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| Product | Description | |
|---|---|---|
| 2-(2,4-Dichlorophenyl)-2-methyl-4-propyl-1,3-dioxolane | An impurities of Propiconazole. Propiconazole is a triazole fungicide inhibiting fungicide due to its binding with and inhibiting the 14-alpha demethylase enzyme from demethylating a precursor to ergosterol. Synonyms: 2-(2,4-Dichlorophenyl)-2-methyl-4-propyl-1,3-dioxolane; 83833-32-3; EINECS 281-007-8; 1,3-Dioxolane,2-(2,4-dichlorophenyl)-2-methyl-4-propyl-; SCHEMBL8336206; DTXSID10868759; SR-01000390593; SR-01000390593-1. Grades: > 95%. CAS No. 83833-32-3. Molecular formula: C13H16Cl2O2. Mole weight: 275.18. |  |
| 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase | Binds 2 Mg2+ ions that are essential for activity. The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the bacterium Streptococcus pneumoniae also harbours the activity of EC 4.1.2.25, dihydroneopterin aldolase, the enzyme from the plant Arabidopsis thaliana harbours the activity of EC 2.5.1.15, dihydropteroate synthase, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with both of the two above mentioned activities. Group: Enzymes. Synonyms: 2-amino-4-hydroxy-6-hydroxymethyldi. Enzyme Commission Number: EC 2.7.6.3. CAS No. 37278-23-2. 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-3222; 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase; EC 2.7.6.3; 37278-23-2; 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase; H2-pteridine-CH2OH pyrophosphokinase; 7,8-dihydroxymethylpterin-pyrophosphokinase; HPPK; 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase; hydroxymethyldihydropteridine pyrophosphokinase; ATP:2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine 6'-diphosphotransferase. Cat No: EXWM-3222. |  |
| 3-ketovalidoxylamine C-N-lyase | Requires Ca2+. Eliminates 4-nitroaniline from 4-nitrophenyl-3-ketovalidamine, or 4-nitrophenol from 4-nitrophenyl-α-D-3-dehydroglucoside. Involved in the degradation of the fungicide validamycin A by Flavobacterium saccharophilum. Group: Enzymes. Synonyms: 3-ketovalidoxylamine A C-N-lyase; p-nitrophenyl-3-ketovalidamine p-nitroaniline lyase; 4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase. Enzyme Commission Number: EC 4.3.3.1. CAS No. 99889-98-2. 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-5302; 3-ketovalidoxylamine C-N-lyase; EC 4.3.3.1; 99889-98-2; 3-ketovalidoxylamine A C-N-lyase; p-nitrophenyl-3-ketovalidamine p-nitroaniline lyase; 4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase. Cat No: EXWM-5302. | |
| adenylyl-sulfate kinase | The human phosphoadenosine-phosphosulfate synthase (PAPSS) system is a bifunctional enzyme (fusion product of two catalytic activities). In a first step, sulfate adenylyltransferase catalyses the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate. The second step is catalysed by the adenylylsulfate kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme-bound APS and ATP. In contrast, in bacteria, yeast, fungi and plants, the formation of PAPS is carried out by two individual polypeptides, sulfate adenylyltransferase (EC 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25). Group: Enzymes. Synonyms: adenylylsulfate kinase (phosphorylating); 5'-phosphoadenosine sulfate kinase; adenosine 5'-phosphosulfate kinase; adenosine phosphosulfate kinase; adenosine phosphosulfokinase; . Enzyme Commission Number: EC 2.7.1.25. CAS No. 9012-38-8. 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-3055; adenylyl-sulfate kinase; EC 2.7.1.25; 9012-38-8; adenylylsulfate kinase (phosphorylating); 5'-phosphoadenosine sulfate kinase; adenosine 5'-phosphosulfate kinase; adenosine phosphosulfate kinase; adenosine phosphosulfokinase; adenosine-5'-phosphosulfate-3'-phosphokinase; APS kinase. Cat No: EXWM-3055. | |
| agroclavine dehydrogenase | The enzyme participates in the biosynthesis of ergotamine, an ergot alkaloid produced by some fungi of the Clavicipitaceae family. The reaction is catalysed in the opposite direction to that shown. The substrate for the enzyme is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione. Group: Enzymes. Synonyms: easG (gene name). Enzyme Commission Number: EC 1.5.1.46. 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-1527; agroclavine dehydrogenase; EC 1.5.1.46; easG (gene name). Cat No: EXWM-1527. | |
| alcohol oxidase | The enzymes from the fungi Candida methanosorbosa and several Basidiomycetes species contain an FAD cofactor. The enzyme from the phytopathogenic fungi Colletotrichum graminicola and Colletotrichum gloeosporioides utilize a mononuclear copper-radical mechanism. The enzyme acts on primary alcohols and unsaturated alcohols, and has much lower activity with branched-chain and secondary alcohols. Group: Enzymes. Synonyms: ethanol oxidase; alcohol:oxygen oxidoreductase. Enzyme Commission Number: EC 1.1.3.13. CAS No. 9073-63-6. Alcohol 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-0395; alcohol oxidase; EC 1.1.3.13; 9073-63-6; ethanol oxidase; alcohol:oxygen oxidoreductase. Cat No: EXWM-0395. | |
| α-glucuronidase | Considerable differences in the specificities of the enzymes from different fungi for α-D-glucosiduronates have been reported. Activity is also found in the snail. Group: Enzymes. Synonyms: α-glucosiduronase. Enzyme Commission Number: EC 3.2.1.139. CAS No. 37259-81-7. α-Glucuronidase. 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-3821; α-glucuronidase; EC 3.2.1.139; 37259-81-7; α-glucosiduronase. Cat No: EXWM-3821. | |
| aristolochene synthase | The initial internal cyclization produces the monocyclic intermediate germacrene A; further cyclization and methyl transfer converts the intermediate into aristolochene. While in some species germacrene A remains as an enzyme-bound intermediate, it has been shown to be a minor product of the reaction in Penicillium roqueforti (see also EC 4.2.3.23, germacrene-A synthase). The enzyme from Penicillium roqueforti requires Mg2+. Mn2+ can partially substitute, at low concentrations. Aristolochene is the likely parent compound for a number of sesquiterpenes produced by filamentous fungi. Group: Enzymes. Synonyms: sesquiterpene cyclase; trans,trans-farnesyl diphosphate aristolochene-lyase; trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, aristolochene-forming). Enzyme Commission Number: EC 4.2.3.9. CAS No. 94185-89-4. 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-5253; aristolochene synthase; EC 4.2.3.9; 94185-89-4; sesquiterpene cyclase; trans,trans-farnesyl diphosphate aristolochene-lyase; trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, aristolochene-forming). Cat No: EXWM-5253. | |
