Recombinant Human AKR1A1 protein (Tag Free)
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Recombinant Human AKR1A1 protein (Tag Free) is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
ALDR1, ALR, AKR1A1, Aldo-keto reductase family 1 member A1, Alcohol dehydrogenase [NADP(+)], Aldehyde reductase, Glucuronate reductase, Glucuronolactone reductase, S-nitroso-CoA reductase, ScorR
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human AKR1A1 protein (Tag Free) (AB95472)
15% SDS-PAGE analysis of 3μg ab95472.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
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.
Pathways
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.
Specifications
Form
Liquid
Additional notes
ab95472 was purified using conventional chromatography techniques.
General info
Function
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).
Sequence similarities
Belongs to the aldo/keto reductase family.
Target data
Complementary Products
Product promise
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