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| Product | Description | |
|---|---|---|
| dihydropyrimidine dehydrogenase (NAD+) | An iron-sulfur flavoenzyme. The enzyme was originally discovered in the uracil-fermenting bacterium, Clostridium uracilicum, which utilizes uracil and thymine as nitrogen and carbon sources for growth. Since then the enzyme was found in additional organisms including Alcaligenes eutrophus, Pseudomonas strains and Escherichia coli. Group: Enzymes. Synonyms: dihydropyrimidine dehydrogenase; dihydrothymine dehydrogenase; pyrimidine reductase; thymine reductase; uracil reductase; dihydrouracil dehydrogenase (NAD+). Enzyme Commission Number: EC 1.3.1.1. CAS No. 9026-89-5. 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-1270; dihydropyrimidine dehydrogenase (NAD+); EC 1.3.1.1; 9026-89-5; dihydropyrimidine dehydrogenase; dihydrothymine dehydrogenase; pyrimidine reductase; thymine reductase; uracil reductase; dihydrouracil dehydrogenase (NAD+). Cat No: EXWM-1270. |  |
| Dimethylglycine oxidase from Arthrobacter globifomis, Recombinant | Dimethylglycine oxidase (DMGO) is a covalent flavoenzyme from Arthrobacter globiformis that catalyzes the oxidative demethylation of dimethylglycine to yield sarcosine, formaldehyde, and hydrogen peroxide. The N-terminal region binds FAD covalently so it is yellowish. Dimethylglycine oxidase recombinant originated from arthrobacter globifomis fused to his tag at n-terminal produced in e. coli is a single, non-glycosylated, polypeptide chain containing 850 amino acids and having a molecular mass of 92.1 kda. the dmgo is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: DMGO; Dimethylglycine Oxidase. CAS No. 74870-79-4. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. DMGO. Mole weight: 92.1 kDa. Stability: Dimethylglycine Oxidase Recombinant although stable at 4°C for 30 days, should be stored desiccated below -20°C for periods greater than 30 days. Please prevent freeze-thaw cycles. Appearance: Sterile filtered liquid formulation 1 mg/ml. Source: E. coli. Species: Arthrobacter globifomis. DMGO; Dimethylglycine Oxidase. Cat No: NATE-0826. | |
| 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 | |
| FAD disodium salt | FAD disodium salt is the salt form of FAD, which is a coenzyme that facilitates the transfer of electrons by flavoenzymes in oxidation-reduction reactions in cells. Nutritional supplement in health care products. Uses: Ingredient of health care products. Synonyms: FAD-Na2; FAD Na2; FADNa2; Flavin Adenine Dinucleotide Disodium Salt. CAS No. 84366-81-4. Molecular formula: C27H31N9Na2O15P2. Mole weight: 829.52. |  |
| Glutathione reductase from E. coli, Recombinant | Glutathione reductase (GR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the precess is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl prote...e; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Enzyme Commission Number: EC 1.8.1.7. CAS No. 9001-48-3. Purity: >95% as judged by SDS-PAGE. GR. Mole weight: 49.5 kDa. Activity: 35 U/mg protein, 98 U/ml. Storage: Glutathione reductase should be stored at 4 °C or and will remain stable up to 3 years if stored as specified. Form: 3.2 M ammonium sulphate. Source: E. coli. Species: E. coli. GR; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Cat No: NATE-1574. | |
| glycine oxidase | A flavoenzyme containing non-covalently bound FAD. The enzyme from Bacillus subtilis is active with glycine, sarcosine, N-ethylglycine, D-alanine, D-α-aminobutyrate, D-proline, D-pipecolate and N-methyl-D-alanine. It differs from EC 1.4.3.3, D-amino-acid oxidase, due to its activity on sarcosine and D-pipecolate. The intermediate 2-iminoacetate is used directly by EC 2.8.1.10, thiazole synthase. Group: Enzymes. Enzyme Commission Number: EC 1.4.3.19. CAS No. 39307-16-9. 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-1473; glycine oxidase; EC 1.4.3.19; 39307-16-9. Cat No: EXWM-1473. | |
