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| Product | Description | |
|---|---|---|
| FAD-dependent glucose dehydrogenase | FAD-dependent glucose dehydrogenase (EC 1.1.5.9), or glucose dehydrogenase (FAD)/Pseudomonas glucose dehydrogenase. Glucose 1-dehydrogenase is an enzyme used as a regeneration cofactor to convert glucose and NAD(P) into NAD(P)H and gluconic acid [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: FAD-GDH; Glucose 1-dehydrogenase. CAS No. 37250-84-3. Pack Sizes: 1 KU. Product ID: HY-E70014. |  |
| FAD-dependent urate hydroxylase | A flavoprotein. The reaction is part of the purine catabolic pathway in the bacterium Klebsiella pneumoniae. The enzyme is different from EC 1.7.3.3, factor-independent urate hydroxylase, found in most plants, which produces hydrogen peroxide. The product of the enzyme is a substrate for EC 3.5.2.17, hydroxyisourate hydrolase. Group: Enzymes. Synonyms: HpxO enzyme; FAD-dependent urate oxidase; urate hydroxylase. Enzyme Commission Number: EC 1.14.13.113. 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-0713; FAD-dependent urate hydroxylase; EC 1.14.13.113; HpxO enzyme; FAD-dependent urate oxidase; urate hydroxylase. Cat No: EXWM-0713. |  |
| Native Microorganism Glucose Dehydrogenase (FAD-dependent) | FAD-GDH catalyses the oxidation of glucose in the presence of an electron acceptor, such as 2,6-dichlorophenolindophenol or potassium ferricyanide. Applications: Blood glucose monitoring (biosensors) biosensors. Group: Enzymes. Synonyms: D-glucose:acceptor 1-oxidoreductase; glucose dehydrogenase (Aspergillus); glucose dehydrogenase (decarboxylating); D-glucose: (acceptor) 1-oxidoreductase; Glucose Dehydrogenase (FAD-dependent); FAD-GDH; EC 1.1.99.10; 9035-82-9. Enzyme Commission Number: EC 1.1.99.10. CAS No. 9035-82-9. Activity: ≥ 800U/mg protein. Storage: Store desiccated at-15°C or below. Allow to come to room temperature before opening. Before returning to storage, re-desiccate under vacuum over silica gel for a minimum of four hours. Form: A yellow freeze dried material. Source: Microorganism. D-glucose:acceptor 1-oxidoreductase; glucose dehydrogenase (Aspergillus); glucose dehydrogenase (decarboxylating); D-glucose: (acceptor) 1-oxidoreductase; Glucose Dehydrogenase (FAD-dependent); FAD-GDH; EC 1.1.99.10; 9035-82-9. Cat No: NATE-0251. | |
| 1,3,7-trimethyluric acid 5-monooxygenase | The enzyme, characterized from the bacterium Pseudomonas sp. CBB1, is part of the bacterial C-8 oxidation-based caffeine degradation pathway. The product decomposes spontaneously to a racemic mixture of 3,6,8-trimethylallantoin. The enzyme shows no acitivity with urate. cf. EC 1.14.13.113, FAD-dependent urate hydroxylase. Group: Enzymes. Synonyms: tmuM (gene name). Enzyme Commission Number: EC 1.14.13.212. 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-0814; 1,3,7-trimethyluric acid 5-monooxygenase; EC 1.14.13.212; tmuM (gene name). Cat No: EXWM-0814. | |
| (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA 1,5-monooxygenase | A FAD dependent enzyme isolated from Pseudomonas putida. Forms part of the catabolism pathway of camphor. It acts on the CoA ester in preference to the free acid. Group: Enzymes. Synonyms: 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase; 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-CoA 1,2-monooxygenase; OTEMO. Enzyme Commission Number: EC 1.14.13.160. 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-0760; (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA 1,5-monooxygenase; EC 1.14.13.160; 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase; 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-CoA 1,2-monooxygenase; OTEMO. Cat No: EXWM-0760. | |
| (6-4)DNA photolyase | A flavoprotein (FAD). The overall repair reaction consists of two distinct steps, one of which is light-independent and the other one light-dependent. In the initial light-independent step, a 6-iminium ion is thought to be generated via proton transfer induced by two histidines highly conserved among the (6-4) photolyases. This intermediate spontaneously rearranges to form an oxetane intermediate by intramolecular nucleophilic attack. In the subsequent light-driven reaction, one electron is believed to be transferred from the fully reduced FAD cofactor (FADH-) to the oxetane intermediate thus forming a neutral FADH radical and an anionic oxetane radical, which spontaneously fractures. The excess electron is then back-transferred to the flavin radical restoring the fully reduced flavin cofactor and a pair of pyrimidine bases. Group: Enzymes. Synonyms: DNA photolyase; H64PRH; NF-10; phr (6-4); PL-(6-4); OtCPF1; (6-4) PHR; At64PHR. Enzyme Commission Number: EC 4.1.99.13. CAS No. 37290-70-3. 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-4928; (6-4)DNA photolyase; EC 4.1.99.13; 37290-70-3; DNA photolyase; H64PRH; NF-10; phr (6-4); PL-(6-4); OtCPF1; (6-4) PHR; At64PHR. Cat No: EXWM-4928. | |
| aclacinomycin-A oxidase | A flavoprotein (FAD). This bifunctional enzyme is a secreted flavin-dependent enzyme that is involved in the modification of the terminal sugar residues in the biosynthesis of aclacinomycins. The enzyme utilizes the same active site to catalyse the oxidation of the rhodinose moiety of aclacinomycin N to the cinerulose A moiety of aclacinomycin A (cf. EC 1.1.3.45) and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y. Group: Enzymes. Synonyms: AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous). Enzyme Commission Number: EC 1.3.3.14. 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-1375; aclacinomycin-A oxidase; EC 1.3.3.14; AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous). Cat No: EXWM-1375. | |
