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| Product | Description | |
|---|---|---|
| hydrogen dehydrogenase | An iron-sulfur flavoprotein (FMN or FAD). Some forms of this enzyme contain nickel. Group: Enzymes. Synonyms: H2:NAD+ oxidoreductase; NAD-linked hydrogenase; bidirectional hydrogenase; hydrogenase. Enzyme Commission Number: EC 1.12.1.2. CAS No. 9027-5-8. 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-0517; hydrogen dehydrogenase; EC 1.12.1.2; 9027-05-8; H2:NAD+ oxidoreductase; NAD-linked hydrogenase; bidirectional hydrogenase; hydrogenase. Cat No: EXWM-0517. |  |
| hydrogen dehydrogenase (NADP+) | The protein from the bacterium Desulfovibrio fructosovorans is an iron-sulfur protein that exclusively functions as a hydrogen dehydrogenase, while the enzyme from the archaeon Pyrococcus furiosus is a nickel, iron, iron-sulfur protein, that is part of a heterotetrameric complex where the α and Δ subunits function as a hydrogenase while the β and γ subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.5, hydrogen dehydrogenase [NAD(P)+]. Group: Enzymes. Synonyms: NADP+-linked hydrogenase; NADP+-reducing hydrogenase; hydrogenase (ambiguous); hydrogenase I (ambiguous). Enzyme Commission Number: EC 1.12.1.3. CAS No. 9027-5-8. 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-0518; hydrogen dehydrogenase (NADP+); EC 1.12.1.3; 9027-05-8; NADP+-linked hydrogenase; NADP+-reducing hydrogenase; hydrogenase (ambiguous); hydrogenase I (ambiguous). Cat No: EXWM-0518. | |
| hydrogen dehydrogenase [NAD(P)+] | A nickel, iron, iron-sulfur protein. The enzyme from the archaeon Pyrococcus furiosus is part of a heterotetrameric complex where the α and Δ subunits function as a hydrogenase while the β and γ subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.3, hydrogen dehydrogenase (NADP+). Group: Enzymes. Synonyms: hydrogenase II (ambiguous). Enzyme Commission Number: EC 1.12.1.5. 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-0520; hydrogen dehydrogenase [NAD(P)+]; EC 1.12.1.5; hydrogenase II (ambiguous). Cat No: EXWM-0520. | |
| 3α(or 20β)-hydroxysteroid dehydrogenase | The 3α-hydroxy group or 20β-hydroxy group of pregnane and androstane steroids can act as donor. Group: Enzymes. Synonyms: cortisone reductase; (R)-20-hydroxysteroid dehydrogenase; dehydrogenase, 20β-hydroxy steroid; Δ4-3-ketosteroid hydrogenase; 20β-hydroxysteroid dehydrogenase; 3α,20β-hydroxysteroid:NAD+-oxidoreductase; NADH-20β-hydroxysteroid dehydrogenase; 20β-HSD. Enzyme Commission Number: EC 1.1.1.53. CAS No. 9028-42-6. 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-0338; 3α(or 20β)-hydroxysteroid dehydrogenase; EC 1.1.1.53; 9028-42-6; cortisone reductase; (R)-20-hydroxysteroid dehydrogenase; dehydrogenase, 20β-hydroxy steroid; Δ4-3-ketosteroid hydrogenase; 20β-hydroxysteroid dehydrogenase; 3α,20β-hydroxysteroid:NAD+-oxidoreductase; NADH-20β-hydroxysteroid dehydrogenase; 20β-HSD. Cat No: EXWM-0338. | |
| 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. | |
| anaerobic carbon-monoxide dehydrogenase | This prokaryotic enzyme catalyses the reversible reduction of CO2 to CO. The electrons are transferred to redox proteins such as ferredoxin. In purple sulfur bacteria and methanogenic archaea it catalyses the oxidation of CO to CO2, which is incorporated by the Calvin-Benson-Basham cycle or released, respectively. In acetogenic and sulfate-reducing microbes it catalyses the reduction of CO2 to CO, which is incorporated into acetyl CoA by EC 2.3.1.169, CO-methylating acetyl CoA synthase, with which the enzyme forms a tight complex in those organisms. The enzyme contains five metal clusters per homodimeric enzyme: two nickel-iron-sulfur clusters called the C-Clusters, one [...