Creative Enzymes - Products
Enzyme manufacturing for life science research and medicines, food, alcohol, fabric, paper etc. Uses include: drug discovery, cancer and infectious disease research, microbiology and personalized medicine.
| Product | Description | |
|---|---|---|
| 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 Lactobacillus leichmanii D-Lactic Dehydrogenase | D-lactic dehydrogenase catalyzes the conversion of D-lactate into D-pyruvate while reducing NAD+ to NADH and H+. Applications: In the food industry, the primary catalysis is coupled to conversion of nadh and h+ to nad+ with diaphorase coupled with converting the non-fluorescent resazurin to the highly fluorescent substance resorufin to measure the content of d-lactate in food products. Group: Enzymes. Synonyms: EC 1.1.1.28, D-Lactic Dehydrogenase; 9028-36-8; lactic acid dehydrogenase; D-specific lactic dehydrogenase; D-(-)-lactate dehydrogenase (NAD); D-lactic acid dehydrogenase; D-lactic dehydrogenase; (R)-Lactate:NAD+ oxidoreductase; D-LDH. Enzyme Commission Number: EC 1.1.1.28. CAS No. 9028-36-8. D-LDH. Activity: > 30 units/mg protein; ~1000 U/mL; 250-500 units/mg protein (biuret); 150-300 units/mg protein; 1,000-3,000 units/mg protein (biuret). Storage: 2-8°C. Form: Suspension in 3.2 M (NH4)2SO4, 0.1 M potassium phosphate, pH 7.0. Source: Lactobacillus leichmanii. EC 1.1.1.28, D-Lactic Dehydrogenase; 9028-36-8; lactic acid dehydrogenase; D-specific lactic dehydrogenase; D-(-)-lactate dehydrogenase (NAD); D-lactic acid dehydrogenase; D-lactic dehydrogenase; (R)-Lactate:NAD+ oxidoreductase; D-LDH. Cat No: NATE-0195. | |
| Native Lactobacillus reuteri Glucansucrase (α-glucanotransferase) | A moderately thermostable Glucansucrase (4,6-Alpha-Glucanotransferase, reuteransucrase). The enzyme transfers glucose units from sucrose to make a highly branched, high molecular weight alpha-D-Glucan with α (1?4) glucosidic linkages and also some α (1?6) linked glucosyl units. Group: Enzymes. Synonyms: Alpha-glucanotransferase; glucosyltransferase; 4,6-alpha-Glucanotransferase; EC 2.4.1.-. Enzyme Commission Number: EC 2.4.1.-. Glucansucrase. Source: Lactobacillus reuteri strain 121. Species: Lactobacillus reuteri. Alpha-glucanotransferase; glucosyltransferase; 4,6-alpha-Glucanotransferase; EC 2.4.1.-. Cat No: NATE-0304. | |
| Native Lactobacillus sp. Maltose Epimerase | Maltose 1-epimerase (MER), is an enzyme that catalyzes the interconversion of αand β anomers of maltose. Maltose 1-epimerase (mer), is an enzyme that catalyzes the interconversion of α and β anomers of maltose. Applications: Maltose epimerase has been used in a study to assess metabolite gene regulation. it has also been used in a study to investigate saccharogenic determination of α-amylase in serum and urine. Group: Enzymes. Synonyms: maltose epimerase; EC 5.1.3.21; maltose 1-epimerase; MER. Enzyme Commission Number: EC 5.1.3.21. MER. Mole weight: mol wt ~45 kDa by SDS-PAGE. Storage: -20°C. Source: Lactobacillus sp. maltose epimerase; EC 5.1.3.21; maltose 1-epimerase; MER. Cat No: NATE-0450. | |
| Native Leuconostoc mesenteroides 6-Phosphogluconolactonase | 6-Phosphogluconolactonase is an enzyme in the pentose phosphate pathway. It converts 6-phosphogluconolactone to 6-phosphogluconate. Hydrolase that catalyzes the conversion of 6-phosphogluconolactone to 6-phosphogluconate. increase the sensitivity of your creatine kinase assay. Applications: Use 6-phosphogluconolactonase in diagnostic tests for the determination of creatine kinase or glucose in the combination with hexokinase, glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase. Group: Enzymes. Synonyms: 6-Phosphogluconolactonase. 6-Phosphogluconolactonase. Mole weight: 38 kD (SDS). Activity: >50 U/mg. Stability: At -15 to -25°C within specification range for 12 months. Appearance: White lyophilizate. Source: Leuconostoc mesenteroides. Species: Leuconostoc mesenteroides. 6-Phosphogluconolactonase. Cat No: NATE-0889. | |
| Native Leuconostoc mesenteroides Dextran Sucrase | Dextransucrases are glucansucrases that are able to produce dextran, a glucose polymer linked mainly through α1-6 bonds. However, α1-3, α1-6, α1-4 and α1-2 bonds are also found, in both the main chain and the branching linkages. The peptide has approximately 1600 amino acids. The aspartic acid in position 551 is essential for catalytic activity, while glutamic acid 589 and aspartic acid 662 complement the catalytic triad. The activity of dextransucrase is decreased by EDTA, and is restored by the addition of calcium ions. Zinc, cadmium, lead, mercury and copper ions are inhibitory to various degrees. Applications: Dextran sucrase from leu... immobilized sphere for the production of dextran from sucrose. Group: Enzymes. Synonyms: EC 2.4.1.5, sucrose 6-glucosyltransferase; SGE; CEP; sucrose-1,6-α-glucan glucosyltransferase; sucrose:1,6-α-D-glucan 6-α-D-glucosyltransferase; 9032-14-8. Enzyme Commission Number: EC 2.4.1.5. CAS No. 9032-14-8. SGE. Activity: > 100 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing dextran, MES buffer salts and CaCl2. Source: Leuconostoc mesenteroides. EC 2.4.1.5, sucrose 6-glucosyltransferase; SGE; CEP; sucrose-1,6-α-glucan glucosyltransferase; sucrose:1,6-α-D-glucan 6-α-D-glucosyltransferase; 9032-14-8. Cat No: NATE-0669. | |
| 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 Leuconostoc mesenteroides Glucose-6-phosphate Dehydrogenase | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ ? 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Applications: Glucose-6-phosphate dehydrogenase was used as a model to test the effect of seed protein fractions on enzyme protection during dehydration. g-6-pdh has been utilized in assays for nicotinamide adenine dinucleotide and tissue pyridine nucleotides. Group: Enzymes. Synonyms: EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-p. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Activity: 20U/mg-solid or more. Storage: 2-8°C. Form: Freeze dried powder. Source: Leuconostoc mesenteroides. EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase; 9001-40-5. Cat No: DIA-321. | |
| Native Leuconostoc mesenteroides Mannitol Dehydrogenase | In enzymology, a mannitol 2-dehydrogenase (EC 1.1.1.67) is an enzyme that catalyzes the chemical reaction:D-mannitol + NAD+<-> D-fructose + NADH + H+. Thus, the two substrates of this enzyme are D-mannitol and NAD+, whereas its 3 products are D-fructose, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in fructose and mannose metabolism. Applications: This preparation is useful in the determination of mannitol in urine. can be used for the production of d-mannitol. it has been used in a study to assess glucosylglycerol and glucosylglycerate as enzyme stabilizers. Group: Enzymes. Synonyms: mannitol dehydrogenase; D-mannitol dehydrogenase; mannitol dehydrogenase; mannitol 2-dehydrogenase; EC 1.1.1.67; 9001-65-4. Enzyme Commission Number: EC 1.1.1.67. CAS No. 9001-65-4. Mannitol Dehydrogenase. Mole weight: 136 kDa. Activity: > 60 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing buffer salts, potassium phosphate, and dithiothreitol. Source: Leuconostoc mesenteroides. mannitol dehydrogenase; D-mannitol dehydrogenase; mannitol dehydrogenase; mannitol 2-dehydrogenase; EC 1.1.1.67; 9001-65-4. Cat No: NATE-0435. | |
| Native Leuconostoc Mesenteroides Sucrose Phosphorylase | Sucrose phosphorylase (EC. 2.4.1.7) is an important enzyme in the metabolism of sucrose and regulation of other metabolic intermediates. Sucrose phosphorylase is in the class of hexosyltransferases. More specifically it has been placed in the retaining glycoside hydrolases family although it catalyzes a transglycosidation rather than hydrolysis. Sucrose phosphorylase catalyzes the conversion of sucrose to D-fructose and α-D-glucose-1-phosphate. It has been shown in multiple experiments that the enzyme catalyzes this conversion by a double displacement mechanism. Group: Enzymes. Synonyms: Sucrose Phosphorylase; EC 2.4.1.7; sucrose glucosyltransferase; disaccharide glucosyltransferase; Sucrose:orthophosphate α-D-glucosytransferase. Enzyme Commission Number: EC. 2.4.1.7. CAS No. 9074-06-0. Sucrose Phosphorylase. Activity: > 100 units/mg protein. Storage: Store at -20°C. Form: Lyophilized powder. Source: Leuconostoc Mesenteroides. Sucrose Phosphorylase; EC 2.4.1.7; sucrose glucosyltransferase; disaccharide glucosyltransferase; Sucrose:orthophosphate α-D-glucosytransferase. Cat No: NATE-0890. | |
