Mouse, Rat | ||||||||
| Source | Rabbit | MW | 40 kDa | ||||||
| Storage Buffer | PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3 | Storage (from the date of receipt) |
-20°C (avoid freeze-thaw cycles), 2 years | ||||||
References
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