-4S] clusters exist, presumably as part of the electron transfer chain. In purple sulfur bacteria the enzyme forms complexes with the Ni-Fe-S protein EC 1.12.7.2, ferredoxin hydrogenase, which catalyse the overall reaction: CO + H2O = CO2 + H2. cf. EC 1.2.5.3, aerobic carbon monoxide dehydrogenase. Group: Enzymes. Synonyms: Ni-CODH; carbon-monoxide dehydrogenase (ferredoxin). Enzyme Commission Number: EC 1.2.7.4. 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-1227; anaerobic carbon-monoxide dehydrogenase; EC 1.2.7.4; Ni-CODH; carbon-monoxide dehydrogenase (ferredoxin). Cat No: EXWM-1227. | |
| cytokinin dehydrogenase | A flavoprotein(FAD). Catalyses the oxidation of cytokinins, a family of N6-substituted adenine derivatives that are plant hormones, where the substituent is a dimethylallyl or other prenyl group. Although this activity was previously thought to be catalysed by a hydrogen-peroxide-forming oxidase, this enzyme does not require oxygen for activity and does not form hydrogen peroxide. 2,6-Dichloroindophenol, methylene blue, nitroblue tetrazolium, phenazine methosulfate and Cu(II) in the presence of imidazole can act as acceptors. This enzyme plays a part in regulating rice-grain production, with lower levels of the enzyme resulting in enhanced grain production. Group: Enzymes. Synonyms: N6-dimethylallyladenine:(acceptor) oxidoreductase; 6-N-dimethylallyladenine:acceptor oxidoreductase; OsCKX2; CKX; cytokinin oxidase/dehydrogenase. Enzyme Commission Number: EC 1.5.99.12. CAS No. 55326-39-1. 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-1566; cytokinin dehydrogenase; EC 1.5.99.12; 55326-39-1; N6-dimethylallyladenine:(acceptor) oxidoreductase; 6-N-dimethylallyladenine:acceptor oxidoreductase; OsCKX2; CKX; cytokinin oxidase/dehydrogenase. Cat No: EXWM-1566. | |
| formate dehydrogenase | The enzyme from most aerobic organisms is devoid of redox-active centres but that from the proteobacterium Methylosinus trichosporium contains iron-sulfur centres, flavin and a molybdenum centre. Together with EC 1.12.1.2 hydrogen dehydrogenase, forms a system previously known as formate hydrogenlyase. Group: Enzymes. Synonyms: formate-NAD oxidoreductase; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Enzyme Commission Number: EC 1.2.1.2. CAS No. 9028-85-7. FDH. 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-1125; formate dehydrogenase; EC 1.2.1.2; 9028-85-7; formate-NAD oxidoreductase; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Cat No: EXWM-1125. | |
| formate dehydrogenase (acceptor) | Formate dehydrogenase H is a cytoplasmic enzyme that oxidizes formate without oxygen transfer, transferring electrons to a hydrogenase. The two enzymes form the formate-hydrogen lyase complex. The enzyme contains an [4Fe-4S] cluster, a selenocysteine residue and a molybdopterin cofactor. Group: Enzymes. Synonyms: FDHH; FDH-H; FDH-O; formate dehydrogenase H; formate dehydrogenase O. Enzyme Commission Number: EC 1.1.99.33. 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-0462; formate dehydrogenase (acceptor); EC 1.1.99.33; FDHH; FDH-H; FDH-O; formate dehydrogenase H; formate dehydrogenase O. Cat No: EXWM-0462. | |