| Native Lignin Peroxidase | Lignin peroxidase is a fungal enzyme which has a key role in the ligninolytic cycle, the process by which the structural component of plant walls, lignin, is degraded. Group: Enzymes. Synonyms: lignin peroxidase; diarylpropane oxygenase; ligninase I; diarylpropane peroxidase; diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving); LiP; 42613-30-9. CAS No. 42613-30-9. LiP. Activity: >0.1 units/mg. Storage: -20°C. Form: powder; slightly beige. lignin peroxidase; diarylpropane oxygenase; ligninase I; diarylpropane peroxidase; diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving); LiP; 42613-30-9. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0396. | |
| Native Lignin Peroxidase from Phanerochaete chrysosporium | Lignin peroxidase is a fungal enzyme which has a key role in the ligninolytic cycle, the process by which the structural component of plant walls, lignin, is degraded. Applications: Demethoxylation cα-cβ cleavage benzylic alcohol oxidation degradation of lignins, polycyclic aromatic hydrocarbons and xenobiotic compounds. Group: Enzymes. Synonyms: lignin peroxidase; diarylpropane oxygenase; ligninase I; diarylpropane peroxidase; diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving); LiP; 42613-30-9. Enzyme Commission Number: EC 1.11.1.14. CAS No. 93792-13-3. LiP. Stability: 6 months. Storage: store at -20 °C. Form: Freeze-dried powder, no stabilizing agent added. Source: Phanerochaete chrysosporium. lignin peroxidase; diarylpropane oxygenase; ligninase I; diarylpropane peroxidase; diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving); LiP; 42613-30-9. Cat No: NATE-1579. | |
| Native Limpets (Patella vulgata) β-Glucuronidase | β-glucuronidase catalyzes the breakdown of complex carbohydrates. In humans it converts conjugated bilirubin into the unconjugated form, making bilirubin suitable for reabsorption. Type l-ii, lyophilized powder, 1 kda kda-3 kda kda units/g solid; aqueous solution, > 85 kda units/ml. Group: Enzymes. Synonyms: β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase; EC 3.2.1.31; 9001-45-0; β-D-glucuronoside glucuronosohydrolase; GUSB. Enzyme Commission Number: EC 3.2.1.31. CAS No. 9001-45-0. GUSB. Form: lyophilized powder or aqueous solution (Aqueous solution in 0.9% NaCl with 0.02% sodium azide as preservative). Source: Limpets (Patella vulgata). β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase; EC 3.2.1.31; 9001-45-0; β-D-glucuronoside glucuronosohydrolase; GUSB. Cat No: NATE-0332. | |
| Native Lysobacter enzymogenes Endoproteinase Lys-C | Endoproteinase Lys-C inactivates the enzyme inositol monophosphatase by cleaving it at a single site directly after Lys 36. Endoproteinase lys-c is an enzyme that preferentially cleaves at the carboxyl side of lysine residues. Applications: Endoproteinase lys-c from lysobacter enzymogenes is useful in the determination of primary structures of proteins. it has been used in a study to investigate the evidence for trisulfide bonds in a recombinant variant of a human igg2 mon oclonal antibody. endoproteinase lys-c has been used for the digestion mon oclonal antibodies for disulfide bond assignment. Group: Enzymes. Synonyms: EC 3.4.21.50; chromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; 72561-05-8; Achromobacter proteinase I; Endoproteinase Lys-C. Enzyme Commission Number: EC 3.4.21.50. CAS No. 72561-05-8. Achromopeptidase. Storage: 2-8°C. Form: lyophilized powder. Source: Lysobacter enzymogenes. EC 3.4.21.50; chromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; 72561-05-8; Achromobacter proteinase I; Endoproteinase Lys-C. Cat No: NATE-0220. | |
| Native Lysozyme Biotin-Caproyl | Total activity of conjugate against immobilized avidin >95%. Contains approx. two moles biotin to one mole of lysozyme. Group: Enzymes. Synonyms: Lysozyme Biotin-Caproyl. Lysozyme. Activity: >20,000 U/mg. Storage: Store at 2-8°C. Form: Lyophilized powder containing potassium phosphate and sodium chloride. Lysozyme Biotin-Caproyl. Pack: 0.2 mg in glass bottle. Cat No: NATE-0891. | |
| Native Malate dehydrogenase (Decarboxylating) from Thermophillic bacteria | Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses ...; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; S-malate: NAD+ oxidoreductase; EC 1.1.1.38; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.38. CAS No. 9080-52-8. MDH. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD- | |
| Native Malate dehydrogenase from Thermophillic bacteria | Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner...e dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; S-malate: NAD+ oxidoreductase; EC 1.1.1.37; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidored | |
| Native Mammalian Ubiquitin Conjugating Enzyme Fractions | Ubiquitin-conjugating enzymes perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. The ubiquitination process covalently attaches ubiquitin, a short protein of 76 amino acids, to a lysine residue on the target protein. Once a protein has been tagged with one ubiquitin molecule, additional rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein that allows passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell. Applications: Ubiquitin conjugating enzyme fractions mammalian may be used in transferring the activated ubiquitin from e1 to the substrate through an additional high energy thiol ester intermediate e2-s-ubiquitin. ubiquitin-conjugating enzymes, also known as e2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. Group: Enzymes. Synonyms: Ubiquitin con. Ubiquitin Conjugating Enzyme. Storage: -70°C. Source: Mammalian. Ubiquitin conjugating enzymes; Ubiquitin Conjugating Enzyme Fractions; E2 enzymes; ubiquitin-carrier enzymes. Cat No: NATE-0727. | |
| Native Microbial α-phosphoglucomutase | Phosphoglucomutase (EC 5.4.2.2) is an enzyme that transfers a phosphate group on an α-D-glucose monomer from the 1' to the 6' position in the forward direction or the 6' to the 1' position in the reverse direction. More precisely, it facilitates the interconversion of glucose 1-phosphate and glucose 6-phosphate. High purity recombinant α-phosphoglucomutase (microbial) for use in research, biochemical enzyme assays and in vitro diagnostic analysis. Group: Enzymes. Synonyms: α-phosphoglucomutase; Phosphoglucomutase; EC 5.4.2.2; Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent); Glucose phosphomutase; Phosphoglucose mutase. Enzyme Commission Number: EC 5.4.2.2. CAS No. 9001-81-4. Phosphoglucomutase. Mole weight: MW ~ 59.2 kDa. Source: Microbial. α-phosphoglucomutase; Phosphoglucomutase; EC 5.4.2.2; Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent); Glucose phosphomutase; Phosphoglucose mutase. Cat No: DIA-265. | |
| Native Microbial Creatinine Deiminase | In enzymology, a creatinine deaminase (EC 3.5.4.21) is an enzyme that catalyzes the chemical reaction: creatinine + H2O <-> N-methylhydantoin + NH3. Thus, the two substrates of this enzyme are creatinine and H2O, whereas its two products are N-methylhydantoin and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is creatinine iminohydrolase. Applications: Creatinine deiminase has been used in a study to assess the application of a creatinine-sensitive biosensor for hemodialysis control. creatinine deiminase has also been used in a study to investigate the bioelectronic tongue for the simultaneous determination of urea, creatinine and alkaline ions in clinical samples. Group: Enzymes. Synonyms: EC 3.5.4.21, creatinine hydrolase; creatinine desiminase; creatinine deaminase; 37289-15-9. Enzyme Commission Number: EC 3.5.4.21. CAS No. 37289-15-9. Creatinine Deiminase. Mole weight: mol wt ~260 kDa. Activity: > 25 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing mannitol as stabilizer. Source: Microbial. EC 3.5.4.21, creatinine hydrolase; creatinine desiminase; creatinine deaminase; 37289-15-9. Cat No: NATE-0164. | |
