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| Product | Description | |
|---|---|---|
| nicotinate dehydrogenase | A flavoprotein containing non-heme iron. The enzyme is capable of acting on a variety of nicotinate analogues to varying degrees, including pyrazine-2-carboxylate, pyrazine 2,3-dicarboxylate, trigonelline and 6-methylnicotinate. The enzyme from Clostridium barkeri also possesses a catalytically essential, labile selenium that can be removed by reaction with cyanide. Group: Enzymes. Synonyms: nicotinic acid hydroxylase; nicotinate hydroxylase. Enzyme Commission Number: EC 1.17.1.5. CAS No. 9059-3-4. 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-1083; nicotinate dehydrogenase; EC 1.17.1.5; 9059-03-4; nicotinic acid hydroxylase; nicotinate hydroxylase. Cat No: EXWM-1083. |  |
| nicotinate dehydrogenase (cytochrome) | This two-component enzyme from Pseudomonas belongs to the family of xanthine dehydrogenases, but differs from most other members of this family. While most members contain an FAD cofactor, the large subunit of this enzyme contains three c-type cytochromes, enabling it to interact with the electron transfer chain, probably by delivering the electrons to a cytochrome oxidase. The small subunit contains a typical molybdopterin cytosine dinucleotide(MCD) cofactor and two [2Fe-2S] clusters. Group: Enzymes. Synonyms: nicotinic acid hydroxylase; nicotinate hydroxylase. Enzyme Commission Number: EC 1.17.2.1. 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-1085; nicotinate dehydrogenase (cytochrome); EC 1.17.2.1; nicotinic acid hydroxylase; nicotinate hydroxylase. Cat No: EXWM-1085. | |
| 6-hydroxynicotinate dehydrogenase | Contains [2Fe-2S] iron-sulfur centres, FAD and molybdenum. It also has a catalytically essential, labile selenium that can be removed by reaction with cyanide. In Bacillus niacini, this enzyme is required for growth on nicotinic acid. Group: Enzymes. Synonyms: 6-hydroxynicotinic acid hydroxylase; 6-hydroxynicotinic acid dehydrogenase; 6-hydroxynicotinate hydroxylase; 6-hydroxynicotinate:O2 oxidoreductase. Enzyme Commission Number: EC 1.17.3.3. CAS No. 122191-32-6. 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-1089; 6-hydroxynicotinate dehydrogenase; EC 1.17.3.3; 122191-32-6; 6-hydroxynicotinic acid hydroxylase; 6-hydroxynicotinic acid dehydrogenase; 6-hydroxynicotinate hydroxylase; 6-hydroxynicotinate:O2 oxidoreductase. Cat No: EXWM-1089. | |
| 2-hydroxymethylglutarate dehydrogenase | NADP+ cannot replace NAD+. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Other enzymes involved in this pathway are EC 1.17.1.5 (nicotinate dehydrogenase), EC 1.3.7.1 (6-hydroxynicotinate reductase), EC 3.5.2.18 (enamidase), EC 5.4.99.4 (2-methyleneglutarate mutase), EC 5.3.3.6 (methylitaconate Δ-isomerase), EC 4.2.1.85 (dimethylmaleate hydratase) and EC 4.1.3.32 (2,3-dimethylmalate lyase). Group: Enzymes. Synonyms: HgD. Enzyme Commission Number: EC 1.1.1.291. CAS No. 1073478-76-8. 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-0200; 2-hydroxymethylglutarate dehydrogenase; EC 1.1.1.291; 1073478-76-8; HgD. Cat No: EXWM-0200. | |
| enamidase | Contains iron and Zn2+.Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Other enzymes involved in this pathway are EC 1.17.1.5 (nicotinate dehydrogenase), EC 1.3.7.1 (6-hydroxynicotinate reductase), EC 1.1.1.291 (2-hydroxymethylglutarate dehydrogenase), EC 5.4.99.4 (2-methyleneglutarate mutase), EC 5.3.3.6 (methylitaconate Δ-isomerase), EC 4.2.1.85 (dimethylmaleate hydratase) and EC 4.1.3.32 (2,3-dimethylmalate lyase). Group: Enzymes. Enzyme Commission Number: EC 3.5.2.18. 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-4501; enamidase; EC 3.5.2.18. Cat No: EXWM-4501. | |
| 12β-hydroxysteroid dehydrogenase | Acts on a number of bile acids, both in their free and conjugated forms. Group: Enzymes. Synonyms: 12β-hydroxy steroid (nicotinamide adenine dinucleotide phosphate) dehydrogenase. Enzyme Commission Number: EC 1.1.1.238. CAS No. 118390-62-8. 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-0145; 12β-hydroxysteroid dehydrogenase; EC 1.1.1.238; 118390-62-8; 12β-hydroxy steroid (nicotinamide adenine dinucleotide phosphate) dehydrogenase. Cat No: EXWM-0145. | |
| 15-hydroxyprostaglandin-D dehydrogenase (NADP+) | Specific for prostaglandins D [cf. EC 1.1.1.141 15-hydroxyprostaglandin dehydrogenase (NAD+) and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+)]. Group: Enzymes. Synonyms: prostaglandin-D 15-dehydrogenase (NADP); dehydrogenase, prostaglandin D2; NADP-PGD2 dehydrogenase; dehydrogenase, 15-hydroxyprostaglandin (nicotinamide adenine dinucleotide phosphate); 15-hydroxy PGD2 dehydrogenase; 15-hydroxyprostaglandin dehydrogenase (NADP); NADP-dependent 15-hydroxyprostaglandin dehydrogenase; prostaglandin . Enzyme Commission Number: EC 1.1.1.196. CAS No. 84399-95-1. 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-0099; 15-hydroxyprostaglandin-D dehydrogenase (NADP+); EC 1.1.1.196; 84399-95-1; prostaglandin-D 15-dehydrogenase (NADP); dehydrogenase, prostaglandin D2; NADP-PGD2 dehydrogenase; dehydrogenase, 15-hydroxyprostaglandin (nicotinamide adenine dinucleotide phosphate); 15-hydroxy PGD2 dehydrogenase; 15-hydroxyprostaglandin dehydrogenase (NADP); NADP-dependent 15-hydroxyprostaglandin dehydrogenase; prostaglandin D2 dehydrogenase; NADP-linked 15-hydroxyprostaglandin dehydrogenase; NADP-specific 15-hydroxyprostaglandin dehydrogenase; NADP-linked prostaglandin D2 dehydrogenase; 15-hydroxyprostaglandin-D dehydrogenase (NADP). Cat No: EXWM-0099. | |
| 21-hydroxysteroid dehydrogenase (NADP+) | Acts on a number of 21-hydroxycorticosteroids. Group: Enzymes. Synonyms: 21-hydroxy steroid dehydrogenase; 21-hydroxy steroid (nicotinamide adenine dinucleotide phosphate) dehydrogenase; 21-hydroxy steroid dehydrogenase (nicotinamide adenine dinucleotide phosphate); NADP-21-hydroxysteroid dehydrogenase; 21-hydroxysteroid dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.151. CAS No. 37250-76-3. 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-0056; 21-hydroxysteroid dehydrogenase (NADP+); EC 1.1.1.151; 37250-76-3; 21-hydroxy steroid dehydrogenase; 21-hydroxy steroid (nicotinamide adenine dinucleotide phosphate) dehydrogenase; 21-hydroxy steroid dehydrogenase (nicotinamide adenine dinucleotide phosphate); NADP-21-hydroxysteroid dehydrogenase; 21-hydroxysteroid dehydrogenase (NADP). Cat No: EXWM-0056. | |
| 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase | The enzyme from Pseudomonas acts equally well on NAD+ or NADP+, while that from Erwinia chrysanthemi and Escherichia coli is more specific for NAD+. Group: Enzymes. Synonyms: 2-keto-3-deoxygluconate 5-dehydrogenase; 2-keto-3-deoxy-D-gluconate dehydrogenase; 2-keto-3-deoxygluconate (nicotinamide adenine dinucleotide (phosphate)) dehydrogenase; 2-keto-3-deoxy-D-gluconate (3-deoxy-D-glycero-2,5-hexodiulosonic acid) dehydrogenase. Enzyme Commission Number: EC 1.1.1.127. CAS No. 37250-56-9. 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-0031; 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase; EC 1.1.1.127; 37250-56-9; 2-keto-3-deoxygluconate 5-dehydrogenase; 2-keto-3-deoxy-D-gluconate dehydrogenase; 2-keto-3-deoxygluconate (nicotinamide adenine dinucleotide (phosphate)) dehydrogenase; 2-keto-3-deoxy-D-gluconate (3-deoxy-D-glycero-2,5-hexodiulosonic acid) dehydrogenase. Cat No: EXWM-0031. | |