| aclacinomycin-N oxidase | A flavoprotein (FAD). This bifunctional enzyme is a secreted flavin-dependent enzyme that is involved in the modification of the terminal sugar residues in the biosynthesis of aclacinomycins. The enzyme utilizes the same active site to catalyse the oxidation of the rhodinose moiety of aclacinomycin N to the cinerulose A moiety of aclacinomycin A and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y (cf. EC 1.3.3.14, aclacinomycin A oxidase). Group: Enzymes. Synonyms: AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous). Enzyme Commission Number: EC 1.1.3.45. 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-0418; aclacinomycin-N oxidase; EC 1.1.3.45; AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous). Cat No: EXWM-0418. | |
| assimilatory sulfite reductase (NADPH) | Contains siroheme, [4Fe-4S] cluster, FAD and FMN. The enzyme, which catalyses the six-electron reduction of sulfite to sulfide, is involved in sulfate assimilation in bacteria and yeast. Different from EC 1.8.99.5, dissimilatory sulfite reductase, which is involved in prokaryotic sulfur-based energy metabolism. cf. EC 1.8.7.1, assimilatory sulfite reductase (ferredoxin). Group: Enzymes. Synonyms: sulfite reductase (NADPH); sulfite (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH-sulfite reductase; NADPH-dependent sulfite reductase; H2S-NADP oxidoreductase; sulfite reductase (NADPH2); MET5 (gene name); MET10 (gene name); cysI (gene name); cysJ (gene name). Enzyme Commission Number: EC 1.8.1.2. CAS No. 9029-35-0. 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-1646; assimilatory sulfite reductase (NADPH); EC 1.8.1.2; 9029-35-0; sulfite reductase (NADPH); sulfite (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH-sulfite reductase; NADPH-dependent sulfite reductase; H2S-NADP oxidoreductase; sulfite reductase (NADPH2); MET5 (gene name); MET10 (gene name); cysI (gene name); cysJ (gene name). Cat No: EXWM-1646. | |
| aurachin C monooxygenase/isomerase | The aurachin C monooxygenase from the bacterium Stigmatella aurantiaca accepts both NADH and NADPH as cofactor, but has a preference for NADH. It catalyses the initial steps in the conversion of aurachin C to aurachin B. The FAD-dependent monooxygenase catalyses the epoxidation of the C2-C3 double bond of aurachin C, which is followed by a semipinacol rearrangement, causing migration of the farnesyl group from C3 to C4. Group: Enzymes. Synonyms: auaG (gene name); aurachin C monooxygenase. Enzyme Commission Number: EC 1.14.13.222. 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-0825; aurachin C monooxygenase/isomerase; EC 1.14.13.222; auaG (gene name); aurachin C monooxygenase. Cat No: EXWM-0825. | |
| coenzyme F420 hydrogenase | An iron-sulfur flavoprotein (FAD) containing nickel. The enzyme from some sources contains selenocysteine. The enzyme also reduces the riboflavin analogue of F420, flavins and methylviologen, but to a lesser extent. The hydrogen acceptor coenzyme F420 is a deazaflavin derivative. Group: Enzymes. Synonyms: 8-hydroxy-5-deazaflavin-reducing hydrogenase; F420-reducing hydrogenase; coenzyme F420-dependent hydrogenase. Enzyme Commission Number: EC 1.12.98.1. 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-0524; coenzyme F420 hydrogenase; EC 1.12.98.1; 9027-05-8; 8-hydroxy-5-deazaflavin-reducing hydrogenase; F420-reducing hydrogenase; coenzyme F420-dependent hydrogenase. Cat No: EXWM-0524. | |
| Cytochrome P450 Reductase from Human, Recombinant | Cytochrome P450 reductase is a membrane bound enzyme required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. The cytochrome P450 enzyme system is mainly involved in the detoxification of xenobiotics in the liver. It also participates in the activation of procarcinogens and the metabolism of endogeneous substrates such as steroids. Applications: Human cytochrome p450 reductase has been used in a study to assess the biocatalytic synthesis and structure elucidation of cyclized metabolites of the deacetylase inhibitor panobinostat. human cytochrome p450 reductase has also been u...AD-cytochrome c reductase; NADPH-dependent cytochrome c reductase; NADPH:P-450 reductase. Enzyme Commission Number: EC 1.6.2.4. CAS No. 9023-3-4. Purity: >90% (SDS-PAGE). CPR. Mole weight: 76.5 kDa. Activity: >30 U/mg. Storage: Store at -70°C. Form: Supplied in a solution containing 10 mM potassium phosphate, pH 7.4, 0.1 mM EDTA, 0.5 mM DTT, 20% (v/v) glycerol. Source: Baculovirus infected insect cells. Species: Human. EC 1.6.2.4; NADPH:ferrihemoprotein oxidoreductase; NADPH:hemoprotein oxidoreductase; NADPH:P450 oxidoreductase; P450 reductase; CPR; 9039-06-9; FAD-cytochrome c reductase; NADPH-dependent cytochrome c reductase; NADPH:P-450 reductase. Cat No: NATE-1586. | |
| D-lactate dehydrogenase (cytochrome) | A flavoprotein (FAD). Group: Enzymes. Synonyms: lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Enzyme Commission Number: EC 1.1.2.4. CAS No. 37250-79-6. 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-0386; D-lactate dehydrogenase (cytochrome); EC 1.1.2.4; 37250-79-6; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Cat No: EXWM-0386. | |
| D-Lactate dehydrogenase from Bacteria, Recombinant | In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c<-> pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. Group: Enzymes. Synonyms: EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Enzyme Commission Number: EC 1.1.1.28. CAS No. 9028-36-8. D-LDH. Mole weight: 44 kD (SDS-PAGE). Activity: > 800 U/mg Protein. Storage: Below -20°C. Form: Lyophilized powder. Source: E. coli. Species: Bacteria. EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Cat No: NATE-1042. | |