| Native Microbial Xanthine Oxidase | Xanthine oxidase is a molybdenum-containing enzyme that is found in the cytosol, and may be strongly inhibited by flavonoids. It plays a vital role in the metabolism of some drugs, as well as purines and pyrimidines. It is also known to be a biological source of reactive oxygen species. Xanthine oxidase was shown to be involved in the reduction of cytochrome c by the generation of superoxide anions following the oxidation of xanthine. These free radicals are responsible for reducing cytochrome c. Allopurinol is a synthetic drug show to inhibit xanthine oxidase. Applications: This enzyme is useful for enzymatic determination of inorganic phosphorus, 5?-nucleotidase and adenosine deaminase when coupled with purine-nucleoside phosphorylase and uricase. Group: Enzymes. Synonyms: Xanthine oxidase; XO; xanthine oxidoreductase; EC 1.17. Enzyme Commission Number: EC 1.17.3.2. CAS No. 9002-17-9. XAO. Mole weight: mol wt ~160 kDa. Activity: > 7 units/mg solid. Storage: -20°C. Form: Lyophilized powder containing BSA and sodium glutamate as stabilizers. Source: Microbial. Xanthine oxidase; XO; xanthine oxidoreductase; EC 1.17.3.2; 9002-17-9; XOD; Xanthine:oxygen oxidoreductase; hypoxanthine oxidase; hypoxanthine:oxygen oxidoreductase; Schardinger enzyme; hypoxanthine-xanthine oxidase; xanthine:O2 oxidoreductase; xanthine:xanthine oxidase. Cat No: NATE-0733. | |
| Native Micrococcus lysodeikticus Catalase | Catalase activates the decomposition of hydrogen peroxide, a reactive oxygen species, into water and oxygen. It functions as a natural antioxidant, protecting cells against oxidative damage to proteins, lipids and nucleic acids. Catalase has also been used to study the role reactive oxygen species play in gene expression and apoptosis. Group: Enzymes. Synonyms: EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase; 9001-05-2. Enzyme Commission Number: EC 1.11.1.6. CAS No. 9001-5-2. CAT. Mole weight: Mr ~230 kDa. Storage: 2-8°C. Form: solution. Source: Micrococcus lysodeikticus. EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase; 9001-05-2. Cat No: NATE-0109. | |
| Native Microorganism Alkaline phosphatase | Alkaline phosphatase (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Group: Enzymes. Synonyms: Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Enzyme Commission Number: EC 3.1.3.1. CAS No. 9001-78-9. ALP. Storage: Storage at 2-8 centigrade. Source: Microorganism. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Cat No: DIA-181. | |
| Native Microorganism α-Glucosidase (MALTASE) | Glycoside hydrolases (also called glycosidases or glycosyl hydrolases) assist in the hydrolysis of glycosidic bonds in complex sugars. They are extremely common enzymes with roles in nature including degradation of biomass such as cellulose and hemicellulose, in anti-bacterial defense strategies (e.g., lysozyme), in pathogenesis mechanisms (e.g., viral neuraminidases) and in normal cellular function (e.g., trimming mannosidases involved in N-linked glycoprotein biosynthesis). Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds. Applications: This enzyme is useful for structural investi...tase; alpha-D-glucosidase; alpha-glucoside hydrolase; alpha-1,4-glucosidase; alpha-D-glucoside glucohydrolase; glycosidases; glycosyl hydrolases; α-Glucosidase. Enzyme Commission Number: EC 3.2.1.20. CAS No. 9001-42-7. Activity: 20U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Alpha-glucosidase; EC 3.2.1.20; maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; alpha-glucopyranosidase; glucosidoinvertase; alpha-D-glucosidase; alpha-glucoside hydrolase; alpha-1,4-glucosidase; alpha-D-glucoside glucohydrolase; glycosidases; glycosyl hydrolases; α-Glucosidase. Cat No: DIA-194. | |
| Native Microorganism Cholesterol Esterase | Sterol esterase belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is steryl-ester acylhydrolase. This enzyme participates in bile acid biosynthesis. Applications: This enzyme is useful for enzymatic determination of total cholesterol when coupled with cholesterol oxidase in clinical analysis. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; Sterol esterase. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Cholesterol Esterase. Activity: GradeIII 5.0U/mg-solid or more. Stability: Store at -20°C. Appearance: Light brown amorphous powder, lyophilized. Source: Microorganism. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; Sterol esterase. Cat No: DIA-135. | |
| Native Microorganism Cholesterol Oxidase | Recombinant Cholesterol Oxidase belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. This enzyme participates in bile acid biosynthesis. Applications: This enzyme is useful for enzymatic determination of cholesterol in serum when coupled with cholesterol esterase in clinical analysis. Group: Enzymes. Synonyms: Cholesterol-O2 oxidoreductase; 3 beta-Hydroxy steroid oxidoreductase; 3β-hydroxysteroid: oxygen oxidoreductase; cholesterol: oxygen oxidoreductase; cholesterol oxidase; EC 1.1.3.6. Enzyme Commission Number: EC 1.1.3.6. CAS No. 9028-76-6. CHOD. Mole weight: approx. 55 kDa (by gel-filtration). Activity: GradeIII 12U/mg-solid or more. Stability: Stable at-20°C for at least 9 months. Appearance: Yellowish amorphous powder, lyophilized. Source: Microorganism. Cholesterol-O2 oxidoreductase; 3 beta-Hydroxy steroid oxidoreductase; 3β-hydroxysteroid: oxygen oxidoreductase; cholesterol: oxygen oxidoreductase; cholesterol oxidase; EC 1.1.3.6. Cat No: DIA-138. | |
| Native Microorganism Creatine Amidinohydrolase | Creatine Amidinohydrolase catalyzes the hydrolytic reaction converting creatine to sarcosine and urea. The enzyme is purified from a microorganism. The molecular weight of the enzyme is approximately 67,000. The enzyme is useful for the enzymatic assay of creatine and creatinine when coupled with other related enzymes. creatine + H2O ? sarcosine + urea. Applications: This enzyme is useful for enzymatic determination of creatinine when coupled with creatinine amidohydrolase, sarcosine dehydrogenase or sarcosine oxidase and formaldehyde dehydrogenase in clinical analysis. Group: Enzymes. Synonyms: Creatine Amidinohydrolase; Creatinase; EC 3.5.3.3. Enzyme Commission Number: EC 3.5.3.3. CAS No. 37340-58-2. Creatinase. Mole weight: approx. 67 kDa (by gel filtration). Activity: Grade? 4.0 U/mg-solid or more. Stability: Stable at -20°C for at least one year. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Creatine amidohydrolase; Creatinase; EC 3.5.3.3. Cat No: DIA-185. | |
| Native Microorganism Creatine Amidohydrolase | In enzymology, a creatinase (EC 3.5.3.3) is an enzyme that catalyzes the chemical reaction: creatine + H2O ?sarcosine + urea. Thus, the two substrates of this enzyme are creatine and H2O, whereas its two products are sarcosine and urea. The native enzyme was shown to be made up of two subunit monomers via SDS-polyacrylamide gel electrophoresis. Creatinase has been found to be most active at pH 8 and is most stable between ph 6-8 for 24 hrs. at 37 degrees. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. This enzyme participates in arginine and proline metabolism. Applications: This enzyme is useful for enzymatic determination of creatinine when coupled with creatine amidinohydrolase, sarcosine dehydrogenase or sarcosine oxidase and formaldehyde dehydrogenase in clinical analysis. Group: Enzymes. Synonyms: Creatine amidohydrolase; Creatinase; EC 3.5.3.3. Enzyme Commission Number: EC 3.5.3.3. CAS No. 37340-58-2. Mole weight: approx. 67 kDa (by gel filtration). Activity: 4.0 U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Creatine amidohydrolase; Creatinase; EC 3.5.3.3. Cat No: DIA-185. | |