| 3-Amino-3-methylbutanoic Acid, 90% | 3-Amino-3-methylbutanoic Acid acts as a reagent in the preparation of arylsulfonyl methylbutanamides of cycloalkylamines, particularly adamantylamines, as selective inhibitors of human and murine 11 β-hydroxysteroid dehydrogenase type 1. Synthesis of acetylcholine and carbamoylcholine analogs as a functionally selective α4 β2 nicotinic acetylcholine receptor agonist. Phenamide preparation by coupling reaction. Group: Biochemicals. Grades: Highly Purified. CAS No. 625-05-8. Pack Sizes: 250mg, 1g. Molecular Formula: C5H11NO2. US Biological Life Sciences. |  Worldwide |
| 3-(Aminocarbonyl)-1-(2,3,5-tri-O-acetyl- β-D-ribofuranosyl)-pyridinium-d4 Triflate | 3-(Aminocarbonyl)-1-(2,3,5-tri-O-acetyl- β-D-ribofuranosyl)-pyridinium-d4 Triflate is an intermediate in the synthesis of β-NADH-d5 (d5-major) Diammonium Salt (N201487). β-NADH-d4 is labelled β-NADH (N201480, Disodium salt). β-NADH is one of the biologically active forms of nicotinic acid. Serves as a coenzyme of hydrogenases and dehydrogenases. NAD usually acts as a hydrogen acceptor, forming NADH which then serves as a hydrogen donor in the respiratory chain. Present in living cells primarily in the reduced form (NADPH) and is involved in synthetic reactions. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 2.5mg, 25mg. Molecular Formula: C17H17D4N2O8+; CF3O3S-. US Biological Life Sciences. | Worldwide |
| 3-hydroxybutyryl-CoA dehydrogenase | This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-3-hydroxybutanoyl-CoA:NADP+ oxidoreductase. Other names in common use include beta-hydroxybutyryl coenzyme A dehydrogenase, L(+)-3-hydroxybutyryl-CoA dehydrogenase, BHBD, dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide adenine, dinucleotide phosphate), L-(+)-3-hydroxybutyryl-CoA dehydrogenase, and beta-hydroxybutyryl-CoA dehydrogenase. This enzyme participates in benzoate degradation via coa ligation and butanoate metabolism. Group: Enzymes. Synonyms: β-hydroxybutyryl coenzyme A dehydrogenase; L(+)-3-hydroxybutyryl-CoA dehydrogenase; BHBD; dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide ade. Enzyme Commission Number: EC 1.1.1.157. CAS No. 39319-78-3. 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-0061; 3-hydroxybutyryl-CoA dehydrogenase; EC 1.1.1.157; 39319-78-3; β-hydroxybutyryl coenzyme A dehydrogenase; L(+)-3-hydroxybutyryl-CoA dehydrogenase; BHBD; dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide adenine dinucleotide phosphate); L-(+)-3-hydroxybutyryl-CoA dehydrogenase; β-hydroxybutyryl-CoA dehydrogenase. Cat No: EXWM-0061. | |
| 3-oxo-5α-steroid 4-dehydrogenase (NADP+) | The enzyme catalyses the conversion of assorted 3-oxo-Δ4 steroids into their corresponding 5α form. Substrates for the mammalian enzyme include testosterone, progesterone, and corticosterone. Substrates for the plant enzyme are brassinosteroids such as campest-4-en-3-one and (22α)-hydroxy-campest-4-en-3-one. cf. EC 1.3.99.5, 3-oxo-5α-steroid 4-dehydrogenase (acceptor). Group: Enzymes. Synonyms: cholestenone 5α-reductase; testosterone Δ4-5&. Enzyme Commission Number: EC 1.3.1.22. CAS No. 37255-34-8. 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-1297; 3-oxo-5α-steroid 4-dehydrogenase (NADP+); EC 1.3.1.22; 37255-34-8; cholestenone 5α-reductase; testosterone Δ4-5α-reductase; steroid 5α-reductase; 3-oxosteroid Δ4-dehydrogenase; 5α-reductase; steroid 5α-hydrogenase; 3-oxosteroid 5α-reductase; testosterone Δ4-hydrogenase; 4-ene-3-oxosteroid 5α-reductase; reduced nicotinamide adenine dinucleotide phosphate:Δ4-3-ketosteroid 5α-oxidoreductase; 4-ene-5α-reductase; Δ4-3-ketosteroid 5α-oxidoreductase; cholest-4-en-3-one 5α-reductase; testosterone 5α-reductase; 3-oxo-5α-steroid 4-dehydrogenase. Cat No: EXWM-1297. | |
| 3-succinoylsemialdehyde-pyridine dehydrogenase | The enzyme has been characterized from the soil bacterium Pseudomonas sp. HZN6. It participates in the nicotine degradation pathway. Group: Enzymes. Enzyme Commission Number: EC 1.2.1.83. 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-1186; 3-succinoylsemialdehyde-pyridine dehydrogenase; EC 1.2.1.83. Cat No: EXWM-1186. | |
| 6-hydroxypseudooxynicotine dehydrogenase | Contains a cytidylyl molybdenum cofactor. The enzyme, which participates in the nicotine degradation pathway, has been characterized from the soil bacterium Arthrobacter nicotinovorans. Group: Enzymes. Enzyme Commission Number: EC 1.5.99.14. 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-1568; 6-hydroxypseudooxynicotine dehydrogenase; EC 1.5.99.14. Cat No: EXWM-1568. | |
| acyl-CoA dehydrogenase (NADP+) | The liver enzyme acts on enoyl-CoA derivatives of carbon chain length 4 to 16, with optimum activity on 2-hexenoyl-CoA. In Escherichia coli, cis-specific and trans-specific enzymes exist [EC 1.3.1.37 cis-2-enoyl-CoA reductase (NADPH) and EC 1.3.1.38 trans-2-enoyl-CoA reductase (NADPH)]. Group: Enzymes. Synonyms: 2-enoyl-CoA reductase; dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide phosphate); enoyl coenzyme A reductase; crotonyl coenzyme A reductase; crotonyl-CoA reductase; acyl-CoA dehydrogenase (NADP+). Enzyme Commission Number: EC 1.3.1.8. CAS No. 37251-07-3. 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-1349; acyl-CoA dehydrogenase (NADP+); EC 1.3.1.8; 37251-07-3; 2-enoyl-CoA reductase; dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide phosphate); enoyl coenzyme A reductase; crotonyl coenzyme A reductase; crotonyl-CoA reductase; acyl-CoA dehydrogenase (NADP+). Cat No: EXWM-1349. | |
| 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 (nicotinoprotein) | Contains Zn2+. Nicotinoprotein alcohol dehydrogenases are unique medium-chain dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a tightly bound NAD+/NADH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro.The enzyme from the Gram-positive bacterium Amycolatopsis methanolica can accept many primary alcohols as substrates, including benzylalcohol. Group: Enzymes. Synonyms: NDMA-dependent alcohol dehydrogenase; nicotinoprotein alcohol dehydrogenase; np-ADH; ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase. Enzyme Commission Number: EC 1.1.99.36. 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-0464; alcohol dehydrogenase (nicotinoprotein); EC 1.1.99.36; NDMA-dependent alcohol dehydrogenase; nicotinoprotein alcohol dehydrogenase; np-ADH; ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase. Cat No: EXWM-0464. | |
| 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. | |
| AZD4017 | AZD4017 is a potent, selective, and orally bioavailable11β-HSD1 inhibitor (11β-hydroxysteroid dehydrogenase type 1 inhibitor). Inhibition of 11β-HSD1 is an attractive mechanism for the treatment of obesity and other elements of the metabolic syndrome. AZD4017 is a nicotinic amide derived carboxylic acid class of inhibitors that has good potency, selectivity, and pharmacokinetic characteristics. AZD4017) is an effective inhibitor of 11β-HSD1 in human adipocytes and exhibits good druglike properties and as a consequence was selected for clinical development. Uses: Designed for use in research and industrial production. Additional or Alternative Names: AZD4017; AZD-4017; AZD 4017. Product Category: Inhibitors. Appearance: Solid powder. CAS No. 1024033-43-9. Molecular formula: C22H33N3O3S. Mole weight: 419.58. Purity: >98%. IUPACName: 2-[(3S)-1-[5-(cyclohexylcarbamoyl)-6-propylsulfanylpyridin-2-yl]-3-piperidyl]acetic acid. Canonical SMILES: O=C(O)C[C@H]1CN(C2=NC(SCCC)=C(C(NC3CCCCC3)=O)C=C2)CCC1. Product ID: ACM1024033439. Alfa Chemistry ISO 9001:2015 Certified. |  |
