Recombinant Human AKR1A1 protein is a Human Full Length protein, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
M A A S C V L L H T G Q K M P L I G L G T W K S E P G Q V K A A V K Y A L S V G Y R H I D C A A I Y G N E P E I G E A L K E D V G P G K A V P R E E L F V T S K L W N T K H H P E D V E P A L R K T L A D L Q L E Y L D L Y L M H W P Y A F E R G D N P F P K N A D G T I C Y D S T H Y K E T W K A L E A L V A K G L V Q A L G L S N F N S R Q I D D I L S V A S V R P A V L Q V E C H P Y L A Q N E L I A H C Q A R G L E V T A Y S P L G S S D R A W R D P D E P V L L E E P V V L A L A E K Y G R S P A Q I L L R W Q V Q R K V I C I P K S I T P S R I L Q N I K V F D F T F S P E E M K Q L N A L N K N W R Y I V P M L T V D G K R V P R D A G H P L Y P F N D P Y
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols (PubMed:10510318, PubMed:30538128). 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 (PubMed:10510318, PubMed:30538128). Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes (By similarity). Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic (By similarity). 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) (PubMed:11306097, PubMed:18276838). Also acts as an inhibitor of protein S-nitrosylation by mediating degradation of S-nitroso-coenzyme A (S-nitroso-CoA), a cofactor required to S-nitrosylate proteins (PubMed:30538128). S-nitroso-CoA reductase activity is involved in reprogramming intermediary metabolism in renal proximal tubules, notably by inhibiting protein S-nitrosylation of isoform 2 of PKM (PKM2) (By similarity). Also acts as a S-nitroso-glutathione reductase by catalyzing the NADPH-dependent reduction of S-nitrosoglutathione (PubMed:31649033). Displays no reductase activity towards retinoids (By similarity).
ALDR1, ALR, AKR1A1, Aldo-keto reductase family 1 member A1, Alcohol dehydrogenase [NADP(+)], Aldehyde reductase, Glucuronate reductase, Glucuronolactone reductase, S-nitroso-CoA reductase, ScorR
Recombinant Human AKR1A1 protein is a Human Full Length protein, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl, 0.29% Sodium chloride
ab95472 was purified using conventional chromatography techniques.
Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols (PubMed:10510318, PubMed:30538128). 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 (PubMed:10510318, PubMed:30538128). Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes (By similarity). Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic (By similarity). 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) (PubMed:11306097, PubMed:18276838). Also acts as an inhibitor of protein S-nitrosylation by mediating degradation of S-nitroso-coenzyme A (S-nitroso-CoA), a cofactor required to S-nitrosylate proteins (PubMed:30538128). S-nitroso-CoA reductase activity is involved in reprogramming intermediary metabolism in renal proximal tubules, notably by inhibiting protein S-nitrosylation of isoform 2 of PKM (PKM2) (By similarity). Also acts as a S-nitroso-glutathione reductase by catalyzing the NADPH-dependent reduction of S-nitrosoglutathione (PubMed:31649033). Displays no reductase activity towards retinoids (By similarity).
Belongs to the aldo/keto reductase family.
AKR1A1 also known as aldehyde reductase or aldo-keto reductase is a member of the aldo-keto reductase family. It functions mechanically as a reductase enzyme that converts aldehydes and ketones to their corresponding alcohols via NADPH as a cofactor. The enzyme has a molecular mass of approximately 36 kDa. AKR1A1 is expressed in a wide range of tissues including liver kidney and brain indicating its broad role in metabolic processes.
AKR1A1 is involved in the detoxification of aldehydes produced during metabolism and oxidative stress. This function occurs as part of a larger detoxification system. Being part of the aldo-keto reductase family it contributes to maintaining homeostasis by regulating the levels of reactive aldehydes. Through this activity it affects cellular responses to stress and the metabolism of xenobiotics.
AKR1A1 has significant involvement in metabolic and detoxification pathways notably in glycolysis and xenobiotic metabolism. It interacts with various aldehydes formed as intermediates in these pathways. Related proteins in these pathways include AKR1B1 which also plays a role in reducing sugar-derived aldehydes emphasizing the importance of AKR1A1 in controlling toxic aldehyde levels and protecting cellular components from damage.
AKR1A1 has been linked to diabetic complications due to its role in polyol pathway where it contributes to the conversion of glucose to sorbitol. This pathway can lead to osmotic and oxidative stress when dysregulated contributing to retinal and renal dysfunctions in diabetes. Additionally AKR1A1 is connected to cancer development where it affects oxidative stress levels and tumor progression alongside proteins like AKR1C1 which are also involved in lipid and steroid metabolism further influencing disease outcomes.
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15% SDS-PAGE analysis of 3μg ab95472.
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