| Monoamine Oxidase B from Human, Recombinant | MAO's are proteins of the mitochondrial membrane. These enzymes are responsible for catalyzing oxidative deamination of endo-and xenobiotic amines. Substrate specificity differs for each isozyme. Monoamine oxidase b is a mit ochondrial outermembrane flavoenzyme that is a target for antidepressant and neuroprotective drugs. Applications: Drugs that inhibit monoamine oxidase b activity are used for the treatment of various neurological disorders including depression. monoamine oxidase b has been used in a study to assess the effect of age in 23 different regions of the human brain. it has also been used in a study to determine the specific l ocations of monoamine oxidase in the human brain. Group: Enzymes. Synonyms: MAO-B; MAOB; EC 1.4.3.4; Monoamine Oxida. Enzyme Commission Number: EC 1.4.3.4. CAS No. 231-791-2. Monoamine Oxidase. Storage: -70°C. Source: Baculovirus infected BTI insect cells. Species: Human. MAO-B; MAOB; EC 1.4.3.4; Monoamine Oxidase B; adrenalin oxidase; adrenaline oxidase; amine oxidase (ambiguous); amine oxidase (flavin-containing); amine:oxygen oxidoreductase (deaminating) (flavin-containing); epinephrine oxidase; monoamine:O2 oxidoreductase (deaminating); polyamine oxidase (ambiguous); serotonin deaminase; spermidine oxidase (ambiguous); spermine oxidase (ambiguous); tyraminase; tyramine oxidase. Cat No: NATE-0441. | |
| Native Bacillus sp. Sarcosine Oxidase | Sarcosine oxidase is an enzyme (EC 1.5.3.1) that catalyzes the oxidative demethylation of sarcosine to yield glycine, H2O2, 5,10-CH2-tetrahydrofolate in a reaction requiring H4-tetrahydrofolate and oxygen. Corynebacterial sarcosine oxidase is a heterotetramer and is produced as an inducible enzyme when Corynebacterium sp.is grown with sarcosine as source of carbon and energy. Monomeric sarcosine oxidase (msox) is a flavoenzyme that catalyzes the oxidative demethylation of sarcosine (n-methylglycine) to yield glycine, formaldehyde, and hydrogen peroxide. monomeric sarcosine oxidase can oxidize other secondary amino acids such as n-methyl-l-alanine, n-ethylglycine, and l-proline. Applications: Sarcosine oxidase has been used in a study as part of a multienzyme cascade, that when immobilized constructed amperometric biosensors. sarcosine oxidase has also been used in a study to investigate oxidation of amines by flavoproteins. Group: Enzymes. Synonyms: Sarcosine oxidase; EC 1.5.3.1; 9029-22-5; sarcosine:oxygen oxidoreductase (demethylating). Enzyme Commission Number: EC 1.5.3.1. CAS No. 9029-22-5. SAO. Activity: 25-50 units/mg solid. Storage: -20°C. Form: lyophilized powder; No stabilizers added. Source: Bacillus sp. Sarcosine oxidase; EC 1.5.3.1; 9029-22-5; sarcosine:oxygen oxidoreductase (demethylating). Cat No: NATE-0664. | |
| Native Baker's yeast (S. cerevisiae) Glutathione Reductase | Glutathione reductase (GR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the precess is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl ...reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Enzyme Commission Number: EC 1.6.4.2. CAS No. 9001-48-3. GR. Mole weight: mol wt 118 kDa. Activity: 100-300 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4, pH 7.0, containing 0.1 mM dithiothreitol. Source: Baker's yeast (S. cerevisiae). EC 1.6.4.2; 9001-48-3; Glutathione Reductase; GR; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Cat No: NATE-0317. | |