| Formate Dehydrogenase (Crude Enzyme) | Formate Dehydrogenases are a set of enzymes that catalyse the oxidation of formate to carbon dioxide, donating the electrons to a second substrate, such as NAD + in formate:NAD + oxidoreductase (EC 1. 2. 1. 2) or to a cytochrome in formate:ferricytochrome-b1 oxidoreductase (EC 1. 2. 2. 1). This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; biotechnology; medicine; analysis. Group: Enzymes. Synonyms: formate-NAD oxidoreductase; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Enzyme Commission Number: EC 1.2.1.2. CAS No. 9028-85-7. FDH. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. formate-NAD oxidoreductase; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Pack: 100ml. Cat No: NATE-1799. | |
| Formate Dehydrogenase from Recombinant E. coli | Formate dehydrogenase is involved in the stress response of plants and catalyzes the reduction of NAD+ to NADH. Group: Enzymes. Synonyms: EC 1.2.1.2; 9028-85-7; formate-NAD oxidoreductase; FDH; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Enzyme Commission Number: EC 1.2.1.2. CAS No. 9028-85-7. Purity: 5% - 25%. FDH. Activity: 0.5-2.0 u/mg. Storage: 0-10°C. Form: Powder. Source: E. coli. EC 1.2.1.2; 9028-85-7; formate-NAD oxidoreductase; FDH; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Cat No: NATE-1783. | |
| glycine dehydrogenase (cyanide-forming) | The enzyme from Pseudomonas sp. contains FAD. The enzyme is membrane-bound, and the 2-electron acceptor is a component of the respiratory chain. The enzyme can act with various artificial electron acceptors, including phenazine methosulfate. Group: Enzymes. Synonyms: hydrogen cyanide synthase; HCN synthase. Enzyme Commission Number: EC 1.4.99.5. 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-1491; glycine dehydrogenase (cyanide-forming); EC 1.4.99.5; hydrogen cyanide synthase; HCN synthase. Cat No: EXWM-1491. | |
| 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. | |
| NADH dehydrogenase | A flavoprotein containing iron-sulfur centres. After preparations have been subjected to certain treatments, cytochrome c may act as an acceptor. Under normal conditions, two protons are extruded from the cytoplasm or the intramitochondrial or stromal compartment. Present in a mitochondrial complex as EC 1.6.5.3, NADH dehydrogenase (ubiquinone). Group: Enzymes. Synonyms: cytochrome c reductase; type 1 dehydrogenase; β-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine dinucleotide dehydrogenase; diphosphopyridine diaphorase; DPNH diaphorase; NADH diaphorase; NADH hydroge. Enzyme Commission Number: EC 1.6.99.3. CAS No. 9079-67-8. Diaphorase. 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-1601; NADH dehydrogenase; EC 1.6.99.3; 9079-67-8; cytochrome c reductase; type 1 dehydrogenase; β-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine dinucleotide dehydrogenase; diphosphopyridine diaphorase; DPNH diaphorase; NADH diaphorase; NADH hydrogenase; NADH oxidoreductase; NADH-menadione oxidoreductase; reduced diphosphopyridine nucleotide diaphorase; NADH:cytochrome c oxidoreductase; NADH2 dehydrogenase; NADH:(acceptor) oxidoreductase. Cat No: EXWM-1601. | |
| Native Candida boidinii Formate Dehydrogenase | Formate dehydrogenase is involved in the stress response of plants and catalyzes the reduction of NAD+ to NADH. Fdh is an abundant enzyme from yeast candida boidinii (cbfdh) that plays an important role in the energy supply of methylotrophic microorganisms and in the stress response of plants. Applications: Formate dehydrogenase (fdh) is used for diagnostics in large scale industrial pr ocesses. its used in the production of an unnatural amino acid, tert-l-leucine, a component of some hiv protease and matrix metalloprotease inhibitors. Group: Enzymes. Synonyms: EC 1.2.1.2; 9028-85-7; formate-NAD oxidoreductase; FDH; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate. Enzyme Commission Number: EC 1.2.1.2. CAS No. 9028-85-7. FDH. Activity: Type I, 5.0-15.0 units/mg protein; Type II, 0.3-0.6 units/mg; Type III, ~50 U/mL. Storage: -20°C. Form: Type I, lyophilized powder; Type II, powder; Type III, clear brown liquid. Source: Candida boidinii. EC 1.2.1.2; 9028-85-7; formate-NAD oxidoreductase; FDH; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Cat No: NATE-0254. | |