| Native Microorganism Creatinine Deiminase | In enzymology, a creatinine deaminase (EC 3.5.4.21) is an enzyme that catalyzes the chemical reaction: creatinine + H2O <-> N-methylhydantoin + NH3. Thus, the two substrates of this enzyme are creatinine and H2O, whereas its two products are N-methylhydantoin and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is creatinine iminohydrolase. Applications: This enzyme is useful for enzymatic determination of creatinine when coupled with glutamate dehydrogenase in clinical analysis. Group: Enzymes. Synonyms: Creatinine hydrolase; Creatinine deaminase; EC 3.5.4.21. Enzyme Commission Number: EC 3.5.4.21. CAS No. 37289-15-9. Creatinine Deiminase. Mole weight: approx. 260 kDa. Activity: Grade? 10U/mg-solid or more (containing approx. 30% of stabilizer). Stability: Stable at-20°C for at least one year. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Creatinine hydrolase; Creatinine deaminase; EC 3.5.4.21. Cat No: DIA-186. | |
| Native Microorganism D-lactate dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: This enzyme is useful for enzymatic determination of numerous metabolites, e.g.atp, adp, glucose, creatinine, pyruvate, lactate and glycerol, and of enzyme activities, e.g.gpt, pk and cpk when coupled with the related enzymes. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. Activity: 400U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Storage: Store at -20°C. Form: Freeze dried powder. Source: Microorganism. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: DIA-207. | |
| Native Microorganism Glucose-6-phosphate Dehydrogenase | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ ? 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Applications: The enzyme is useful for enzymatic determination of nad+(nadp+) and g-6-p, and activities of phosphoglucose isomerase, phosphoglucomutase and hexokinase. the enzyme is also used for enzymatic determination of glucose and creatine phosphokinase activity when coupled with hexokinase. Group: Enzymes. Synonyms: Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-ph. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Mole weight: approx. 140 kDa (by gel filtration). Activity: 200U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; GPD. Cat No: DIA-145. | |
| 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. | |
| Native Microorganism Glucose Dehydrogenase (PQQ-dependent) | In enzymology, a quinoprotein glucose dehydrogenase (EC 1.1.5.2) is an enzyme that catalyzes the chemical reaction: D-glucose + ubiquinone <->D-glucono-1,5-lactone + ubiquinol. Thus, the two substrates of this enzyme are D-glucose and ubiquinone, whereas its two products are D-glucono-1,5-lactone and ubiquinol. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a quinone or similar compound as acceptor. This enzyme participates in pentose phosphate pathway. It employs one cofactor, PQQ. Applications: This enzyme is useful for enzymatic determination of d-glucose. Group: Enzymes. Synonyms: Glucose Dehydrogenase; EC 1.1.5.2; D-glucose:ubiquinone oxidoreductase; D-glucose:(pyrroloquinoline-quinone) 1-oxi. Enzyme Commission Number: EC 1.1.5.2. CAS No. 81669-60-5. Glucose Dehyrogenase. Mole weight: approx. 100 kDa (by gel filtration). Activity: Grade? 500 U/mg-solid or more. Stability: Store at -20°C. Appearance: Purple amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Glucose Dehydrogenase; EC 1.1.5.2; D-glucose:ubiquinone oxidoreductase; D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase; glucose dehydrogenase (PQQ-dependent); glucose dehydrogenase (pyrroloquinoline-quinone); quinoprotein D-glucose dehydrogenase. Cat No: DIA-192. | |
| Native Microorganism Glucose Dehyrogenase (NAD(P)-dependent) | In enzymology, a glucose 1-dehydrogenase (EC 1.1.1.47) is an enzyme that catalyzes the chemical reaction: beta-D-glucose + NAD(P)+ ? D-glucono-1,5-lactone + NAD(P)H + H+. The 3 substrates of this enzyme are beta-D-glucose, NAD+, and NADP+, whereas its 4 products are D-glucono-1,5-lactone, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. Applications: This enzyme is useful for enzymatic determination of d-glucose. Group: Enzymes. Synonyms: Glucose Dehyrogenase; EC 1.1.1.47; beta-D-glucose: NAD(P)+ 1-oxidoreductase; D-glucose dehydrogenase (NAD(P)+). Enzyme Commission Number: EC 1.1.1.47. CAS No. 9028-53-9. Mole weight: approx. 101 kDa (Gel filtration). Activity: 250U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Glucose Dehyrogenase; EC 1.1.1.47; beta-D-glucose: NAD(P)+ 1-oxidoreductase; D-glucose dehydrogenase (NAD(P)+). Cat No: DIA-191. | |
| Native Microorganism Glucose Dehyrogenase (PQQ-dependent) | In enzymology, a quinoprotein glucose dehydrogenase (EC 1.1.5.2) is an enzyme that catalyzes the chemical reaction: D-glucose + ubiquinone ?D-glucono-1,5-lactone + ubiquinol. Thus, the two substrates of this enzyme are D-glucose and ubiquinone, whereas its two products are D-glucono-1,5-lactone and ubiquinol. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a quinone or similar compound as acceptor. This enzyme participates in pentose phosphate pathway. It employs one cofactor, PQQ. Applications: This enzyme is useful for enzymatic determination of d-glucose. Group: Enzymes. Synonyms: Glucose Dehyrogenase; EC 1.1.5.2; D-glucose:ubiquinone oxidoreductase; D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase; glucose dehydrogenase (PQQ-dependent); glucose d. Enzyme Commission Number: EC 1.1.5.2. CAS No. 81669-60-5. Mole weight: approx. 100 kDa (by gel filtration). Activity: 500 U/mg-solid or more. Appearance: Purple amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Glucose Dehyrogenase; EC 1.1.5.2; D-glucose:ubiquinone oxidoreductase; D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase; glucose dehydrogenase (PQQ-dependent); glucose dehydrogenase (pyrroloquinoline-quinone); quinoprotein D-glucose dehydrogenase. Cat No: DIA-192. | |
| Native Microorganism Glutamate Dehydrogenase (NAD-dependent) | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Applications: This enzyme is useful for enzymatic determination of nh3, α-ketoglutaric acid and l-glutamic acid, and for assay of leucine aminopeptidase and urea...ating); EC 1.4.1.2; GLDH. Enzyme Commission Number: EC 1.4.1.2. CAS No. 9001-46-1. Mole weight: approx. 260 kDa. Activity: 100 U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Glutamate Dehydrogenase; glutamic dehydrogenase; glutamate dehydrogenase (NAD); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD-dependent glutamate dehydrogenase; NAD-dependent glutamic dehydrogenase; NAD-glutamate dehydrogenase; NAD-linked glutamate dehydrogenase; NAD-linked glutamic dehydrogenase; NAD-specific glutamic dehydrogenase; NAD-specific glutamate dehydrogenase; NAD: gluta | |
| Native Microorganism Glycerol Kinase | The activity of glycerol kinase is found widely in nature. In microorganisms GK makes possible the utilization of glycerol as a carbon source. In mammals the enzyme represents a juncture of sugar and fat metabolism; The enzyme is important to the clinical chemist in the determination of glycerol. GK is also useful in the assay of glyceraldehydes and dihydroxyacetone following their quantitative reduction to glycerol with sodium borohydride. Applications: This enzyme is useful for enzymatic determination of glycerol and triglyceride when coupled with glycerol-3-phosphate dehydrogenase, glycerol-3-phosphate oxidase or pyruvate kinase and lactate dehydrogenase, lipoprotein lipase in clinical analysis. Group: Enzymes. Synonyms: glycerokinase; GK; ATP: glycerol-3-phosphotransferase; glycerol kinase phosphorylating; glyceric kinase; EC 2.7.1.30. Enzyme Commission Number: EC 2.7.1.30. CAS No. 9030-66-4. GK. Mole weight: approx. 220 kDa (by gel filtration). Activity: Grade? 30 U/mg-solid or more. Stability: Stable at-20°C. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. glycerokinase; GK; ATP: glycerol-3-phosphotransferase; glycerol kinase phosphorylating; glyceric kinase; EC 2.7.1.30. Cat No: DIA-149. | |