| aspartate-semialdehyde dehydrogenase | In enzymology, an aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) is an enzyme that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. It forms an early branch point in the metabolic pathway forming lysine, methionine, leucine and isoleucine from aspartate. This pathway also produces diaminopimelate which plays an essential role in bacterial cell wall formation. There is particular interest in ASADH as disabling this enzyme proves fatal to the organism giving rise to the possibility of a new class of antibiotics, fungicides, and herbicides aimed at inhibiting it. Group: Enzymes. Synonyms: aspartate semialdehyde dehydrogenase; aspartic semialdehyde dehydrogenase; L-aspartate-β-semialdehyde:NADP+ oxidoreductase (phosphorylating); aspartic β-semialdehyde dehydrogenase; ASA dehydrogenase. Enzyme Commission Number: EC 1.2.1.11. CAS No. 9000-98-0. 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-1117; aspartate-semialdehyde dehydrogenase; EC 1.2.1.11; 9000-98-0; aspartate semialdehyde dehydrogenase; aspartic semialdehyde dehydrogenase; L-aspartate-β-semialdehyde:NADP+ oxidoreductase (phosphorylating); aspartic β-semialdehyde dehydrogenase; ASA dehydrogenase. Cat No: EXWM-1117. | |
| Cellobiohydrolase I from Hypocrea jecorina, Recombinant | Cellulose 1,4-beta-cellobiosidase (non-reducing end) is an enzyme with system name 4-beta-D-glucan cellobiohydrolase (non-reducing end). This enzyme catalyses the following chemical reaction:Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing [cellobiose] from the non-reducing ends of the chains. Cellubiohydrolase i is an enzyme present in many fungi, but particularly wood rot fungi. it is a monomer of 53 kda with a catalytic domain and a cellulose binding domain. the reaction adds water to the glucose bonds in cellulose (non-reducing ends of the chain), yielding cellobiose. Applications: Cellobiohydrolase i can be used in com...ellobiohydrolase; 1,4-beta-D-glucan cellobiohydrolase. Enzyme Commission Number: EC 3.2.1.91. CAS No. 253-465-9. Cellulose 1,4-beta-cellobiosidase. Activity: 0.13 U/mg. Form: Enzyme is provided in a sodium acetate and ammonium sulfate solution, containing 0.02% sodium azide. Source: Corn. Species: Hypocrea jecorina. Cellobiohydrolase I; Cellobiosidase; EC 3.2.1.91; Cel7A; Cellulase; exo-cellobiohydrolase; beta-1,4-glucan cellobiohydrolase; beta-1,4-glucan cellobiosylhydrolase; 1,4-beta-glucan cellobiosidase; exoglucanase; avicelase; CBH 1; C1 cellulase; cellobiohydrolase; exo-beta-1,4-glucan cellobiohydrolase; 1,4-beta-D-glucan cellobiohydrolase. Cat No: NATE-0112. | |
| cellobionic acid phosphorylase | The enzyme occurs in cellulolytic bacteria and fungi. It catalyses the reversible phosphorolysis of cellobionic acid. In the synthetic direction it produces 4-O-β-D-glucopyranosyl-D-glucuronate from α-D-glucose 1-phosphate and D-glucuronate with low activity. Group: Enzymes. Enzyme Commission Number: EC 2.4.1.321. 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-2558; cellobionic acid phosphorylase; EC 2.4.1.321. Cat No: EXWM-2558. | |
| Chitinase 18A from Bacillus cereus, Recombinant | Chitosanase catalyzes the endohydrolysis of β (1,4) linkages between N-acetyl-D-glucosamine and D-glucosamine residues in partially deacetylated chitosan. Chitosanase from Streptomyces griseus is capable of hydrolyzing both chitosan and carboxymethyl cellulose. It is used for the lysis of cell walls of fungi belonging to the group Mucorales. It is found in several types of microorganisms. Group: Enzymes. Synonyms: Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase. Enzyme Commission Number: EC 3.2.1.14. Purity: >90% by SDS-PAGE. Chitosanase. Mole weight: 38.3 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacillus cereus. Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase; Chitosanase 18A. Cat No: NATE-1377. | |
| Chitinase 18A from Bacillus licheniformis, Recombinant | Chitosanase catalyzes the endohydrolysis of β (1,4) linkages between N-acetyl-D-glucosamine and D-glucosamine residues in partially deacetylated chitosan. Chitosanase from Streptomyces griseus is capable of hydrolyzing both chitosan and carboxymethyl cellulose. It is used for the lysis of cell walls of fungi belonging to the group Mucorales. It is found in several types of microorganisms. Group: Enzymes. Synonyms: Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase. Enzyme Commission Number: EC 3.2.1.14. Purity: >90% by SDS-PAGE. Chitosanase. Mole weight: 49.2 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacillus licheniformis. Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase; Chitosanase 18A. Cat No: NATE-1378. | |
| Chitinase 18A from Clostridium thermocellum, Recombinant | Chitosanase catalyzes the endohydrolysis of β (1,4) linkages between N-acetyl-D-glucosamine and D-glucosamine residues in partially deacetylated chitosan. Chitosanase from Streptomyces griseus is capable of hydrolyzing both chitosan and carboxymethyl cellulose. It is used for the lysis of cell walls of fungi belonging to the group Mucorales. It is found in several types of microorganisms. Group: Enzymes. Synonyms: Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase. Enzyme Commission Number: EC 3.2.1.14. Purity: >90% by SDS-PAGE. Chitosanase. Mole weight: 43.9 kDa. Activity: 25 U/mg. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Clostridium thermocellum. Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase; Chitosanase 18A. Cat No: NATE-1379. | |
| Chitosanase 46A from Bacillus subtilis, Recombinant | Chitosanase catalyzes the endohydrolysis of β (1,4) linkages between N-acetyl-D-glucosamine and D-glucosamine residues in partially deacetylated chitosan. Chitosanase from Streptomyces griseus is capable of hydrolyzing both chitosan and carboxymethyl cellulose. It is used for the lysis of cell walls of fungi belonging to the group Mucorales. It is found in several types of microorganisms. Group: Enzymes. Synonyms: Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase. Enzyme Commission Number: EC 3.2.1.132. CAS No. 51570-20-8. Purity: >90% by SDS-PAGE. Chitosanase. Mole weight: 29.5 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacillus subtilis. Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase; Chitosanase 46A. Cat No: NATE-1376. | |
| Chitosanase 8B from Bacillus cereus, Recombinant | Chitosanase catalyzes the endohydrolysis of β (1,4) linkages between N-acetyl-D-glucosamine and D-glucosamine residues in partially deacetylated chitosan. Chitosanase from Streptomyces griseus is capable of hydrolyzing both chitosan and carboxymethyl cellulose. It is used for the lysis of cell walls of fungi belonging to the group Mucorales. It is found in several types of microorganisms. Group: Enzymes. Synonyms: Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase. Enzyme Commission Number: EC 3.2.1.132. CAS No. 51570-20-8. Purity: >90% by SDS-PAGE. Chitosanase. Mole weight: 47.8 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacillus cereus. Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase; Chitosanase 8B. Cat No: NATE-1375. | |
| Destriazolyl Bromo Propiconazole (Mixture of Diastereomers) | An impurities of Propiconazole. Propiconazole is a triazole fungicide inhibiting fungicide due to its binding with and inhibiting the 14-alpha demethylase enzyme from demethylating a precursor to ergosterol. Synonyms: 2-(Bromomethyl)-2-(2,4-dichlorophenyl)-4-propyl-1,3-dioxolane; 2-Bromomethyl-2-(2,4-dichlorophenyl)-4-propyldioxolane. Grades: > 95%. CAS No. 60207-89-8. Molecular formula: C13H15BrCl2O2. Mole weight: 354.07. | |
