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| Product | Description | |
|---|---|---|
| aldehyde reductase | Has wide specificity. Group: Enzymes. Synonyms: aldose reductase; polyol dehydrogenase (NADP+); ALR2; alditol:NADP oxidoreductase; alditol:NADP+ 1-oxidoreductase; NADPH-aldopentose reductase; NADPH-aldose reductase. Enzyme Commission Number: EC 1.1.1.21. CAS No. 9028-31-3. Aldose reductase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0114; aldehyde reductase; EC 1.1.1.21; 9028-31-3; aldose reductase; polyol dehydrogenase (NADP+); ALR2; alditol:NADP oxidoreductase; alditol:NADP+ 1-oxidoreductase; NADPH-aldopentose reductase; NADPH-aldose reductase. Cat No: EXWM-0114. |  |
| Aflatoxin B1 aldehyde reductase member 2 from Human, Recombinant | Aflatoxin B1 aldehyde reductase member 2 catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. May have an important role in producing the neuromodulator gamma-hydroxybutyrate (GHB). Has broad substrate specificity. Has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). Can reduce 1,2-naphthoquinone and 9,10-phenanthrenequinone (in vitro). Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen. Group: Enzymes. Synonyms: AFB1 aldehyde reductase 1; AFB1-AR 1; Aldoketoreductase 7; Succinic semialdehyde reductase. Enzyme Commission Number: EC 1.1.1.n11. AKR7A2. Mole weight: 39588.9 Da. Source: Human. AFB1 aldehyde reductase 1; AFB1-AR 1; Aldoketoreductase 7; Succinic semialdehyde reductase; EC 1.1.1.n11; AKR7A2; Aflatoxin B1 aldehyde reductase member 2. Cat No: NATE-1196. | |
| artemisinic aldehyde Δ11(13)-reductase | Cloned from Artemisia annua. In addition to the reduction of artemisinic aldehyde it is also able to a lesser extent to reduce artemisinic alcohol and artemisinic acid. Part of the biosyntheis of artemisinin. Group: Enzymes. Synonyms: Dbr2. Enzyme Commission Number: EC 1.3.1.92. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1362; artemisinic aldehyde Δ11(13)-reductase; EC 1.3.1.92; Dbr2. Cat No: EXWM-1362. | |
| chanoclavine-I aldehyde reductase | Contains FMN. The enzyme participates in the biosynthesis of fumigaclavine C, an ergot alkaloid produced by some fungi of the Trichocomaceae family. The enzyme catalyses the reduction of chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde. This hydrolyses spontaneously to form 6,8-dimethyl-6,7-didehydroergoline, which is converted to festuclavine by EC 1.5.1.44, festuclavine dehydrogenase. Group: Enzymes. Synonyms: FgaOx3; easA (gene name). Enzyme Commission Number: EC 1.3.1.100. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1272; chanoclavine-I aldehyde reductase; EC 1.3.1.100; FgaOx3; easA (gene name). Cat No: EXWM-1272. | |
| 1,5-anhydro-D-fructose reductase | Also reduces pyridine-3-aldehyde and 2,3-butanedione. Acetaldehyde, 2-dehydroglucose (glucosone) and glucuronate are poor substrates, but there is no detectable action on glucose, mannose and fructose. Group: Enzymes. Enzyme Commission Number: EC 1.1.1.263. CAS No. 206138-19-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0169; 1,5-anhydro-D-fructose reductase; EC 1.1.1.263; 206138-19-4. Cat No: EXWM-0169. | |
| 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) | This enzyme is present in some but not all Rhizobium species and belongs in the GFO/IDH/MocA protein family. This enzyme differs from hepatic 1,5-anhydro-D-fructose reductase, which yields 1,5-anhydro-D-glucitol as the product (see EC 1.1.1.263). In Sinorhizobium morelense, the product of the reaction, 1,5-anhydro-D-mannitol, can be further metabolized to D-mannose. The enzyme also reduces 1,5-anhydro-D-erythro-hexo-2,3-diulose and 2-ketoaldoses (called osones), such as D-glucosone (D-arabino-hexos-2-ulose) and 6-deoxy-D-glucosone. It does not reduce common aldoses and ketoses, or non-sugar aldehydes and ketones. Group: Enzymes. Synonyms: 1,5-anhydro-D-fructose reductase (ambiguous); AFR. Enzyme Commission Number: EC 1.1.1.292. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0201; 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming); EC 1.1.1.292; 1,5-anhydro-D-fructose reductase (ambiguous); AFR. Cat No: EXWM-0201. | |
| 2-alkenal reductase (NADP+) | Shows highest activity with 1-nitrocyclohexene but also has significant activity with 2-methylpentenal and trans-cinnamaldehyde. Involved in the detoxication of α,β-unsaturated aldehydes and ketones. Has very low activity with NAD as reductant (cf. EC 1.3.1.74, 2-alkenal reductase [NAD(P)+]). Group: Enzymes. Synonyms: NADPH-dependent alkenal/one oxidoreductase; NADPH:2-alkenal α,β-hydrogenase. Enzyme Commission Number: EC 1.3.1.102. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1274; 2-alkenal reductase (NADP+); EC 1.3.1.102; NADPH-dependent alkenal/one oxidoreductase; NADPH:2-alkenal α,β-hydrogenase. Cat No: EXWM-1274. | |
