| Description: | 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. Aldose-reductase Protein, Human is the recombinant human-derived Aldose-reductase protein, expressed by E. coli , with tag free. The total length of Aldose-reductase Protein, Human is 316 a.a., . |