| D-lactate Dehydrogenase from E. coli, Recombinant | In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c<-> pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. This protein is fused with 6x his tag at n terminus and the protein has a calculated mw of 39.1 kda (353aa). Group: Enzymes. Synonyms: EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c . Enzyme Commission Number: EC 1.1.1.28. Purity: > 95% by SDS-PAGE. D-LDH. Mole weight: 39.1 kDa. Activity: > 200 units/mg. Storage: Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles. Form: Liquid. Source: E. coli. EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D- (-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D- (-)-lactic cytochrome c reductase; D-lactate Dehydrogenase. Cat No: NATE-1654. | |
| factor-independent urate hydroxylase | This enzyme was previously thought to be a copper protein, but it is now known that the enzymes from soy bean (Glycine max), the mould Aspergillus flavus and Bacillus subtilis contains no copper nor any other transition-metal ion. The 5-hydroxyisourate formed decomposes spontaneously to form allantoin and CO2, although there is an enzyme-catalysed pathway in which EC 3.5.2.17, hydroxyisourate hydrolase, catalyses the first step. The enzyme is different from EC 1.14.13.113 (FAD-dependent urate hydroxylase). Group: Enzymes. Synonyms: uric acid oxidase; uricase; uricase II; urate oxidase. Enzyme Commission Number: EC 1.7.3.3. CAS No. 9002-12-4. UO. 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-1626; factor-independent urate hydroxylase; EC 1.7.3.3; 9002-12-4; uric acid oxidase; uricase; uricase II; urate oxidase. Cat No: EXWM-1626. | |
| FAD reductase (NADH) | The enzyme from Burkholderia phenoliruptrix can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. Unlike EC 1.5.1.36, flavin reductase (NADH), the enzyme can not reduce riboflavin. The enzyme does not use NADPH as acceptor. Group: Enzymes. Synonyms: NADH-FAD reductase; NADH-dependent FAD reductase; NADH:FAD oxidoreductase; NADH:flavin adenine dinucleotide oxidoreductase. Enzyme Commission Number: EC 1.5.1.37. 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-1518; FAD reductase (NADH); EC 1.5.1.37; NADH-FAD reductase; NADH-dependent FAD reductase; NADH:FAD oxidoreductase; NADH:flavin adenine dinucleotide oxidoreductase. Cat No: EXWM-1518. | |
| ferric-chelate reductase (NADPH) | Contains FAD. The enzyme, which is widespread among bacteria, catalyses the reduction of ferric iron bound to a variety of iron chelators (siderophores), including ferric triscatecholates and ferric dicitrate, resulting in the release of ferrous iron. The enzyme from the bacterium Escherichia coli has the highest efficiency with the hydrolysed ferric enterobactin complex ferric N-(2,3-dihydroxybenzoyl)-L-serine. cf. EC 1.16.1.7, ferric-chelate reductase (NADH) and EC 1.16.1.10, ferric-chelate reductase [NAD(P)H]. Group: Enzymes. Synonyms: ferric chelate reductase (ambiguous); iron chelate reductase (ambiguous); NADPH:Fe3+-EDTA reductase; NADPH-dependent ferric reductase; yqjH (gene name); Fe(II):NADP+ oxidoreductase. Enzyme Commission Number: EC 1.16.1.9. CAS No. 120720-17-4. 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-1074; ferric-chelate reductase (NADPH); EC 1.16.1.9; 120720-17-4; ferric chelate reductase (ambiguous); iron chelate reductase (ambiguous); NADPH:Fe3+-EDTA reductase; NADPH-dependent ferric reductase; yqjH (gene name); Fe(II):NADP+ oxidoreductase. Cat No: EXWM-1074. | |
| flavin reductase (NADH) | The enzyme from Escherichia coli W catalyses the reduction of free flavins by NADH. The enzyme has similar affinity to FAD, FMN and riboflavin. Activity with NADPH is more than 2 orders of magnitude lower than activity with NADH. Group: Enzymes. Synonyms: NADH-dependent flavin reductase; flavin:NADH oxidoreductase. Enzyme Commission Number: EC 1.5.1.36. 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-1517; flavin reductase (NADH); EC 1.5.1.36; NADH-dependent flavin reductase; flavin:NADH oxidoreductase. Cat No: EXWM-1517. | |
| 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. | |
| FMN reductase (NADH) | The enzyme often forms a two-component system with monooxygenases. Unlike EC 1.5.1.38, FMN reductase (NADPH), and EC 1.5.1.39, FMN reductase [NAD(P)H], this enzyme has a strong preference for NADH over NADPH, although some activity with the latter is observed.While FMN is the preferred substrate, FAD can also be used with much lower activity. Group: Enzymes. Synonyms: NADH-FMN reductase; NADH-dependent FMN reductase; NADH:FMN oxidoreductase; NADH:flavin oxidoreductase. Enzyme Commission Number: EC 1.5.1.42. 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-1523; FMN reductase (NADH); EC 1.5.1.42; NADH-FMN reductase; NADH-dependent FMN reductase; NADH:FMN oxidoreductase; NADH:flavin oxidoreductase. Cat No: EXWM-1523. | |
| formate dehydrogenase (coenzyme F420) | The enzyme from methanogenic archaea is a involved in formate-dependent H2 production. It contains noncovalently bound FAD. Group: Enzymes. Synonyms: coenzyme F420 reducing formate dehydrogenase; coenzyme F420-dependent formate dehydrogenase. Enzyme Commission Number: EC 1.2.99.9. 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-1237; formate dehydrogenase (coenzyme F420); EC 1.2.99.9; coenzyme F420 reducing formate dehydrogenase; coenzyme F420-dependent formate dehydrogenase. Cat No: EXWM-1237. | |