| 2-alkenal reductase [NAD(P)+] | Highly specific for 4-hydroxynon-2-enal and non-2-enal. Alk-2-enals of shorter chain have lower affinities. Exhibits high activities also for alk-2-enones such as but-3-en-2-one and pent-3-en-2-one. Inactive with cyclohex-2-en-1-one and 12-oxophytodienoic acid. Involved in the detoxication of α,β-unsaturated aldehydes and ketones [cf. EC 1.3.1.102, 2-alkenal reductase (NADP+)]. Group: Enzymes. Synonyms: NAD(P)H-dependent alkenal/one oxidoreductase; NADPH:2-alkenal α,β-hydrogenase; 2-alkenal reductase. Enzyme Commission Number: EC 1.3.1.74. CAS No. 52227-95-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1343; 2-alkenal reductase [NAD(P)+]; EC 1.3.1.74; 52227-95-9; NAD(P)H-dependent alkenal/one oxidoreductase; NADPH:2-alkenal α,β-hydrogenase; 2-alkenal reductase. Cat No: EXWM-1343. | |
| 3-Acetylpyridine-Adenine Dinucleotide, Oxidized (APAD) | 3-Acetylpyridine adenine dinucleotide is an NAD analog with higher oxidation potential than NAD. It can substitute for NAD as a hydrogen-accepting cofactor in many dehydrogenase reactions. For example lactate dehydrogenase from Toxoplasma, Clonorchis, and Plasmodium, bacterial lipoamide dehydrogenase, as well as mammalian dehydrogenases. This compound can also act as a proton acceptor in various transhydrogenation reactions with NADH or NADPH. Group: Coenzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NA. Enzyme Commission Number: EC 1.1.1.1. CAS No. 1986-8-8. Purity: Determined by increase in absorbance at 363 nm on enzymatic reduction with ADH* at pH 10.0 > 92% *ADH = Alcohol dehydrogenase (Horse liver) (EC 1.1.1.1.). APAD. Mole weight: 662.44. Storage: Keep tightly stoppered in the dark below 5°C. Moisture will reduce the purity. For prolonged storage, keep below-20°C. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1; APAD. Cat No: NATE-0077. | |
| 3-Acetylpyridine-Adenine Dinucleotide, Reduced (APADH) | Molecular Formula: C22H28N6O14P2. Group: Coenzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1; APADH. Enzyme Commission Number: EC 1.1.1.1. CAS No. 102029-93-6. Purity: Determined by decrease in absorbance at 363 nm on enzymatic oxidation with ADH* at pH 7.5 (> 92%) *ADH = Alcohol dehydrogenase (horse liver) (EC 1.1.1.1.). APADH. Mole weight: 708.42. Storage: Keep tightly stoppered in the dark below-20°C. Moisture will reduce the purity. For Prolonged storage, keep below-80°C. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1; APADH. Cat No: NATE-0078. | |
| 3-methylbutanal reductase | The enzyme purified from Saccharomyces cerevisiae catalyses the reduction of a number of straight-chain and branched aldehydes, as well as some aromatic aldehydes. Group: Enzymes. Enzyme Commission Number: EC 1.1.1.265. CAS No. 214265-44-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0171; 3-methylbutanal reductase; EC 1.1.1.265; 214265-44-8. Cat No: EXWM-0171. | |
| AL-3152 | AL-3152 is a aldehyde reductase inhibitors originated by Alcon. But clinical trials was discontinued for the treatment of Diabetic nephropathies, Diabetic neuropathies and Diabetic retinopathy. Uses: Diabetic nephropathies; diabetic neuropathies; diabetic retinopathy. Synonyms: AL-3152; AL 3152; AL3152; 2,7-difluoro-4-methoxy-Spiro(9H-fluorene-9,4'-imidazolidine)-2',5'-dione. Grades: 98%. CAS No. 126048-33-7. Molecular formula: C16H10F2N2O3. Mole weight: 316.62. |  |
| alcohol dehydrogenase | A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols. Group: Enzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0001; alcohol dehydrogenase; EC 1.1.1.1; 9031-72-5; aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase. Cat No: EXWM-0001. | |
| Alcohol Dehydrogenase (Crude Enzyme) | This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; medicine. Group: Enzymes. Synonyms: aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP + -aldehyde reductase; NADP + -dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.2. CAS No. 9028-12-0. ALR. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP + -aldehyde reductase; NADP + -dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Pack: 100ml. Cat No: NATE-1792. | |
