Analytical Data
-
Gene name
ADH1
- Application
-
Alternative Names
ADH1；ADH1；Alcohol dehydrogenase 1A
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P07327
-
Expression Region
2-375aa
-
AA Sequence
STAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAVGICGTD DHVVSGTMVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLAIPQCGK CRICKNPESN YCLKNDVSNP QGTLQDGTSR FTCRRKPIHH FLGISTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVNVAKV TPGSTCAVFG LGGVGLSAIM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ NLSMNPMLLL TGRTWKGAIL GGFKSKECVP KLVADFMAKK FSLDALITHV LPFEKINEGF DLLHSGKSIR TILMF
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
ADH1 (Alcohol Dehydrogenase 1) is an enzyme primarily involved in the oxidative metabolism of alcohol in the human liver, playing a crucial role in alcohol detoxification. Its research background is rooted in the understanding of alcohol-related disorders and metabolism. Variability in ADH1 gene expression and protein activity among individuals can significantly influence alcohol clearance and susceptibility to alcohol-related diseases, such as alcoholic liver disease and various forms of cancer. Furthermore, ADH1 is of particular interest in biochemical and pharmacological studies since its activity affects the pharmacokinetics of drugs that are metabolized by alcohol dehydrogenases. Recent studies have focused on recombinant ADH1 proteins to unravel the enzyme's kinetic properties, substrate specificity, and structural dynamics. The ability to produce ADH1 as a recombinant protein enables researchers to explore its enzymatic functions in detail, develop potential therapeutic applications, and assess its role in personalized medicine. Additionally, advancements in recombinant DNA technology have opened avenues for engineering ADH1 variants with enhanced stability and activity, which could have implications in biotechnological applications such as bioremediation and biofuel production. Overall, the study of recombinant ADH1 proteins not only contributes to our understanding of alcohol metabolism but also holds promise for innovative therapeutic strategies and industrial applications.
