ADH7 Antibody (C-Term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P40394 |
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Gene ID | 131 |
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Other Names | Alcohol dehydrogenase class 4 mu/sigma chain, Alcohol dehydrogenase class IV mu/sigma chain, Gastric alcohol dehydrogenase, Retinol dehydrogenase, ADH7 |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | ADH7 (HGNC:256) |
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Function | Catalyzes the NAD-dependent oxidation of all-trans-retinol, alcohol, and omega-hydroxy fatty acids and their derivatives (PubMed:15369820, PubMed:16787387, PubMed:9600267). Oxidizes preferentially all trans-retinol, all-trans-4-hydroxyretinol, 9-cis- retinol, 2-hexenol, and long chain omega-hydroxy fatty acids such as juniperic acid (PubMed:15369820, PubMed:16787387, PubMed:9600267). In vitro can also catalyzes the NADH-dependent reduction of all-trans- retinal and aldehydes and their derivatives (PubMed:15369820, PubMed:16787387, PubMed:9600267). Reduces preferentially all trans- retinal, all-trans-4-oxoretinal and hexanal (PubMed:15369820, PubMed:16787387). Catalyzes in the oxidative direction with higher efficiency (PubMed:16787387, PubMed:15369820). Therefore may participate in retinoid metabolism, fatty acid omega-oxidation, and elimination of cytotoxic aldehydes produced by lipid peroxidation (PubMed:9600267, PubMed:15369820, PubMed:16787387). |
Cellular Location | Cytoplasm. |
Tissue Location | Preferentially expressed in stomach. |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes class IV alcohol dehydrogenase 7 mu or sigma subunit, which is 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 enzyme encoded by this gene is inefficient in ethanol oxidation, but is the most active as a retinol dehydrogenase; thus it may participate in the synthesis of retinoic acid, a hormone important for cellular differentiation. The expression of this gene is much more abundant in stomach than liver, thus differing from the other known gene family members.
References
Kedishvili, N.Y., et al. J. Biol. Chem. 270(8):3625-3630(1995)Cheung, B., et al. Alcohol. Clin. Exp. Res. 19(1):185-186(1995)Farres, J., et al. Eur. J. Biochem. 224(2):549-557(1994)Pares, X., et al. FEBS Lett. 303(1):69-72(1992)
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