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| Product | Description | |
|---|---|---|
| Microorganism blend for Denitrification Treatment in Waste Water | WME-2710 contains various selected microorganisms, is our superior product specially applied in waste water treatment and bioremediation. It is suitable to aerobic treatment system and can be widely used in wastewater treatment of urban domestic, slaughterhouse, coking, tannery, and waste leachate, etc. Applications: It is significantly effective in the process of ammonia nitrogen removal of sewage treatment facilities, crashed system recovery, and improving the handling ability to nitration system in cold seasons. Group: Enzymes. Synonyms: Product for Denitrification Treatment in Waste Water. Waste Management. Form: Tan liquid. Product for Denitrification Treatment in Waste Water; Denitrification; Waste Water; waste water treatment and bioremediation. Cat No: WME-2710. |  |
| Microorganisms and enzymes blend for Petroleum sewage | This product is a microbial product, mixed by a number of high concentrations of non-pathogenic aerobic and autotrophic microorganisms and a variety of enzymes, these microorganisms can grow under aerobic and anaerobic conditions and is capable of degrading various cellulose and other organic substances in oil wastewater. This product also contains high active enzymes, can help degrade suspended solids and complex matters in the sludge. Group: Enzymes. Synonyms: microbial products; non-pathogenic aerobic microorganisms; autotrophic microorganisms; enzymes; oil wastewater; cellulose; organic substances; suspended solids; sludge; Natural microflora; Waste Management. Waste Management. Activity: 3×108 CFU/g. Appearance: Pale yellow to light brown powder. Storage: Below 25°C. microbial products; non-pathogenic aerobic microorganisms; autotrophic microorganisms; enzymes; oil wastewater; cellulose; organic substances; suspended solids; sludge; Natural microflora; Waste Management. Cat No: WME-2700. | |
| 35-Colony count and calculation of number of microorganisms | 35-Colony count and calculation of number of microorganisms. Uses: For analytical and research use. Group: Food & beverage proficiency testing. Catalog: APS004494. Format: Participants will be provided with a photograph and a scenario in order to count the number of colonies and calculate the number of microorganisms in the original sample. |  |
| 5'-Nucleotidase from Microorganism | 5'-nucleotidase is an enzyme with system name 5'-ribonucleotide phosphohydrolase. This enzyme catalyses the following chemical reaction:a 5'-ribonucleotide + H2O? a ribonucleoside + phosphate. This enzyme has a wide specificity for 5'-nucleotides. Group: Enzymes. Synonyms: uridine 5'-nucleotidase; 5'-adenylic phosphatase; adenosine 5'-phosphatase; AMP phosphatase; adenosine monophosphatase; 5'-mononucleotidase; AMPase; UMPase; snake venom 5'-nucleotidase; thimidine monophosphate nucleotidase; 5'-AMPase; 5'-AMP nucleotidase; AMP phosphohydrolase; IMP 5'-nucleotidase; EC 3.1.3.5. Enzyme Commission Number: EC 3.1.3.5. CAS No. 9027-73-0. Activity: >50U/mg protein. Storage: Store at -20°C. Form: White amorphous powder. Source: Microorganism. uridine 5'-nucleotidase; 5'-adenylic phosphatase; adenosine 5'-phosphatase; AMP phosphatase; adenosine monophosphatase; 5'-mononucleotidase; AMPase; UMPase; snake venom 5'-nucleotidase; thimidine monophosphate nucleotidase; 5'-AMPase; 5'-AMP nucleotidase; AMP phosphohydrolase; IMP 5'-nucleotidase; EC 3.1.3.5; 5'NT. Cat No: NATE-1717. | |
| 5-Nucleotidase, Microorganism | 5-Nucleotidase, Microorganism (CD73) is an intrinsic membrane glycoprotein present as an ectoenzyme. 5-Nucleotidase catalyzes hydrolysis of 5-nucleotides to their corresponding nucleosides [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: CD73; 5-NT. CAS No. 9027-73-0. Pack Sizes: 200 U; 500 U. Product ID: HY-P3260. |  |