| 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 Yeast Formate Dehydrogenase | Formate dehydrogenase is involved in the stress response of plants and catalyzes the reduction of NAD+ to NADH. Dehydrogenase that catalyzes the interconversion of formate to carbon dioxide. rely on the proven diagnostic quality of this product. Applications: Use formate dehydrogenase in diagnostic tests for the determination of oxalate in combination with oxalate decarboxylase or for the determination of formic acid. also used in cofactor recycling systems for nadh. Group: Enzymes. Synonyms: formate-NAD oxidoreductase; FDH; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. FDH. Activity: >0.4 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White lyophilizate. Source: Yeast. EC 1.2.1.2; 9028-85-7; formate-NAD oxidoreductase; FDH; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Cat No: NATE-0978. | |
| (R)-4-hydroxyphenyllactate dehydrogenase | Also acts, more slowly, on (R)-3-phenyllactate, (R)-3-(indol-3-yl)lactate and (R)-lactate. Group: Enzymes. Synonyms: (R)-aromatic lactate dehydrogenase; D-hydrogenase, D-aryllactate. Enzyme Commission Number: EC 1.1.1.222. CAS No. 101754-02-3. 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-0128; (R)-4-hydroxyphenyllactate dehydrogenase; EC 1.1.1.222; 101754-02-3; (R)-aromatic lactate dehydrogenase; D-hydrogenase, D-aryllactate. Cat No: EXWM-0128. | |
| (R)-mandelate dehydrogenase | The enzyme, found in bacteria and fungi, can also accept a number of substituted mandelate derivatives, such as 3-hydroxymandelate, 4-hydroxymandelate, 2-methoxymandelate, 4-hydroxy-3-methoxymandelate and 3-hydroxy-4-methoxymandelate. The enzyme has no activity with (S)-mandelate (cf. EC 1.1.99.31, (S)-mandelate dehydrogenase). The enzyme transfers the pro-R-hydrogen from NADH. Group: Enzymes. Synonyms: ManDH2; D-ManDH2; D-mandelate dehydrogenase (ambiguous). Enzyme Commission Number: EC 1.1.1.379. 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-0297; (R)-mandelate dehydrogenase; EC 1.1.1.379; ManDH2; D-ManDH2; D-mandelate dehydrogenase (ambiguous). Cat No: EXWM-0297. | |
| short-chain acyl-CoA dehydrogenase | Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme catalyses the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R-hydrogen atoms. The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms. The highest activity was reported with either butanoyl-CoA or pentanoyl-CoA. The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA. cf. EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC ...name). Enzyme Commission Number: EC 1.3.8.1. CAS No. 9027-88-7. 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-1405; short-chain acyl-CoA dehydrogenase; EC 1.3.8.1; 9027-88-7; butyryl-CoA dehydrogenase; butanoyl-CoA dehydrogenase; butyryl dehydrogenase; unsaturated acyl-CoA reductase; ethylene reductase; enoyl-coenzyme A reductase; unsaturated acyl coenzyme A reductase; butyryl coenzyme A dehydrogenase; short-chain acyl CoA dehydrogenase; short-chain acyl-coenzyme A dehydrogenase; 3-hydroxyacyl CoA reductase; butanoyl-CoA:(acceptor) 2,3-oxidoreductase; ACADS (gene name). Cat No: EXWM-1405. | |