| β-NADH, Reduced Disodium Salt (Nicotinamide Adenine Dinucleotide) | Beta-nicotinamide adenine dinucleotide hydrate. Can be used as a cofactor in reactions with NAD-dependent histone deacetylase enzymes.NAD is a coenzyme formed from the nucleotide, nicotinamide, adenosine monophosphateand a phosphate group joining the first two components. NADP has the same structure with the addition of an extra phosphate group to AMP. NAD can be reduced to NADH during coupling with reactions which oxidize various organic substrates. For example, the reaction catalyzed by glyceraldehyde phosphate dehydrogenase during glycolysis. NADH then passes to the inside of mitochondria where it donates the electrons it is carrying to the electron tran...accomplished by the removal of hydrogen atoms. Both of these coenzymes play crucial roles in this. Each molecule of NAD+ (or NADP+) can acquire two electrons; that is, be reduced by two electrons. However, only one proton accompanies the reduction. The other proton produced as two hydrogen atoms are removed from the molecule being oxidized is liberated into the surrounding medium. Group: Biochemicals. Alternative Names: β-DPNH; β-NADH; DPNH; Diphosphopyridine nucleotide, reduced form; NADH. Grades: Highly Purified. CAS No. 606-68-8. Pack Sizes: 1g, 5g, 10g. Molecular Formula: C21H27N7O14P2Na2, Molecular Weight: 709.41. US Biological Life Sciences. | Worldwide |
| β-NADPH Tetrasodium Salt Hydrate | One of the biologically active forms of nicotinic acid. Differs from NAD by an additional phosphate group at the 2'-position of the adenosine moiety. Serves as a coenzyme of hydrogenases and dehydrogenases. Present in living cells primarily in the reduced form (NADPH) and is involved in synthetic reactions. Synonyms: 2'-(Dihydrogen Phosphate) 5'-(Trihydrogen Pyrophosphate)adenosine 5'5'-Ester 1,4-Dihydro-1-β-D-ribofuranosylnicotinamide Tetrasodium Salt Hydrate;β-NADPH; 2'-NADPH Hydrate; Coenzyme II Reduced Tetrasodium Salt Hydrate; Triphosphopyridine Nucleotide Reduced Tetrasodium Salt Hydrate; Dihydronicotinamide Adenine Dinucleotide Phosphate Tetrasodium Salt Hydrate. Grades: 95%. Molecular formula: C21H26N7Na4O17P3 XH2O. Mole weight: 833.35. |  |
| β-Nicotinamide-Adenine Dinucleotide Phosphate, Oxidized Form (β-NADP-K) | β-Nicotinamide adenine dinucleotide 2?-phosphate (NADP+) and β-Nicotinamide adenine dinucleotide 2?-phosphate, reduced (NADPH) comprise a coenzyme redox pair (NADP+:NADPH) involved in a wide range of enzyme catalyzed oxidation reduction reactions. The NADP+/NADPH redox pair facilitates electron transfer in anabolic reactions such as lipid and cholesterol biosynthesis and fatty acyl chain elongation. The NADP+/NADPH redox pair is used in a variety of antioxidation mechanism where it protects agains reactive oxidation species accumulation. NADPH is generated in vivio by the pentose phosphate pathway (PPP). Group: Coenzymes. Synonyms: β-Nicotinamide-Adenine Dinucleotide Phosphate, Oxidized Form (β-NADP-K); β-Nicotinamide-Adenine Dinucleotide Phosphate;. CAS No. 698999-85-8. Purity: Determined by increase in absorbance at 340nm on enzymatic reduction with G6PDH* at pH 10 (More than 95%) *G6PDH = Glucose-6-phosphate dehydrogenase (yeast) (EC 1.1.1.49.). β-NADP-K. Mole weight: 781.5. Storage: Keep tightly stoppered in the dark below 5°C. Moisture will reduce the purity. For prolonged storage, keep below-20°C. β-Nicotinamide-Adenine Dinucleotide Phosphate, Oxidized Form (β-NADP-K); β-Nicotinamide-Adenine Dinucleotide Phosphate; β-NADP-K. Cat No: NATE-0788. | |
| 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. | |
| b-Nicotinamide Adenine Dinucleotide Phosphate, reduced form, tetrasodium salt ( β-NADPH) | One of the biologically active forms of nicotinic acid. Differs from NAD by an additional phosphate group at the 2-position of the adenosine moiety. Serves as a coenzyme of hydrogenases and dehydrogenases. Present in living cells primarily in the reduced form (NADPH) and is involved in synthetic reactions. Group: Biochemicals. Alternative Names: 2'-(Dihydrogen Phosphate) 5'-(Trihydrogen Pyrophosphate) adenosine 5'5'-Ester 1,4-Dihydro-1- β -D-ribofuranosyl nicotinamide Tetrasodium Salt Hydrate; β-NADPH; 2?-NADPH Hydrate; Coenzyme II Reduced Tetrasodium Salt Hydrate; Triphosphopyridine Nucleotide Reduced Tetrasodium Salt Hydrate; Dihydronicotinamide Adenine Dinucleotide Phosphate Tetrasodium Salt Hydrate. Grades: Highly Purified. CAS No. 2646-71-1. Pack Sizes: 100mg, 250mg, 500mg, 1g. Molecular Formula: C??H??N?Na?O??P?; xH?O, Molecular Weight: 833.35. US Biological Life Sciences. | Worldwide |
| Chemically modified Glucose-6-phosphate Dehydrogenase from Leuconostoc mesenteroides | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Applications: Use glucose-6-phosphate dehydrogenase for the determination of blood glucose or creatine kinase. Group: Enzymes. Synonyms: D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glu. Glucose-6-phosphate dehydrogenase. Mole weight: 110 kD (2 identical subunits 55,000 D). Activity: >30 U/mg lyophilizate. Stability: At +2 to +8°C within specification range for 18 months. Store dry. Appearance: White lyophilizate. Source: E. coli. Species: Leuconostoc mesenteroides. EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase; 9001-40-5. Cat No: DIA-280. | |
| Cholesterol Dehydrogenase from Nocardia sp. | Cholesterol dehydrogenase is an enzyme that uses nicotinamide adenine dinucleotide/nicotinamide adenine dinucleotide phosphate (NAD(P)) as its cofactor in oxidizing cholesterol to form cholest-4-en-3-one. This enzyme oxidizes the hydroxyl group at the 3 position of the sterol ring to form a ketone. Group: Enzymes. Synonyms: Cholesterol Dehydrogenase; CDH. CAS No. 67775-34-2. Activity: 10U/mg-solid or more. Storage: at -20°C. Form: Freeze dried powder. Source: Nocardia sp. Cholesterol Dehydrogenase; CDH. Cat No: NATE-0892. | |
| cis-1,2-dihydrobenzene-1,2-diol dehydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydrobenzene-1,2-diol:NAD+ oxidoreductase. Other names in common use include cis-benzene glycol dehydrogenase, cis-1,2-dihydrocyclohexa-3,5-diene (nicotinamide adenine, and dinucleotide) oxidoreductase. This enzyme participates in 4 metabolic pathways: gamma-hexachlorocyclohexane degradation, toluene and xylene degradation, naphthalene and anthracene degradation, and styrene degradation. Group: Enzymes. Synonyms: cis-benzene glycol dehydrogenase; cis-1,2-dihydrocyclohexa-3,5-diene (nicotinamide adenine dinucleotide) oxidoreductase. Enzyme Commission Number: EC 1.3.1.19. CAS No. 51923-03-6. 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-1293; cis-1,2-dihydrobenzene-1,2-diol dehydrogenase; EC 1.3.1.19; 51923-03-6; cis-benzene glycol dehydrogenase; cis-1,2-dihydrocyclohexa-3,5-diene (nicotinamide adenine dinucleotide) oxidoreductase. Cat No: EXWM-1293. | |
| dihydropyrimidine dehydrogenase (NADP+) | Also acts on dihydrothymine. Group: Enzymes. Synonyms: dihydrothymine dehydrogenase; dihydrouracil dehydrogenase (NADP+); 4,5-dihydrothymine: oxidoreductase; DPD; DHPDH; dehydrogenase, dihydrouracil (nicotinamide adenine dinucleotide phosphate); DHU dehydrogenase; hydropyrimidine dehydrogenase; dihydropyrimidine dehydrogenase (NADP). Enzyme Commission Number: EC 1.3.1.2. CAS No. 9029-01-0. 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-1294; dihydropyrimidine dehydrogenase (NADP+); EC 1.3.1.2; 9029-01-0; dihydrothymine dehydrogenase; dihydrouracil dehydrogenase (NADP+); 4,5-dihydrothymine: oxidoreductase; DPD; DHPDH; dehydrogenase, dihydrouracil (nicotinamide adenine dinucleotide phosphate); DHU dehydrogenase; hydropyrimidine dehydrogenase; dihydropyrimidine dehydrogenase (NADP). Cat No: EXWM-1294. | |
