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 catalyze 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:15369820, PubMed:16787387). Therefore may participate in retinoid metabolism, fatty acid omega-oxidation, and elimination of cytotoxic aldehydes produced by lipid peroxidation (PubMed:15369820, PubMed:16787387, PubMed:9600267).

All-trans-retinol dehydrogenase [NAD(+)] ADH7 (EC 1.1.1.105) (Alcohol dehydrogenase class 4 mu/sigma chain) (EC 1.1.1.1) (Alcohol dehydrogenase class IV mu/sigma chain) (Gastric alcohol dehydrogenase) (Omega-hydroxydecanoate dehydrogenase ADH7) (EC 1.1.1.66) (Retinol dehydrogenase)
ADH7 ADH4

P40394

Human, Mouse, Rat

WB,IHC,FC

WB 1:2000
IHC 1:150
FC 1:100

41.3 kDa

Mouse

Full length human recombinant protein of human ADH7(NP_000664) produced in HEK293T cell.

Monoclonal

Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G)

PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.

Store at -20 °C. Stable for 12 months from date of receipt.