| 3-Acetylpyridine Adenine Dinucleotide (APAD) | APAD is an NAD analog with higher oxidation potential than NAD. It can substitute for NAD as a hydrogen-accepting cofactor in many dehydrogenase reactions; e.g. lactate dehydrogenase from Toxoplasma, Clonorchis, and Plasmodium, bacterial lipoamide dehydrogenase, as well as mammalian dehydrogenases. It can also act as a proton acceptor in various transhydrogenation reactions with NADH or NADPH. Group: Biochemicals. Alternative Names: APAD; adenosine 5'-(trihydrogen diphosphate), P?5-ester with 3-acetyl-1- β -D-ribofuranosyl pyridinium , inner salt. Grades: Purified. CAS No. 86-08-8. Pack Sizes: 10mg, 25mg, 50mg, 100mg, 250mg. Molecular Formula: C22H28N6O14P2, Molecular Weight: 662.44. US Biological Life Sciences. |  Worldwide |
| 3-Acetylpyridine-Adenine Dinucleotide, Oxidized (APAD) | 3-Acetylpyridine adenine dinucleotide is an NAD analog with higher oxidation potential than NAD. It can substitute for NAD as a hydrogen-accepting cofactor in many dehydrogenase reactions. For example lactate dehydrogenase from Toxoplasma, Clonorchis, and Plasmodium, bacterial lipoamide dehydrogenase, as well as mammalian dehydrogenases. This compound can also act as a proton acceptor in various transhydrogenation reactions with NADH or NADPH. Group: Coenzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NA. Enzyme Commission Number: EC 1.1.1.1. CAS No. 1986-8-8. Purity: Determined by increase in absorbance at 363 nm on enzymatic reduction with ADH* at pH 10.0 > 92% *ADH = Alcohol dehydrogenase (Horse liver) (EC 1.1.1.1.). APAD. Mole weight: 662.44. Storage: Keep tightly stoppered in the dark below 5°C. Moisture will reduce the purity. For prolonged storage, keep below-20°C. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1; APAD. Cat No: NATE-0077. | |
| 3-(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 |
| 5,10-methenyltetrahydromethanopterin hydrogenase | Does not catalyse the reduction of artificial dyes. Does not by itself catalyse a H2/H+ exchange reaction. Does not contain nickel or iron-sulfur clusters. Group: Enzymes. Synonyms: H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase; nonmetal hydrogenase; N5,N10-methenyltetrahydromethanopterin hydrogenase; hydrogen:N5,N10-methenyltetrahydromethanopterin oxidoreductase. Enzyme Commission Number: EC 1.12.98.2. CAS No. 100357-01-5. 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-0525; 5,10-methenyltetrahydromethanopterin hydrogenase; EC 1.12.98.2; 100357-01-5; H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase; nonmetal hydrogenase; N5,N10-methenyltetrahydromethanopterin hydrogenase; hydrogen:N5,N10-methenyltetrahydromethanopterin oxidoreductase. Cat No: EXWM-0525. | |
| 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. |  |
| 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 |
| D-Amino Acid Oxidase (Crude Enzyme) | D-Amino Acid Oxidase (DAAO; also DAO, OXDA, DAMOX) is a peroxisomal enzyme containing FAD as cofactor that is expressed in a wide range of species from yeasts to human. It is not present in plants or in bacteria which instead use D-amino acid dehydrogenase. Its function is to oxidize D-amino acids to the corresponding imino acids, producing ammonia and hydrogen peroxide. DAAO is a candidate susceptibility gene and together with G72 may play a role in the glutamatergic mechanisms of schizophrenia. Risperidone andsodium benzoate are inhibitors of DAAO. DAAO is used as a biocatalyst in several biotechnological applications, such as the oxidation of cephalosporin C, the deracem...n may use the morpheein model of allosteric regulation. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Biotechnology; industry; drug development; medicine; pharmacology; analysis; diagnostics; synthesis. Group: Enzymes. Synonyms: ophio-amino-acid oxidase; L-amino acid:O 2 oxidoreductase; new yellow enzyme. Enzyme Commission Number: EC 1.4.3.3. CAS No. 9000-88-8. DAAO. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. ophio-amino-acid oxidase; L-amino acid:O 2 oxidoreductase; new yellow enzyme. Pack: 100ml. Cat No: NATE-1807. | |