| DT Diaphorase from human, Recombinant | DT Diaphorase is a flavoenzyme that catalyzes the oxidation of reduced di-and triphosphopyridine nucleotides. It contains one mole of FAD per mole of enzyme. The enzyme found in rat liver catalyzes the oxidation of NADH and NADPH by various dyes and quinones. The molecular weight is found to be approximately 48 kDa Da. The pH optimum of the enzyme purified from rat liver is found to be 5.0. It is a cytosolic enzyme that catalyzes the two-electron reduction of various quinones. It catalyzes the conversion of vitamin K to vitamin K hydroquinone for utilization in the post-translational γ-glutamyl carboxylation reactions. These reactions are necessary for several proteins involved in blood coagulation. Applications: Human dt diaphorase has been used in a study to assess the development of novel quinone phosphorodiamidate prodrugs. human dt diaphorase has also been used to investigate its crystal structure for the development of a model for its interaction with the cytotoxic prodrug 5-(aziridin-1-yl)-2,4-dinitrobenzamide (cb1954). Group: Enzymes. Synonyms: menadione reductase; phylloquinone reductase; quinone reductase; dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone); DT-diaphorase; flavoprotein NAD (P)H-q. Enzyme Commission Number: EC 1.6.99.2. Diaphorase. Mole weight: monomer mol wt 31 kDa. Storage: 2-8°C. F | |
| DT Diaphorase from rat, Recombinant | DT Diaphorase is a flavoenzyme that catalyzes the oxidation of reduced di-and triphosphopyridine nucleotides. It contains one mole of FAD per mole of enzyme. The enzyme found in rat liver catalyzes the oxidation of NADH and NADPH by various dyes and quinones. The molecular weight is found to be approximately 48 kDa Da. The pH optimum of the enzyme purified from rat liver is found to be 5.0. It is a cytosolic enzyme that catalyzes the two-electron reduction of various quinones. It catalyzes the conversion of vitamin K to vitamin K hydroquinone for utilization in the post-translational γ-glutamyl carboxylation reactions. These reactions are necessary for several proteins involved in blood coagulation. Applications: Dt diaphorase from rat has been used in a study to investigate the two-electron reduction of quinones by rat liver. dt diaphorase from rat has also been used in a study to investigate colon cancer chemopreventive efficacy of silibinin through perturbation of xenobiotic metabolizing enzymes. Group: Enzymes. Synonyms: menadione reductase; phylloquinone reductase; quinone reductase; dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone); DT-diaphorase; flavoprotein NAD (P)H-qui. Enzyme Commission Number: EC 1.6.99.2. Purity: ~90% (SDS-PAGE). Diaphorase. Mole weight: monomer mol wt 31 kDa. Storage: 2-8°C. Form | |
| D-xylose 1-dehydrogenase (NADP+) | Also acts, more slowly, on L-arabinose and D-ribose. Group: Enzymes. Synonyms: D-xylose (nicotinamide adenine dinucleotide phosphate) dehydrogenase; D-xylose-NADP dehydrogenase; D-xylose:NADP+ oxidoreductase; D-xylose 1-dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.179. CAS No. 83534-37-6. 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-0082; D-xylose 1-dehydrogenase (NADP+); EC 1.1.1.179; 83534-37-6; D-xylose (nicotinamide adenine dinucleotide phosphate) dehydrogenase; D-xylose-NADP dehydrogenase; D-xylose:NADP+ oxidoreductase; D-xylose 1-dehydrogenase (NADP). Cat No: EXWM-0082. | |
| enoyl-[acyl-carrier-protein] reductase (NADPH) | The enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to the acyl-carrier protein, in an NADPH-dependent manner. This entry stands for enzymes whose stereo-specificity with respect to NADP+ is not known. [cf. EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific), EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH)]. Group: Enzymes. Synonyms: acyl-ACP dehydrogenase (ambiguous); enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl-ACP reductase (ambiguous); fabL (gene name). Enzyme Commission Number: EC 1.3.1.104. 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-1276; enoyl-[acyl-carrier-protein] reductase (NADPH); EC 1.3.1.104; acyl-ACP dehydrogenase (ambiguous); enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl-ACP reductase (ambiguous); fabL (gene name). Cat No: EXWM-1276. | |
| enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) | This enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to an acyl-carrier protein. It is one of the activities of EC 2.3.1.85, animal fatty-acid synthase. The mammalian enzyme is Re-specific with respect to NADP+. cf. EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH). Group: Enzymes. Synonyms: acyl-ACP dehydrogenase; enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase. Enzyme Commission Number: EC 1.3.1.39. 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-1311; enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific); EC 1.3.1.39; acyl-ACP dehydrogenase; enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl-ACp reductase; enoyl-[acyl-carrier-protein] reductase (NADPH2, A-specific); acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (A-specific); enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific); acyl-[acyl-carrier protein]:NADP+ oxidoreductase (A-specific). Cat No: EXWM-1311. | |
| enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) | One of the activities of EC 2.3.1.86, fatty-acyl-CoA synthase, an enzyme found in yeasts (Ascomycota and the Basidiomycota). Catalyses the reduction of enoyl-acyl-[acyl-carrier protein] derivatives of carbon chain length from 4 to 16. The yeast enzyme is Si-specific with respect to NADP+. cf. EC 1.3.1.39, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH), which describes enzymes whose stereo-specificity towards NADPH is not known. See also EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH). Group: Enzymes. Synonyms: acy. Enzyme Commission Number: EC 1.3.1.10. CAS No. 37251-09-5. 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-1271; enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific); EC 1.3.1.10; 37251-09-5; acyl-ACP dehydrogenase (ambiguous); enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl acyl-carrier-protein reductase (ambiguous); enoyl-ACP reductase (ambiguous); acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (B-specific); acyl-[acyl-carrier protein]:NADP+ oxidoreductase (B-specific); enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific). Cat No: EXWM-1271. | |
| farnesol dehydrogenase (NADP+) | Also acts, more slowly, on (2Z,6E)-farnesol, geraniol, citronerol and nerol. Group: Enzymes. Synonyms: NADP+-farnesol dehydrogenase; farnesol (nicotinamide adenine dinucleotide phosphate) dehydrogenase. Enzyme Commission Number: EC 1.1.1.216. CAS No. 89089-75-8, 90804-55-0. 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-0121; farnesol dehydrogenase (NADP+); EC 1.1.1.216; 89089-75-8, 90804-55-0; NADP+-farnesol dehydrogenase; farnesol (nicotinamide adenine dinucleotide phosphate) dehydrogenase. Cat No: EXWM-0121. | |
| Farudodstat | Farudodstat is an orally active and potent inhibitor of DHODH (human dihydroorotate dehydrogenase). It inhibits the proliferation of MOLM-14 and KG-1 acute myeloid leukemia (AML) cells (IC50s = 0.582 and 0.382 μM, respectively), as well as induces apoptosis in the same cells when used at concentrations of 0.5 and 1 μM. Synonyms: 2-[(3,5-difluoro-3'-methoxy-[1,1'-biphenyl]-4-yl)amino]pyridine-3-carboxylic acid; ASLAN003; 2-[(3,5-Difluoro-3'-methoxy-4-biphenylyl)amino]nicotinic Acid; 3-Pyridinecarboxylic acid, 2-[(3,5-difluoro-3'-methoxy-[1,1'-biphenyl]-4-yl)amino]-; 2-((3,5-Difluoro-3'-methoxy-[1,1'-biphenyl]-4-yl)amino)nicotinic acid; 2-[(3,5-difluoro-3'-methoxy[1,1'-biphenyl]-4-yl)amino]-3-pyridinecarboxylic acid. Grades: ≥98%. CAS No. 1035688-66-4. Molecular formula: C19H14F2N2O3. Mole weight: 356.32. | |
