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AKR1A1 Antibody (C-Terminus)
Goat Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | P14550 |
| Reactivity | Human, Mouse, Rat, Rabbit, Hamster, Monkey, Pig, Horse, Xenopus, Bovine, Dog |
| Host | Goat |
| Clonality | Polyclonal |
| Calculated MW | 37kDa |
| Dilution | ELISA (1:16000), IHC-P (2.5 µg/ml), WB (0.5-2 µg/ml) |
| Gene ID | 10327 |
|---|---|
| Other Names | Alcohol dehydrogenase [NADP(+)], 1.1.1.2, Aldehyde reductase, Aldo-keto reductase family 1 member A1, AKR1A1, ALDR1, ALR |
| Target/Specificity | Human AKR1A1. Both reported variants (NP_006057.1and NP_697021.1) represent identical protein |
| Reconstitution & Storage | Store at -20°C. Minimize freezing and thawing. |
| Precautions | AKR1A1 Antibody (C-Terminus) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | AKR1A1 |
|---|---|
| Synonyms | ALDR1, ALR |
| 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). |
| Cellular Location | Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JII6}. Apical cell membrane {ECO:0000250|UniProtKB:Q9JII6} |
| Tissue Location | Widely expressed. Highly expressed in kidney, salivary gland and liver. Detected in trachea, stomach, brain, lung, prostate, placenta, mammary gland, small intestine and lung |
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Provided below are standard protocols that you may find useful for product applications.
Background
Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. In vitro substrates include succinic semialdehyde, 4- nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D- glucuronic acid. 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).
References
Bohren K.M.,et al.J. Biol. Chem. 264:9547-9551(1989).
Fujii J.,et al.Cytogenet. Cell Genet. 84:230-232(1999).
Barski O.A.,et al.Genomics 60:188-198(1999).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Ebert L.,et al.Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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