| DEXTRANASE | DEXTRANASE. Synonyms: dextranase from paecilomyces lilacinus;Dextranase Paecilomyces lilacinus;dextranase partially purified. CAS No. 9025-70-1. Product ID: CDF4-0042. Category: Enzyme Preparations. Product Keywords: Food Ingredients; Enzyme Preparations; DEXTRANASE; CDF4-0042; 9025-70-1; 232-803-9; 9025-70-1. Purity: 0.99. Color: Brown. EC Number: 232-803-9. Physical State: Solution. Storage: 2-8°C. Product Description: Dextranase from fungi belong to the glycoside hydrolase families (GH) 49. Dextranase from Penicillium sp. are stable at varying temperature and pH. |  |
| dihydromonacolin L hydroxylase | A heme-thiolate protein (cytochrome P-450). The dehydration of 3α-hydroxy-3,5-dihydromonacolin L acid is believed to be spontaneous. The enzyme from fungi also catalyses the reaction of EC 1.14.13.198, monacolin L hydroxylase. Group: Enzymes. Synonyms: LovA (ambiguous). Enzyme Commission Number: EC 1.14.13.197. 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-0797; dihydromonacolin L hydroxylase; EC 1.14.13.197; LovA (ambiguous). Cat No: EXWM-0797. | |
| dihydroneopterin aldolase | The enzyme participates in folate (in bacteria, plants and fungi) and methanopterin (in archaea) biosynthesis. The enzymes from the bacterium Escherichia coli and the plant Arabidopsis thaliana also catalyse the epimerisation of the 2' hydroxy-group (EC 5.1.99.8, 7,8-dihydroneopterin epimerase). The enzyme from the bacterium Mycobacterium tuberculosis is trifunctional and also catalyses EC 5.1.99.8 and EC 1.13.11.81, 7,8-dihydroneopterin oxygenase. The enzyme from the yeast Saccharomyces cerevisiae also catalyses the two subsequent steps in the folate biosynthesis pathway - EC 2.7.6.3, 2-amino-4-hydroxy-6-(hydroxymethyl)dihydropteridine diphosphokinase, and EC 2.5.1.15, dihydropteroate synthase. Group: Enzymes. Synonyms: 7,8-dihydroneopterin aldolase; 2-amino-. Enzyme Commission Number: EC 4.1.2.25. CAS No. 37290-59-8. 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-4864; dihydroneopterin aldolase; EC 4.1.2.25; 37290-59-8; 7,8-dihydroneopterin aldolase; 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine glycolaldehyde-lyase; 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine glycolaldehyde-lyase (2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-forming); DHNA; mptD (gene name); folB (gene name). Cat No: EXWM-4864. | |
| dihydropteroate synthase | The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the plant Arabidopsis thaliana also harbors the activity of EC 2.7.6.3, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with the two above mentioned activities as well as EC 4.1.2.25, dihydroneopterin aldolase. Group: Enzymes. Synonyms: dihydropteroate pyrophosphorylase; DHPS; 7,8-dihydropteroate synthase; 7,8-dihydr. Enzyme Commission Number: EC 2.5.1.15. CAS No. 9055-61-2. 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-2751; dihydropteroate synthase; EC 2.5.1.15; 9055-61-2; dihydropteroate pyrophosphorylase; DHPS; 7,8-dihydropteroate synthase; 7,8-dihydropteroate synthetase; 7,8-dihydropteroic acid synthetase; dihydropteroate synthetase; dihydropteroic synthetase; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-diphosphate:4-aminobenzoate 2-amino-4-hydroxydihydropteridine-6-methenyltransferase; (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl-diphosphate:4-aminobenzoate 2-amino-4-hydroxydihydropteridine-6-methenyltransferase. Cat No: EXWM-2751. | |
| dye decolorizing peroxidase | Heme proteins with proximal histidine secreted by basidiomycetous fungi and eubacteria. They are similar to EC 1.11.1.16 versatile peroxidase (oxidation of Reactive Black 5, phenols, veratryl alcohol), but differ from the latter in their ability to efficiently oxidize a number of recalcitrant anthraquinone dyes, and inability to oxidize Mn(II). The model substrate Reactive Blue 5 is converted with high efficiency via a so far unique mechanism that combines oxidative and hydrolytic steps and leads to the formation of phthalic acid. Bacterial TfuDyP catalyses sulfoxidation. Group: Enzymes. Synonyms: DyP; DyP-type peroxidase. Enzyme Commission Number: EC 1.11.1.19. 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-0500; dye decolorizing peroxidase; EC 1.11.1.19; DyP; DyP-type peroxidase. Cat No: EXWM-0500. | |
| germacradienol synthase | Requires Mg2+ for activity. H-1si of farnesyl diphosphate is lost in the formation of (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol. Formation of (-)-germacrene D involves a stereospecific 1,3-hydride shift of H-1si of farnesyl diphosphate. Both products are formed from a common intermediate. Other enzymes produce germacrene D as the sole product using a different mechanism. The enzyme mediates a key step in the biosynthesis of geosmin (see EC 4.1.99.16 geosmin synthase), a widely occurring metabolite of many streptomycetes, bacteria and fungi. Also catalyses the reaction of EC 4.2.3.75, (-)-germacrene D synthase. Group: Enzymes. Synonyms: germacradienol/germacrene-D synthase; 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase [(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol-forming]. Enzyme Commission Number: EC 4.2.3.22. CAS No. 211049-88-6. 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-5179; germacradienol synthase; EC 4.2.3.22; 211049-88-6; germacradienol/germacrene-D synthase; 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase [(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol-forming]. Cat No: EXWM-5179. | |
| glutamyl-tRNA reductase | This enzyme forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as theC5 pathway.The route shown in the diagram is used in most eubacteria, and in all archaebacteria, algae and plants. However, in the α-proteobacteria, EC 2.3.1.37, 5-aminolevulinate synthase, is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic α-proteobacterium. Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37. Group: Enzymes. Enzyme Commission Number: EC 1.2.1.70. CAS No. 119940-26-0. 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-1172; glutamyl-tRNA reductase; EC 1.2.1.70; 119940-26-0. Cat No: EXWM-1172. | |
| inorganic diphosphatase | Specificity varies with the source and with the activating metal ion. The enzyme from some sources may be identical with EC 3.1.3.1 (alkaline phosphatase) or EC 3.1.3.9 (glucose-6-phosphatase). A form of this enzyme with a molecular mass of about 90 kDa is found in tonoplasts of plants and fungi, where it imports protons from the cytosol into the vacuolar lumen. Group: Enzymes. Enzyme Commission Number: EC 3.6.1.1. CAS No. 9024-82-2. Inorganic pyrophosphatase. 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-4593; inorganic diphosphatase; EC 3.6.1.1; 9024-82-2. Cat No: EXWM-4593. | |
| Kresoxim-methyl | Kresoxim-methyl (BAS 490 F), a Strobilurin-based fungicide, inhibits the respiration at the complex III (cytochrome bc1 complex). Kresoxim-methyl binds to complex III from yeast with an apparent K d of 0.07 μM proving a high affinity for this enzyme [1] [2]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: BAS 490 F. CAS No. 143390-89-0. Pack Sizes: 5 mg; 10 mg; 25 mg. Product ID: HY-125776. |  |
