Analytical Data
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Gene name
ADH
- Application
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Alternative Names
ADH；Alcohol dehydrogenase 6
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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
P41181
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Expression Region
1-271aa
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AA Sequence
MWELRSIAFSRAVFAEFLATLLFVFFGLGSALNWPQALPSVLQIAMAFGLGIGTLVQALGHISGAHINPAVTVACLVGCHVSVLRAAFYVAAQLLGAVAGAALLHEITPADIRGDLAVNALSNSTTAGQAVTVELFLTLQLVLCIFASTDERRGENPGTPALSIGFSVALGHLLGIHYTGCSMNPARSLAPAVVTGKFDDHWVFWIGPLVGAILGSLLYNYVLFPPAKSLSERLAVLKGLEPDTDWEEREVRRRQSVELHSPQSLPRGTKA
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Molecular Weight
30.3 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
ADH, or Alcohol Dehydrogenase, is a crucial enzyme involved in the metabolism of alcohol, converting ethanol into acetaldehyde, which is subsequently metabolized to less toxic substances. The significance of ADH extends beyond alcohol metabolism; it plays a vital role in the detoxification process of various xenobiotics and is implicated in several metabolic pathways. Research on recombinant ADH proteins, generated through techniques such as genetic engineering and recombinant DNA technology, has gained momentum due to their potential applications in biotechnology and pharmacology. Recombinant ADHs offer advantages over native enzymes, including improved stability, enhanced activity, and the ability to tailor their properties for specific industrial applications, such as in the production of fine chemicals, biofuels, and pharmaceuticals. Furthermore, studying the structural and functional aspects of these recombinantly produced enzymes provides valuable insights into enzyme mechanisms and interactions, which can lead to the development of novel inhibitors or drug candidates for conditions related to alcohol metabolism disorders. The progress in recombinant ADH research is supported by advances in techniques like site-directed mutagenesis, molecular docking, and high-throughput expression systems, paving the way for innovative solutions in health and industry and underscoring the importance of ADH as a focal point for scientific inquiry.
