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Amino acids 2-374 constitute the expression domain of recombinant Human ADH5. The theoretical molecular weight of the ADH5 protein is 66.6 kDa. The ADH5 protein was expressed in e.coli. The N-terminal GST tag was fused into the coding gene segment of ADH5, making it easier to detect and purify the ADH5 recombinant protein in the later stages of expression and purification.Alcohol dehydrogenase class-3 (ADH5) is a protein involved in ethanol metabolism, with research covering multiple aspects. The primary focus lies in its role in the ethanol degradation pathway, particularly its expression and activity regulation in the liver. Scientists are committed to figuring out how ADH5 works in breaking down ethanol, with the goal of revealing its roles in diseases related to alcohol and drinking behavior. Besides, ADH5 is associated with some drug metabolism and toxicity, making it a subject of considerable interest in the fields of pharmacology and toxicology. Recent studies suggest that ADH5 may play a crucial role in certain types of cancer, making it a hot target in cancer research as well.
Amino acids 2-374 constitute the expression domain of recombinant Human ADH5. The theoretical molecular weight of the ADH5 protein is 66.6 kDa. The ADH5 protein was expressed in e.coli. The N-terminal GST tag was fused into the coding gene segment of ADH5, making it easier to detect and purify the ADH5 recombinant protein in the later stages of expression and purification.Alcohol dehydrogenase class-3 (ADH5) is a protein involved in ethanol metabolism, with research covering multiple aspects. The primary focus lies in its role in the ethanol degradation pathway, particularly its expression and activity regulation in the liver. Scientists are committed to figuring out how ADH5 works in breaking down ethanol, with the goal of revealing its roles in diseases related to alcohol and drinking behavior. Besides, ADH5 is associated with some drug metabolism and toxicity, making it a subject of considerable interest in the fields of pharmacology and toxicology. Recent studies suggest that ADH5 may play a crucial role in certain types of cancer, making it a hot target in cancer research as well.
| Cat.No | ACP04841 | Target Name | ADH5 |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 2-374aa | Mol Weight | 66.6kDa |
| Protein Length | Full Length of Mature Protein | Purity | Greater than 90% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P11766 |
|---|
Uniprot Id
P11766
Target Species
Human
Target Name
ADH5
Target Full Name
Alcohol dehydrogenase class-3
Target Function
Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione. Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate. Class-III ADH is remarkably ineffective in oxidizing ethanol.
Target Subcellular Location
Cytoplasm.
Target Protein Families
Zinc-containing alcohol dehydrogenase family, Class-III subfamily
Target Research Area
Metabolism
Target Synonyms
ADH 3; ADH5; ADHX ; ADHX_HUMAN; Alcohol dehydrogenase (class III) chi polypeptide; alcohol dehydrogenase 5 (class III) chi polypeptide; Alcohol dehydrogenase 5; Alcohol dehydrogenase class 3; Alcohol dehydrogenase class chi chain; Alcohol dehydrogenase class III ; Alcohol dehydrogenase class-3; Alcohol dehydrogenase class-III; class III alcohol dehydrogenase 5 chi subunit ; FALDH; FDH; formaldehyde dehydrogenase; Glutathione dependent formaldehyde dehydrogenase; Glutathione-dependent formaldehyde dehydrogenase; GSH-FDH; GSNOR; hydroxymethyllutathione dehydrogenase; S-(hydroxymethyl)glutathione dehydrogenase
Target Background
This gene encodes a member of the alcohol dehydrogenase family. Members of this family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. The encoded protein forms a homodimer. It has virtually no activity for ethanol oxidation, but exhibits high activity for oxidation of long-chain primary alcohols and for oxidation of S-hydroxymethyl-glutathione, a spontaneous adduct between formaldehyde and glutathione. This enzyme is an important component of cellular metabolism for the elimination of formaldehyde, a potent irritant and sensitizing agent that causes lacrymation, rhinitis, pharyngitis, and contact dermatitis. The human genome contains several non-transcribed pseudogenes related to this gene.
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