| Laccase | Laccase. Synonyms: Denilase ii s;Novozyme 809;p-Diphenol oxidase;Sp 504;Urushiol oxidase;Laccase from Rhus vernicifera,Benzenediol:oxygen oxidoreductase;Laccase, from Trametes versicolor, >=0.5units/mg;LACCASE FROM TRAMETES SPEC., 0.8+ UMG POWDER. CAS No. 80498-15-3. Pack Sizes: 1 kg. Product ID: CDF4-0053. Category: Enzyme Preparations. Product Keywords: Food Ingredients; Enzyme Preparations; Laccase; CDF4-0053; 80498-15-3; 420-150-4; 80498-15-3. Purity: 0.99. Color: Slightly beige. EC Number: 420-150-4. Physical State: Powder. Storage: 2-8°C. Application: Laccase is polyphenol oxidase found in many plants, fungi and microorganisms. Laccases may be useful in enzymatic biofuel systems, teeth whitening, textile dyeing, and in other applications that require the removal of oxygen. Density: 1.37[at 20°C]. Product Description: Laccase is a kind of copper-containing oxidase existing in many kinds of plants, fungi and microbes. It mainly takes effect on phenol-like compounds including phenols, polyphenols and anilines, performing one-electron oxidation. | |
| lignin peroxidase | A hemoprotein, involved in the oxidative breakdown of lignin by white-rot basidiomycete fungi. The reaction involves an initial oxidation of the heme iron by hydrogen peroxide, forming compound I (FeIV=O radical cation) at the active site. A single one-electron reduction of compound I by an electron derived from a substrate molecule yields compound II (FeIV=O non-radical cation), followed by a second one-electron transfer that returns the enzyme to the ferric oxidation state. The electron transfer events convert the substrate molecule into a transient cation radical intermediate that fragments spontaneously. The enzyme can act on a wide range of aromatic compounds, including methoxy...escued by interaction with two molecules of the free radical products. In the case of veratryl alcohol, such an interaction yields two molecules of veratryl aldehyde. Group: Enzymes. Synonyms: diarylpropane oxygenase; ligninase I; diarylpropane peroxidase; LiP; diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving); 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol:hydrogen-peroxide oxidoreductase (incorrect); (3,4-dimethoxyphenyl)methanol:hydrogen-peroxide oxidoreductase. Enzyme Commission Number: EC 1.11.1.14. CAS No. 93792-13-3. LiP. 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-0 | |
| mitochondrial processing peptidase | Known from the mitochondrial matrix of fungi and mammals. Formed from two subunits, both homologous with pitrilysin, and the products of the MAS1 and MAS2 genes in yeast. In peptidase family M16 (pitrilysin family). Group: Enzymes. Synonyms: processing enhancing peptidase (for one of two subunits); mitochondrial protein precursor-processing proteinase; matrix peptidase; matrix processing peptidase; matrix processing proteinase; mitochondrial protein precursor-processing proteinase; MPP. Enzyme Commission Number: EC 3.4.24.64. CAS No. 86280-61-7. 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-4347; mitochondrial processing peptidase; EC 3.4.24.64; 86280-61-7; processing enhancing peptidase (for one of two subunits); mitochondrial protein precursor-processing proteinase; matrix peptidase; matrix processing peptidase; matrix processing proteinase; mitochondrial protein precursor-processing proteinase; MPP. Cat No: EXWM-4347. | |
| monacolin L hydroxylase | A heme-thiolate protein (cytochrome P-450). The enzyme from fungi also catalyses the reaction of EC 1.14.13.197, dihydromonacolin L hydroxylase. Group: Enzymes. Synonyms: LovA (ambiguous). Enzyme Commission Number: EC 1.14.13.198. 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-0798; monacolin L hydroxylase; EC 1.14.13.198; LovA (ambiguous). Cat No: EXWM-0798. | |
| mucorpepsin | Isolated from the zygomycete fungi Mucor pusillus and M. miehei. The two species variants show 83% sequence identity and are immunologically crossreactive. In peptidase family A1 (pepsin A family). Formerly included in EC 3.4.23.6. Group: Enzymes. Synonyms: Mucor rennin; Mucor aspartic proteinase; Mucor acid proteinase; Mucor acid protease; Mucor miehei aspartic proteinase; Mucor miehei aspartic protease; Mucor aspartic proteinase; Mucor pusillus emporase; Fromase 100; Mucor pusillus rennin; Fromase 46TL; Mucor miehei rennin. Enzyme Commission Number: EC 3.4.23.23. CAS No. 148465-73-0. Rennin. 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-4261; mucorpepsin; EC 3.4.23.23; 148465-73-0; Mucor rennin; Mucor aspartic proteinase; Mucor acid proteinase; Mucor acid protease; Mucor miehei aspartic proteinase; Mucor miehei aspartic protease; Mucor aspartic proteinase; Mucor pusillus emporase; Fromase 100; Mucor pusillus rennin; Fromase 46TL; Mucor miehei rennin. Cat No: EXWM-4261. | |
| Myriocin (Thermozymocidin, ISP) | Myriocin is an a-amino fatty acid derived from species of several genera of fungi, notably Myriococcum, Melanconis and Isaria. Myriocin is a potent inhibitor of sphingosine biosynthesis by blocking the first enzyme in the pathway, serine palmitoyltransferase. Myriocin induces apoptosis by depletion of cellular sphingolipids, inhibits proliferation of IL-2-dependent mouse cytotoxic cells and is a potent immunosuppressant. Group: Biochemicals. Grades: Highly Purified. CAS No. 35891-70-4. Pack Sizes: 2.5mg. US Biological Life Sciences. |  Worldwide |
| Native Arthrobacter luteus Lyticase | Lyticase hydrolyzes poly-β (1?3)-glucose such as yeast cell wall glucan. Applications: Yeast cells are difficult to disrupt because the cell walls may form capsules or resistant spores. dna can be extracted from yeast by using lysing enzymes such as lyticase, chitinase, zymolase, and gluculase to induce partial spheroplast formation; spheroplasts are subsequently lysed to release dna. lyticase is preferred to digest cell walls of yeast and generate spheroplasts from fungi for transformation. reported to be useful for lysis of ashbya, candida, debaryomyces, eremothecium, endomyces, hansenula, hanseniaspora, kloeckera, kluyveromyces, lipomyces, metschikowia, pichia, pullularia, torulopsis, saccharomyces, saccharomycopsis, saccharomycodes, and schwanniomyces species. Group: Enzymes. Synonyms: Lyticase; 37340-57-1. CAS No. 37340-57-1. Lyticase. Activity: > 200 units/mg solid; > 1,500 units/mg protein; > 2,000 units/mg protein, Protein > 20 % by biuret. Storage: 2-8°C. Form: lyophilized powder. Source: Arthrobacter luteus. Lyticase; 37340-57-1. Cat No: NATE-0431. | |
| Native Aspergillus niger Cellulase | Cellulase is any of several enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis, the decomposition of cellulose and of some related polysaccharides; specifically, the hydrolysis of the 1,4-beta-D-glycosidic linkages in cellulose, hemicellulose, lichenin, and cereal beta-D-glucans. Cellulases break down the cellulose molecule into monosaccharides ("simple sugars") such as beta-glucose, or shorter polysaccharides and oligosaccharides. The name is also used for any naturally occurring mixture or complex of various such enzymes, that act serially or synergistically to decompose cellulosic material. The fda recognizes cellulase from a. niger as ...;-1,4-endoglucan hydrolase; celluase A; cellulosin AP; endoglucanase D; alkali cellulase; cellulase A 3; celludextrinase; 9.5 cellulase; avicelase; pancellase SS; 1,4-(1,3; 1,4)-β-D-glucan 4-glucanohydrolase; EC 3.2.1.4. Enzyme Commission Number: EC 3.2.1.4. CAS No. 9012-54-8. Cellulase. Activity: > 0.3 units/mg solid. Storage: 2-8°C. Form: powder. Source: Aspergillus niger. endo-1,4-β-D-glucanase; β-1,4-glucanase; β-1,4-endoglucan hydrolase; celluase A; cellulosin AP; endoglucanase D; alkali cellulase; cellulase A 3; celludextrinase; 9.5 cellulase; avicelase; pancellase SS; 1,4-(1,3; 1,4)-β-D-glucan 4-glucanohydrolase; EC 3.2.1.4. Cat No: NATE-0118. | |
