Analytical Data
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Gene name
ADH1C
- Application
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Alternative Names
ADH1C；ADH3；Alcohol dehydrogenase 1C
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P00326
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Expression Region
1-375aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSTAGK VIKCKAAVLW ELKKPFSIEE VEVAPPKAHE VRIKMVAAGI CRSDEHVVSG NLVTPLPVIL GHEAAGIVES VGEGVTTVKP GDKVIPLFTP QCGKCRICKN PESNYCLKND LGNPRGTLQD GTRRFTCSGK PIHHFVGVST FSQYTVVDEN AVAKIDAASP LEKVCLIGCG FSTGYGSAVK VAKVTPGSTC AVFGLGGVGL SVVMGCKAAG AARIIAVDIN KDKFAKAKEL GATECINPQD YKKPIQEVLK EMTDGGVDFS FEVIGRLDTM MASLLCCHEA CGTSVIVGVP PDSQNLSINP MLLLTGRTWK GAIFGGFKSK ESVPKLVADF MAKKFSLDAL ITNILPFEKI NEGFDLLRSG KSIRTVLTF
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Molecular Weight
42 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
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Protein Description
ADH1C, or alcohol dehydrogenase 1C, is an important enzyme involved in the metabolism of alcohol, converting ethanol to acetaldehyde in the liver. Variants of the ADH1C gene can influence an individual's alcohol metabolism, which in turn affects their susceptibility to alcohol-related disorders such as alcoholism and liver disease. Research on ADH1C recombinant proteins has gained traction due to the protein's role in determining alcoholic beverage preferences and variations in alcohol tolerance among different populations. Studies have shown that genetic polymorphisms in the ADH1C gene can lead to different enzyme activity levels, impacting the rate of alcohol metabolism. Understanding the biochemical properties of ADH1C and its variants through recombinant protein studies allows researchers to explore the enzyme's structure-function relationships, define its kinetic parameters, and assess how these factors contribute to individual differences in alcohol metabolism. Moreover, recombinant ADH1C can be utilized in biotechnological applications, such as the development of biosensors for alcohol detection and the design of targeted therapies for alcohol use disorders. Therefore, the study of ADH1C recombinant proteins not only provides insights into fundamental biochemical processes related to alcohol metabolism but also has potential implications for public health and therapeutic interventions.
