Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids, with a preference for negatively charged substrates, such as glucuronate and succinic semialdehyde . Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes. Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic. Involved also in the detoxification of lipid-derived aldehydes like acrolein (By similarity). Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN) . Displays no reductase activity towards retinoids (By similarity).

AKR1A1;ALDR1; ALR; ARM; DD3; HEL-S-6

p14550

Human,Mouse,Rat

WB,IHC,FC

WB 1:2000
IHC 1:50
FC 1:100

Monoclonal

36.6 kDa

Mouse

Full length human recombinant protein of human AKR1A1 (NP_006057) produced in HEK293T cell.

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 +4°C short term. Store at -20°C long term. Avoid freeze / thaw cycle.