| flavin reductase (NADPH) | The enzyme reduces riboflavin, and, less efficiently, FMN and FAD. NADH is oxidized less efficiently than NADPH. Group: Enzymes. Synonyms: NADPH:flavin oxidoreductase; riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide phosphate) reductase; flavin mononucleotide reductase; flavine mononucleotide reductase; FMN reductase (NADPH); NADPH-dependent FMN reductase; NADPH-flavin reductase; NADPH-FMN reductase; NADPH-specific FMN reductase; riboflavin mononucleotide reductase; riboflavine mononucleotide reductase; NADPH2 dehydrogenase (flavin); NADPH2:riboflavin oxidoreductase. Enzyme Commission Number: EC 1.5.1.30. CAS No. 56626-29-0. 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-1512; flavin reductase (NADPH); EC 1.5.1.30; 56626-29-0; NADPH:flavin oxidoreductase; riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide phosphate) reductase; flavin mononucleotide reductase; flavine mononucleotide reductase; FMN reductase (NADPH); NADPH-dependent FMN reductase; NADPH-flavin reductase; NADPH-FMN reductase; NADPH-specific FMN reductase; riboflavin mononucleotide reductase; riboflavine mononucleotide reductase; NADPH2 dehydrogenase (flavin); NADPH2:riboflavin oxidoreductase. Cat No: EXWM-1512. | |
| formaldehyde dismutase | The enzyme contains a tightly but noncovalently bound NADP(H) cofactor, as well as Zn2+ and Mg2+. Enzyme-bound NADPH formed by oxidation of formaldehyde to formate is oxidized back to NADP+ by reaction with a second formaldehyde, yielding methanol. The enzyme from the bacterium Mycobacterium sp. DSM 3803 also catalyses the reactions of EC 1.1.99.36, alcohol dehydrogenase (nicotinoprotein) and EC 1.1.99.37, methanol dehydrogenase (nicotinoprotein). Formaldehyde and acetaldehyde can act as donors; formaldehyde, acetaldehyde and propanal can act as acceptors. Group: Enzymes. Synonyms: aldehyde dismutase; cannizzanase; nicotinoprotein aldehyde dismutase. Enzyme Commission Number: EC 1.2.98.1. CAS No. 85204-94-0. 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-1232; formaldehyde dismutase; EC 1.2.98.1; 85204-94-0; aldehyde dismutase; cannizzanase; nicotinoprotein aldehyde dismutase. Cat No: EXWM-1232. | |
| fructose 5-dehydrogenase (NADP+) | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-fructose:NADP+ 5-oxidoreductase. Other names in common use include 5-ketofructose reductase (NADP+), 5-keto-D-fructose reductase (NADP+), fructose 5-(nicotinamide adenine dinucleotide phosphate), dehydrogenase, D-(-)fructose:(NADP+) 5-oxidoreductase, and fructose 5-dehydrogenase (NADP+). Group: Enzymes. Synonyms: 5-ketofructose reductase (NADP); 5-keto-D-fructose reductase (NADP+); fructose 5-(nicotinamide adenine dinucleotide phosphate) dehydrogenase; D-(-)fructose:(NADP+) 5-oxidoreductase; fructose 5-dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.124. CAS No. 37250-53-6. 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-0028; fructose 5-dehydrogenase (NADP+); EC 1.1.1.124; 37250-53-6; 5-ketofructose reductase (NADP); 5-keto-D-fructose reductase (NADP+); fructose 5-(nicotinamide adenine dinucleotide phosphate) dehydrogenase; D-(-)fructose:(NADP+) 5-oxidoreductase; fructose 5-dehydrogenase (NADP). Cat No: EXWM-0028. | |
| GAPDH, rabbit muscle | Glyceraldehyde phosphate dehydrogenase (EC 1.2.1.12) is the target of anti-thymocyte and anti-apoptotic agents. Glyceraldehyde phosphate dehydrogenase catalyzes the chain oxidation of reduced nicotinamide adenine dinucleotide by perhydroxyl radicals [1] [2]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: GADPH; G3PDH; Glyceraldehyde phosphate dehydrogenase. CAS No. 9001-50-7. Pack Sizes: 100 U; 500 U. Product ID: HY-P2804. |  |
| glucose 1-dehydrogenase (NADP+) | Also oxidizes D-mannose, 2-deoxy-D-glucose and 2-amino-2-deoxy-D-mannose. Group: Enzymes. Synonyms: nicotinamide adenine dinucleotide phosphate-linked aldohexose dehydrogenase; NADP-linked aldohexose dehydrogenase; NADP-dependent glucose dehydrogenase; glucose 1-dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.119. CAS No. 37250-50-3. 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-0022; glucose 1-dehydrogenase (NADP+); EC 1.1.1.119; 37250-50-3; nicotinamide adenine dinucleotide phosphate-linked aldohexose dehydrogenase; NADP-linked aldohexose dehydrogenase; NADP-dependent glucose dehydrogenase; glucose 1-dehydrogenase (NADP). Cat No: EXWM-0022. | |
| Glucose-6-phosphate Dehydrogenase from E. coli, Recombinant | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Group: Enzymes. Synonyms: EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate . Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Mole weight: ~ 56,770. Activity: 172 U/mg. Stability: > 2 years. Storage: 4°C. Form: In 3.2 M ammonium sulphate. Source: E. coli. Species: E. coli. EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase; 9001-40-5. Cat No: DIA-407. | |
| glutamate dehydrogenase (NADP+) | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. Group: Enzymes. Synonyms: glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP). Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. 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-1459; glutamate dehydrogenase (NADP+); EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP). Cat No: EXWM-1459. | |
| Glutamate Dehydrogenase (NAD(P)) from E.coli, Recombinant | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Applications: Use recombinant glutamate dehydrogenase in diagnostic tests for the determination of ammonia, urea, l-glutamate, glutamate pyruvate transaminase and leucine aminopeptidase. Group: Enzymes. Synonyms: glu. CAS No. 9029-12-3. GLDH. Mole weight: ~2 200 kD for the associated enzyme with 8 subunits; 280 kD for one subunit. Activity: >80 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White lyophilizate. Source: E.coli. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: NATE-0981. | |
| glutamate synthase (NADPH) | Binds FMN, FAD, 2 [4Fe-4S] clusters and 1 [3Fe-4S] cluster. The reaction takes place in the opposite direction to that shown. The protein is composed of two subunits, α and &beta. The α subunit is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.4, glutamate dehydrogenase [NADP+]). The β subunit transfers electrons to the cosubstrate. The NH3 is channeled through a 31 ? channel in the active protein. In the absence of the β subunit, coupling between the two domains of the α subunit...mmission Number: EC 1.4.1.13. CAS No. 37213-53-9. 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-1446; glutamate synthase (NADPH); EC 1.4.1.13; 37213-53-9; glutamate (reduced nicotinamide adenine dinucleotide phosphate) synthase; L-glutamate synthase; L-glutamate synthetase; glutamate synthetase (NADP); NADPH-dependent glutamate synthase; glutamine-ketoglutaric aminotransferase; NADPH-glutamate synthase; NADPH-linked glutamate synthase; glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP); L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing; GOGAT. Cat No: EXWM-1446. | |