| Native Microorganism Hexokinase | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Applications: The enzyme is useful for enzymatic determination of glucose, adenosine-5'-triphosphate (atp) and creatine phosphokinase when coupled with glucose-6-phosphate dehydrogenase. Group: Enzymes. Synonyms: Hexokinase; EC 2.7.1.1; hexokinase type IV glucokinase; hexokinase D; hexokinase type IV; hexokinase (phosphorylating); ATP-dependen. Enzyme Commission Number: EC 2.7.1.1. Mole weight: approx. 82 kDa (by gel filtration). Activity: 150U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Hexokinase; EC 2.7.1.1; hexokinase type IV glucokinase; hexokinase D; hexokinase type IV; hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; ATP: D-hexose 6-phosphotransferase. Cat No: DIA-202. | |
| Native Microorganism Lactate oxidase | Native Microorganism Lactate oxidase. Applications: This enzyme is useful for enzymatic determination of l-lactate. Group: Enzymes. Synonyms: Lactate oxidase; EC 1.1.3.2; lactate oxidative decarboxylase; lactic oxygenase; lactate oxygenase; lactic oxidase. Enzyme Commission Number: EC 1.1.3.2. Lactate oxidase. Mole weight: approx. 160 kDa (by gel filtration). Activity: Grade? 80U/mg-solid or more. Stability: Stable at-20°C for at least 6 months. Appearance: Yellowish amorphous powder, lyophilized. Source: Microorganism. Lactate oxidase; EC 1.1.3.2; lactate oxidative decarboxylase; lactic oxygenase; lactate oxygenase; lactic oxidase. Cat No: DIA-208. | |
| Native Microorganism L-α-glycerophosphate oxidase | In enzymology, a glycerol-3-phosphate oxidase (EC 1.1.3.21) is an enzyme that catalyzes the chemical reaction: sn-glycerol 3-phosphate + O2 <-> glycerone phosphate + H2O2. Thus, the two substrates of this enzyme are sn-glycerol 3-phosphate and O2, whereas its two products are glycerone phosphate and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. This enzyme participates in glycerophospholipid metabolism. It employs one cofactor, FAD. Applications: This enzyme is useful for enzymatic determination of triglyceride when coupled with lipoprotein lipase and glycerokinase in clin...ate oxidase; EC 1.1.3.21. Enzyme Commission Number: EC 1.1.3.21. CAS No. 9046-28-0. Glycerol-3-phosphate oxidase. Mole weight: approx. 93 kDa (by gel filtration). Activity: Grade? 15 U/mg-solid or more (containing approx. 60% of stabilizers). Stability: Stable at-20°C for at least 6 months. Appearance: Yellowish amorphous powder, lyophilized. Source: Microorganism. L-α-glycerophosphate oxidase; sn-glycerol-3-phosphate: oxygen 2-oxidoreductase; glycerol phosphate oxidase; glycerol-1-phosphate oxidase; glycerol phosphate oxidase; L-alpha-glycerophosphate oxidase; alpha-glycerophosphate oxidase; L-alpha-glycerol-3-phosphate oxidase; EC 1.1.3.21. Cat No: DIA-200. | |
| Native Microorganism Lipoprotein lipase | Lipoprotein lipase (LPL) (EC 3.1.1.34) is a member of the lipase gene family, which includes pancreatic lipase, hepatic lipase, and endothelial lipase. It is a water soluble enzyme that hydrolyzes triglycerides in lipoproteins, such as those found in chylomicrons and very low-density lipoproteins (VLDL), into two free fatty acids and one monoacylglycerol molecule. It is also involved in promoting the cellular uptake of chylomicron remnants, cholesterol-rich lipoproteins, and free fatty acids. LPL requires ApoC-II as a cofactor. Applications: This enzyme is useful for enzymatic determination of triglyceride in serum when coupled with l-α-glycerophosphate oxidase and glycerol kinase. usually, the reaction can be completed in 5 minutes at 37°c by using 2.5~3.0 units of the enzyme per test (3.0ml) at ph around 7.0. Group: Enzymes. Synonyms: Lipoprotein lipase; LPL; EC 3.1.1.34; Clearing factor lipase; Diacylglycerol lipase; Diglyceride lipase. Enzyme Commission Number: EC 3.1.1.34. CAS No. 9004-2-8. LPL. Activity: Grade??1.0U/mg-solid or more. Stability: Store at -20°C. Appearance: Light brown amorphous powder, lyophilized. Source: Microorganism. Lipoprotein lipase; LPL; EC 3.1.1.34; Clearing factor lipase; Diacylglycerol lipase; Diglyceride lipase. Cat No: DIA-211. | |
| Native Microorganism Malate Dehydrogenase | Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner mitoch...-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; S-malate: NAD+ oxidoreductase; EC 1.1.1.37; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. Activity: 40U/mg-solid or more. Appearance: Slightly yellowish amorphous powder, lyophilized. Storage: Stable at-20°C for at least one year. Form: Freeze dried powder. Source: Microorganism. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific m | |
| Native Microorganism Mutarotase | In enzymology, an aldose 1-epimerase (EC 5.1.3.3) is an enzyme that catalyzes the chemical reaction:alpha-D-glucose<-> beta-D-glucose. Hence, this enzyme has one substrate, alpha-D-glucose, and one product, beta-D-glucose. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. This enzyme participates in glycolysis and gluconeogenesis. Applications: This enzyme is useful for enzymatic determination of glucose. Group: Enzymes. Synonyms: mutarotase; aldose mutarotase; galactose mutarotase; galactose 1-epimerase; D-galactose 1-epimerase; aldose 1-epimerase; EC 5.1.3.3. Enzyme Commission Number: EC 5.1.3.3. CAS No. 9031-76-9. Mutarotase. Mole weight: ca. 39,500. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Microorganism. mutarotase; aldose mutarotase; galactose mutarotase; galactose 1-epimerase; D-galactose 1-epimerase; aldose 1-epimerase; EC 5.1.3.3. Cat No: NATE-1907. | |
| Native Microorganism N-Acetylneuraminic acid aldolase | In enzymology, a N-acetylneuraminate lyase (EC 4.1.3.3) is an enzyme that catalyzes the chemical reaction: N-acetylneuraminate <-> N-acetyl-D-mannosamine + pyruvate. Hence, this enzyme has one substrate, N-acetylneuraminate, and two products, N-acetyl-D-mannosamine and pyruvate. This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. Applications: This enzyme is useful for enzymatic determination of n-acetylneuraminic acid and sialic acid when coupled with the related enzymes in clinical analysis. for industrial use, this enzyme is useful for enzymatic synthesis of sialic acid. Group: Enzymes. Synonyms: N-Ace...ity: Grade III 15U/mg-solid or more (30U/mg-protein or more), (containing approx. 30% of stabilizers). Stability: Stable at-20°C for at least 6 months. Appearance: Yellowish amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. N-Acetylneuraminate Pyruvate Lyase; N-Acetylneuraminic Acid Lyase; NANA Aldolase; EC 4.1.3.3; N-acetylneuraminate pyruvate-lyase (N-acetyl-D-mannosamine-forming); N-acetylneuraminic acid aldolase; acetylneuraminate lyase; sialic aldolase; sialic acid aldolase; sialate lyase; N-acetylneuraminic aldolase; neuraminic aldolase; N-acetylneuraminate aldolase; neuraminic acid aldolase; N-acetylneuraminic acid aldolase; neu | |
| Native Microorganism Phosphoenolpyruvate carboxylase | Phosphoenolpyruvate carboxylase is an enzyme in the family of carboxy-lyases found in plants and some bacteria that catalyzes the addition of bicarbonate (HCO3-) to phosphoenolpyruvate (PEP) to form the four-carbon compound oxaloacetate and inorganic phosphate: PEP + HCO3-? oxaloacetate + Pi. This reaction is used for carbon fixation in CAM (crassulacean acid metabolism) and C4 organisms, as well as to regulate flux through the citric acid cycle (also known as Krebs or TCA cycle) in bacteria and plants. The enzyme structure and its two step catalytic, irreversible mechanism have been well studied. PEP carboxylase is highly regulated, both by phosphorylation and allostery. Applications: This enzyme is useful for enzymatic determination of carbon dioxide when coupled with malate dehydrogenase in clinical analysis. Group: Enzymes. Synonyms: PEP carboxylase; PEPCase; PEPC; EC 4.1.1.31; Phosphoenolpyruvate carboxylase; PDB ID: 3ZGE. Enzyme Commission Number: EC 4.1.1.31. CAS No. 9067-77-0. PEPC. Mole weight: approx. 390 kDa (by gel filtration). Activity: Grade? 5.0U/mg-solid or more. Stability: Stable at-20°C for at least one year. Appearance: White amorphous powder, lyophilized. Source: Microorganism. PEP carboxylase; PEPCase; PEPC; EC 4.1.1.31; Phosphoenolpyruvate carboxylase; PDB ID: 3ZGE. Cat No: DIA-212. | |
