protein

AKR1A1 Protein, Human (His)

HY-P76137

20 μg;100 μg

255;715 USD

AKR1A1 Protein, Human (His)

proteins

E. coli

20 μg;100 μg

255;715 USD

The AKR1A1 protein uses NADPH to reduce various carbonyl compounds to alcohols. AKR1A1 Protein, Human (His) is the recombinant human-derived AKR1A1 protein, expressed by E. coli , with N-His labeled tag. The total length of AKR1A1 Protein, Human (His) is 325 a.a., with molecular weight of ~39 KDa.

Human

AKR1A1, a versatile enzyme, catalyzes the NADPH-dependent reduction of a broad spectrum of carbonyl-containing compounds to their respective alcohols. Exhibiting enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides, and bile acids, AKR1A1 demonstrates a preference for negatively charged substrates like glucuronate and succinic semialdehyde. Functioning as a detoxifying enzyme, it plays a crucial role in reducing toxic aldehydes, including methylglyoxal and 3-deoxyglucosone, which accumulate under hyperglycemic conditions and exert cytotoxic effects. Additionally, AKR1A1 contributes to the detoxification of lipid-derived aldehydes, such as acrolein. The enzyme is implicated in the activation of procarcinogens, including polycyclic aromatic hydrocarbon trans-dihydrodiols, and participates in the metabolism of various xenobiotics and drugs, such as the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN). Notably, AKR1A1 does not exhibit reductase activity towards retinoids. This diverse substrate specificity underscores its pivotal role in cellular detoxification processes and its potential relevance in therapeutic interventions.

Aldo-keto reductase family 1 member A1; Aldehyde reductase; Glucuronate reductase; ALDR1; ALR

Greater than 90% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.5. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

Room temperature in continental US; may vary elsewhere.