| glyceraldehyde-3-phosphate dehydrogenase (NADP+) | Glyceraldehyde-3-phosphate dehydrogenase (NADP+) (EC 1.2.1.9) (GAPN) is an enzyme that irreversibly catalyzes the oxidation of glyceraldehyde-3-phosphate (GAP) to 3-phosphoglycerate (3-PG or 3-PGA) using the reduction of NADP+ to NADPH. GAPN is used in a variant of glycolysis that conserves energy as NADPH rather than as ATP. The NADPH and 3-PG can then be used for synthesis. The most familiar variant of glycolysis uses glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoglycerate kinase to produce ATP. GAPDH is phosphorylating. GAPN is non-phosphorylating. GAPN was reported first by Rosenberg and Arnon in 1954. It has been found in plants, algae, and bacteria... it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1193; glyceraldehyde-3-phosphate dehydrogenase (NADP+); EC 1.2.1.9; 9028-92-6; triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate); glyceraldehyde phosphate dehydrogenase (NADP); glyceraldehyde 3-phosphate dehydrogenase (NADP); NADP-glyceraldehyde phosphate dehydrogenase; NADP-glyceraldehyde-3-phosphate dehydrogenase; glyceraldehyde-3-phosphate:NADP reductase; nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase; glyceraldehyde-3-phosphate dehydrogenase (NADP). Cat No: EXWM-1193. | |
| glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) | 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 the Calvin cycle which is an autotrophic carbon fixation pathway. Group: Enzymes. Synonyms: triosephosphate dehydrogenase (NADP+); dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate) (phosphorylating); glyceraldehyde phosphate dehydrogenase (nicotinamide adenine dinucleotide phosphate) (phosphoryla. Enzyme Commission Number: EC 1.2.1.13. CAS No. 37250-87-6. 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-1119; glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating); EC 1.2.1.13; 37250-87-6; triosephosphate dehydrogenase (NADP+); dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate) (phosphorylating); glyceraldehyde phosphate dehydrogenase (nicotinamide adenine dinucleotide phosphate) (phosphorylating); NADP+-glyceraldehyde-3-phosphate dehydrogenase; NADP+-glyceraldehyde phosphate dehydrogenase; NADP+-dependent glyceraldehyde phosphate dehydrogenase; NADP+-triose phosphate dehydrogenase; glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating); GAPDH. Cat No: EXWM-1119. | |
| glycerol 2-dehydrogenase (NADP+) | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glycerol:NADP+ 2-oxidoreductase (glycerone-forming). Other names in common use include dihydroxyacetone reductase, dihydroxyacetone (reduced nicotinamide adenine dinucleotide, phosphate) reductase, dihydroxyacetone reductase (NADPH), DHA oxidoreductase, and glycerol 2-dehydrogenase (NADP+). This enzyme participates in glycerolipid metabolism. Group: Enzymes. Synonyms: dihydroxyacetone reductase; dihydroxyacetone (reduced nicotinamide adenine dinucleotide phosphate) reductase; dihydroxyacetone reductase (NADPH); DHA oxidoreductase; glycerol 2-dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.156. CAS No. 39342-20-6. 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-0060; glycerol 2-dehydrogenase (NADP+); EC 1.1.1.156; 39342-20-6; dihydroxyacetone reductase; dihydroxyacetone (reduced nicotinamide adenine dinucleotide phosphate) reductase; dihydroxyacetone reductase (NADPH); DHA oxidoreductase; glycerol 2-dehydrogenase (NADP). Cat No: EXWM-0060. | |
| glycerol-3-phosphate 1-dehydrogenase (NADP+) | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is sn-glycerol-3-phosphate:NADP+ 1-oxidoreductase. Other names in common use include glycerol phosphate (nicotinamide adenine dinucleotide phosphate), dehydrogenase, L-glycerol 3-phosphate:NADP+ oxidoreductase, glycerin-3-phosphate dehydrogenase, NADPH-dependent glycerin-3-phosphate dehydrogenase, and glycerol-3-phosphate 1-dehydrogenase (NADP+). Group: Enzymes. Synonyms: glycerol phosphate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; L-glycerol 3-phosphate:NADP+ oxidoreductase; glycerin-3-phosphate dehydrogenase; NADPH-dependent glycerin-3-phosphate dehydrogenase; NADP-specific glycerol 3-phosp. Enzyme Commission Number: EC 1.1.1.177. CAS No. 37213-46-0. 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-0080; glycerol-3-phosphate 1-dehydrogenase (NADP+); EC 1.1.1.177; 37213-46-0; glycerol phosphate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; L-glycerol 3-phosphate:NADP+ oxidoreductase; glycerin-3-phosphate dehydrogenase; NADPH-dependent glycerin-3-phosphate dehydrogenase; NADP-specific glycerol 3-phosphate 1-dehydrogenase. Cat No: EXWM-0080. | |
| glycerol-3-phosphate dehydrogenase [NAD(P)+] | The enzyme from Escherichia coli shows specificity for the B side of NADPH. Group: Enzymes. Synonyms: L-glycerol-3-phosphate:NAD(P) oxidoreductase; glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide (phosphate)); glycerol 3-phosphate dehydrogenase (NADP); glycerol-3-phosphate dehydrogenase [NAD(P)]. Enzyme Commission Number: EC 1.1.1.94. CAS No. 37250-30-9. 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-0378; glycerol-3-phosphate dehydrogenase [NAD(P)+]; EC 1.1.1.94; 37250-30-9; L-glycerol-3-phosphate:NAD(P) oxidoreductase; glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide (phosphate)); glycerol 3-phosphate dehydrogenase (NADP); glycerol-3-phosphate dehydrogenase [NAD(P)]. Cat No: EXWM-0378. | |
| isocitrate dehydrogenase (NAD+) | Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.42, isocitrate dehydrogenase (NADP+), oxalosuccinate cannot be used as a substrate. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD+-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP+-linked enzyme that is found in both mitochondria and cytoplasm. The enzyme from some species can also use NADP+ but much more slowly. Group: Enzymes. Synonyms: isocitric dehydrogenase; β-ketoglutaric-isocitric carboxylase; isocitric acid dehydrogenase; NAD dependent isocitrate dehydrogenase; NAD isocitrate dehydrogenase; NAD-linked isocitrate dehydrogenase; NAD-specific isocitrate dehydr. Enzyme Commission Number: EC 1.1.1.41. CAS No. 9001-58-5. IDH. 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-0326; isocitrate dehydrogenase (NAD+); EC 1.1.1.41; 9001-58-5; isocitric dehydrogenase; β-ketoglutaric-isocitric carboxylase; isocitric acid dehydrogenase; NAD dependent isocitrate dehydrogenase; NAD isocitrate dehydrogenase; NAD-linked isocitrate dehydrogenase; NAD-specific isocitrate dehydrogenase; NAD isocitric dehydrogenase; isocitrate dehydrogenase (NAD); IDH (ambiguous); nicotinamide adenine dinucleotide isocitrate dehydrogenase. Cat No: EXWM-0326. | |
| Isocitrate dehydrogenase (NAD+) from Bacteria, Recombinant | Isocitrate dehydrogenase (IDH) is an enzyme that catalyzes the oxidative decarboxylation of Isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2. This is a two-step process, which involves oxidation of Isocitrate (a secondary alcohol) to oxalosuccinate (a ketone), followed by the decarboxylation of the carboxyl group beta to the ketone, forming alpha-ketoglutarate. In humans, IDH exists in three isoforms:IDH3 catalyzes the third step of the citric acid cycle while converting NAD+ to NADH in the mitochondria. The isoforms IDH1 and IDH2 catalyze the same reaction outside the context of the citric acid cycle and use NADP+ as a cofactor instead o...namide adenine dinucleotide Isocitrate dehydrogenase; EC 1.1.1.41. Enzyme Commission Number: EC 1.1.1.41. CAS No. 9001-58-5. IDH. Mole weight: 40 kD (SDS-PAGE). Activity: > 40 Units / mg. Storage: Below -20°C. Form: Lyophilized powder. Source: E. coli. Species: Bacteria. Beta-ketoglutaric-isocitric carboxylase; IDH; Isocitrate dehydrogenase (NAD); Isocitric acid dehydrogenase; Isocitric dehydrogenase; NAD dependent Isocitrate dehydrogenase; NAD Isocitrate dehydrogenase; NAD isocitric dehydrogenase; NAD-linked Isocitrate dehydrogenase; NAD-specific Isocitrate dehydrogenase; Nicotinamide adenine dinucleotide Isocitrate dehydrogenase; EC 1.1.1.41. Cat No: NATE-1041. | |