| Native Aspergillus niger Glucose Oxidase | The glucose oxidase enzyme (GOx) also known as notatin (EC number 1.1.3.4) is an oxido-reductase that catalyses the oxidation of glucose to hydrogen peroxide and D-glucono-δ-lactone. This enzyme is produced by certain species of fungi and insects and displays antibacterial activity when oxygen and glucose are present. Glucose oxidase from aspergillus niger is a dimer consisting of 2 equal subunits with a molecular mass of 80 kda each. each subunit contains one flavin adenine dinulceotide moiety and one iron. the enzyme is a glycoprotein containing ~16% neutral sugar and 2% amino sugars. the enzyme also contains 3 cysteine residues and 8 potential sites for n-linked ...xidase oxidizes β-d-glucose to d-gluconolactate and hydrogen peroxide, horseradish peroxidase is often used as the coupling enzyme for glucose determination. although glucose oxidase is specific for β-d-glucose, solutions of d-glucose can be quantified as α-d-glucose will mutorotate to β-d-glucose as the β-d-glucose is consumed by the enzymatic reaction. Applications: Glucose oxidase is widely used in the food and pharmaceutical industries as well as a major component of glucose biosensors. Group: Enzymes. Synonyms: EC 1.1.3.4; glucose oxyhydrase; corylophyline; penatin; glucose aerodehydrogenase; microcid; β-D-glucose oxidase; D-glucose oxi | |
| Native Aspergillus oryzae α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. amylases from aspergillus oryzae are commonly used as baking additives to prevent staling in the baking industry, clarify haze from fruit juices and alcoholic beverages, and to produce glucose and maltose syrup products. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Mole weight: Mr ~51 kDa. Activity: > 150 units/mg protein (biuret); ~1.5 units/mg; ~30 units/mg. Storage: -20°C. Form: powder containing dextrin. Source: Aspergillus oryzae. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0740. | |
| Native Bacillus amyloliquefaciens α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. this product is from bacillus amyloliquefaciens and is supplied as a liquid. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. α-amylase from bacillus amy...ng sugars, which are then used for ethanol fermentation by saccharomyces cerevisiae fncc 3012. the enzyme catalyzes amylolysis of gelatinised waxy maize starch to produce reducing sugars. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Mole weight: 55 kDa. Activity: > 250 units/g. Form: liquid. Source: Bacillus amyloliquefaciens. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0741. | |
| Native Bacillus licheniformis α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. this product is from bacillus licheniformis and is type xii-a. α-amylase, from creative enzymes, has been used in various plant studies, such as metabolism studies in arabidopsis. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Activity: Type XII-A, saline solution, > 500 units/mg protein (biuret); Type B, liquid. Source: Bacillus licheniformis. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0742. | |
| Native Bacillus subtilis Xylanase Enzyme (Food Grade) | Xylanase is the name given to a class of enzymes which degrade the linear polysaccharide beta-1,4-xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls. As such, it plays a major role in micro-organisms thriving on plant sources for the degradation of plant matter into usable nutrients. Xylanases are produced by fungi, bacteria, yeast, marine algae, protozoans, snails, crustaceans, insect, seeds, etc., (mammals do not produce xylanases). Xylanase which made from the best strain of bacillus subtilis. it is a kind of purified endo-bacteria-xylanase. it can be applied in the flour treatment for bread powder and steam brea...and chewy. 2) in the storage of bread, the appropriate xylanase can retrad bread staling, improve the water holding capacity of the bread and optimize the gluten network, thereby, preventing water loss and re-allocate, stabilize the organizational structure of the bread. Group: Enzymes. Synonyms: EC 3.2.1.8; endo-(1?4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-β-xylan xylanohydrolase; β-xylanase; β-1,4-xylan xylanohydrolase; endo-1,4-β-xylanase; β-D-xylanase; endo-1,4-β-xylanase. Enzyme Commission Number: EC 3.2.1.8. CAS | |
| Native Coriolus versicolor Laccase | Laccases are copper-containing oxidase enzymes that are found in many plants, fungi, and microorganisms. The copper is bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. Type 1 copper is available to action of solvents, such as water. It can be displaced by mercury, substituted by cobalt or removed via a copper complexone. Removal of type 1 copper causes a decrease in laccase activity. Cyanide can remove all copper from the enzyme however re-embedding with type 1 and type 2 copper has been shown to be impossible. Type 3 copper however can be embed back into the enzyme. Laccases act on phenols and simila...ganisms. the copper is bound in several sites; type 1, type 2, and/or type 3. the ensemble of types 2 and 3 copper is called a trinuclear cluster. type 1 copper is available to action of solvents, such as water. it can be displaced by mercury, substituted by cobalt or removed via a copper complexone. removal of type 1 copper causes a decrease in laccase activity. cyanide can remove all copper from the enzyme however re-embedding with type 1 and type 2 copper has been shown to be impossible. type 3 copper however can be embed back into the enzyme. laccases act on phenols and similar molecules, performing a one-electron oxidations, which remain poorly defined. it is proposed t | |
| Native Human α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. α-amylase from human saliva has been used to study the development of nutraceuticals, which may aid the treatment of diabetes and obesity. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Activity: 1,000-3,000 units/mg protein; 300-1,500 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing (NH4)2SO4 and sodium Citrate. Source: Human saliva. Species: Human. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0743. | |
