Technical Data

A1331-07C
Clone Type
Polyclonal
Host
Goat
Source
Human
Isotype
IgG
Grade
Affinity Purified
Applications
E
Crossreactivity
Hu Mo
Accession #
NP_000664.2
Gene ID
131
Shipping Temp
Blue Ice
Storage Temp
-20°C
Goat Anti-ADH7 (Alcohol Dehydrogenase Class 4 mu/sigma Chain, Alcohol Dehydrogenase Class IV mu/sigma Chain, Gastric Alcohol Dehydrogenase, Retinol Dehydrogenase)

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.

Applications
Suitable for use in ELISA. Other applications not tested.
Recommended Dilution
ELISA: 1:32,000 Optimal dilutions to be determined by the researcher.
Storage and Stability
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Immunogen
Synthetic peptide corresponding to CISPKDSTKPISE, from ADH7, at the internal region of the protein (NP_000664.2).
Form
Supplied as a liquid in Tris saline, 0.02% sodium azide, pH 7.3, 0.5% BSA.
Purity
Purified by immunoaffinity chromatography.
Specificity
Recognizes ADH7. Species sequence homology: Human and mouse.

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.

References
1. Zgombic-Knight M, Foglio MH, Duester G. Genomic structure and expression of the ADH7 gene encoding human class IV alcohol dehydrogenase, the form most efficient for retinol metabolism in vitro. J Biol Chem. 1995 Mar 3;270(9):4305-11.
USBio References
No references available
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