| Native Porcine NAD(P)H Dehydrogenase (quinone) | 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 pr...hydrogenase; NAD (P)H menadione reductase; NAD (P)H-quinone dehydrogenase; NAD (P)H-quinone oxidoreductase; NAD (P)H: (quinone-acceptor)oxidoreductase. CAS No. 9032-20-6. Diaphorase. Activity: >25 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Appearance: Yellow suspension in ammonium sulfate, 3.2 mol/l. Source: Porcine heart. Species: Porcine. menadione reductase; phylloquinone reductase; quinone reductase; dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone); DT-diaphorase; flavoprotein NAD (P)H-quinone reductase; menadione oxidoreductase; NAD (P)H dehydrogenase; NAD (P)H menadione reductase; NAD (P)H-quinone dehydro | |
| Native Spinach Glutathione Reductase | Glutathione reductase (GR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the precess is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl proteases, ...PH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Enzyme Commission Number: EC 1.6.4.2. CAS No. 9001-48-3. GR. Mole weight: mol wt 118 kDa. Activity: 100-200 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4 mM, 10 mM potassium phosphate, pH 7.0. Source: Spinach. EC 1.6.4.2; 9001-48-3; Glutathione Reductase; GR; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Cat No: NATE-0318. | |
| Native Wheat germ Glutathione Reductase | Glutathione reductase (GR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the precess is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl proteases, Citrate synthase, EF hands, hemoglobins, lipecalins, and α/β hydrolases. GR is stimulated by melatonin and is reportedly irreversibly inhibited by a number of oxygen radical generating systems. Group: Enzymes. Synonyms: EC 1.6.4.2; 9. Enzyme Commission Number: EC 1.6.4.2. CAS No. 9001-48-3. GR. Mole weight: mol wt 118 kDa. Activity: > 0.08 units/mg protein. Storage: -20°C. Source: Wheat germ. EC 1.6.4.2; 9001-48-3; Glutathione Reductase; GR; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Cat No: NATE-0319. | |
| tRNA-dihydrouridine20a/20b synthase [NAD(P)+] | A flavoenzyme. The enzyme specifically modifies uracil20a and uracil20b in tRNA. Group: Enzymes. Synonyms: Dus4p. Enzyme Commission Number: EC 1.3.1.90. 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-1360; tRNA-dihydrouridine20a/20b synthase [NAD(P)+]; EC 1.3.1.90; Dus4p. Cat No: EXWM-1360. | |
| tRNA-dihydrouridine20 synthase [NAD(P)+] | A flavoenzyme. The enzyme specifically modifies uracil20 in tRNA. Group: Enzymes. Synonyms: Dus2p; tRNA-dihydrouridine synthase 2. Enzyme Commission Number: EC 1.3.1.91. 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-1361; tRNA-dihydrouridine20 synthase [NAD(P)+]; EC 1.3.1.91; Dus2p; tRNA-dihydrouridine synthase 2. Cat No: EXWM-1361. | |
| tRNA-dihydrouridine47 synthase [NAD(P)+] | A flavoenzyme. The enzyme specifically modifies uracil47 in tRNA. Group: Enzymes. Synonyms: Dus3p; tRNA-dihydrouridine synthase 3. Enzyme Commission Number: EC 1.3.1.89. 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-1358; tRNA-dihydrouridine47 synthase [NAD(P)+]; EC 1.3.1.89; Dus3p; tRNA-dihydrouridine synthase 3. Cat No: EXWM-1358. | |
| UDP-galactopyranose mutase | A flavoenzyme which generates UDP-α-D-glactofuranose required for cell wall formation in bacteria, fungi, and protozoa. Group: Enzymes. Synonyms: UGM; UDP-D-galactopyranose furanomutase. Enzyme Commission Number: EC 5.4.99.9. CAS No. 174632-18-9. 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-5609; UDP-galactopyranose mutase; EC 5.4.99.9; 174632-18-9; UGM; UDP-D-galactopyranose furanomutase. Cat No: EXWM-5609. | |
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