| glucose 1-dehydrogenase (FAD, quinone) | A glycoprotein containing one mole of FAD per mole of enzyme. 2,6-Dichloroindophenol can act as acceptor. cf. EC 1.1.5.2, quinoprotein glucose dehydrogenase. Group: Enzymes. Synonyms: glucose dehydrogenase (Aspergillus); FAD-dependent glucose dehydrogenase; D-glucose:(acceptor) 1-oxidoreductase; glucose dehydrogenase (acceptor); gdh (gene name). Enzyme Commission Number: EC 1.1.5.9. CAS No. 37250-84-3. 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-0437; glucose 1-dehydrogenase (FAD, quinone); EC 1.1.5.9; 37250-84-3; glucose dehydrogenase (Aspergillus); FAD-dependent glucose dehydrogenase; D-glucose:(acceptor) 1-oxidoreductase; glucose dehydrogenase (acceptor); gdh (gene name). Cat No: EXWM-0437. | |
| glucose-6-phosphate dehydrogenase (coenzyme-F420) | The enzyme is very specific for D-glucose 6-phosphate. No activity with NAD+, NADP+, FAD and FMN. Group: Enzymes. Synonyms: coenzyme F420-dependent glucose-6-phosphate dehydrogenase; F420-dependent glucose-6-phosphate dehydrogenase; FGD1; Rv0407; F420-dependent glucose-6-phosphate dehydrogenase 1. Enzyme Commission Number: EC 1.1.98.2. 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-0439; glucose-6-phosphate dehydrogenase (coenzyme-F420); EC 1.1.98.2; coenzyme F420-dependent glucose-6-phosphate dehydrogenase; F420-dependent glucose-6-phosphate dehydrogenase; FGD1; Rv0407; F420-dependent glucose-6-phosphate dehydrogenase 1. Cat No: EXWM-0439. | |
| glutamate synthase (ferredoxin) | Binds a [3Fe-4S] cluster as well as FAD and FMN. The protein 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. The NH3 is channeled through a 24 ? channel in the active protein. No hydrolysis of glutamine takes place without ferredoxin and 2-oxoglutarate being bound to the protein. Group: Enzymes. Synonyms: ferredoxin-dependent glutamate synthase; ferredoxin-glutamate synthase; glutamate synthase (ferredoxin-dependent). Enzyme Commission Number: EC 1.4.7.1. CAS No. 62213-56-3. 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-1487; glutamate synthase (ferredoxin); EC 1.4.7.1; 62213-56-3; ferredoxin-dependent glutamate synthase; ferredoxin-glutamate synthase; glutamate synthase (ferredoxin-dependent). Cat No: EXWM-1487. | |
| 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. | |
| glutathione amide reductase | A dimeric flavoprotein (FAD). The enzyme restores glutathione amide disulfide, which is produced during the reduction of peroxide by EC 1.11.1.17 (glutathione amide-dependent peroxidase), back to glutathione amide (it catalyses the reaction in the opposite direction to that shown). The enzyme belongs to the family of flavoprotein disulfide oxidoreductases, but unlike other members of the family, which are specific for NADPH, it prefers NADH. Group: Enzymes. Synonyms: GAR. Enzyme Commission Number: EC 1.8.1.16. 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-1642; glutathione amide reductase; EC 1.8.1.16; GAR. Cat No: EXWM-1642. | |
| glutathione-disulfide reductase | A dimeric flavoprotein (FAD); activity is dependent on a redox-active disulfide in each of the active centres. Group: Enzymes. Synonyms: glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; 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. GR. 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-1651; glutathione-disulfide reductase; EC 1.8.1.7; 9001-48-3; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Cat No: EXWM-1651. | |
| glycerol-3-phosphate dehydrogenase | This flavin-dependent dehydrogenase is an essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis. In bacteria, the enzyme is localized to the cytoplasmic membrane, while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane. In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8, glycerol-3-phosphate dehydrogenase (NAD+), forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD+ by the mitochondrial electron-transport chain.This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix. Insect flight muscle uses only CoQ10 as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ9. The enzyme is activated by calcium. Group: Enzymes. Synonyms: α-glycerophosphate dehydrogenase; α-glycerophosphate dehydrogenase (acceptor); anaerobic glycerol-3-phosphate dehydrogenase; DL-glycerol 3-phosphate oxidase (misleading); FAD-dependent glycerol-3-phosphate dehydrogenase; FAD-dependent sn-glycerol-3-phosphate dehydrogenase; FAD-GPDH; FAD-linked glycerol 3-phosphate dehydrogenase; FAD-linked L-glycerol-3-phosphate dehydrogenase; flavin-linked glycerol-3-phosphate dehydrogenas | |
| malate dehydrogenase (quinone) | A flavoprotein (FAD). Vitamin K and several other quinones can act as acceptors. Different from EC 1.1.1.37 (malate dehydrogenase (NAD+)), EC 1.1.1.82 (malate dehydrogenase (NADP+)) and EC 1.1.1.299 (malate dehydrogenase [NAD(P)+]). Group: Enzymes. Synonyms: FAD-dependent malate-vitamin K reductase; malate-vitamin K reductase; (S)-malate:(acceptor) oxidoreductase; L-malate-quinone oxidoreductase; malate:quinone oxidoreductase; malate quinone oxidoreductase; MQO; malate:quinone reductase; malate dehydrogenase (acceptor); FAD-dependent malate dehydrogenase. Enzyme Commission Number: EC 1.1.5.4. 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-0432; malate dehydrogenase (quinone); EC 1.1.5.4; FAD-dependent malate-vitamin K reductase; malate-vitamin K reductase; (S)-malate:(acceptor) oxidoreductase; L-malate-quinone oxidoreductase; malate:quinone oxidoreductase; malate quinone oxidoreductase; MQO; malate:quinone reductase; malate dehydrogenase (acceptor); FAD-dependent malate dehydrogenase. Cat No: EXWM-0432. | |
