Analytical Data
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Gene name
ADH3
- Application
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Alternative Names
ADH3；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
MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAAGICRSDEHVVSGNLVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRICKNPESNYCLKNDLGNPRGTLQDGTRRFTCSGKPIHHFVGVSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVKVAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQNLSINPMLLLTGRTWKGAIFGGFKSKESVPKLVADFMAKKFSLDALITNILPFEKINEGFDLLRSGKSIRTVLTF
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Molecular Weight
66.7 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
ADH3, or alcohol dehydrogenase class III, is an enzyme that plays a crucial role in the metabolism of alcohols and aldehydes and is predominantly expressed in the liver and other tissues. Its significance extends beyond alcohol metabolism; it is also involved in the oxidation of various substrates, including retinol and fatty acids. Research on ADH3 is particularly important due to its implications in various physiological and pathological processes, including the metabolism of drugs and the development of certain diseases, such as alcoholic liver disease and cancer. ADH3 exhibits polymorphic variants, which can influence individual responses to alcohol and susceptibility to alcohol-related disorders. The development of recombinant ADH3 proteins has provided valuable tools for studying the structure-function relationships of the enzyme, its enzymatic activity, and its interactions with various substrates and inhibitors. These recombinant proteins are also useful for high-throughput screening in drug discovery and for understanding the enzyme's role in metabolic pathways. The study of ADH3 and its recombinant forms is essential for further elucidating its biological functions and therapeutic potential, thereby contributing to advancements in biochemistry, pharmacology, and personalized medicine.