| Δ4-3-oxosteroid 5β-reductase | The enzyme from human efficiently catalyses the reduction of progesterone, androstenedione, 17α-hydroxyprogesterone and testosterone to 5β-reduced metabolites; it can also act on aldosterone, corticosterone and cortisol, but to a lesser extent. The bile acid intermediates 7α,12α-dihydroxy-4-cholesten-3-one and 7α-hydroxy-4-cholesten-3-one can also act as substrates. Group: Enzymes. Synonyms: 3-oxo-Δ4-steroid 5β-reductase; 5β-reductase; androstenedione 5β-reductase; cholestenone 5β-reductase; cortis. Enzyme Commission Number: EC 1.3.1.3. CAS No. 9029-8-7. 3-oxo-5-beta-steroid 4-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-1303; Δ4-3-oxosteroid 5β-reductase; EC 1.3.1.3; 9029-08-7; 3-oxo-Δ4-steroid 5β-reductase; 5β-reductase; androstenedione 5β-reductase; cholestenone 5β-reductase; cortisone 5β-reductase; cortisone β-reductase; cortisone Δ4-5β-reductase; steroid 5β-reductase; testosterone 5β-reductase; Δ4-3-ketosteroid 5β-reductase; Δ4-5β-reductase; Δ4-hydrogenase; 4,5β-dihydrocortisone:NADP+ Δ4-oxidoreductase; 3-oxo-5β-steroid:NADP+ Δ4-oxidoreductase. Cat No: EXWM-1303. | |
| 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 |
| Native Bacillus licheniformis NADH Oxidase | NADH Oxidase from Bacillus licheniformis was shown to display hydrogen peroxide-forming activity. Nadh oxidase is a surface enzyme with increased oxidative activity in polymorphonuclear leukocytes during phagocytosis. Applications: Nadh oxidase from bacillus licheniformis has been used in a study to assess nitrogen assimilation by bacillus licheniformis growing in chemostat cultures. it has also been used in a study to investigate the role of glutamate dehydrogenase in ammonia assimilation in bacillus macerans. Group: Enzymes. Synonyms: NADH Oxidase; 9032-21-7. CAS No. 9032-21-7. NADH Oxidase. Activity: > 35 units/mg protein. Form: lyophilized powder. Source: Bacillus licheniformis. NADH Oxidase; 9032-21-7. Pack: vial of > 15 units. Cat No: NATE-0473. | |
| Native Bacillus megaterium Diaphorase (NADH) | In enzymology, a NADPH dehydrogenase is an enzyme that catalyzes In enzymology, a NAD (P)H dehydrogenase (quinone) (EC 1.6.5.2) is an enzyme that catalyzes the chemical reaction NAD (P)H + H+ + a quinone<-> NAD (P)+ + a hydroquinone. The 4 substrates of this enzyme are NADH, NADPH, H+, and quinone, whereas its 3 products are NAD+, NADP+, and hydroquinone. Native diaphorase (ec 1.6.5.2) was purified from bacillus megaterium. Applications: Useful for enzymatic determination of reduced nad. Group: Enzymes. Synonyms: EC 1.6.99.3; cytochrome c reductase; type 1 dehydrogenase; beta-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydr. Enzyme Commission Number: EC 1.6.99.3. CAS No. 9079-67-8. Diaphorase. Activity: 30-60 U/mg. Appearance: Yellow dried powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus megaterium. EC 1.6.99.3; cytochrome c reductase; type 1 dehydrogenase; beta-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine dinucleotide dehydrogenase; diphosphopyridine diaphorase; DPNH diaphorase; NADH diaphorase; NADH hydrogenase; NADH oxidoreductase; NADH-menadione oxidoreductase; reduced diphosphopyridine nucleotide diaphorase; Beta-NADH dehydrogenase dinucleotide. Cat No: DIA-142. | |
