"ADH4" Related Products


Recombinant Human ADH4, GST-tagged

Cat.No.: ADH4-9419H
Product Overview: Recombinant Human ADH4 protein, fused to GST-tag, was expressed in E.coli and purified by GSH-sepharose.
Description: This gene encodes class II alcohol dehydrogenase 4 pi subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Class II alcohol dehydrogenase is a homodimer composed of 2 pi subunits. It exhibits a high activity for oxidation of long-chain aliphatic alcohols and aromatic alcohols and is less sensitive to pyrazole. This gene is localized to chromosome 4 in the cluster of alcohol dehydrogenase genes.
Source: E.coli
Species: Human
Tag: GST
Protein length: 1-380a.a.
Storage: The protein is stored in PBS buffer at -20℃. Avoid repeated freezing and thawing cycles.
Storage Buffer: 1M PBS (58mM Na2HPO4,17mM NaH2PO4, 68mM NaCl, pH8. ) added with 100mM GSH and 1% Triton X-100,15%glycerol.
Gene Name: ADH4 alcohol dehydrogenase 4 (class II), pi polypeptide [ Homo sapiens ]
Official Symbol: ADH4
Synonyms: ADH4; alcohol dehydrogenase 4 (class II), pi polypeptide; alcohol dehydrogenase 4; ADH 2; aldehyde reductase; alcohol dehydrogenase class II pi chain; ADH-2;
Gene ID: 127
mRNA Refseq: NM_000670
Protein Refseq: NP_000661
MIM: 103740
UniProt ID: P08319
Chromosome Location: 4q22
Pathway: Biological oxidations, organism-specific biosystem; Drug metabolism - cytochrome P450, organism-specific biosystem; Drug metabolism - cytochrome P450, conserved biosystem; Ethanol oxidation, organism-specific biosystem; Fatty Acid Omega Oxidation, organism-specific biosystem; Fatty acid metabolism, organism-specific biosystem; Fatty acid metabolism, conserved biosystem;
Function: NAD binding; NADPH:quinone reductase activity; alcohol dehydrogenase (NAD) activity; alcohol dehydrogenase activity, zinc-dependent; alditol:NADP+ 1-oxidoreductase activity; all-trans retinal binding; benzaldehyde dehydrogenase activity; metal ion binding

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