| Native Mucor miehei Rennin | Mucorpepsin is an enzyme that catalyses the following chemical reaction: Hydrolysis of proteins, favouring hydrophobic residues at P1 and P1'. Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen. This enzyme is isolated from the zygomycete fungi Mucor pusillus and M. miehei. Group: Enzymes. Synonyms: Mucorpepsin; EC 3.4.23.23; Mucor rennin; Mucor aspartic proteinase; Mucor acid proteinase; Mucor acid protease; Mucor miehei aspartic proteinase; Mucor miehei aspartic protease; Mucor aspartic proteinase; Mucor pusillus emporase; Fromase 100; Mucor pusillus rennin; Fromase 46TL; Mucor miehei rennin; 9073-79-4. Enzyme Commission Number: EC 3.4.23.23. CAS No. 9073-79-4. Rennin. Mole weight: Mr ~40 kDa. Activity: ~0.1 units/mg. Storage: -20°C. Form: lyophilized powder; slightly brown. Source: Mucor miehei. Mucorpepsin; EC 3.4.23.23; Mucor rennin; Mucor aspartic proteinase; Mucor acid proteinase; Mucor acid protease; Mucor miehei aspartic proteinase; Mucor miehei aspartic protease; Mucor aspartic proteinase; Mucor pusillus emporase; Fromase 100; Mucor pusillus rennin; Fromase 46TL; Mucor miehei rennin; 9073-79-4. Cat No: NATE-0652. | |
| Native Porcine α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. this product is from porcine pancreas and is type i-a. α-amylase, from creative enzymes, has been used in various plant studies, such as metabolism studies in arabidopsis. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Mole weight: 51-54 kDa. Activity: > 1000 units/mg protein (E1%/280); > 10 units/mg solid; 700-1400 units/mg protein (E1%/280). Storage: 2-8°C. Form: saline suspension. Suspension in 2.9 M NaCl solution containing 3 mM CaCl2. Source: Porcine pancreas. Species: Porcine. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0745. | |
| Native Streptomyces griseus Chitosanase | Chitosanase catalyzes the endohydrolysis of β (1,4) linkages between N-acetyl-D-glucosamine and D-glucosamine residues in partially deacetylated chitosan. Chitosanase from Streptomyces griseus is capable of hydrolyzing both chitosan and carboxymethyl cellulose. It is used for the lysis of cell walls of fungi belonging to the group Mucorales. It is found in several types of microorganisms. Applications: Chitosanase from streptomyces griseus has been used in a study to assess the effect of chitin sources on production of chitinase and chitosanase. chitosanase from streptomyces griseus has also been used in a study to investigate the effective production of chitinase an...cete aphanomyces euteiches, a major parasite of legume plants. it has also been used for the enzymatic hydrolysis of the fully de-n-acetylated chitosan to get chitosan oligomer mixtures during the preparation of biocompatible chitosan-alginate gel. Group: Enzymes. Synonyms: Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase. Enzyme Commission Number: EC 3.2.1.132. CAS No. 51570-20-8. Chitosanase. Activity: >50 units/mg protein (Bradford). Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Streptomyces griseus. Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase. Cat No: NATE-0125. | |
| Native Trichoderma longibrachiatum β-Glucanase | β-glucanases degrade β-1,4-glucans of cellulose, xyloglucan and β-1,4-xylan. β-Glucanase represents a group of carbohydrate enzymes which break down glycosidic bonds within beta-glucan. It forms the main constituent of fungal cell walls and could be a potential structural and storage polysaccharide of marine macro-algae. It has the ability to degrade fungal cell walls and may be involved in defense mechanism of plants against pathogenic fungi. Applications: Β-glucanase was used as a cellulase enzyme in the combined biological and chemical pretreatment method for lignocellulosic ethanol production from energy cane. it was also used in the enz...-(1,3; 1,4)-β-D-glucan 3 (4)-glucanohydrolase; EC 3.2.1.6. Enzyme Commission Number: EC 3.2.1.6. CAS No. 62213-14-3. β-glucanase. Form: powder. contains maltodextrin, silica and sodium benzoate. Source: Trichoderma longibrachiatum. endo-1,3-β-D-glucanase; laminarinase; laminaranase; β-1,3-glucanase; β-1,3-1,4-glucanase; endo-1,3-β-glucanase; endo-β-1,3 (4)-glucanase; endo-β-1,3-1,4-glucanase; endo-β-(1?3)-D-glucanase; endo-1,3-1,4-β-D-glucanase; endo-β-(1-3)-D-glucanase; endo-β-1,3-glucanase IV; endo-1,3-β-D-glucanase; 1,3-(1,3; 1,4)-β-D-glucan 3 (4)-glucanohydrolase; EC 3.2.1.6. Cat No: NATE-0768. | |
| Nitrilase (Crude Enzyme) | Nitrilase enzymes catalyse the hydrolysis of nitriles to carboxylic acids and ammonia, without the formation of "free" amide intermediates. Nitrilases are involved in natural product biosynthesis and post translational modifications in plants, animals, fungi and certain prokaryotes. Nitrilases can also be used as catalysts in preparative organic chemistry. Among others, nitrilases have been used for the resolution of racemic mixtures. Nitrilase should not be confused with nitrile hydratase (nitrile hydro-lyase; EC 4. 2. 1. 84) which hydrolyses nitriles to amides. Nitrile hydratases are almost invariably co-expressed with an amidase, which converts the amide to the carboxylic acid, consequently it can sometimes be difficult to distinguish nitrilase activity from nitrile hydratase plus amidase activity. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; industry. Group: Enzymes. Synonyms: acetonitrilase; benzonitrilase. Enzyme Commission Number: EC 3.5.5.1. CAS No. 9024-90-2. Nitrilase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. acetonitrilase; benzonitrilase. Pack: 100ml. Cat No: NATE-1842. | |
| nitrite reductase [NAD(P)H] | An iron-sulfur flavoprotein (FAD) containing siroheme. The enzymes from the fungi Neurospora crassa, Emericella nidulans and Candida nitratophila and the bacterium Aliivibrio fischeri can use either NADPH or NADH as electron donor. cf. EC 1.7.1.15, nitrite reductase (NADH). Group: Enzymes. Synonyms: nitrite reductase (reduced nicotinamide adenine dinucleotide (phosphate)); assimilatory nitrite reductase (ambiguous); nitrite reductase [NAD(P)H2]; NAD(P)H2:nitrite oxidoreductase; nit-6 (gene name). Enzyme Commission Number: EC 1.7.1.4. CAS No. 9029-29-2. 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-1611; nitrite reductase [NAD(P)H]; EC 1.7.1.4; 9029-29-2; nitrite reductase (reduced nicotinamide adenine dinucleotide (phosphate)); assimilatory nitrite reductase (ambiguous); nitrite reductase [NAD(P)H2]; NAD(P)H2:nitrite oxidoreductase; nit-6 (gene name). Cat No: EXWM-1611. | |
| Phosphoglycerate mutase 1 from Human, Recombinant | Phosphoglycerate mutase (PGM) is an enzyme that catalyzes step 8 of glycolysis. It catalyzes the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme (EC 5.4.2.11) is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM (EC 5.4.2.12) class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase. Group: Enzymes. Synonyms: Pgam-1; PGAM1. Enzyme Commission Number: EC 5.4.2.1. Purity: > 90% by SDS-PAGE. Mole weight: 30.9 kDa. Activity: >300 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 and fused to His-tag at N-terminus. Species: Human. Pgam-1; PGAM1; Phosphoglycerate mutase 1; Phosphoglycerate mutase. Cat No: NATE-1647. | |
| Phosphoglycerate mutase 1 from Mouse, Recombinant | Phosphoglycerate mutase (PGM) is an enzyme that catalyzes step 8 of glycolysis. It catalyzes the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme (EC 5.4.2.11) is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM (EC 5.4.2.12) class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase. Group: Enzymes. Synonyms: Pgam-1; PGAM1. Enzyme Commission Number: EC 5.4.2.1. Purity: > 95% by SDS-PAGE. Mole weight: 31.4 kDa. Activity: >150 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 and fused to His-tag at N-terminus. Species: Mouse. Pgam-1; PGAM1; Phosphoglycerate mutase 1; Phosphoglycerate mutase. Cat No: NATE-1646. | |
| phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) | The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His10 in man and Escherichia coli, His8 in Saccharomyces cerevisiae). This phosphate can be transferred to the free OH of 2-phospho-D-glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. cf. EC 5.4.2.12 phosphoglycerate mutase. The enzyme has no requirement for metal ions. This enzyme also catalyse, slowly, the reacti... dPGM. Enzyme Commission Number: EC 5.4.2.11. 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-5522; phosphoglycerate mutase (2,3-diphosphoglycerate-dependent); EC 5.4.2.11; glycerate phosphomutase (diphosphoglycerate cofactor); 2,3-diphosphoglycerate dependent phosphoglycerate mutase; cofactor dependent phosphoglycerate mutase; phosphoglycerate phosphomutase (ambiguous); phosphoglyceromutase (ambiguous); monophosphoglycerate mutase (ambiguous); monophosphoglyceromutase (ambiguous); GriP mutase (ambiguous); PGA mutase (ambiguous); MPGM; PGAM; PGAM-d; PGM; dPGM. Cat No: EXWM-5522. | |
| phosphoglycerate mutase (2,3-diphosphoglycerate-independent) | The enzymes from higher plants, algae, fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. cf. EC 5.4.2.11 phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). The enzyme contains two Mn2+ (or in some species two Co2+ ions). The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. Both metal ions are involved in the reaction. Group: Enzymes. Synonyms: cofactor independent phosphoglycerate mutase; 2,3-diphosphoglycerate-independent phosphoglycerate mutase; phosphoglycerate phosphomutase (ambiguous); pho. Enzyme Commission Number: EC 5.4.2.12. 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-5523; phosphoglycerate mutase (2,3-diphosphoglycerate-independent); EC 5.4.2.12; cofactor independent phosphoglycerate mutase; 2,3-diphosphoglycerate-independent phosphoglycerate mutase; phosphoglycerate phosphomutase (ambiguous); phosphoglyceromutase (ambiguous); monophosphoglycerate mutase (ambiguous); monophosphoglyceromutase (ambiguous); GriP mutase (ambiguous); PGA mutase (ambiguous); iPGM; iPGAM; PGAM-i. Cat No: EXWM-5523. | |
| Phosphoglycerate mutase 2 from Human, Recombinant | Phosphoglycerate mutase (PGM) is an enzyme that catalyzes step 8 of glycolysis. It catalyzes the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme (EC 5.4.2.11) is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM (EC 5.4.2.12) class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase. Group: Enzymes. Synonyms: GSD10; PGAM-M; PGAMM; PGAM2. Enzyme Commission Number: EC 5.4.2.11. Purity: > 95% by SDS-PAGE. Mole weight: 30.9 kDa. Activity: >100 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 and fused to His-tag at N-terminus. Species: Human. GSD10; PGAM-M; PGAMM; PGAM2; Phosphoglycerate mutase 2; Phosphoglycerate mutase. Cat No: NATE-1643. | |
| Propiconazole-4H-1,2,4-triazole (Mixture of Diastereomers) | An impurities of Propiconazole. Propiconazole is a triazole fungicide inhibiting fungicide due to its binding with and inhibiting the 14-alpha demethylase enzyme from demethylating a precursor to ergosterol. Synonyms: 4-[[2-(2,4-Dichlorophenyl)-4-propyl-1,3-dioxolan-2-yl]methyl]-4H-1,2,4-triazole. Grades: > 95%. CAS No. 221132-58-7. Molecular formula: C15H17Cl2N3O2. Mole weight: 342.23. | |
| (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. | |
| sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming) | This enzyme catalyses the final step in the de novo synthesis of tetrahydrobiopterin from GTP. The enzyme, which is found in higher animals and some fungi and bacteria, produces the erythro form of tetrahydrobiopterin. cf. EC 1.1.1.325, sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming). Group: Enzymes. Synonyms: SR. Enzyme Commission Number: EC 1.1.1.153. CAS No. 9059-48-7. 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-0058; sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming); EC 1.1.1.153; 9059-48-7; SR. Cat No: EXWM-0058. | |
| sphingolipid 4-desaturase | The enzyme, which has been characterized from plants, fungi, and mammals, generates a trans double bond at position 4 of sphinganine bases in sphingolipids. The preferred substrate is dihydroceramide, but the enzyme is also active with dihydroglucosylceramide. Unlike EC 1.14.19.29, sphingolipid 8-desaturase, this enzyme does not contain an integral cytochrome b5 domain and requires an external cytochrome b5. The product serves as an important signalling molecules in mammals and is required for spermatide differentiation. Group: Enzymes. Synonyms: dehydroceramide desaturase. Enzyme Commission Number: EC 1.14.19.17. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0979; sphingolipid 4-desaturase; EC 1.14.19.17; dehydroceramide desaturase. Cat No: EXWM-0979. | |
| sphingolipid C9-methyltransferase | The enzyme, characterized from the fungi Komagataella pastoris and Fusarium graminearum, acts only on ceramides and has no activity with free sphingoid bases or glucosylceramides. Group: Enzymes. Enzyme Commission Number: EC 2.1.1.317. 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-1925; sphingolipid C9-methyltransferase; EC 2.1.1.317. Cat No: EXWM-1925. | |
| Streptonigrin (Bruneomycin, Nigrin, Rufocromomycin, Valacidin, Antibiotic RP 5278) | Streptonigrin is an unusual aminoquinone with broad biological activity against bacteria, fungi, nematodes, viruses and tumor cells. Streptonigrin acts as a bioreductive agent, highly dependent on interactions with metal ions, notably iron, and plays an important role in free radical production through redox cycling of NAD(P)H:quinone oxidoreductase (NQO1). Streptonigrin from Streptomyces flocculus is an aminoquinone antitumor antibiotic. Its antineoplastic activity requires reductive activation by Xanthine-converting enzymes. It induces apoptosis by a mechanism involving NF-κB. DNA cleavage reaction and chromosome damage by Streptonigrin are influenced by the nature of the metal ion present and dependent on the production of free radicals. Its antibiotic activity is iron-activated. Group: Biochemicals. Alternative Names: EC Number 223-501-8; 5278RP; AO 50165L302; Abbott Crystalline antibiotic; Bruneomycin; NSC 45383; NSC 56748; NSC 83950; Nigrin; Rufocromomycin; SN; STP; Streptonigran; Streptonigrin; 5-Amino-6-(7-amino-5,8-dihydro-6-methoxy-5,8-dioxo-2-quinolyl)-4-(2-hydroxy-3,4-dimethoxyphenyl)-3-methylpicolinic Acid; (4R)-5-Amino-6-(7-amino-5,8-dihydro-6-methoxy-5,8-dioxo-2-quinolinyl)-4-(2-hydroxy-3,4-dimethoxyphenyl)-3-methyl-2-pyridinecarboxylic Acid; (R)-Streptonigrin. Grades: Highly Purified. CAS No. 3930-19-6. Pack Sizes: 1mg. Molecular Formula: C??H??N?O?, Molecular Weight: 506.46. US Biological Life Sciences. | Worldwide |