| 6-Phosphogluconic Dehydrogenase from Microorganism | In enzymology, a phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) is an enzyme that catalyzes the chemical reaction:6-phospho-D-gluconate + NADP+<-> D-ribulose 5-phosphate + CO2 + NADPH. Thus, the two substRates of this enzyme are 6-phospho-D-gluconate and NADP+, whereas its 3 products are D-ribulose 5-phosphate, CO2, and NADPH. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. Group: Enzymes. Synonyms: 6-Phosphogluconic Dehydrogenase; phosphogluconic acid dehydrogenase; 6-phosphogluconic dehydrogenase; 6-phosphogluconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase; EC 1.1.1.44; phosphogluconate dehydrogenase; decarboxylating; 9073-95-4. Enzyme Commission Number: EC 1.1.1.44. 6-Phosphogluconic Dehydrogenase. Mole weight: ca. 132,000. Activity: >40 U/mg protein. Storage: Stable at -20 °C for at least six months. Form: Lyophilized. Source: Microorganism. 6-Phosphogluconic Dehydrogenase; phosphogluconic acid dehydrogenase; 6-phosphogluconic dehydrogenase; 6-phosphogluconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase; EC 1.1.1.44; phosphogluconate dehydrogenase; decarboxylating; 9073-95-4. Cat No: NATE-1937. | |
| Acyl-CoA oxidase from Microorganism | In enzymology, an acyl-CoA oxidase (EC 1.3.3.6) is an enzyme that catalyzes the chemical reaction acyl-CoA + O2? trans-2, 3-dehydroacyl-CoA + H2O2. Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2, 3-dehydroacyl-CoA and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in 3 metabolic pathways: fatty acid metabolism, polyunsaturated fatty acid biosynthesis, and ppar signaling pathway. It employs one cofactor, FAD. Group: Enzymes. Synonyms: acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; fatty acyl-coenzyme A oxidase; ACO. Enzyme Commission Number: EC 1.3.3.6. CAS No. 61116-22-1. Mole weight: 78 kDa (SDS-PAGE). Activity: >30U/mg protein. Storage: Store at -20°C. Form: Yellow powder, lyophilized. Source: Microorganism. acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; fatty acyl-coenzyme A oxidase; ACO. Cat No: NATE-1711. | |
| Acyl-CoA synthetase from Microorganism | Acetylcoenzyme A synthetase (ACS, EC 6.2.1.3)catalyzes the formation of acetyl coenzyme A with free fatty acids and coenzyme A. The ACS provided by our company is gene recombinant protein. It is of high purity and good activity. Group: Enzymes. Synonyms: EC 6.2.1.3; ACS; acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetas. Enzyme Commission Number: EC 6.2.1.3. CAS No. 9013-18-7. Mole weight: 63 kDa (SDS-PAGE). Activity: >20U/mg protein. Storage: Store at -20°C. Form: White powder, lyophilized. Source: Microorganism. EC 6.2.1.3; ACS; acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetase; acyl coenzyme A synthetase; acyl-CoA ligase; palmitoyl coenzyme A synthetase; thiokinase; palmitoyl-CoA ligase; acyl-coenzyme A ligase; fatty acid CoA ligase; long-chain fatty acyl coenzyme A synthetase; oleoyl-CoA synthetase; stearoyl-CoA synthetase; long chain fatty acyl-CoA synthetase; long-chain acyl CoA synthetase; fatty acid elongase; LCFA synthetase; pristanoyl-CoA synthetase; ACS3; long-chain acyl-CoA synthetase I; long-chain acyl-CoA synthetase II; fatty acyl-coenzyme A synthetase; long-chain acyl-coenzyme A synthetase; FAA1. Cat No: NATE-1712. | |
| Adenosine deaminase, microorganism | Adenosine deaminase (RnADA) (EC 3.5.4.4) is an enzyme that catalyzes the irreversible deamination of adenosine and 2'-deoxyadenosine to inosine and 2'-deoxyinosine, respectively. Uses: Scientific research. Group: Signaling pathways. Alternative Names: RnADA. CAS No. 9026-93-1. Pack Sizes: 1 mg. Product ID: HY-114175. | |
| Arginase, Microorganism | Arginase, Microorganism (L-Arginine amidinase) is an enzyme of the urea cycle. Arginase catalyzes the hydrolysis of L-arginine to L-ornithine and urea [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: L-Arginine amidinase. CAS No. 9000-96-8. Pack Sizes: 1 KU. Product ID: HY-P3190. | |
