ADH5 Antibody - N-terminal region
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB |
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Primary Accession | P11766 |
Other Accession | NP_000662 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 41kDa |
Gene ID | 128 |
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Alias Symbol | ADH5, ADHX, FDH, |
Other Names | Alcohol dehydrogenase class-3, 1.1.1.1, Alcohol dehydrogenase 5, Alcohol dehydrogenase class chi chain, Alcohol dehydrogenase class-III, Glutathione-dependent formaldehyde dehydrogenase, FALDH, FDH, GSH-FDH, 1.1.1.-, S-(hydroxymethyl)glutathione dehydrogenase, 1.1.1.284, ADH5 (HGNC:253), ADHX, FDH |
Format | Liquid. Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose. |
Reconstitution & Storage | Add 50 &mu, l of distilled water. Final Anti-ADH5 antibody concentration is 1 mg/ml in PBS buffer with 2% sucrose. For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles. |
Precautions | ADH5 Antibody - N-terminal region is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | ADH5 (HGNC:253) |
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Synonyms | ADHX, FDH |
Function | Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione (PubMed:8460164). 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 (PubMed:16081420). Class-III ADH is remarkably ineffective in oxidizing ethanol (PubMed:8460164). Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage (PubMed:33355142). Also acts as a S-nitroso-glutathione reductase by catalyzing the NADH-dependent reduction of S- nitrosoglutathione, thereby regulating protein S-nitrosylation (By similarity). |
Cellular Location | Cytoplasm. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione.
References
Sharma C.P.,et al.Biochem. Biophys. Res. Commun. 164:631-637(1989).
Giri P.R.,et al.Biochem. Biophys. Res. Commun. 164:453-460(1989).
Hur M.W.,et al.Gene 121:305-311(1992).
Halleck A.,et al.Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
Kalnine N.,et al.Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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