| methylenetetrahydrofolate-tRNA-(uracil54-C5)-methyltransferase (FADH2-oxidizing) | Up to 25% of the bases in mature tRNA are post-translationally modified or hypermodified. One almost universal post-translational modification is the conversion of U54 into ribothymidine in the TψC loop, and this modification is found in most species studied to date. Unlike this enzyme, which uses 5,10-methylenetetrahydrofolate and FADH2 to supply the atoms for methylation of U54, EC 2.1.1.35, tRNA (uracil54-C5)-methyltransferase, uses S-adenosyl-L-methionine. Group: Enzymes. Synonyms: folate-dependent ribothymidyl synthase; methylenetetrahydrofolate-transfer ribonucleate uracil 5-methyltransferase; 5,10-methylenetetrahydrofolate:tRNA-UψC (uracil-5-)-methyl-tran. Enzyme Commission Number: EC 2.1.1.74. CAS No. 56831-74-4. 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-1975; methylenetetrahydrofolate-tRNA-(uracil54-C5)-methyltransferase (FADH2-oxidizing); EC 2.1.1.74; 56831-74-4; folate-dependent ribothymidyl synthase; methylenetetrahydrofolate-transfer ribonucleate uracil 5-methyltransferase; 5,10-methylenetetrahydrofolate:tRNA-UψC (uracil-5-)-methyl-transferase; 5,10-methylenetetrahydrofolate:tRNA (uracil-5-)-methyl-transferase; TrmFO; folate/FAD-dependent tRNA T54 methyltransferase. Cat No: EXWM-1975. | |
| NADPH-hemoprotein reductase | A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases (e.g. EC 1.14.14.1, unspecific monooxygenase) by stabilizing the one-electron reduced form of the flavin cofactors FAD and FMN. It also reduces cytochrome b5 and cytochrome c. The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction. Group: Enzymes. Synonyms: CPR; FAD-cytochrome c reductase; NADP-cytochrome c reductase; NADP-cytochrome reductase; NADPH-dependent cytochrome c reductase; NADPH:P-450 reductase; NADPH:ferrihemoprotein oxidoreductase; NADPH-cytochrome P-450 oxidoreductase; NADPH-cytochrome c oxidoreductase; NA. Enzyme Commission Number: EC 1.6.2.4. CAS No. 9023-3-4. CPR. 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-1580; NADPH-hemoprotein reductase; EC 1.6.2.4; 9023-03-4; CPR; FAD-cytochrome c reductase; NADP-cytochrome c reductase; NADP-cytochrome reductase; NADPH-dependent cytochrome c reductase; NADPH:P-450 reductase; NADPH:ferrihemoprotein oxidoreductase; NADPH-cytochrome P-450 oxidoreductase; NADPH-cytochrome c oxidoreductase; NADPH-cytochrome c reductase; NADPH-cytochrome p-450 reductase; NADPH-ferri | |
| NAD(P)H sulfur oxidoreductase (CoA-dependent) | This FAD-dependent enzyme, characterized from the archaeon Pyrococcus furiosus, is responsible for NAD(P)H-linked sulfur reduction. The activity with NADH is about half of that with NADPH. The reaction is dependent on CoA, although the nature of this dependency is not well understood. Group: Enzymes. Synonyms: NADPH NSR; S0 reductase; coenzyme A-dependent NADPH sulfur oxidoreductase. Enzyme Commission Number: EC 1.8.1.18. 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-1644; NAD(P)H sulfur oxidoreductase (CoA-dependent); EC 1.8.1.18; NADPH NSR; S0 reductase; coenzyme A-dependent NADPH sulfur oxidoreductase. Cat No: EXWM-1644. | |
| Native Escherichia coli Thioredoxin Reductase | Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide. Applications: Thioredoxin reductase from escherichia coli can be used in peroxidase-coupled thioredoxin system assay for assessing the peroxidase activitiy of cys-based thiol peroxidases. the product was used for determining the enzymatic activity of his6-ahp1p. Group: Enzymes. Synonyms: NADP-thioredoxi. Enzyme Commission Number: EC 1.8.1.9. CAS No. 9074-14-0. TrxR. Activity: >25 units/mg protein (Bradford). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4 containing 30 mM potassium phosphate buffer, pH 7.5, and 2 mM EDTA. Source: Escherichia coli. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR. Cat No: NATE-0718. | |
| Native Lactobacillus delbrückii D-Lactate Dehydrogenase, Grade I | In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c<-> pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. Dehydrogenase that catalyzes the interconversion of d(-)-lactate to pyruvate. rely on the proven diagnostic quality of this product. benefit from the...ase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. CAS No. 9028-36-8. D-LDH. Activity: >180 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White to yellowish lyophilizate. Source: Lactobacillus delbrückii. EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Cat No: NATE-0976. | |
| Native Lactobacillus delbrückii D-Lactate Dehydrogenase, Grade II | In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c<-> pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. Dehydrogenase that catalyzes the interconversion of d(-)-lactate to pyruvate. rely on the proven diagnostic quality of this product. Applications: U...ase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. CAS No. 9028-36-8. D-LDH. Activity: >150 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White to yellowish lyophilizate. Source: Lactobacillus delbrückii. EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Cat No: NATE-0977. | |
| Native Leuconostoc mesenteroides D-Lactic Dehydrogenase | In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c<-> pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. Group: Enzymes. Synonyms: EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Enzyme Commission Number: EC 1.1.1.28. CAS No. 9028-36-8. D-LDH. Activity: 1,000-3,000 units/mg protein (biuret). Stability: 2-8°C. Form: ammonium sulfate suspension. Source: Leuconostoc mesenteroides. EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Cat No: NATE-0196. | |