| Bilirubin oxidase from Microorganism | 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. Group: Enzymes. Synonyms: bilirubin oxidase M-1; bilirubin oxidase; EC 1.3.3.5; bilirubin: oxygen oxidoreductase. Enzyme Commission Number: EC 1.3.3.5. CAS No. 80619-01-8. Activity: >20U/mg. Storage: Store at -20°C. Form: Blue powder, lyophilized. Source: Microorganism. bilirubin oxidase M-1; bilirubin oxidase; EC 1.3.3.5; bilirubin: oxygen oxidoreductase; BOD. Cat No: NATE-1713. | |
| Cholesterol Esterase from Microorganism | Cholesterol esterase (CE) is also known as cholesterol ester hydrolase. This enzyme catalyzes the following reaction: Sterol Ester --------> Sterol + Fatty Acid. Cholesterol esterase activity has been demonstrated in pancreas, intestine, liver and kidney. The enzyme is inactivated by proteolytic enzymes but stabilized by proteolytic enzyme inhibitors and by bile salts. 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. Activity: 5.0U/mg-solid or more. Form: Freeze dried powder. 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. | |
| Cholesterol Oxidase from Microorganism | 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: 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. Activity: 12U/mg-solid or more. Form: Freeze dried powder. 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. | |
| Cholesterol oxidase, Microorganism | Cholesterol oxidase, Microorganism (ChOx) is a bacterial flavin oxidase containing FAD, commonly used in biochemical research. Cholesterol oxidase catalyzes the oxidation of the C(3)-OH group of cholesterol (and other sterols) to cholest-5-en-3-one and isomerizes it to cholest-4-en-3-one [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: ChOx. CAS No. 9028-76-6. Pack Sizes: 100 U; 500 U; 1 KU. Product ID: HY-P2848. | |
| Creatinase, microorganism | Creatine amidinohydrolase, microorganism is a hydrolytic enzyme that catalyzes the hydrolysis of creatine into creatinine and urea, playing a crucial role in the measurement of creatinine concentration. Creatine amidinohydrolase, microorganism can be used in the development of biosensors for measuring serum creatinine levels [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Creatine amidinohydrolase, microorganism. CAS No. 37340-58-2. Pack Sizes: 1 KU; 5 KU. Product ID: HY-P2893B. | |
| Creatininase, Microorganism | Creatininase, Microorganism (Creatinine amidohydrolase; CAH), namely creatinine amidohydrolase, from Pseudomonas putida , is a homohexameric enzyme commonly used in biochemical research. Creatininase acts on carbon-nitrogen bonds other than peptide bonds, and can catalyze the hydrolysis of creatinine to creatine, which can then be metabolized by creatinase to urea and sarcosine [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Creatinine amidohydrolase; CAH. CAS No. 9025-13-2. Pack Sizes: 1 KU. Product ID: HY-P2838. | |
| Cystathionine β-lyase, Recombinant Microorganisms | Cystathionine β-lyase, Recombinant Microorganisms (CBL) is an enzyme that catalyzes the breakdown of cystathionine to homocysteine, the penultimate step in methionine biosynthesis. Cystathionine β-lyase is important for bacterial virulence [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: CBL. CAS No. 9055-5-4. Pack Sizes: 100 U; 500 U. Product ID: HY-E70079. | |
| D-3-hydroxybutyrate dehydrogenase from Microorganism | In enzymology, a 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) is an enzyme that catalyzes the chemical reaction: (R)-3-hydroxybutanoate + NAD+ ? acetoacetate + NADH + H+. Thus, the two substrates of this enzyme are (R)-3-hydroxybutanoate and NAD+, whereas its three products are acetoacetate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in synthesis and degradation of ketone bodies and butanoate metabolism. Group: Enzymes. Synonyms: (R)-3-hydroxybutanoate: NAD+ oxidoreductase; NAD+-beta-hydroxybutyrate dehydro. Enzyme Commission Number: EC 1.1.1.30. CAS No. 9028-38-0. Mole weight: 27.5 kDa (SDS-PAGE). Activity: >300U/mg. Storage: Store at -20°C. Form: Yellowish powder, lyophilized. Source: Microorganism. (R)-3-hydroxybutanoate: NAD+ oxidoreductase; NAD+-beta-hydroxybutyrate dehydrogenase; hydroxybutyrate oxidoreductase; beta-hydroxybutyrate dehydrogenase; D-beta-hydroxybutyrate dehydrogenase; D-3-hydroxybutyrate dehydrogenase; D-( - )-3-hydroxybutyrate dehydrogenase; beta-hydroxybutyric acid dehydrogenase; 3-D-hydroxybutyrate dehydrogenase; beta-hydroxybutyric dehydrogenase; EC 1.1.1.30; 9028-38-0; HBDH; β-Hydroxybutyrate Dehydrogenase; 3-Hydroxybutyrate Dehydrogenase. Cat No: NATE-1714. | |