| isocitrate dehydrogenase (NADP+) | Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+), oxalosuccinate can be used as a substrate. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD+-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP+-linked enzyme that is found in both mitochondria and cytoplasm. The enzyme from some species can also use NAD+ but much more slowly. Group: Enzymes. Synonyms: ox. Enzyme Commission Number: EC 1.1.1.42. CAS No. 9028-48-2. IDH. 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-0327; isocitrate dehydrogenase (NADP+); EC 1.1.1.42; 9028-48-2; oxalosuccinate decarboxylase; oxalsuccinic decarboxylase; isocitrate (NADP) dehydrogenase; isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; NADP-specific isocitrate dehydrogenase; NADP-linked isocitrate dehydrogenase; NADP-dependent isocitrate dehydrogenase; NADP isocitric dehydrogenase; isocitrate dehydrogenase (NADP-dependent); NADP-dependent isocitric dehydrogenase; triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase; NADP+-linked isocitrate dehydrogenase; IDH (ambiguous); dual-cofactor-specific isocitrate dehydrogenase; NADP+-ICDH; NADP+-IDH; IDP; IDP1; IDP2; IDP3. | |
| Isocitrate Dehydrogenase (NADP+) from Bacteria, Recombinant | Isocitrate dehydrogenase (IDH) (EC 1.1.1.42) is an enzyme that catalyzes the oxidative decarboxylation of Isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2. This is a two-step process, which involves oxidation of Isocitrate (a secondary alcohol) to oxalosuccinate (a ketone), followed by the decarboxylation of the carboxyl group beta to the ketone, forming alpha-ketoglutarate. In humans, IDH exists in three isoforms:IDH3 catalyzes the third step of the citric acid cycle while converting NAD+ to NADH in the mitochondria. The isoforms IDH1 and IDH2 catalyze the same reaction outside the context of the citric acid cycle and use NADP+ as a cof...rogenase (NADP+); EC 1.1.1.42; IDH; Isocitrate Dehydrogenase; Dual-cofactor-specific Isocitrate dehydrogenase; IDP; Isocitrate (NADP) dehydrogenase; Isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; Isocitrate dehydrogenase (NADP); Isocitrate dehydrogenase (NADP-dependent); NADP isocitric dehydrogenase; NADP (+)-ICDH; NADP (+)-IDH; NADP (+)-linked Isocitrate dehydrogenase; NADP-dependent Isocitrate dehydrogenase; NADP-dependent isocitric dehydrogenase; NADP-linked Isocitrate dehydrogenase; NADP-specific Isocitrate dehydrogenase; Oxalosuccinate decarboxylase; Oxalsuccinic decarboxylase; Triphosphopyridine nucleotide-linked Isocitrate dehydrog | |
| Isocitrate Dehydrogenase (NADP+) from Yeast, Recombinant | Isocitrate dehydrogenase (IDH) (EC 1.1.1.42) is an enzyme that catalyzes the oxidative decarboxylation of Isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2. This is a two-step process, which involves oxidation of Isocitrate (a secondary alcohol) to oxalosuccinate (a ketone), followed by the decarboxylation of the carboxyl group beta to the ketone, forming alpha-ketoglutarate. In humans, IDH exists in three isoforms:IDH3 catalyzes the third step of the citric acid cycle while converting NAD+ to NADH in the mitochondria. The isoforms IDH1 and IDH2 catalyze the same reaction outside the context of the citric acid cycle and use NADP+ as a cofactor instead of NAD+. They localize to the cytosol as well as the mitochondrion and peroxisome. Group: Enzymes. Synonyms: Isocitrate Dehydrogenase (NADP+); EC 1.1.1.42; IDH; Isocitrate . Enzyme Commission Number: EC 1.1.1.42. CAS No. 9028-48-2. IDH. Activity: r-ICDH activity = 100%. Storage: -20°C. Form: Liquid. Source: Pichia pastoris. Species: Yeast. Isocitrate Dehydrogenase (NADP+); EC 1.1.1.42; IDH; Isocitrate Dehydrogenase; Dual-cofactor-specific Isocitrate dehydrogenase; IDP; Isocitrate (NADP) dehydrogenase; Isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; Isocitrate dehydrogenase (NADP); Isocitrate dehydrogenase (NADP-dependent); NADP | |
| lactaldehyde 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 (S)-lactaldehyde:NAD+ oxidoreductase. Other names in common use include L-lactaldehyde:NAD+ oxidoreductase, and nicotinamide adenine dinucleotide (NAD+)-linked dehydrogenase. This enzyme participates in pyruvate metabolism. Group: Enzymes. Synonyms: L-lactaldehyde:NAD oxidoreductase; nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase. Enzyme Commission Number: EC 1.2.1.22. CAS No. 37250-90-1. Lactaldehyde 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-1128; lactaldehyde dehydrogenase; EC 1.2.1.22; 37250-90-1; L-lactaldehyde:NAD oxidoreductase; nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase. Cat No: EXWM-1128. | |
| Lactaldehyde dehydrogenase from Escherichia coli, Recombinant | In enzymology, a lactaldehyde dehydrogenase (EC 1.2.1.22) is an enzyme that catalyzes the chemical reaction: (S)-lactaldehyde + NAD+ + H2O <-> (S)-lactate + NADH + 2 H+. The 3 substrates of this enzyme are (S)-lactaldehyde, NAD+, and H2O, whereas its 3 products are (S)-lactate, NADH, and H+. 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. Group: Enzymes. Synonyms: E.C. 1.2.1.22; lactaldehyde dehydrogenase; L-lactaldehyde:NAD oxidoreductase; nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase; (S)-lactaldehyde:NAD+ oxidoreductase. Enzyme Commission Number: EC 1.2.1.22. CAS No. 37250-90-1. Lactaldehyde dehydrogenase. Mole weight: 53337.9 Da. Source: Escherichia coli. E.C. 1.2.1.22; lactaldehyde dehydrogenase; L-lactaldehyde:NAD oxidoreductase; nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase; (S)-lactaldehyde:NAD+ oxidoreductase. Cat No: NATE-1213. | |
| lactaldehyde reductase (NADPH) | May be identical with EC 1.1.1.2 alcohol dehydrogenase (NADP+). Group: Enzymes. Synonyms: lactaldehyde (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADP-1,2-propanediol dehydrogenase; propanediol dehydrogenase; 1,2-propanediol:NADP+ oxidoreductase; lactaldehyde reductase (NADPH2). Enzyme Commission Number: EC 1.1.1.55. CAS No. 9028-43-7. 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-0340; lactaldehyde reductase (NADPH); EC 1.1.1.55; 9028-43-7; lactaldehyde (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADP-1,2-propanediol dehydrogenase; propanediol dehydrogenase; 1,2-propanediol:NADP+ oxidoreductase; lactaldehyde reductase (NADPH2). Cat No: EXWM-0340. | |
| L-aminoadipate-semialdehyde dehydrogenase | (S)-2-amino-6-oxohexanoate undergoes a spontaneous dehydration forming the cyclic (S)-2,3,4,5-tetrahydropyridine-2-carboxylate, which serves as a substrate for the hydrogenation reaction. Group: Enzymes. Synonyms: aminoadipate semialdehyde dehydrogenase; 2-aminoadipate semialdehyde dehydrogenase; α-aminoadipate-semialdehyde dehydrogenase; α-aminoadipate reductase; 2-aminoadipic semialdehyde dehydrogenase; L-α-aminoadipate Δ-semialdehyde oxidoreductase; L-α-aminoadipate Δ-semialdehyde:NAD+ oxidoreductase; L-α-aminoadipate Δ-semialdehyde:. Enzyme Commission Number: EC 1.2.1.31. CAS No. 9067-87-2. 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-1138; L-aminoadipate-semialdehyde dehydrogenase; EC 1.2.1.31; 9067-87-2; aminoadipate semialdehyde dehydrogenase; 2-aminoadipate semialdehyde dehydrogenase; α-aminoadipate-semialdehyde dehydrogenase; α-aminoadipate reductase; 2-aminoadipic semialdehyde dehydrogenase; L-α-aminoadipate Δ-semialdehyde oxidoreductase; L-α-aminoadipate Δ-semialdehyde:NAD+ oxidoreductase; L-α-aminoadipate Δ-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase; L-2-aminoadipate 6-semialdehyde:NAD(P)+ 6-oxidoreductase. Cat No: EXWM-1138. | |