| Native Microorganism Pyruvate oxidase | In enzymology, a pyruvate oxidase (EC 1.2.3.3) is an enzyme that catalyzes the chemical reaction: pyruvate + phosphate + O2 <-> acetyl phosphate + CO2 + H2O2. The 3 substrates of this enzyme are pyruvate, phosphate, and O2, whereas its 3 products are acetyl phosphate, CO2, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. This enzyme participates in pyruvate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate. Applications: This enzyme is useful for enzymatic determination of pyruvate, got, gpt in clinical analysis. Group: Enzymes. Synonyms: EC 1.2.3.3; pyruvate: oxygen 2-oxidoreductase (phosphorylating); pyruvic oxidase; phosphate-dependent pyruvate oxidase. Enzyme Commission Number: EC 1.2.3.3. CAS No. 9001-96-1. Pyruvate oxidase. Mole weight: approx. 260 kDa. Activity: Grade? 1.5U/mg-solid or more. Stability: Stable at-20°C for at least one year. Appearance: Yellowish amorphous powder, lyophilized. Source: Microorganism. EC 1.2.3.3; pyruvate: oxygen 2-oxidoreductase (phosphorylating); pyruvic oxidase; phosphate-dependent pyruvate oxidase. Cat No: DIA-215. | |
| Native Microorganisms Pyruvate Oxidase | Pyruvate Oxidase consists of four subunits with identical molecular weights. PoxB reacts with certain aldehydes and phosphate can be replaced by arsenate. Oxygen as well as several artificial compounds can function as electron acceptors. Pyruvate Oxidase is activated by phospholipids as well as monomeric and micellar amphiphiles. Applications: Pyruvate oxidase (poxb) converts pyruvate directly to acetate and co2. it is used to study pyruvate metabolism. it is used to study aerobic metabolism of bacterium, such as lactobacillus plantarumand strept oc occus pneumoniae. pyruvate oxidase is used for enzymatic determination of pyruvate, got, and gpt in clinical analysis. Group: Enzymes. Synonyms: pyruvate oxidase; EC 1.2.3.3; pyruvic oxidase; phosphate-dependent pyruvate oxidase; 9001-96-1; Pyruvate:oxygen oxidoreductase (phosphorylating); PoxB. Enzyme Commission Number: EC 1.2.3.3. CAS No. 9001-96-1. Pyruvate oxidase. Mole weight: mol wt ~260 kDa. Activity: > 1.5 units/mg; > 35 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized powder containing FAD and sugar as stabilizer. Source: Microorganisms. pyruvate oxidase; EC 1.2.3.3; pyruvic oxidase; phosphate-dependent pyruvate oxidase; 9001-96-1; Pyruvate:oxygen oxidoreductase (phosphorylating); PoxB. Cat No: NATE-0613. | |
| Native Rabbit Cytochrome P450 Reductase induced with phenobarbital | The enzyme catalyses electron transfer to cytochrome P450. This system plays a major role in detoxification of drugs and xenobiotics, activation of carcinogens, and metabolism of endogenous substrates such as steroids. Group: Enzymes. Synonyms: EC 1.6.2.4; NADPH:ferrihemoprotein oxidoreductase; NADPH:hemoprotein oxidoreductase; NADPH:P450 oxidoreductase; P450 reductase; CPR; 9039-06-9; FAD-cytochrome c reductase; NADPH-dependent cytochrome c reductase; NADPH:P-450 reductase. Enzyme Commission Number: EC 1.6.2.4. CAS No. 9023-82-9. Purity: ~90% (SDS-PAGE). CPR. Mole weight: mol wt ~80 kDa. Activity: 25-75 units/mg protein (Bradford). Storage: -20°C. Form: buffered aqueous glycerol solution. Solution in 30 mM potassium phosphate buffer, pH 7.7, and 0.1 mM EDTA containing 50% (v/v) glycerol. Source: Rabbit liver. Species: Rabbit. EC 1.6.2.4; NADPH:ferrihemoprotein oxidoreductase; NADPH:hemoprotein oxidoreductase; NADPH:P450 oxidoreductase; P450 reductase; CPR; 9039-06-9; FAD-cytochrome c reductase; NADPH-dependent cytochrome c reductase; NADPH:P-450 reductase. Cat No: NATE-0158. | |
| Native Rat Thioredoxin Reductase | Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide. Applications: Thioredoxin reductase from rat liver can be used for studying the uptake and reduction of a-lipoic acid... NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR; 9074-14-0. Enzyme Commission Number: EC 1.8.1.9. CAS No. 9074-14-0. TrxR. Activity: > 100 units/mg protein (Bradford). Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 1 mM EDTA, and 10% glycerol. Source: Rat liver. Species: Rat. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR; 9074-14-0. Cat No: NATE-0713. | |
| Native Spinacia oleracea (Spinach) Ferredoxin-NADP+ Reductase | Ferredoxin-NADP+ reductase catalyzes the reversible conversion of reduced ferredoxin to oxidized ferredoxin during photosynthesis. Ferredoxin-NADP (H) reductase constitutes a family of hydrophilic FAD-containing monomeric enzymes that deliver NADPH or low potential one-electron donors to redox-based metabolisms in plastids, mitochondria, and bacteria. Applications: Ferredoxin-nadp+ reductase was used in in vitro ferredoxin-dependent desaturation of fatty acids in cyanobacterial thylakoid membranes. it was also used to regulate glyceraldehyde-3-phosphate dehydrogenase. Group: Enzymes. Synonyms: EC 1.18.1.2; ferredoxin-nicotinamide adenine dinucleotide phosphate reductase; ferredoxin-NADP+ reducta. Enzyme Commission Number: EC 1.18.1.2. CAS No. 9029-33-8. FNR. Activity: > 15 units/mg solid, secondary activity: > 10 units/mg solid NADPH diaphorase. Storage: -20°C. Form: lyophilized powder. Source: Spinacia oleracea (Spinach). EC 1.18.1.2; ferredoxin-nicotinamide adenine dinucleotide phosphate reductase; ferredoxin-NADP+ reductase; TPNH-ferredoxin reductase; ferredoxin-NADP+oxidoreductase; NADP+:ferredoxin oxidoreductase; ferredoxin-TPN reductase; ferredoxin-NADP+-oxidoreductase; NADPH:ferredoxin oxidoreductase; ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase; 9029-33-8; FNR. Cat No: NATE-0256. | |