| Alcohol dehydrogenase from E. coli, Recombinant | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Applications: High purity recombinant alcohol dehyd...l dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. Mole weight: ~ 38,642 Da. Activity: 6.7 U/mg protein at pH 8.5 and 25°C. Storage: Store at 4°C. Do not store the enzyme in presence of sodium azide. Form: In 3.2 M ammonium sulphate. Source: E. coli. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Cat No: NATE-0803. | |
| Alcohol dehydrogenase from Equine, Recombinant | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Group: Enzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcoh. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. Activity: >0.5 U/mg. Storage: Store at -20°C. Source: E. coli. Species: Equine. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Cat No: NATE-1584. | |
| Alcohol dehydrogenase from Human, Recombinant | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Group: Enzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcoh. Enzyme Commission Number: EC 1.1.1.2. Alcohol dehydrogenase. Mole weight: 36573.0 Da. Source: Human. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.2. Cat No: NATE-1197. | |
| alcohol dehydrogenase (NADP+) | A zinc protein. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. May be identical with EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate reductase (NADPH)] and EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. Re-specific with respect to NADPH. Group: Enzymes. Synonyms: aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.2. CAS No. 9028-12-0. ALR. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0103; alcohol dehydrogenase (NADP+); EC 1.1.1.2; 9028-12-0; aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Cat No: EXWM-0103. | |
| alcohol dehydrogenase [NAD(P)+] | Reduces aliphatic aldehydes of carbon chain length from 2 to 14, with greatest activity on C4, C6 and C8 aldehydes; also reduces retinal to retinol. Group: Enzymes. Synonyms: retinal reductase (ambiguous); aldehyde reductase (NADPH/NADH); alcohol dehydrogenase [NAD(P)]. Enzyme Commission Number: EC 1.1.1.71. CAS No. 37250-10-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0355; alcohol dehydrogenase [NAD(P)+]; EC 1.1.1.71; 37250-10-5; retinal reductase (ambiguous); aldehyde reductase (NADPH/NADH); alcohol dehydrogenase [NAD(P)]. Cat No: EXWM-0355. | |
| Alcohol Dehydrogenase (NADP+ dependent) from E. coli, Recombinant | Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an enzyme that in humans is encoded by the AKR1A1 gene. This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. This member, also known as aldehyde reductase, is involved in the reduction of biogenic and xenobiotic aldehydes and is present in virtually every tissue. Alternative splicing of this gene results in two transcript variants encoding the same protein. Group: Enzymes. Synonyms: EC 1.1.1.2; Aromatic Alcohol Dehydrogenase; Alcohol:NADP+ oxidoreductase; AKR1A1; ALDR1; ALR; . Enzyme Commission Number: EC 1.1.1.2. CAS No. 9028-12-0. ALR. Activity: >500 U/ml. Form: Liquid. Source: E. coli. Species: E. coli. EC 1.1.1.2; Aromatic Alcohol Dehydrogenase; Alcohol:NADP+ oxidoreductase; AKR1A1; ALDR1; ALR; ARM; DD3; HEL-S-6; aldehyde reductase; aldo-keto reductase family 1 member A1; alcohol dehydrogenase (NADP+); aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Cat No: NATE-1589. | |
| Alcohol Dehydrogenase (NADP+ dependent) from Entamoeba species, Recombinant | NADP-dependent isopropanol dehydrogenase belongs to the superfamily of alcohol dehydrogenases with a preference for medium chain secondary alcohols, such as 2- butanol and isopropanol, while it has low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. It is also active with acetaldehyde and propionaldehyde. Group: Enzymes. Synonyms: EC 1.1.1.2; Aromatic Alcohol Dehy. Purity: > 95% by SDS-PAGE. ALR. Mole weight: ~40.9 kDa (SDS-PAGE). Activity: > 60U/mg. Storage: Aliquot and store at -20°C. Avoid repeated freeze thaw cycles. Form: Liquid, 1 mg/mL solution in 50 mM Tris-HCl buffer (pH 8.0) containing 100 mM NaCl and 50% glycerol. Source: E. coli. Species: Entamoeba species. EC 1.1.1.2; Aromatic Alcohol Dehydrogenase; Alcohol:NADP+ oxidoreductase; AKR1A1; ALDR1; ALR; ARM; DD3; HEL-S-6; aldehyde reductase; aldo-keto reductase family 1 member A1; alcohol dehydrogenase (NADP+); aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Cat No: NATE-1590. | |