| Native Microorganism P-hydroxybenzoate hydroxylase | In enzymology, a 4-hydroxybenzoate 3-monooxygenase (EC 1.14.13.2) is an enzyme that catalyzes the chemical reaction: 4-hydroxybenzoate + NADPH + H+ + O2 <-> protocatechuate + NADP+ + H2O. The 4 substrates of this enzyme are 4-hydroxybenzoate, NADPH, H+, and O2, whereas its 3 products are protocatechuate, NADP+, and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. This enzyme participates in benzoate degradation...4.13.2. CAS No. 9059-23-8. p-Hydroxybenzoate Hydroxylase. Mole weight: 55 kDa~60 kDa. Activity: Grade? 20U/mg-solid or more (containing approx. 40% of stabilizers). Stability: Stable at-20°C for at least one year. Appearance: Yellowish amorphous powder, lyophilized. Source: Microorganism. 4-hydroxybenzoate; NADPH: oxygen oxidoreductase (3-hydroxylating); p-hydroxybenzoate hydrolyase; p-hydroxybenzoate hydroxylase; 4-hydroxybenzoate 3-hydroxylase; 4-hydroxybenzoate monooxygenase; 4-hydroxybenzoic hydroxylase; p-hydroxybenzoate-3-hydroxylase; p-hydroxybenzoic acid hydrolase; p-hydroxybenzoic acid hydroxylase; p-hydroxybenzoic hydroxylase; EC 1.14.13.2. Cat No: DIA-203. | |
| Native Microorganism Purine-nucleoside phosphorylase | In enzymology, a purine-nucleoside phosphorylase (EC 2.4.2.1) is an enzyme that catalyzes the chemical reaction: purine nucleoside + phosphate <-> purine + alpha-D-ribose 1-phosphate. Thus, the two substrates of this enzyme are purine nucleoside and phosphate, whereas its two products are purine and alpha-D-ribose 1-phosphate. This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. Applications: This enzyme is useful for enzymatic determination of inorganic phosphorus, 5'-nucleotidase and adenosine deaminase when coupled with xanthine oxidase and uricase. Group: Enzymes. Synonyms: EC 2.4.2.1; inosine phosphorylase; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynuc. Enzyme Commission Number: EC 2.4.2.1. CAS No. 9030-21-1. PNPase. Mole weight: approx. 120 kDa. Activity: Grade? 15U/mg-solid or more. Stability: Stable at-20°C for at least 12 months. Appearance: White amorphous powder, lyophilized. Source: Microorganism. EC 2.4.2.1; inosine phosphorylase; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase; purine ribonucleoside phosphorylase; purine-nucleoside: phosphate ribosyltransferase. Cat No: DIA-216. | |
| 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 Microorganism Sarcosine Oxidase | Sarcosine oxidase (SAO) is an enzyme that catalyzes the oxidative demethylation of sarcosine to yield glycine, H2O2, 5, 10-CH2-tetrahydrofolate in a reaction requiring H4-tetrahydrofolate and oxygen. sarcosine + H2O + O2 = glycine + formaldehyde + H2O2. Applications: This enzyme is useful for enzymatic determination of creatinine, creatine, and sarcosine when coupling with creatinine amidohydrolase and creatine amidinohydrolase.-341 is newer type of sarosine oxidase, with improved stability in antimicrobial reagent. Group: Enzymes. Synonyms: Sarcosine Oxidase; EC 1.5.3.1; SAO. Enzyme Commission Number: EC 1.5.3.1. CAS No. 9029-22-5. SAO. Mole weight: approx. 65 kDa (by gel filtration). Activity: Grade? 8.0U/mg-solid or more. Stability: Stable at-20°C for at least one year. Appearance: Yellowish amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Sarcosine Oxidase; EC 1.5.3.1; SAO. Cat No: DIA-171. | |
| Native microorganisms Creatininase | Creatininase from Pseudomonas sp. is a homohexameric enzyme with a molecular mass of 28.4 kDa per subunit. It is a cyclic amidohydrolase catalysing the reversible conversion of creatinine to creatine. Each monomer contains a binuclear zinc centre near the C termini of the β-strands and the N termini of the main α-helices. These zinc ions indicate the location of the active site. Protein determined by biuret. Applications: This enzyme is useful for enzymatic determination of creatinine when coupled with creatine amidinohydrolase, sarcosine dehydrogenase or sarcosine oxidase and formaldehyde dehydrogenase in clinical analysis. Group: Enzymes. Synonyms: EC 3.5.2.10, creatinine hydrolase; Creatininase; 9025-13-2. Enzyme Commission Number: EC 3.5.2.10. CAS No. 9025-13-2. Creatininase. Mole weight: mol wt ~175 kDa. Activity: 100-300 units/mg protein. Storage: 2-8°C. Form: Lyophilized powder containing sucrose and BSA as stabilizers. Source: microorganisms. EC 3.5.2.10, creatinine hydrolase; Creatininase; 9025-13-2. Cat No: NATE-0163. | |
| Native Microorganisms Nucleoside Phosphorylase | In enzymology, a purine-nucleoside phosphorylase (EC 2.4.2.1) is an enzyme that catalyzes the chemical reaction:purine nucleoside + phosphate<-> purine + alpha-D-ribose 1-phosphate. Thus, the two substrates of this enzyme are purine nucleoside and phosphate, whereas its two products are purine and alpha-D-ribose 1-phosphate. This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. This enzyme participates in 3 metabolic pathways:purine metabolism, pyrimidine metabolism, and nicotinate and nicotinamide metabolism. Applications: Nucleoside phosphorylase is used in coupled enzyme systems to measure protein dephosphorylation. this e...osphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase; purine ribonucleoside phosphorylase; 9030-21-1; EC 2.4.2.1. Enzyme Commission Number: EC 2.4.2.1. CAS No. 9030-21-1. PNPase. Mole weight: mol wt ~120 kDa. Activity: > 10 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium gluconate, mannitol and EDTA. Source: Microorganisms. purine-nucleoside phosphorylase; inosine phosphorylase; PNP; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; pu | |
| Native Microorganism Sorbitol Dehydrogenase | Sorbitol dehydrogenase (or SDH) is a cytosolic enzyme. In humans this protein is encoded by the SORD gene. Sorbitol dehydrogenase is an enzyme in carbohydrate metabolism converting sorbitol, the sugar alcohol form of glucose, into fructose. Together with aldose reductase, it provides a way for the body to produce fructose from glucose without using ATP. Sorbitol dehydrogenase uses NAD+ as a cofactor; its reaction is sorbitol + NAD+--> fructose + NADH + H+. A zinc ion is also involved in catalysis. Organs that use it most frequently include the liver and seminal vesicle; it is found in all kinds of organisms from bacteria to humans. A secondary use is the metabolism of d... glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase. Enzyme Commission Number: EC 1.1.1.14. CAS No. 9028-21-1. SDH. Mole weight: ca. 68,000; Subunit molecular weight : ca. 26,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Microorganism. Sorbitol Dehydrogenase; SDH; EC 1.1.1.14; 9028-21-1; L-iditol 2-dehydrogenase; polyol dehydrogenase; sorbitol dehydrogenase; L-iditol:NAD+ 5-oxidoreductase; L-iditol (sorbitol) dehydrogenase; glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase. Cat No: NATE-1909. | |
| 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 Microorganism Xanthine oxidase | Xanthine oxidase is a form of xanthine oxidoreductase, a type of enzyme that generates reactive oxygen species. These enzymes catalyze the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid. These enzymes play an important role in the catabolism of purines in some species, including humans. Applications: This enzyme is useful for enzymatic determination of inorganic phosphorus, 5'-nucleotidase and adenosine deaminase when coupled with purine-nucleoside phosphorylase and uricase. Group: Enzymes. Synonyms: EC 1.1.3.22; Xanthine oxidase; XO; XAO. Enzyme Commission Number: EC 1.1.3.22. CAS No. 9054-84-6. XAO. Mole weight: approx. 160 kDa. Activity: Grade? 10U/mg-solid or more. Stability: Stable at-20°C for at least year. Appearance: Reddish brown amorphous powder, lyophilized. Source: Microorganism. EC 1.1.3.22; Xanthine oxidase; XO; XAO. Cat No: DIA-218. | |