| Native Bacillus stearothermophilus Diaphorase 1 | Diaphorase catalyzes the reaction of a reduced di- or tri-phosphopyridine nucleotide hydrogen donor with a hydrogen acceptor, usually a dye in the leucoform. Applications: The enzyme is useful for the measurement of various dehydrogenase reactions in visible spectral range. Group: Enzymes. Synonyms: Diaphorase 1; Di-1; EC 1.6.99 -. Enzyme Commission Number: EC 1.6.99.-. Diaphorase. Mole weight: ca. 30,000. Appearance: Lyophilized. Storage: Stable at -20 to 5 °C for at least one year. Source: Bacillus stearothermophilus. Diaphorase 1; Di-1; EC 1.6.99 -. Cat No: NATE-1901. | |
| Native Clostridium sp. Diaphorase | Native Clostridium sp. Diaphorase. Applications: This enzyme is useful for colorimetric determination of nad(p)h and many dehydrogenases when coupled with various dyes which act as hydrogen acceptors from nad(p)h. Group: Enzymes. Synonyms: Diaphorase; EC 1.6.99.-. Enzyme Commission Number: EC 1.6.99.-. Diaphorase. Mole weight: 24 kDa. Activity: Grade? 30U/mg-solid or more (containing approx. 15% of stabilizers). Stability: Stable at-20°C for at least one year. Appearance: Yellowish amorphous powder, lyophilized. Form: Freeze dried powder. Source: Clostridium sp. Diaphorase; EC 1.6.99.-. Cat No: DIA-187. | |
| Native Porcine Cytochrome c Reductase | Cytochrome c reductase is a flavoprotein that completes the oxidation-reduction chain between hexosemonophosphate and cytochrome c. The molecular weight of cytochrome c reductase is found to be approximately 78 kDa Da. The prosthetic group of cytochrome c reductase is alloxazine mononucleotide. The enzyme is very unstable with respect to low pH and to denaturation by heat. Group: Enzymes. Synonyms: EC 1.6.99.3; cytochrome c reductase; type 1 dehydrogenase; β-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine . Enzyme Commission Number: EC 1.6.99.3. CAS No. 9027-14-9. Cytochrome c Reductase. Activity: > 1.0 units/mg protein. Storage: -20°C. Form: lyophilized powder. Crude, lyophilized powder containing potassium phosphate, pH approx. 7.0. Source: Porcine heart. Species: Porcine. EC 1.6.99.3; cytochrome c reductase; type 1 dehydrogenase; β-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine dinucleotide dehydrogenase; diphosphopyridine diaphorase; DPNH diaphorase; NADH diaphorase; NADH hydrogenase; NADH oxidoreductase; NADH-menadione oxidoreductase; reduced diphosphopyridine nucleotide diaphorase; NADH:cytochrome c oxidoreductase; NADH2 dehydrogenase; NADH: (acceptor) oxidoreductase; 9027-14-9. Cat No: NATE-0179. | |
| sulfhydrogenase | An iron-sulfur protein. The enzyme from the hyperthermophilic archaeon Pyrococcus furiosus is part of two heterotetrameric complexes where the β and γ subunits function as sulfur reductase and the α and Δ subunits function as hydrogenases (EC 1.12.1.3, hydrogen dehydrogenase [NADP+] and EC 1.12.1.4, hydrogen dehydrogenase [NAD(P)+], respectively). Sulfur can also be used as substrate, but since it is insoluble in aqueous solution and polysulfide is generated abiotically by the reaction of hydrogen sulfide and sulfur, polysulfide is believed to be the true substrate. Group: Enzymes. Synonyms: sulfur reductase. Enzyme Commission Number: EC 1.12.98.4. 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-0527; sulfhydrogenase; EC 1.12.98.4; sulfur reductase. Cat No: EXWM-0527. | |
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