| alcohol-forming fatty acyl-CoA reductase | The enzyme has been characterized from the plant Simmondsia chinensis (jojoba). The alcohol is formed by a four-electron reduction of fatty acyl-CoA. Although the reaction proceeds through an aldehyde intermediate, a free aldehyde is not released. The recombinant enzyme was shown to accept saturated and mono-unsaturated fatty acyl-CoAs of 16 to 22 carbons. Group: Enzymes. Synonyms: FAR (gene name); long-chain acyl-CoA:NADPH reductase. Enzyme Commission Number: EC 1.2.1.84. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1187; alcohol-forming fatty acyl-CoA reductase; EC 1.2.1.84; FAR (gene name); long-chain acyl-CoA:NADPH reductase. Cat No: EXWM-1187. | |
| aldehyde oxygenase (deformylating) | Contains a diiron center. Involved in the biosynthesis of alkanes. The enzyme from the cyanobacterium Nostoc punctiforme PCC 73102 is only active in vitro in the presence of ferredoxin, ferredoxin reductase and NADPH, and produces mostly C15 and C17 alkanes. The enzyme from pea (Pisum sativum) produces alkanes of chain length C18 to C32 and is inhibited by metal-chelating agents. The substrate for this enzyme is formed by EC 1.2.1.80, acyl-[acyl-carrier protein] reductase. Group: Enzymes. Synonyms: decarbonylase; aldehyde decarbonylase; octadecanal decarbonylase; octadecanal alkane-lyase. Enzyme Commission Number: EC 4.1.99.5. CAS No. 94185-90-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4937; aldehyde oxygenase (deformylating); EC 4.1.99.5; 94185-90-7; decarbonylase; aldehyde decarbonylase; octadecanal decarbonylase; octadecanal alkane-lyase. Cat No: EXWM-4937. | |
| Aldose reductase from Human, Recombinant | In enzymology, aldose reductase (or aldehyde reductase) (EC 1.1.1.21) is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. It is primarily known for catalyzing the reduction of glucose to sorbitol, the first step in polyol pathway of glucose metabolism. Group: Enzymes. Synonyms: Aldehyde reductase; Aldo-keto reductase family 1 member B1. Enzyme Commission Number: EC 1.1.1.21. CAS No. 9028-31-3. Aldose reductase. Mole weight: 35853.4 Da. Source: Human. Aldehyde reductase; Aldo-keto reductase family 1 member B1; EC 1.1.1.21; Aldose reductase. Cat No: NATE-1198. | |
| aryl-alcohol dehydrogenase (NADP+) | Also acts on some aliphatic aldehydes, but cinnamaldehyde was the best substrate found. Group: Enzymes. Synonyms: aryl alcohol dehydrogenase (nicotinamide adenine dinucleotide phosphate); coniferyl alcohol dehydrogenase; NADPH-linked benzaldehyde reductase; aryl-alcohol dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.91. CAS No. 37250-27-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0375; aryl-alcohol dehydrogenase (NADP+); EC 1.1.1.91; 37250-27-4; aryl alcohol dehydrogenase (nicotinamide adenine dinucleotide phosphate); coniferyl alcohol dehydrogenase; NADPH-linked benzaldehyde reductase; aryl-alcohol dehydrogenase (NADP). Cat No: EXWM-0375. | |
| aryl-aldehyde dehydrogenase (NADP+) | This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is aryl-aldehyde:NADP+ oxidoreductase (ATP-forming). Other names in common use include aromatic acid reductase, and aryl-aldehyde dehydrogenase (NADP+). Group: Enzymes. Synonyms: aromatic acid reductase; aryl-aldehyde dehydrogenase (NADP). Enzyme Commission Number: EC 1.2.1.30. CAS No. 9074-94-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1137; aryl-aldehyde dehydrogenase (NADP+); EC 1.2.1.30; 9074-94-6; aromatic acid reductase; aryl-aldehyde dehydrogenase (NADP). Cat No: EXWM-1137. | |
| β-Nicotinamide-Adenine Dinucleotide, Reduced Form (β-NADH) | NADH is a coenzyme that functions as a regenerating electron donor in catabolic processes including glycolysis, beta-oxidation and the citric acid cycle (Krebs cycle, TCA cycle). It participates in cell signaling events as well, for example as a substrate for the poly (ADP-ribose) polymerases (PARPs) during the DNA damage response. The NAD+/NADH dependent sirtuins play key roles in stress responses during events involving energy metabolism, with implications in cancer biology, diabetes and neurodegenerative disease. Group: Coenzymes. Synonyms. Enzyme Commission Number: EC 1.1.1.1. CAS No. 606-68-8. Purity: Dertermined by decrease in absorbance at 340 nm on enzymatic oxidation with ADH* at pH 10.0 > 95% *ADH = Alcohol dehydrogenase (yeast) (EC 1.1.1.1.). β-NADH. Mole weight: 709.41. Storage: Keep tightly stoppered in the dark below 5°C. Moisture will reduce the purity. For prolonged storage, keep below-20°C. Unstable in acids, but relatively stable at pH 10-11. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1; β-NADH. Cat No: NATE-0786. | |
