Analytical Data
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Gene name
ADH4
- Application
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Alternative Names
ADH4；ADH2；All-trans-retinol dehydrogenase [NAD(+)] ADH4
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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
P08319
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Expression Region
1-380aa
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AA Sequence
MGTKGKVIKCKAAIAWEAGKPLCIEEVEVAPPKAHEVRIQIIATSLCHTD ATVIDSKFEGLAFPVIVGHEAAGIVESIGPGVTNVKPGDKVIPLYAPLCR KCKFCLSPLTNLCGKISNLKSPASDQQLMEDKTSRFTCKGKPVYHFFGTS TFSQYTVVSDINLAKIDDDANLERVCLLGCGFSTGYGAAINNAKVTPGST CAVFGLGGVGLSAVMGCKAAGASRIIGIDINSEKFVKAKALGATDCLNPR DLHKPIQEVIIELTKGGVDFALDCAGGSETMKAALDCTTAGWGSCTFIGV AAGSKGLTVFPEELIIGRTINGTFFGGWKSVDSIPKLVTDYKNKKFNLDA LVTHTLPFDKISEAFDLMNQGKSIRTILIF
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Molecular Weight
67 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
ADH4, or alcohol dehydrogenase class IV, is an enzyme primarily expressed in the human liver and gastrointestinal tract, playing a crucial role in the metabolism of alcohols and other small lipids. The research on recombinant ADH4 has gained significance due to its therapeutic potential in the treatment of alcohol use disorders and its application in biotechnological processes. Understanding the structure and function of ADH4 at a molecular level can provide insights into its role in metabolic pathways, particularly in the oxidation of ethanol. Given the increasing global alcohol consumption and its associated health risks, the development of recombinant ADH4 presents opportunities to design targeted interventions. Additionally, the enzyme has garnered interest in industrial applications, such as biocatalysis in synthetic chemistry, due to its ability to facilitate the conversion of alcohols into useful products. Thus, the study of recombinant ADH4 not only enhances our comprehension of metabolic regulation but also paves the way for innovative solutions in public health and environmental sustainability.