| Native Mold sn-Glycerol-3-phosphocholine Phosphodiesterase | In enzymology, a glycerophosphocholine phosphodiesterase (EC 3.1.4.2) is an enzyme that catalyzes the chemical reaction:sn-glycero-3-phosphocholine + H2O<-> choline + sn-glycerol 3-phosphate. Thus, the two substrates of this enzyme are sn-glycero-3-phosphocholine and H2O, whereas its two products are choline and sn-glycerol 3-phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. Group: Enzymes. Synonyms: glycerophosphinicocholine diesterase; glycerylphosphorylcholinediesterase; sn-glycero-3-phosphorylcholine diesterase; glycerolphosphorylcholine phosphodiesterase; glycerophosphohydrolase; EC 3.1.4.2; 9025-85-8. Enzyme Commission Number: EC 3.1.4.2. CAS No. 9025-85-8. Glycerophosphocholine phosphodiesterase. Activity: > 5 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salt. Source: Mold. glycerophosphinicocholine diesterase; glycerylphosphorylcholinediesterase; sn-glycero-3-phosphorylcholine diesterase; glycerolphosphorylcholine phosphodiesterase; glycerophosphohydrolase; EC 3.1.4.2; 9025-85-8. Cat No: NATE-0674. | |
| Native Mouse Creatine Kinase MM | Creatine kinase, muscle also known as CKM is a creatine kinase that in humans is encoded by the CKM gene. In the figure to the right, the crystal structure of the muscle-type M-CK monomer is shown. In vivo, two such monomers arrange symmetrically to form the active MM-CK enzyme. In heart, in addition to the MM-CK homodimer, also the heterodimer MB-CK consisting of one muscle (M-CK) and one brain-type (B-CK) subunit is expressed. The latter may be an important serum marker for myocardial infarction, if released from damaged myocardial cells into the blood where it can be detected by clinical chemistry. Group: Enzymes. Synonyms: CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; CK-MM. Purity: > 90% (SDS-PAGE). CK. Mole weight: 43 kDa. Storage: Store at -20° C. Form: Liquid, 50% Glycerol, 50 mM TrisCl, 2.5 mM b-mercaptoethanol, 0.05% NaN3. Source: Mouse Skeletal Muscle. Species: Mouse. CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; CK-MM. Cat No: NATE-1887. | |
| Native Mouse Endoproteinase Arg-C | An Endoglycosidase is an enzyme that releases oligosaccharides from glycoproteins or glycolipids. It may also cleave polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common. It breaks the glycosidic bonds between two sugar monomer in the polymer. It is different from exoglycosidase that it does not do so at the terminal residue. Hence, it is used to release long carbohydrates from conjugated molecules. If an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. An endoglycosidase cleaves, giving a polymeric product. Group: Enzymes. Synonyms: EC 3.4.21.35; glandular kallikrein; pancreatic kallikrein; submandibular. Enzyme Commission Number: EC 3.4.21.35. CAS No. 82047-85-6. Kallikrein. Storage: -20°C. Form: lyophilized powder. Source: Mouse submaxillary gland. Species: Mouse. EC 3.4.21.35; glandular kallikrein; pancreatic kallikrein; submandibular kallikrein; submaxillary kallikrein; kidney kallikrein; urinary kallikrein; kallikrein; salivary kallikrein; kininogenin; kininogenase; callicrein; glumorin; padreatin; padutin; kallidinogenase; bradykininogenase; depot-padutin; urokallikrein; dilminal D; onokrein P; 82047-85-6. Pack: vial of 5 μg. Cat No: NATE-0218. | |
| Native Mucor miehei Lipase | Triacylglycerol lipase is an enzyme with system name triacylglycerol acylhydrolase. This enzyme catalyses the following chemical reaction:triacylglycerol + H2O<-> diacylglycerol + a carboxylate. Applications: Lipase from mucor miehei can be used to drive the synthesis of flavor esters. lipase from mucor miehei has been used in a study to assess the nonthermal effect of microwave irradiation in nonaqueous enzymatic esterification. it has also been used in a study to investigate the hydrolysis of virgin coconut oil using immobilized lipase in a batch reactor. Group: Enzymes. Synonyms: Triacylglycerol acylhydrolase; Triacylglycerol lipase. Enzyme Commission Number: EC 3.1.1.3. CAS ...rol ester hydrolase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969-4-9; Meito MY 30; Tweenesterase; GA 56; capalase L; triglyceride hydrolase; triolein hydrolase; tween-hydrolyzing esterase; amano CE; cacordase; triglyceridase; triacylglycerol ester hydrolase; amano P; amano AP; PPL; glycerol-ester hydrolase; GEH; meito Sangyo OF lipase; hepatic lipase; lipazin; post-heparin plasma protamine-resistant lipase; salt-resistant post-heparin lipase; heparin releasable hepatic lipase; amano CES; amano B; tributyrase; triglyceride lipase; liver lipase; hepatic monoacylglycerol acyltransferase; 9001-62-1. Cat No: NATE-1609. | |
| 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 Murine Catalase | Catalase activates the decomposition of hydrogen peroxide, a reactive oxygen species, into water and oxygen. It functions as a natural antioxidant, protecting cells against oxidative damage to proteins, lipids and nucleic acids. Catalase has also been used to study the role reactive oxygen species play in gene expression and apoptosis. Group: Enzymes. Synonyms: EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase. Enzyme Commission Number: EC 1.11.1.6. CAS No. 9001-5-2. CAT. Mole weight: tetramer mol wt ~250 kDa. Activity: > 500 units/mg protein. Stability: 2-8°C. Form: ammonium sulfate suspension. Source: murine liver. Species: Murine. EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase. Cat No: NATE-0110. | |
| Native Mushrooms Polyphenol Oxidase | Polyphenol oxidase is a tetramer that contains four atoms of copper per molecule, and binding sites for two aromatic compounds and oxygen. The enzyme catalyses the o-hydroxylation of monophenol molecules in which the benzene ring contains a single hydroxyl substituent) to o-diphenols (phenol molecules containing two hydroxyl substituents). It can also further catalyse the oxidation of o-diphenols to produce o-quinones. PPO causes the rapid polymerization of o-quinones to produce black, brown or red pigments (polyphenols) that cause fruit browning. The amino acid tyrosine contains a single phenolic ring that may be oxidised by the action of PPOs to form o-quinone. Hence, PPOs may also be referred to as tyrosinases. Polyphenol oxidase (tyrosinase) is a bifunctional, copper-containing oxidase having catecholase and cresolase activity. a lyophilized powder. store at -20°c. Group: Enzymes. Synonyms: EC 1.14.18.1; Polyphe. Enzyme Commission Number: EC 1.14.18.1. CAS No. 9002-10-2. Tyrosinase. Mole weight: 128 kDa (Duckworth and Coleman 1970). Activity: > 500 units per mg dry weight. Stability: The lyophilized preparation is stable for 6-12 months when stored at-20°C. Storage: Store at -20°C. Form: lyophilized powder. Source: Mushrooms. EC 1.14.18.1; Polyphenol oxidase; monophenol monooxygenase; Polyphenol oxidase I; chloroplastic. Cat No: NATE-0612. | |
| Native Mushroom Tyrosinase | Tyrosinase is a copper-containing oxidase, which has activity for both catechols and cresol. It is responsible for browning reactions. This enzyme is reported to have two binding sites for aromatic substrates and a different binding site for oxygen-copper. Tyrosinase is a copper-containing oxidase, which has activity for both catechols and cresol. it is responsible for browning reactions. the enzyme is reported to have two binding sites for aromatic substrates and a different binding site for oxygen-copper. the copper is probably cu (I), with inactivation involving oxidation to cu (II) ion. tyrosinase is a copper-containing oxidase, which has activity for both catechols and cres...; monophenol dihydroxyphenylalanine:oxygen oxidoreductase; N-acetyl-6-hydroxytryptophan oxidase; monophenol, dihydroxy-L-phenylalanine oxygen oxidoreductase; o-diphenol:O2 oxidoreductase; phenol oxidase. Enzyme Commission Number: EC 1.14.18.1. CAS No. 9002-10-2. Tyrosinase. Mole weight: 128 kDa by sedimentation velocity diffusion; 133 kDa by light-scattering measurements, and 119.5 kDa by electrophoresis. Activity: > 1000 unit/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Mushroom. Tyrosinase; EC 1.14.18.1; 9002-10-2; monophenol monooxygenase; phenolase; monophenol oxidase; cresolase; monophenolase; tyrosine-dopa oxidase; monophenol monooxidase; monophenol dihydrox | |