| carbonyl reductase (NADPH) | Acts on a wide range of carbonyl compounds, including quinones, aromatic aldehydes, ketoaldehydes, daunorubicin and prostaglandins E and F, reducing them to the corresponding alcohol. Si-specific with respect to NADPH [cf. EC 1.1.1.2 alcohol dehydrogenase (NADP+)]. Group: Enzymes. Synonyms: aldehyde reductase 1; prostaglandin 9-ketoreductase; xenobiotic ketone reductase; NADPH-dependent carbonyl reductase; ALR3; carbonyl reductase; nonspecific NADPH-dependent carbonyl reductase; carbonyl reductase (NADPH2). Enzyme Commission Number: EC 1.1.1.184. CAS No. 89700-36-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0086; carbonyl reductase (NADPH); EC 1.1.1.184; 89700-36-7; aldehyde reductase 1; prostaglandin 9-ketoreductase; xenobiotic ketone reductase; NADPH-dependent carbonyl reductase; ALR3; carbonyl reductase; nonspecific NADPH-dependent carbonyl reductase; carbonyl reductase (NADPH2). Cat No: EXWM-0086. | |
| carboxylate reductase | A tungsten protein. Methyl viologen can act as acceptor. In the reverse direction, non-activated acids are reduced by reduced viologens to aldehydes, but not to the corresponding alcohols. Group: Enzymes. Synonyms: aldehyde:(acceptor) oxidoreductase. Enzyme Commission Number: EC 1.2.99.6. CAS No. 125008-36-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1234; carboxylate reductase; EC 1.2.99.6; 125008-36-8; aldehyde:(acceptor) oxidoreductase. Cat No: EXWM-1234. | |
| cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming] | This enzyme, found in several bacterial pathogens, is involved in degradation of the host cholesterol. It catalyses the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol. The products are exclusively in the (25R) conformation. The enzyme also accepts cholesterol as a substrate. cf. EC 1.14.13.141, cholest-4-en-3-one 26-monooxygenase. The enzyme can receive electrons from ferredoxin reductase in vitro, its natural electron donor is not known yet. Group: Enzymes. Synonyms: CYP142. Enzyme Commission Number: EC 1.14.13.221. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0824; cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming]; EC 1.14.13.221; CYP142. Cat No: EXWM-0824. | |
| cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming] | This enzyme, found in several bacterial pathogens, is involved in degradation of the host's cholesterol. It catalyses the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol. The products are exclusively in the (25S) configuration. It is a two-component system consisting of a P-450 (heme thiolate) oxygenase (Cyp125) and a ferredoxin reductase (most likely KshB, which is also a part of EC 1.14.13.142, 3-ketosteroid 9α-monooxygenase). The enzyme also accepts cholesterol as a substrate. cf. EC 1.14.13.221, cholest-4-en-3-one 27-monooxygenase. Group: Enzymes. Synonyms: CYP125; CYP125A1; cholest-4-en-3-one 27-monooxygenase (misleading); cholest-4-en-3-one,NADH:oxygen oxidoreductase (26-hydroxyl. Enzyme Commission Number: EC 1.14.13.141. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0741; cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]; EC 1.14.13.141; CYP125; CYP125A1; cholest-4-en-3-one 27-monooxygenase (misleading); cholest-4-en-3-one,NADH:oxygen oxidoreductase (26-hydroxylating); cholest-4-en-3-one 26-monooxygenase (ambiguous). Cat No: EXWM-0741. | |
| choline dehydrogenase | A quinoprotein. In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyse the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. In plants, the first reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17). The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in plants, animals and bacteria. Group: Enzymes. Synonyms: choline oxidase; choline-cytochrome c reductase; choline:(acceptor) oxidoreductase; choline:(acceptor) 1-oxidoreductase. Enzyme Commission Number: EC 1.1.99.1. CAS No. 9028-67-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0443; choline dehydrogenase; EC 1.1.99.1; 9028-67-5; choline oxidase; choline-cytochrome c reductase; choline:(acceptor) oxidoreductase; choline:(acceptor) 1-oxidoreductase. Cat No: EXWM-0443. | |
| formaldehyde dehydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is formaldehyde:NAD+ oxidoreductase. Other names in common use include NAD+-linked formaldehyde dehydrogenase, s-nitrosoglutathione reductase (GSNO reductase) and NAD+-dependent formaldehyde dehydrogenase. This enzyme participates in methane metabolism. Group: Enzymes. Synonyms: NAD-linked formaldehyde dehydrogenase; NAD-dependent formaldehyde dehydrogenase. Enzyme Commission Number: EC 1.2.1.46. CAS No. 9028-84-6. Formaldehyde Dehydrogenase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1149; formaldehyde dehydrogenase; EC 1.2.1.46; 9028-84-6; NAD-linked formaldehyde dehydrogenase; NAD-dependent formaldehyde dehydrogenase. Cat No: EXWM-1149. | |
