Aldose-reductase Protein, Human (His)

The Aldose-reductase protein reduces carbonyl-containing compounds to alcohols, including retinals. It detoxifies unsaturated carbonyls like crotonaldehyde and 4-hydroxynonenal, but lacks reductase activity towards glucose. Aldose-reductase Protein, Human (His) is the recombinant human-derived Aldose-reductase protein, expressed by E. coli , with N-6*His labeled tag. The total length of Aldose-reductase Protein, Human (His) is 316 a.a., .

Aldose reductase, a multifunctional enzyme, catalyzes the NADPH-dependent reduction of a diverse range of carbonyl-containing compounds, converting them into their corresponding alcohols. Notably, it exhibits robust enzymatic activity towards various retinal isomers, including all-trans-retinal, 9-cis-retinal, and 13-cis-retinal. The enzyme plays a pivotal role in the detoxification of unsaturated carbonyls derived from the diet and lipids, such as crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal, and their glutathione-conjugates carbonyls (GS-carbonyls). Remarkably, despite its broad substrate specificity, Aldose reductase does not display reductase activity towards glucose. This diverse catalytic repertoire highlights its significance in cellular detoxification processes and underscores its potential therapeutic implications in addressing oxidative stress-related conditions.

Human

E. coli

N-6*His

O60218 (M1-Y316)

57016

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.