| sulfate adenylyltransferase | The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme (fusion product of two catalytic activities). In a first step, sulfate adenylyltransferase catalyses the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate. The second step is catalysed by the adenylylsulfate kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme-bound APS and ATP. In contrast, in bacteria, yeast, fungi and plants, the formation of PAPS is carried out by two individual polypeptides, sulfate adenylyltransferase (EC 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25). Group: Enzymes. Synonyms: ATP-sulfurylase; adenosine-5'-triphosphate sulfurylase; adenosinetriphosphate sulfurylase; adenylylsulfate pyrophosphorylase; ATP sulfurylase; ATP-sulfurylase; sulfurylase. Enzyme Commission Number: EC 2.7.7.4. CAS No. 9012-39-9. ATP-sulfurylase. 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-3251; sulfate adenylyltransferase; EC 2.7.7.4; 9012-39-9; ATP-sulfurylase; adenosine-5'-triphosphate sulfurylase; adenosinetriphosphate sulfurylase; adenylylsulfate pyrophosphorylase; ATP sulfurylase; ATP-sulfurylase; sulfurylase. Cat No: EXWM-3251. | |
| Thelephoric acid | Thelephoric acid is a terphenylquinone pigment found in several fungi, such as Omphalotus subilludens and Polyozellus multiplex. It is derived from atromentin, and its precusor can be from cyclovariegatin. Thelephoric acid has been shown to inhibit prolyl endopeptidase, an enzyme that plays a role in processing proteins (specifically, amyloid precursor protein) in Alzheimer's disease. Synonyms: 2,3,8,9-Tetrahydroxybenzo[1,2-b:4,5-b']bisbenzofuran-6,12-dione; Thelephorsaure; PM-B; 2,3'-Carbonyl-3,2'-carbonylbis(5,6-dihydroxybenzofuran); Thelephate. CAS No. 479-64-1. Molecular formula: C18H8O8. Mole weight: 352.25. | |
| ubiquinol oxidase (non-electrogenic) | The enzyme, described from the mitochondria of plants and some fungi and protists, is an alternative terminal oxidase that is not sensitive to cyanide inhibition and does not generate a proton motive force. Unlike the electrogenic terminal oxidases that contain hemes (cf. EC 1.10.3.10 and EC 1.10.3.14), this enzyme contains a dinuclear non-heme iron complex. The function of this oxidase is believed to be dissipating excess reducing power, minimizing oxidative stress, and optimizing photosynthesis in response to changing conditions. Group: Enzymes. Synonyms: plant alternative oxidase; cyanide-insensitive oxidase; AOX (gene name); ubiquinol oxidase; ubiquinol:O2 oxidoreductase (non-electrogenic). Enzyme Commission Number: EC 1.10.3.11. 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-0477; ubiquinol oxidase (non-electrogenic); EC 1.10.3.11; plant alternative oxidase; cyanide-insensitive oxidase; AOX (gene name); ubiquinol oxidase; ubiquinol:O2 oxidoreductase (non-electrogenic). Cat No: EXWM-0477. | |
| Validamycin A | The major analogue of a family of cyclitol disaccharides isolated from streptomyces hygroscopicus var. Limoneus. It is a potent antifungal agent used to control fungi in crop production and acts as a potent inhibitor of trehalase, an important enzyme in carbohydrate storage and ultilisation in fungi. Synonyms: jinggangmycin; Antibiotic T 7545A. Grades: >95% by HPLC. CAS No. 37248-47-8. Molecular formula: C20H35NO13. Mole weight: 497.49. | |
| verruculogen prenyltransferase | Found in a number of fungi. Catalyses the last step in the biosynthetic pathway of the indole alkaloid fumitremorgin A. The enzyme from the fungus Neosartorya fischeri is also active with fumitremorgin B and 12α,13α-dihydroxyfumitremorgin C. Group: Enzymes. Synonyms: FtmPT3. Enzyme Commission Number: EC 2.5.1.107. 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-2723; verruculogen prenyltransferase; EC 2.5.1.107; FtmPT3. Cat No: EXWM-2723. | |
| xanthine dioxygenase | Requires Fe2+ and L-ascorbate. The enzyme, which was characterized from fungi, is specific for xanthine. Group: Enzymes. Synonyms: XanA; α-ketoglutarate-dependent xanthine hydroxylase. Enzyme Commission Number: EC 1.14.11.48. 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-0667; xanthine dioxygenase; EC 1.14.11.48; XanA; α-ketoglutarate-dependent xanthine hydroxylase. Cat No: EXWM-0667. | |
| Zineb | Zineb is an agricultural fungicide of the dithiocarbamate class. Its toxicity is relatively low, and there is little evidence of human harm from exposure. Oxidative stress is one of the main factors contributing to diseases caused by Zineb. Zineb does not alter the activity of any superoxide dismutase enzymes. Catalase (CAT) activity was reduced only by Zineb. Uses: Scientific research. Group: Biochemical assay reagents. Alternative Names: Zinc ethylene-1, 2-bisdithiocarbamate. CAS No. 12122-67-7. Pack Sizes: 10 mM * 1 mL; 50 mg; 100 mg. Product ID: HY-W127739. | |
| 1,1'-(((2R,2'R,4R,4'R)-4,4'-(oxybis(methylene))bis(2-(2,4-difluoro phenyl)tetrahydrofuran-4,2-diyl))bis(methylene))bis(1H-1,2,4-triazole) | 1,1'-(((2R,2'R,4R,4'R)-4,4'-(oxybis(methylene))bis(2-(2,4-difluoro phenyl)tetrahydrofuran-4,2-diyl))bis(methylene))bis(1H-1,2,4-triazole) is an impurity of Posaconazole. Posaconazole is a broad-spectrum triazole compound that is active against fungi by inhibiting the lanosterol 14α-demethylase enzyme. CAS No. 2256739-22-5. Molecular formula: C28H28F4N6O3. Mole weight: 572.56. | |
| 1-((2R,3R)-2-(benzyloxy)pentan-3-yl)-4-(4-(4-(4-hydroxyphenyl)piperazin-1-yl)phenyl)-1H-1,2,4-triazol-5(4H)-one | 1-((2R,3R)-2-(benzyloxy)pentan-3-yl)-4-(4-(4-(4-hydroxyphenyl)piperazin-1-yl)phenyl)-1H-1,2,4-triazol-5(4H)-one is an impurity of Posaconazole. Posaconazole is a broad-spectrum triazole compound that is active against fungi by inhibiting the lanosterol 14α-demethylase enzyme. CAS No. 2243786-01-6. Molecular formula: C30H35N5O3. Mole weight: 513.64. | |
| 1-((2R,3S)-2-(benzyloxy)pentan-3-yl)-4-(4-(4-(4-hydroxyphenyl)piperazin-1-yl)phenyl)-1H-1,2,4-triazol-5(4H)-one | 1-((2R,3S)-2-(benzyloxy)pentan-3-yl)-4-(4-(4-(4-hydroxyphenyl)piperazin-1-yl)phenyl)-1H-1,2,4-triazol-5(4H)-one is an impurity of Posaconazole. Posaconazole is a broad-spectrum triazole compound that is active against fungi by inhibiting the lanosterol 14α-demethylase enzyme. CAS No. 2243786-00-5. Molecular formula: C30H35N5O3. Mole weight: 513.64. | |
| 1-((2S,3R)-2-(benzyloxy)pentan-3-yl)-4-(4-(4-(4-hydroxyphenyl)piperazin-1-yl)phenyl)-1H-1,2,4-triazol-5(4H)-one | 1-((2S,3R)-2-(benzyloxy)pentan-3-yl)-4-(4-(4-(4-hydroxyphenyl)piperazin-1-yl)phenyl)-1H-1,2,4-triazol-5(4H)-one is an impurity of Posaconazole. Posaconazole is a broad-spectrum triazole compound that is active against fungi by inhibiting the lanosterol 14α-demethylase enzyme. CAS No. 2243786-02-7. Molecular formula: C30H35N5O3. Mole weight: 513.64. | |
| 1-(4-Aminophenyl)-4-(4-hydroxyphenyl)piperazine | 1-(4-Aminophenyl)-4-(4-hydroxyphenyl)piperazine is an impurity of Posaconazole. Posaconazole is a broad-spectrum triazole compound that is active against fungi by inhibiting the lanosterol 14α-demethylase enzyme. Synonyms: 4-[4-(4-Aminophenyl)-1-piperazinyl]phendiamineol; 4-[4-(4-aminophenyl)-1-piperazinyl]phenol. Grades: >95%. CAS No. 74853-08-0. Molecular formula: C16H19N3O. Mole weight: 269.34. | |
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