Analytical Data
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Gene name
ADH1A
- Application
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Alternative Names
ADH1A；ADH1；Alcohol dehydrogenase 1A
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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
P07327
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Expression Region
1-375aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMSTAGKVIKCKAAVLWELKKPFSIEEVEVA PPKAHEVRIKMVAVGICGTDDHVVSGTMVTPLPVILGHEAAGIVESVGEG VTTVKPGDKVIPLAIPQCGKCRICKNPESNYCLKNDVSNPQGTLQDGTSR FTCRRKPIHHFLGISTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG YGSAVNVAKVTPGSTCAVFGLGGVGLSAIMGCKAAGAARIIAVDINKDKF AKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASL LCCHEACGTSVIVGVPPDSQNLSMNPMLLLTGRTWKGAILGGFKSKECVP KLVADFMAKKFSLDALITHVLPFEKINEGFDLLHSGKSIRTILMF
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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
The study of ADH1A (Alcohol Dehydrogenase 1A) recombinant protein has garnered significant attention due to its vital role in alcohol metabolism and potential implications in various health-related areas, including alcoholism, liver disease, and metabolic disorders. ADH1A is a key enzyme in the conversion of ethanol to acetaldehyde, a critical step in alcohol detoxification, making it a significant target for understanding individual variations in alcohol tolerance and susceptibility to alcohol-related diseases. The recombinant expression of ADH1A allows researchers to obtain large quantities of the protein for in-depth functional studies, including enzymatic activity assays, structural analysis, and interaction with inhibitors or cofactors. Advances in molecular cloning and protein purification techniques have facilitated the generation of highly purified ADH1A, enabling investigations into its kinetic properties and regulation. Furthermore, studying ADH1A at the molecular level can illuminate the mechanisms underlying its polymorphisms, which are known to influence alcohol metabolism in different populations. This research can lead to better therapeutic strategies for managing alcohol-related conditions and contribute to the development of personalized medicine approaches based on genetic predisposition to alcohol's effects. Additionally, exploring the potential role of ADH1A in other metabolic pathways further emphasizes its importance in human health and disease. As our understanding of this enzyme continues to evolve, ADH1A recombinant protein serves as a crucial tool not only for basic science research but also for developing potential clinical applications that address the challenges associated with alcohol consumption and its metabolic consequences.
