Analytical Data
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Gene name
ADH1B
- Application
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Alternative Names
Alcohol dehydrogenase subunit beta
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P00325
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Expression Region
2-375aa
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Molecular Weight
55.7 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
ADH1B, or alcohol dehydrogenase class I beta, is an important enzyme involved in the metabolism of ethanol and other substrates in the liver. Variants of the ADH1B gene, particularly the ADH1B*2 allele, have been associated with variations in alcohol metabolism and susceptibility to alcohol-related disorders. Research has shown that individuals carrying the ADH1B*2 variant experience a higher rate of ethanol oxidation, leading to increased levels of acetaldehyde, a toxic byproduct of alcohol metabolism. This heightened metabolic response appears to protect these individuals from the effects of excessive alcohol consumption, thereby reducing the incidence of alcohol dependence and related health issues. Studies on recombinant ADH1B proteins facilitate the exploration of the enzyme's kinetic properties and mechanisms of action, allowing researchers to understand the structural and functional basis of its activity. These insights have implications not only for alcohol metabolism but also for drug metabolism and the development of therapeutic strategies targeting alcohol use disorders. Understanding the role of ADH1B in different populations can provide valuable data for personalized medicine approaches, where genetic factors can inform treatment decisions and risk assessments for alcohol-related conditions. Consequently, the study of ADH1B recombinant proteins has become a critical focus in biochemistry, pharmacology, and public health research.