| glucuronate reductase | Also reduces D-galacturonate. May be identical with EC 1.1.1.2 [alcohol dehydrogenase (NADP+)]. Group: Enzymes. Synonyms: aldehyde reductase; L-hexonate:NADP dehydrogenase; TPN-L-gulonate dehydrogenase; aldehyde reductase II; NADP-L-gulonate dehydrogenase; D-glucuronate dehydrogenase; D-glucuronate reductase; L-glucuronate reductase (incorrect). Enzyme Commission Number: EC 1.1.1.19. CAS No. 9028-29-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0092; glucuronate reductase; EC 1.1.1.19; 9028-29-9; aldehyde reductase; L-hexonate:NADP dehydrogenase; TPN-L-gulonate dehydrogenase; aldehyde reductase II; NADP-L-gulonate dehydrogenase; D-glucuronate dehydrogenase; D-glucuronate reductase; L-glucuronate reductase (incorrect). Cat No: EXWM-0092. | |
| glutamate-5-semialdehyde dehydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating). Other names in common use include beta-glutamylphosphate reductase, gamma-glutamyl phosphate reductase, beta-glutamylphosphate reductase, glutamate semialdehyde dehydrogenase, and glutamate-gamma-semialdehyde dehydrogenase. This enzyme participates in urea cycle and metabolism of amino groups. Group: Enzymes. Synonyms: β-glutamylphosphate reductase; γ-glutamyl phosphate reductase; β-glutamylphosphate reductase; glutamate semialdehyde dehydrogenase; glutamate-γ-semialdehyde dehydrogenase. Enzyme Commission Number: EC 1.2.1.41. CAS No. 54596-29-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1145; glutamate-5-semialdehyde dehydrogenase; EC 1.2.1.41; 54596-29-1; β-glutamylphosphate reductase; γ-glutamyl phosphate reductase; β-glutamylphosphate reductase; glutamate semialdehyde dehydrogenase; glutamate-γ-semialdehyde dehydrogenase. Cat No: EXWM-1145. | |
| long-chain acyl-[acyl-carrier-protein] reductase | Catalyses the reaction in the opposite direction. This enzyme, purified from the cyanobacterium Synechococcus elongatus PCC 7942, catalyses the NAD(P)H-dependent reduction of an activated fatty acid (acyl-[acp]) to the corresponding aldehyde. Together with EC 4.1.99.5, octadecanal decarbonylase, it is involved in alkane biosynthesis. The natural substrates of the enzyme are C16 and C18 activated fatty acids. Requires Mg2+. Group: Enzymes. Synonyms: long-chain acyl-[acp] reductase; fatty acyl-[acyl-carrier-protein] reductase; acyl-[acp] reductase. Enzyme Commission Number: EC 1.2.1.80. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1183; long-chain acyl-[acyl-carrier-protein] reductase; EC 1.2.1.80; long-chain acyl-[acp] reductase; fatty acyl-[acyl-carrier-protein] reductase; acyl-[acp] reductase. Cat No: EXWM-1183. | |
| long-chain acyl-protein thioester reductase | Together with a hydrolase component (EC 3.1.2.2 and EC 3.1.2.14) and a synthetase component (EC 6.2.1.19), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC 1.14.14.3). The enzyme is acylated by receiving an acyl group from EC 6.2.1.19, and catalyses the reduction of the acyl group, releasing the aldehyde product. The enzyme is also able to accept the acyl group from a long-chain acyl-CoA. Group: Enzymes. Synonyms: luxC (gene name); acyl-CoA reductase; acyl coenzyme A reductase; long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming); long-chain-fatty-acyl-CoA reductase. Enzyme Commission Number: EC 1.2.1.50. CAS No. 50936-56-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1154; long-chain acyl-protein thioester reductase; EC 1.2.1.50; 50936-56-6; luxC (gene name); acyl-CoA reductase; acyl coenzyme A reductase; long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming); long-chain-fatty-acyl-CoA reductase. Cat No: EXWM-1154. | |
| long-chain-fatty-acid-protein ligase | Together with a hydrolase component (EC 3.1.2.2/EC 3.1.2.14) and a reductase component (EC 1.2.1.50), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC 1.14.14.3). The enzyme activates free long-chain fatty acids, generated by the action of the transferase component, forming a fatty acyl-AMP intermediate, followed by the transfer of the acyl group to an internal L-cysteine residue. It then transfers the acyl group to EC 1.2.1.50, long-chain acyl-protein thioester reductase. Group: Enzymes. Synonyms: luxE (gene name); acyl-protein synthetase; long-chain-fatty-acid-luciferin-component ligase. Enzyme Commission Number: EC 6.2.1.19. CAS No. 82657-98-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5677; long-chain-fatty-acid-protein ligase; EC 6.2.1.19; 82657-98-5; luxE (gene name); acyl-protein synthetase; long-chain-fatty-acid-luciferin-component ligase. Cat No: EXWM-5677. | |