| Native Myokinase from Yeast | Adenylate kinase (EC 2.7.4.3) (also known as ADK or myokinase) is a phosphotransferase enzyme that catalyzes the interconversion of adenine nucleotides, and plays an important role in cellular energy homeostasis. Group: Enzymes. Synonyms: Adenylate kinase; EC 2.7.4.3; ADK; myokinase; 9013-02-9; Adenylic kinase; Adenylokinase. Enzyme Commission Number: EC 2.7.4.3. CAS No. 9013-2-9. Myokinase. Activity: > 200 units/mg protein (at 25°C and pH 7.5). Storage: Below -20°C. Form: 50% Glycerol solution. Source: Yeast. Adenylate kinase; EC 2.7.4.3; ADK; myokinase; 9013-02-9; Adenylic kinase; Adenylokinase. Cat No: NATE-1039. | |
| Native Myrothecium verrucaria Bilirubin Oxidase | In enzymology, a bilirubin oxidase (EC 1.3.3.5) is an enzyme that catalyzes the chemical reaction:2 bilirubin + O2<-> 2 biliverdin + 2 H2O. Thus, the two substRates of this enzyme are bilirubin and O2, whereas its two products are biliverdin and H2O. This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in porphyrin and chlorophyll metabolism. Applications: Bilirubin oxidase is used to degrade bilirubin. bilirubin oxidase, from myrothecium verrucaria, may be used to determine free hemoglobin in icteric specimens. it also has potential application in dye effluent decolorization and is a potential treatment for neonatal jaundice. Group: Enzymes. Synonyms: bilirubin oxidase M-1; EC 1.3.3.5; 80619-01-8; Bilirubin:oxygen oxidoreductase; Bilirubin Oxidase. Enzyme Commission Number: EC 1.3.3.5. CAS No. 80619-01-8. Bilirubin Oxidase. Activity: 15-65 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Myrothecium verrucaria. bilirubin oxidase M-1; EC 1.3.3.5; 80619-01-8; Bilirubin:oxygen oxidoreductase; Bilirubin Oxidase. Cat No: NATE-0094. | |
| Native Naja mossambica mossambica Phospholipase A2 | Phospholipase A2 (PLA2) hydrolyzes the β-ester bond of zwitterionic glycerophospholipids. Preferred substrates are phosphatidylcholine, phosphatidylethanolamine, and their plasmalogen analogues. Phosphatidylinositol and phosphatidylserine are also hydrolyzed. It aggressively attacks phospholipids in membranes of intact cells. PLA2 specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Group: Enzymes. Synonyms: Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Enzyme Commission Number: EC 3.1.1.4. CAS No. 9001-84-7. PLA2. Activity: ~1,500 units/mg protein. Storage: -20°C. Source: Naja mossambica mossambica. Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Cat No: NATE-0586. | |
| Native Nematoloma frowardii Manganese Peroxidase | Manganese peroxidase (MnP) is a hemecontaining glycoprotein that is produced by ligninolytic basidiomycetes. It requires hydrogen peroxide as an oxidant. MnP oxidizes Mn2+ to Mn3+. Mn3+ oxidizes phenolic rings to phenoxy radicals which results in the decomposition of various compounds. Applications: Manganese peroxidase (mnp) is used to oxidize mn2+ to mn3+ in the presence of hydrogen peroxide. it is used for the biodegreadation of macromolecular substances such as lignin and humic substances. Group: Enzymes. Synonyms: manganese peroxidase; peroxidase-M2; Mn-dependent (NADH-oxidizing) peroxidase; EC 1.11.1.13; 114995-15-2; MnP. Enzyme Commission Number: EC 1.11.1.13. CAS No. 114995-15-2. MnP. Activity: > 4.2 units/mg. Storage: -20°C. Source: Nematoloma frowardii. manganese peroxidase; peroxidase-M2; Mn-dependent (NADH-oxidizing) peroxidase; EC 1.11.1.13; 114995-15-2; MnP. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0453. | |
| Native Nitrate Reductase from Aspergillus species | Nitrate reductase (NADH) is an enzyme with system name nitrite:NAD+ oxidoreductase. This enzyme catalises the following chemical reaction:nitrite + NAD+ + H2O<-> nitrate + NADH + H+. Nitrate reductase us an iron-sulfur molybdenum flavoprotein. Applications: Nitrate reductase is used for nitrate determination:assay of nitrite and nitrate in culture media. determination of no3- in serum. Group: Enzymes. Synonyms: EC 1.7.1.2; assimilatory nitrate reductase; assimilatory NAD(P)H-nitrate reductase; NAD(P)H bispecific nitrate reductase; nitrate reductase (reduced nicotinamide adenine dinucleotide (phosphate)); nitrate reductase NAD(P)H; NAD(P)H-nitrat. Enzyme Commission Number: EC 1.7.1.2. CAS No. 9029-27-0. Nitrate reductase. Activity: ~0.4 units/mg protein. Stability: A solution of 20 U Nitrate reductase in 2 ml double-dist. water is stable for one week when stored at 2 to 8 °C; for longer periods, freeze the solution in aliquots. Storage: -20°C. Form: Lyophilized powder. Source: Aspergillus sp. EC 1.7.1.2; assimilatory nitrate reductase; assimilatory NAD(P)H-nitrate reductase; NAD(P)H bispecific nitrate reductase; nitrate reductase (reduced nicotinamide adenine dinucleotide (phosphate)); nitrate reductase NAD(P)H; NAD(P)H-nitrate reductase; nitrate reductase [NAD(P)H2]; NAD(P)H2:nitrate oxidoreductase. Pack: 20 U. Cat No: NATE-0998. | |
| Native Nocardia erythropolis Cholesterol Oxidase | Cholesterol oxidase (CHOD) is a monomeric flavoprotein containing FAD that catalyzes the first step in cholesterol catabolism. This bifunctional enzyme oxidizes cholesterol to cholest-5-en-3-one in an FAD-requiring step, which is then isomerized to cholest-4-en-3-one with the release of H2O2. Group: Enzymes. Synonyms: EC 1.1.3.6; CHOD; cholesterol-O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase; 9028-76-6. Enzyme Commission Number: EC 1.1.3.6. CAS No. 9028-76-6. CHOD. Activity: > 15 U/mL. Stability: Stable at -20°C for at least one year. Storage: 2-8°C. Form: in 1 M ammonium sulfate solution, pH 6, solution (slightly hazy). Source: Nocardia erythropolis. EC 1.1.3.6; CHOD; cholesterol-O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase; 9028-76-6. Cat No: NATE-0127. | |
| Native Nocardia sp. Cholesterol Dehydrogenase | Cholesterol dehydrogenase is an enzyme that uses nicotinamide adenine dinucleotide/nicotinamide adenine dinucleotide phosphate (NAD(P)) as its cofactor in oxidizing cholesterol to form cholest-4-en-3-one. This enzyme oxidizes the hydroxyl group at the 3 position of the sterol ring to form a ketone. Applications: Used in the formulation of cholesterol testing reagents or in biosensor applications. Group: Enzymes. Synonyms: Cholesterol Dehydrogenase; CDH. CDH. Mole weight: 37 kDa (SDS-PAGE). Activity: > 5 U/mg. Appearance: Light yellow to brown powder. Form: Freeze dried powder. Source: Nocardia sp. Cholesterol Dehydrogenase; CDH. Cat No: NATE-0892. | |
| Native Orange peel Pectinesterase | Pectinesterase catalyzes the hydrolysis of the methyl esters of pectin to yield pectate and methanol. Applications: Pectinesterase is used to hydrolyze methyl esters of pectin to pectate and methanol. it contains pectin methylesterase and pectin pectylhydrolase. this product is from orange peel and comes as a lyophilized powder. it contains (nh4)2so4 and sodium chloride. it has been used to study the pectin methylesterase gene. the enzyme from creative enzymes has been used as a standard during the measurement of pectin methylesterase activity in sea buckthorn juices. it has been used in the hydrolysis of cell wall pectins while studying phyllotaxis in arabidopsis. it has also been used to catalyze pectin hydrolysis (using an ultrasonic measurement device) for monitoring biological processes. Group: Enzymes. Synonyms: Pectinesterase; EC 3.1.1.11; pectin demethoxylase; pectin methoxylase; pectin methylesterase; pectase; pectin methyl esterase; . Enzyme Commission Number: EC 3.1.1.11. CAS No. 9025-98-3. Pectinesterase. Activity: > 150 units/mg protein. Storage: 2-8°C. Form: lyophilized powder; Contains (NH4)2SO4 and sodium chloride. Source: Orange peel. Pectinesterase; EC 3.1.1.11; pectin demethoxylase; pectin methoxylase; pectin methylesterase; pectase; pectin methyl esterase; pectinoesterase; pectin pectylhydrolase; 9025-98-3. Cat No: NATE-0537. | |
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