| neopentalenolactone D synthase | A FAD-dependent oxygenase. Isolated from the bacterium Streptomyces avermitilis. The ketone undergoes a biological Baeyer-Villiger reaction. Group: Enzymes. Synonyms: ptlE (gene name). Enzyme Commission Number: EC 1.14.13.171. 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-0769; neopentalenolactone D synthase; EC 1.14.13.171; ptlE (gene name). Cat No: EXWM-0769. | |
| nitric-oxide synthase (NADPH) | Binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin. This eukaryotic enzyme, which is found in plants and animals, consists of oxygenase and reductase domains that are linked via a regulatory calmodulin-binding domain. Upon calcium-induced calmodulin binding, the reductase and oxygenase domains form a complex, allowing electrons to flow from NADPH via FAD and FMN to the active center. May produce superoxide under certain conditions. cf. EC 1.14.13.165, nitric-oxide synthase [NAD(P)H dependent]. Group: Enzymes. Synonyms: nitric oxide synthetase; endothelium-derived relaxation factor-forming enzyme; endothelium-derived relaxing factor synthase; NO synthase; NADPH-diaphorase. Enzyme Commission Number: EC 1.14.13.39. CAS No. 125978-95-2. NOSs. 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-0846; nitric-oxide synthase (NADPH); EC 1.14.13.39; 125978-95-2; nitric oxide synthetase; endothelium-derived relaxation factor-forming enzyme; endothelium-derived relaxing factor synthase; NO synthase; NADPH-diaphorase. Cat No: EXWM-0846. | |
| ORY-1001 dihydrochloride | ORY-1001 is a lysine specific demethylase 1 inhibitor under the development of Oryzon with IC50 value < 20nM. It selectively inhibits related FAD dependent aminoxidases (MAO-A/B, IL4I1, KDM1B > 100uM, SMOX 7uM). ORY-1001 can induce apoptosis in THP-1 and inhibit proliferation and colony formation of MV(4;11) (MLL-AF4) cells (EC50 <1nM). In THP-1 (MLL-AF9) cells, ORY-1001 results in a time-dose dependent me2H3K4 accumulation at KDM1A target genes and concomitant induction of differentiation markers. Synonyms: RG-6016; RG 6016; RG6016; ORY-1001 2HCl; ORY 1001 2HCl; ORY1001 2HCl; (1R,4R)-N1-((1R,2S)-2-phenylcyclopropyl)cyclohexane-1,4-diamine dihydrochloride. Grades: >98%. CAS No. 1431326-61-2. Molecular formula: C15H24Cl2N2. Mole weight: 303.27. |  |
| pentalenolactone D synthase | A FAD-dependent oxygenase. Isolated from the bacteria Streptomyces exfoliatus and Streptomyces arenae. The ketone undergoes a biological Baeyer-Villiger reaction. Part of the pathway of pentalenolactone biosynthesis. Group: Enzymes. Synonyms: penE (gene name); pntE (gene name). Enzyme Commission Number: EC 1.14.13.170. 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-0768; pentalenolactone D synthase; EC 1.14.13.170; penE (gene name); pntE (gene name). Cat No: EXWM-0768. | |
| phenol 2-monooxygenase (FADH2) | The enzyme catalyses the ortho-hydroxylation of simple phenols into the corresponding catechols. It accepts 4-methylphenol, 4-chlorophenol, and 4-fluorophenol as well as 4-nitrophenol, 3-nitrophenol, and resorcinol. The enzyme is part of a two-component system that also includes an NADH-dependent flavin reductase. It is strictly dependent on FADH2 and does not accept FMNH2. cf. EC 1.14.13.7, phenol 2-monooxygenase (NADPH). Group: Enzymes. Synonyms: pheA1 (gene name). Enzyme Commission Number: EC 1.14.14.20. 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-0917; phenol 2-monooxygenase (FADH2); EC 1.14.14.20; pheA1 (gene name). Cat No: EXWM-0917. | |
| protoasukamycin 4-monooxygenase | The enzyme, characterized from the bacterium Streptomyces nodosus subsp. asukaensis, is involved in the biosynthesis of the antibiotic asukamycin. Requires a flavin cofactor, with no preference among FMN, FAD or riboflavin. When flavin concentration is low, activity is enhanced by the presence of the NADH-dependent flavin-reductase AsuE2. Group: Enzymes. Enzyme Commission Number: EC 1.14.13.215. 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-0817; protoasukamycin 4-monooxygenase; EC 1.14.13.215. Cat No: EXWM-0817. | |
| protoporphyrinogen oxidase | This is the last common enzyme in the biosynthesis of chlorophylls and heme. Two isoenzymes exist in plants: one in plastids and the other in mitochondria. This is the target enzyme of phthalimide-type and diphenylether-type herbicides. The enzyme from oxygen-dependent species contains FAD. Also slowly oxidizes mesoporphyrinogen IX. Group: Enzymes. Synonyms: protoporphyrinogen IX oxidase; protoporphyrinogenase; PPO; Protox; HemG; HemY. Enzyme Commission Number: EC 1.3.3.4. CAS No. 53986-32-6. 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-1378; protoporphyrinogen oxidase; EC 1.3.3.4; 53986-32-6; protoporphyrinogen IX oxidase; protoporphyrinogenase; PPO; Protox; HemG; HemY. Cat No: EXWM-1378. | |
| pyranose dehydrogenase (acceptor) | Requires FAD. A number of aldoses and ketoses in pyranose form, as well as glycosides, gluco-oligosaccharides, sucrose and lactose can act as a donor. 1,4-Benzoquinone or ferricenium ion (ferrocene oxidized by removal of one electron) can serve as acceptor. Unlike EC 1.1.3.10, pyranose oxidase, this fungal enzyme does not interact with O2 and exhibits extremely broad substrate tolerance with variable regioselectivity (C-3, C-2 or C-3 + C-2 or C-3 + C-4) for (di)oxidation of different sugars. D-Glucose is exclusively or preferentially oxidized at C-3 (depending on the enzyme source), but can also be oxidized at C-2 + C-3. The enzyme also acts on 1?4-α- and 1?4-β-gluco-oligosaccharides, non-reducing gluco-oligosaccharides and L-arabinose, which are not substrates of EC 1.1.3.10. Sugars are oxidized in their pyranose but not in their furanose form. Group: Enzymes. Synonyms: pyranose dehydrogenase; pyranose-quinone oxidoreductase; quinone-dependent pyranose d. Enzyme Commission Number: EC 1.1.99.29. CAS No. 190606-21-4. 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-0457; pyranose dehydrogenase (acceptor); EC 1.1.99.29; 190606-21-4; pyranose dehydrogenase; pyranose-quinone oxidoreductase; quinone-dependent pyranose dehydrogenase; PDH. Cat No: EXWM-0457. | |