| N-acetyl-γ-glutamyl-phosphate reductase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in urea cycle and metabolism of amino groups. Group: Enzymes. Synonyms: reductase, acetyl-γ-glutamyl phosphate; N-acetylglutamate 5-semialdehyde dehydrogenase; N-acetylglutamic γ-semialdehyde dehydrogenase; N-acetyl-L-glutamate γ-semialdehyde:NADP+ oxidoreductase (phosphorylating). Enzyme Commission Number: EC 1.2.1.38. CAS No. 37251-00-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1142; N-acetyl-γ-glutamyl-phosphate reductase; EC 1.2.1.38; 37251-00-6; reductase, acetyl-γ-glutamyl phosphate; N-acetylglutamate 5-semialdehyde dehydrogenase; N-acetylglutamic γ-semialdehyde dehydrogenase; N-acetyl-L-glutamate γ-semialdehyde:NADP+ oxidoreductase (phosphorylating). Cat No: EXWM-1142. | |
| Native Alcohol dehydrogenase | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. The enzyme is an alcohol dehydrogenase most active on n-butanol but with low activity on ethanol. Group: Enzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcoh. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Cat No: NATE-0034. | |
| Native Photobacterium phosphoreum (Lux) Bacterial Luciferase | P. phosphoreum. Applications: Bacterial luciferase is purified from a photobacterium phosphoreum strain isolated from squid by our team and selected for its brightest luminescence. the luxab gene was amplified by pcr and cloned. the sequences of cloned α and β subunits have shown 94% and 92% identity to p24113 and p12744 proteins of photobacterium phosphoreum (swissprot entry). Group: Enzymes. Synonyms: aldehyde monooxygenase; luciferase; Vibrio fischeri luciferase; alkanal,reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing); alkanal,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing); alkanal monooxygenase (FMN); aldehyde,FMNH2:ox... presence of limiting concentrations of NADH substrate, light intensity is proportional to NAD(P)H concentration. The coupling of bacterial luciferase to FMN-NAD(P)H oxidoreductase has been used to provide ultrasensitive analytical tools for the quantification of NAD(P)H and the substrates of NADH-, NADPH- dependent enzymes (e.g. glucose, lactate, malate, ethanol, sorbitol, oxaloacetate).Bacterial Luciferase can be used for NAD(P)H quantification or in dehydrogenase-coupled assays.The enzyme is provided lyophilized, alone or with lyophilized FMN-reductase. Species: Luciferase. aldehyde monooxygenase; luciferase; Vibrio fischeri luciferase; alkanal,reduced-FMN:ox | |
| Native Saccharomyces cerevisiae Alcohol Dehydrogenase | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Applications: Alcohol dehydrogenase from sacchar...dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Activity: > 300 units/mg protein. Storage: -20°C. Form: Solids containing <2% Citrate buffer salts. Source: Saccharomyces cerevisiae. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Cat No: NATE-0035. | |
| Native Thermoanaerobium brockii Alcohol Dehydrogenase, NADP+ dependent | Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an enzyme that in humans is encoded by the AKR1A1 gene. This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. This member, also known as aldehyde reductase, is involved in the reduction of biogenic and xenobiotic aldehydes and is present in virtually every tissue. Alternative splicing of this gene results in two transcript variants encoding the same protein. Applications: Alcohol dehydrogenase may be used to synthesize enantiomerically pure stereoisomers of chiral alcohols. it may...ase; AKR1A1; ALDR1; ALR; ARM; DD3; HEL-S-6; aldehyde reductase; aldo-keto reductase family 1 member A1; alcohol dehydrogenase (NADP+); aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.2. CAS No. 9028-12-0. ALR. Activity: 5-15 units/mg protein; 30-90 units/mg protein. Stability: -20°C. Form: lyophilized powder. Source: Thermoanaerobium brockii. EC 1.1.1.2; Aro | |
