Analytical Data
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Gene name
ADHFE1
- Application
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Alternative Names
ADH8; ADHFE 1; ADHFe1; Alcohol dehydrogenase iron-containing Protein 1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8IWW8
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Expression Region
1-419aa
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AA Sequence
MAVSNIRYGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCKAANLYASSPHSDFLDYVSAPIGKGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLPYHLRSPCPSNPITRPAYQGSNPISDIWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMYKAKDYNVDHPLVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKLAPRPQSEEDLAALFEASMKLY
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Molecular Weight
71.6 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
ADHFE1, or alcohol dehydrogenase class IV, is an enzyme that plays a critical role in the metabolism of alcohols and other aldehydes in humans and various organisms. It is particularly interesting due to its involvement in detoxification processes and its potential connections to conditions such as alcohol-related liver disease and metabolic disorders. Research on ADHFE1 has gained traction as scientists seek to understand its structure, function, and the regulatory mechanisms governing its expression. Given its dual role in both alcohol metabolism and oxidative stress response, the study of ADHFE1 can provide insights into complex biological pathways and their implications for health and disease. The recombinant expression of ADHFE1 allows for detailed biochemical studies, facilitating the exploration of its enzymatic properties and interactions with potential inhibitors or activators. By utilizing advanced techniques in protein engineering and molecular biology, researchers aim to uncover the physiological significance of ADHFE1, contributing to the development of targeted therapies for disorders associated with alcohol metabolism and oxidative damage. This research not only enhances our understanding of ADHFE1 itself but also opens avenues for exploring its potential in biotechnological applications, including bioremediation and the production of biofuels. Overall, the study of recombinant ADHFE1 represents a promising field of investigation with significant implications for both human health and environmental sustainability.