| pyruvate oxidase | A flavoprotein (FAD) requiring thiamine diphosphate. Two reducing equivalents are transferred from the resonant carbanion/enamine forms of 2-hydroxyethyl-thiamine-diphosphate to the adjacent flavin cofactor, yielding 2-acetyl-thiamine diphosphate (AcThDP) and reduced flavin. FADH2 is reoxidized by O2 to yield H2O2 and FAD and AcThDP is cleaved phosphorolytically to acetyl phosphate and thiamine diphosphate. Group: Enzymes. Synonyms: pyruvic oxidase; phosphate-dependent pyruvate oxidase. Enzyme Commission Number: EC 1.2.3.3. CAS No. 9001-96-1. Pyruvate oxidase. 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-1210; pyruvate oxidase; EC 1.2.3.3; 9001-96-1; pyruvic oxidase; phosphate-dependent pyruvate oxidase. Cat No: EXWM-1210. | |
| riboflavin reductase [NAD(P)H] | Catalyses the reduction of soluble flavins by reduced pyridine nucleotides. Highest activity with riboflavin. When NADH is used as acceptor, the enzyme can also utilize FMN and FAD as substrates, with lower activity than riboflavin. When NADPH is used as acceptor, the enzyme has a very low activity with FMN and no activity with FAD. Group: Enzymes. Synonyms: NAD(P)H-FMN reductase (ambiguous); NAD(P)H-dependent FMN reductase (ambiguous); NAD(P)H:FMN oxidoreductase (ambiguous); NAD(P)H:flavin oxidoreductase (ambiguous); NAD(P)H2 dehydrogenase (FMN) (ambiguous); NAD(P)H2:FMN oxidoreductas. Enzyme Commission Number: EC 1.5.1.41. 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-1522; riboflavin reductase [NAD(P)H]; EC 1.5.1.41; NAD(P)H-FMN reductase (ambiguous); NAD(P)H-dependent FMN reductase (ambiguous); NAD(P)H:FMN oxidoreductase (ambiguous); NAD(P)H:flavin oxidoreductase (ambiguous); NAD(P)H2 dehydrogenase (FMN) (ambiguous); NAD(P)H2:FMN oxidoreductase (ambiguous); riboflavin mononucleotide reductase (ambiguous); flavine mononucleotide reductase (ambiguous); riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide (phosphate)) reductase; flavin mononucleotide reductase (ambiguous); riboflavine mononucleotide reductase (ambiguous); Fre. Cat No: EXWM-1522. | |
| trypanothione-disulfide reductase | Trypanothione disulfide is the oxidized form of N1,N8-bis(glutathionyl)-spermidine from the insect-parasitic trypanosomatid Crithidia fasciculata. The enzyme from Crithidia fasciculata is a flavoprotein (FAD), whose activity is dependent on a redox-active cystine at the active centre. (cf. EC 1.8.1.7, glutathione-disulfide reductase). Group: Enzymes. Synonyms: trypanothione reductase; NADPH2:trypanothione oxidoreductase. Enzyme Commission Number: EC 1.8.1.12. CAS No. 102210-35-5. 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-1638; trypanothione-disulfide reductase; EC 1.8.1.12; 102210-35-5; trypanothione reductase; NADPH2:trypanothione oxidoreductase. Cat No: EXWM-1638. | |
| Uridylyl-(3'-5')-adenosine | Uridylyl-(3'-5')-adenosine, an indispensable enzyme in the field of biomedicine, holds immense significance owing to its pivotal role in nucleotide metabolism. Its involvement in the synthesis of flavin adenine dinucleotide (FAD), a fundamental coenzyme for diverse enzymatic reactions, further amplifies its importance. Prominently employed for investigating FAD-dependent enzymes and their potential implications in a wide array of ailments like cancer, cardiovascular disorders, and neurodegenerative conditions, this product emerges as a scholarly tool in scientific exploration. Synonyms: UpA RNA Dinucleotide (5'-3'); Uridylyladenosine; Uridine-3',5'-adenosine phosphate; (3',5')-Uridylyladenosine. Grades: ≥95% by AX-HPLC. CAS No. 3256-24-4. Molecular formula: C19H24N7O12P. Mole weight: 573.40. | |
| xanthine dehydrogenase | Acts on a variety of purines and aldehydes, including hypoxanthine. The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein. The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The mammalian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). During purification the enzyme is largely converted to an O2-dependent form, xanthine oxidase (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo. Group: Enzymes. Synonyms: NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase. Enzyme Commission Number: EC 1.17.1.4. CAS No. 9054-84-6. XDH. 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-1082; xanthine dehydrogenase; EC 1.17.1.4; 9054-84-6; NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase. Cat No: EXWM-1082. | |
| xanthine oxidase | An iron-molybdenum flavoprotein (FAD) containing [2Fe-2S] centres. Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes, but is distinct from EC 1.2.3.1, aldehyde oxidase. Under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 O2.- + 2 H+. The mammalian enzyme predominantly exists as an NAD-dependent dehydrogenase (EC 1.17.1.4, xanthine dehydrogenase). During purification the enzyme is largely converted to the O2-dependent xanthine oxidase form (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo. Group: Enzymes. Synonyms: hypoxanthine o. Enzyme Commission Number: EC 1.17.3.2. CAS No. 9002-17-9. 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-1088; xanthine oxidase; EC 1.17.3.2; 9002-17-9; hypoxanthine oxidase; hypoxanthine:oxygen oxidoreductase; Schardinger enzyme; xanthine oxidoreductase; hypoxanthine-xanthine oxidase; xanthine:O2 oxidoreductase; xanthine:xanthine oxidase. Cat No: EXWM-1088. | |
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