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| Product | Description | |
|---|---|---|
| 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. |  |
| Native Xanthine Dehydrogenase from Bovine milk | Xanthine oxidoreductase (XOR) catalyzes the formation of uric acid from hypoxanthine and xanthine, last two steps of purine catabolism. The mammalian enzyme is synthesized as a xanthine dehydrogenase form (XDH, EC 1.17.1.4), which uses NAD as the electron acceptor, but is converted into an xanthine oxidase form (XO, EC 1.1.3.22) by reversible (through sulfhydryl group oxidation) or irreversible (proteolysis) manner. Since most industrial protocols of XOR purification includes proteolysis step, commercial XOR enzyme is available only as oxidase form unable to use NAD as a an electron acceptor. Group: Enzymes. Synonyms: xanthine dehydrogenase; NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase; XDH; EC 1.17.1.4. Enzyme Commission Number: EC 1.17.1.4. CAS No. 9054-84-6. XDH. Form: Lyophilized. Source: Bovine milk. Species: Bovine. xanthine dehydrogenase; NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase; XDH; EC 1.17.1.4. Cat No: NATE-1065. | |
| Native Xanthine dehydrogenase from Microorganism | Xanthine dehydrogenase belongs to the group of molybdenum-containing hydroxylases involved in the oxidative metabolism of purines. The enzyme is a homodimer. Xanthine dehydrogenase can be converted to xanthine oxidase by reversible sulfhydryl oxidation or by irreversible proteolytic modification. Applications: Useful for the enzymatic determiantion of inorganic phosphate. Group: Enzymes. Synonyms: xanthine dehydrogenase; NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase; XDH; EC 1.17.1.4. Enzyme Commission Number: EC 1.17.1.4. CAS No. 9054-84-6. XDH. Mole weight: 240 kDa. Activity: > 100 U/mL. Appearance: Brownish solution. Storage: Storage at ?20°C in the presence of a desiccant is recommended. Form: Liquid. Source: Microorganism. xanthine dehydrogenase; NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase; XDH; EC 1.17.1.4. Cat No: NATE-1064. | |
| 2-(3,5-Diformyl-4-isobutoxyphenyl)-4-methylthiazole-5-carboxylic Acid | 2-(3,5-Diformyl-4-isobutoxyphenyl)-4-methylthiazole-5-carboxylic Acid s an impurity of Febuxostat (F229000), a xanthine oxidase/xanthine dehydrogenase inhibitor. Used for treatment of hyperuricemia and chronic gout. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 2.5mg, 5mg. Molecular Formula: C17H17NO5S, Molecular Weight: 347.39. US Biological Life Sciences. |  Worldwide |
| aerobic carbon monoxide dehydrogenase | This enzyme, found in carboxydotrophic bacteria, catalyses the oxidation of CO to CO2 under aerobic conditions. The enzyme contains a binuclear Mo-Cu cluster in which the copper is ligated to a molybdopterin center via a sulfur bridge. The enzyme also contains two [2Fe-2S] clusters and FAD, and belongs to the xanthine oxidoreductase family. The CO2 that is produced is assimilated by the Calvin-Benson-Basham cycle, while the electrons are transferred to a quinone via the FAD site, and continue through the electron transfer chain to a dioxygen terminal acceptor. cf. EC 1.2.7.4, anaerobic carbon monoxide dehydrogenase. Group: Enzymes. Synonyms: MoCu-CODH; coxSML (gene names); molybdoenzyme carbon monoxide dehydrogenase. Enzyme Commission Number: EC 1.2.5.3. 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-1222; aerobic carbon monoxide dehydrogenase; EC 1.2.5.3; MoCu-CODH; coxSML (gene names); molybdoenzyme carbon monoxide dehydrogenase. Cat No: EXWM-1222. | |
| aldehyde dehydrogenase (FAD-independent) | Belongs to the xanthine oxidase family of enzymes. The enzyme from Desulfovibrio sp. contains a molybdenum-molybdopterin-cytosine dinucleotide (MCD) complex and two types of [2Fe-2S] cluster per monomer, but does not contain FAD. Group: Enzymes. Synonyms: aldehyde oxidase; aldehyde oxidoreductase; Mop; AORDd. Enzyme Commission Number: EC 1.2.99.7. 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-1235; aldehyde dehydrogenase (FAD-independent); EC 1.2.99.7; aldehyde oxidase; aldehyde oxidoreductase; Mop; AORDd. Cat No: EXWM-1235. | |
| enzyme-thiol transhydrogenase (glutathione-disulfide) | Converts EC 1.17.1.4 xanthine dehydrogenase into EC 1.17.3.2 xanthine oxidase in the presence of glutathione disulfide; also reduces the disulfide bond of ricin. Not inhibited by Cu2+ or thiol reagents. Group: Enzymes. Synonyms: [xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase; enzyme-thiol transhydrogenase (oxidized-glutathione); glutathione-dependent thiol:disulfide oxidoreductase; thiol:disulphide oxidoreductase. Enzyme Commission Number: EC 1.8.4.7. CAS No. 85030-79-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1673; enzyme-thiol transhydrogenase (glutathione-disulfide); EC 1.8.4.7; 85030-79-1; [xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase; enzyme-thiol transhydrogenase (oxidized-glutathione); glutathione-dependent thiol:disulfide oxidoreductase; thiol:disulphide oxidoreductase. Cat No: EXWM-1673. | |
| Febuxostat | Xanthine oxidase/xanthine dehydrogenase inhibitor. Used for treatment of hyperuricemia and chronic gout. Group: Biochemicals. Alternative Names: 2-[3-Cyano-4-(2-methylpropoxy)phenyl]-4-methyl-5-thiazolecarboxylic Acid; 2-(3-Cyano-4-isobutyloxyphenyl)-4-methyl-5-thiazolecarboxylic Acid; TEI 6720; TMX 67. Grades: Highly Purified. CAS No. 144060-53-7. Pack Sizes: 10mg. US Biological Life Sciences. | Worldwide |
| nicotinate dehydrogenase (cytochrome) | This two-component enzyme from Pseudomonas belongs to the family of xanthine dehydrogenases, but differs from most other members of this family. While most members contain an FAD cofactor, the large subunit of this enzyme contains three c-type cytochromes, enabling it to interact with the electron transfer chain, probably by delivering the electrons to a cytochrome oxidase. The small subunit contains a typical molybdopterin cytosine dinucleotide(MCD) cofactor and two [2Fe-2S] clusters. Group: Enzymes. Synonyms: nicotinic acid hydroxylase; nicotinate hydroxylase. Enzyme Commission Number: EC 1.17.2.1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1085; nicotinate dehydrogenase (cytochrome); EC 1.17.2.1; nicotinic acid hydroxylase; nicotinate hydroxylase. Cat No: EXWM-1085. | |
| 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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