| Leuconostoc mesenteroides Glucose-6-phosphate Dehydrogenase, Recombinant | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Glucose 6-phosphate dehydrogenase (g-6-p-dh) is a key regulatory enzyme in the first step of the pentose phosphate pathway. g-6-p-dh is a glycoprotein with a molecular mass of 128 kda (gel filtration). Applications: Glucose-6-phosphate...its/mg protein (biuret). Storage: 2-8°C. Form: Type I, Lyophilized powder containing Ficoll and Tris buffer salts; Type II, ammonium sulfate suspension, Supplied in 3.2M ammonium sulfate containing 50mM Tris and 1mM magnesium chloride, pH 7.5. Source: E. coli. Species: Leuconostoc mesenteroides. EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase; 9001-40-5. Cat No: DIA-323. | |
| L-glycol dehydrogenase | The 2-hydroxycarbonyl compound formed can be further oxidized to a vicinal dicarbonyl compound. In the reverse direction, vicinal diketones, glyceraldehyde, glyoxal, methylglyoxal, 2-oxo-hydroxyketones and 2-ketoacid esters can be reduced. Group: Enzymes. Synonyms: glycol (nicotinamide adenine dinucleotide (phosphate)) dehydrogenase; L-(+)-glycol:NAD(P) oxidoreductase; L-glycol:NAD(P) dehydrogenase. Enzyme Commission Number: EC 1.1.1.185. CAS No. 77967-75-0. 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-0087; L-glycol dehydrogenase; EC 1.1.1.185; 77967-75-0; glycol (nicotinamide adenine dinucleotide (phosphate)) dehydrogenase; L-(+)-glycol:NAD(P) oxidoreductase; L-glycol:NAD(P) dehydrogenase. Cat No: EXWM-0087. | |
| malate dehydrogenase (NADP+) | Activated by light. Group: Enzymes. Synonyms: NADP-malic enzyme; NADP-malate dehydrogenase; malic dehydrogenase (nicotinamide adenine dinucleotide phosphate); malate NADP dehydrogenase; NADP malate dehydrogenase; NADP-linked malate dehydrogenase; malate dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.82. CAS No. 37250-19-4. 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-0366; malate dehydrogenase (NADP+); EC 1.1.1.82; 37250-19-4; NADP-malic enzyme; NADP-malate dehydrogenase; malic dehydrogenase (nicotinamide adenine dinucleotide phosphate); malate NADP dehydrogenase; NADP malate dehydrogenase; NADP-linked malate dehydrogenase; malate dehydrogenase (NADP). Cat No: EXWM-0366. | |
| mannuronate reductase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-mannonate:NAD(P)+ 6-oxidoreductase. Other names in common use include mannonate dehydrogenase, mannonate (nicotinamide adenine dinucleotide, (phosphate))dehydrogenase, mannonate dehydrogenase, mannuronate reductase, mannonate dehydrogenase (NAD(P)+), D-mannonate:nicotinamide adenine dinucleotide (phosphate, and oxidoreductase (D-mannuronate-forming)). Group: Enzymes. Synonyms: mannonate dehydrogenase; mannonate (nicotinamide adenine dinucleotide (phosphate))dehydrogenase; mannonate dehydrogenase; mannuronate reductase; mannonate dehydrogenase (NAD(P)+); D-mannonate:nicotinamide adenine dinucleotide (phosphate oxidoreductase (D-mannuronate. Enzyme Commission Number: EC 1.1.1.131. CAS No. 37250-62-7. 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-0035; mannuronate reductase; EC 1.1.1.131; 37250-62-7; mannonate dehydrogenase; mannonate (nicotinamide adenine dinucleotide (phosphate))dehydrogenase; mannonate dehydrogenase; mannuronate reductase; mannonate dehydrogenase (NAD(P)+); D-mannonate:nicotinamide adenine dinucleotide (phosphate oxidoreductase (D-mannuronate-forming)). Cat No: EXWM-0035. | |
| methanol dehydrogenase (nicotinoprotein) | Contains Zn2+ and Mg2+. Nicotinoprotein methanol dehydrogenases have a tightly bound NADP+/NADPH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro. The enzyme has been detected in several Gram-positive methylotrophic bacteria, including Amycolatopsis methanolica, Rhodococcus rhodochrous and Rhodococcus erythropolis. These enzymes are decameric, and possess a 5-fold symmetry. Some of the enzymes can also dismutate formaldehyde to methanol and formate. Group: Enzymes. Synonyms: NDMA-dependent methanol dehydrogenase; nicotinoprotein methanol dehydrogenase; methanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase. Enzyme Commission Number: EC 1.1.99.37. 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-0465; methanol dehydrogenase (nicotinoprotein); EC 1.1.99.37; NDMA-dependent methanol dehydrogenase; nicotinoprotein methanol dehydrogenase; methanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase. Cat No: EXWM-0465. | |
| mevaldate reductase (NADPH) | May be identical with EC 1.1.1.2 [alcohol dehydrogenase (NADP+)]. Group: Enzymes. Synonyms: mevaldate (reduced nicotinamide adenine dinucleotide phosphate) reductase; mevaldate reductase (NADPH2). Enzyme Commission Number: EC 1.1.1.33. CAS No. 9028-34-6. 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-0243; mevaldate reductase (NADPH); EC 1.1.1.33; 9028-34-6; mevaldate (reduced nicotinamide adenine dinucleotide phosphate) reductase; mevaldate reductase (NADPH2). Cat No: EXWM-0243. | |
| NADH dehydrogenase (quinone) | Menaquinone can act as acceptor. Inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. Group: Enzymes. Synonyms: reduced nicotinamide adenine dinucleotide (quinone) dehydrogenase; NADH-quinone oxidoreductase; DPNH-menadione reductase; D-diaphorase; NADH2 dehydrogenase (quinone). Enzyme Commission Number: EC 1.6.5.11. CAS No. 37256-36-3. 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-1589; NADH dehydrogenase (quinone); EC 1.6.5.11; 37256-36-3; reduced nicotinamide adenine dinucleotide (quinone) dehydrogenase; NADH-quinone oxidoreductase; DPNH-menadione reductase; D-diaphorase; NADH2 dehydrogenase (quinone). Cat No: EXWM-1589. | |
| NADH Thio, Reduced (Nicotinamide Adenine Dinucleotide), Thio-NADH) | Beta-nicotinamide adenine dinucleotide hydrate. Can be used as a cofactor in reactions with NAD-dependent histone deacetylase enzymes.NAD is a coenzyme formed from the nucleotide, nicotinamide, adenosine monophosphateand a phosphate group joining the first two components. NADP has the same structure with the addition of an extra phosphate group to AMP. NAD can be reduced to NADH during coupling with reactions which oxidize various organic substrates. For example, the reaction catalyzed by glyceraldehyde phosphate dehydrogenase during glycolysis. NADH then passes to the inside of mitochondria where it donates the electrons it is carrying to the electron transp...oth of these coenzymes play crucial roles in this. Each molecule of NAD+ (or NADP+) can acquire two electrons; that is, be reduced by two electrons. However, only one proton accompanies the reduction. The other proton produced as two hydrogen atoms are removed from the molecule being oxidized is liberated into the surrounding medium. For NAD, the reaction is thus:NAD+ + 2H -> NADH + H+. Group: Biochemicals. Alternative Names: Nicotinamide Adenine Dinucleotide; Thio-NADH; Thionicotinamide adenine dinucleotide. Grades: Highly Purified. CAS No. 1921-48-8. Pack Sizes: 100mg. Molecular Formula: C21H29N7O13SP2, Molecular Weight: 681.51. US Biological Life Sciences. | Worldwide |
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