| Description: | AKR1B1, a versatile enzyme, catalyzes the NADPH-dependent reduction of a diverse array of carbonyl-containing compounds to their respective alcohols. It exhibits enzymatic activity towards endogenous metabolites, including aromatic and aliphatic aldehydes, ketones, monosaccharides, bile acids, and xenobiotics substrates. As a key enzyme in the polyol pathway, AKR1B1 plays a critical role in hyperglycemia by catalyzing the reduction of glucose to sorbitol. The enzyme also reduces steroids and their derivatives, prostaglandins, and displays low activity toward retinals. Additionally, AKR1B1 is involved in the detoxification of dietary and lipid-derived unsaturated carbonyls, such as crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal, and their glutathione-conjugate carbonyls (GS-carbonyls). Notably, it catalyzes the reduction of various phospholipid aldehydes generated from the oxidation of phosphatidylcholine and phosphatidylethanolamides, further emphasizing its broad substrate specificity and its integral role in cellular detoxification processes. AKR1B1 Protein, Human (His) is the recombinant human-derived AKR1B1 protein, expressed by E. coli , with N-His, N-10*His labeled tag. The total length of AKR1B1 Protein, Human (His) is 316 a.a., with molecular weight of ~36 kDa. |
