Analytical Data
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Gene name
ADH5
- Application
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Alternative Names
ADH5；ADHX；FDH；Alcohol dehydrogenase class-3
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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
P11766
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Expression Region
1-374aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMANEVI KCKAAVAWEA GKPLSIEEIE VAPPKAHEVR IKIIATAVCH TDAYTLSGAD PEGCFPVILG HEGAGIVESV GEGVTKLKAG DTVIPLYIPQ CGECKFCLNP KTNLCQKIRV TQGKGLMPDG TSRFTCKGKT ILHYMGTSTF SEYTVVADIS VAKIDPLAPL DKVCLLGCGI STGYGAAVNT AKLEPGSVCA VFGLGGVGLA VIMGCKVAGA SRIIGVDINK DKFARAKEFG ATECINPQDF SKPIQEVLIE MTDGGVDYSF ECIGNVKVMR AALEACHKGW GVSVVVGVAA SGEEIATRPF QLVTGRTWKG TAFGGWKSVE SVPKLVSEYM SKKIKVDEFV THNLSFDEIN KAFELMHSGK SIRTVVKI
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Molecular Weight
42 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
ADH5, also known as alcohol dehydrogenase class III, is an important enzyme in the metabolic pathway of alcohol and aldehydes, playing a pivotal role in the oxidation of various alcohols. Research into ADH5 recombinant proteins has garnered attention due to their potential applications in biocatalysis, drug metabolism, and understanding genetic variations in alcohol metabolism among different populations. The study of ADH5 is particularly significant given its involvement in the metabolism of ethanol and other substances, which can influence susceptibility to alcohol-related disorders, including alcoholism and hangover effects. Additionally, ADH5 exhibits a unique substrate specificity, enabling it to catalyze the oxidation of a wider range of alcohols compared to other alcohol dehydrogenases. This characteristic makes ADH5 a valuable candidate for biotechnological applications, such as in the synthesis of fine chemicals or in the development of biosensors. Furthermore, research into the structure and function of recombinant ADH5 has implications for drug development, as it is implicated in the metabolism of certain medications. The study of ADH5 and its recombinant forms thus not only contributes to our understanding of alcohol metabolism but also supports advancements in fields like pharmacology, toxicology, and metabolic engineering. Understanding the recombinant protein's enzymatic properties can lead to enhanced applications in metabolic engineering and therapeutic interventions, emphasizing the significance of ongoing research in this area.