| Native Thermoanaerobium sp. Aromatic Alcohol Dehydrogenase, NADP+ dependent | Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an enzyme that in humans is encoded by the AKR1A1 gene. This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. This member, also known as aldehyde reductase, is involved in the reduction of biogenic and xenobiotic aldehydes and is present in virtually every tissue. Alternative splicing of this gene results in two transcript variants encoding the same protein. Group: Enzymes. Synonyms: EC 1.1.1.2; Aromatic Alcohol Dehydrogenase; Alcohol. Enzyme Commission Number: EC 1.1.1.2. CAS No. 9028-12-0. ALR. Activity: 1-5 units/mg solid. Stability: -20°C. Form: lyophilized powder. Source: Thermoanaerobium sp. EC 1.1.1.2; Aromatic Alcohol Dehydrogenase; Alcohol:NADP+ oxidoreductase; AKR1A1; ALDR1; ALR; ARM; DD3; HEL-S-6; aldehyde reductase; aldo-keto reductase family 1 member A1; alcohol dehydrogenase (NADP+); aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Cat No: NATE-0063. | |
| Native Yeast Alcohol dehydrogenase | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Dehydrogenase that catalyzes the interconversion of alcoho...rimary alcohol dehydrogenase; yeast alcohol dehydrogenase. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Activity: >300 U/mg. Appearance: White lyophilizate (50 mg lyophilizate contain approximately 30 mg enzyme protein,15 mg sucrose, 5 mg phosphate). Storage: -20°C. Form: Solids containing <2% Citrate buffer salts. Source: Yeast. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Cat No: NATE-0975. | |
| Native Zymomonas mobilis Alcohol Dehydrogenase | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Applications: The enzyme is useful for determination of alcohols or aldehydes. Group: Enzymes. Synonyms: aldehyde reductase; ADH;. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. Mole weight: ca. 148,000; Subunit molecular weight : ca. 37,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least six months. Source: Zymomonas mobilis. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1; 9031-72-5. Cat No: NATE-1900. | |
| pheophorbide a oxygenase | This enzyme catalyses a key reaction in chlorophyll degradation, which occurs during leaf senescence and fruit ripening in higher plants. The enzyme from Arabidopsis contains a Rieske-type iron-sulfur cluster and requires reduced ferredoxin, which is generated either by NADPH through the pentose-phosphate pathway or by the action of photosystem I. While still attached to this enzyme, the product is rapidly converted into primary fluorescent chlorophyll catabolite by the action of EC 1.3.7.12, red chlorophyll catabolite reductase. Pheophorbide b acts as an inhibitor. In 18O2 labelling experiments, only the aldehyde oxygen is labelled, suggesting that the other oxygen atom may originate from H2O. Group: Enzymes. Synonyms: pheide a monooxygenase; pheide a oxygenase; PaO; PAO. Enzyme Commission Number: EC 1.14.15.17. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0942; pheophorbide a oxygenase; EC 1.14.15.17; pheide a monooxygenase; pheide a oxygenase; PaO; PAO. Cat No: EXWM-0942. | |
| Prostaglandin F Synthase from human, Recombinant | PGF synthase catalyzes the conversions of 4-androstene-3,17-dione to testosterone, estrone to 17β-estradiol, prostaglandin H2 to PGF2α, and PGD2 to 9α,11β-PGF2. Prostaglandin (PG) F2 is synthesized via three pathways. Applications: Prostaglandin f synthase (pgf synthase) is a member of the aldo-keto reductase superfamily of proteins which catalyze the conversion of aldehydes and ketones to thier corresponding alcohols. prostaglandin f synthase is used in cancer research since it is upregulated in many cancers such as breast and prostate cancer. pgf synthase is also used to study kidney and renal cell carcinoma. Group: Enzymes. Synonyms: prostaglandin-D2 11-reduc. Enzyme Commission Number: EC 1.1.1.188. CAS No. 55976-95-9. Purity: > 90% (SDS-PAGE). PGF synthetase. Mole weight: mol wt ~37 kDa. Storage: -70°C. Source: E. coli. Species: Human. prostaglandin-D2 11-reductase; reductase, 15-hydroxy-11-oxoprostaglandin; PGD2 11-ketoreductase; PGF2α synthetase; prostaglandin 11-ketoreductase; prostaglandin D2-ketoreductase; prostaglandin F synthase; prostaglandin F synthetase; synthetase, prostaglandin F2α; prostaglandin-D2 11-reductase; PGF synthetase; NADPH-dependent prostaglandin D2 11-keto reductase; prostaglandin 11-keto reductase; prostaglandin-F synthase; EC 1.1.1.188; 55976-95-9. Cat No: NATE-0552. | |
| Secondary Alcohol Dehydrogenase (Crude Enzyme) | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD + to NADH). In humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in generation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD +. This product with the indicated enzyme activity wa...DH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase. Pack: 100ml. Cat No: NATE-1786. | |
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