| Diaphorase from microorganism | Diaphorase from microorganism. Better stability and reactivity than dia-187. Group: Enzymes. Synonyms: dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxidoreductase (NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate dehydrogenase; lipoic acid dehydrogenase; lipoyl dehydrogenase; dihydrolipoyl dehydrogenase; Lipoamide Dehydrogenase. Enzyme Commission Number: EC 1.6.99.-. Diaphorase. Source: Microorganism. dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxidoreductase (NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate dehydrogenase; lipoic acid dehydrogenase; lipoyl dehydrogenase; dihydrolipoyl dehydrogenase; EC 1.8.1.4; 9001-18-7; Lipoamide Dehydrogenase. Cat No: DIA-275. | |
| D-Lactate dehydrogenase, Microorganism | D-Lactate dehydrogenase, Microorganism (D-LDH) is an oxidoreductase that uses NAD + or NADP + as an acceptor and acts on the donor CH-OH group, and can catalyze the oxidation of D-lactate to pyruvate. D-Lactate dehydrogenase widely exists in bacteria and fungi, and is often used in biochemical research [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: D-LDH. CAS No. 9028-36-8. Pack Sizes: 500 U; 1 KU. Product ID: HY-P2897. | |
| Fructosyl-amino acid oxidase from Microorganism | Fructosyl-amino acid oxidase from Microorganism. Group: Enzymes. Synonyms: Fructosyl-amino acid oxidase From Microorganism. Fructosyl-amino acid oxidase. Mole weight: approx. 48,000Da (by SDS-PAGE). Activity: 3.0U/mg-solid or more. Appearance: Yelowish amorphous powder,lyophilized. Source: Microorganism. Fructosyl-amino acid oxidase. Cat No: DIA-274. | |
| Glucose-6-phosphate dehydrogenase, Microorganism | Glucose-6-phosphate dehydrogenase, Microorganism (G6PD) is the rate-limiting enzyme of the pentose phosphate pathway. Glucose-6-phosphate dehydrogenase, Microorganism is a primary source of NADPH in antioxidant pathways, nitric oxide synthase, NADPH oxidase, cytochrome p450 systems, and others. Glucose-6-phosphate dehydrogenase, Microorganism is applicable in research related to diabetes, endothelial dysfunction, cancer, and cardiomyopathy [1] [2] [3] [4] [5]. Uses: Scientific research. Group: Natural products. Alternative Names: G6PD. CAS No. 9001-40-5. Pack Sizes: 1 KU; 5 KU. Product ID: HY-125863. | |
| Glycerokinase from Microorganism | Glycerol kinase is a phosphotransferase enzyme involved in triglycerides and glycerophospholipids synthesis. Glycerol kinase catalyzes tge MgATP-dependent phosphorylation of glycerol to produce sn-glycerol-3-phosphate and is the rate limiting enzyme in the utilization of glycerol. It is also subject to feedback regulation by fructose-1,6-bisphosphate. 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. Activity: 30 U/mg-solid or more. 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. | |
| Glycerol-3-phosphate oxidase from Microorganism | 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 clinical analysis. Group: Enzymes. Synonyms: L-α-glycerophosphate oxidase; sn-glycerol-3-phosphate: oxygen 2-oxidoreductase; glycerol phosph. Enzyme Commission Number: EC 1.1.3.21. CAS No. 9046-28-0. Activity: 15 U/mg-solid or more (containing approx. 60% of stabilizers). Appearance: Yellowish amorphous powder, lyophilized. Form: Freeze dried powder. 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. | |
| Hexokinase, microorganism | Hexokinase (ScHEX1) (EC 2.7.1.1) is a glycolytic enzyme hexokinase that is inhibited by n-acetylglucosamine. Inhibition of Hexokinase (ScHEX1) by n-acetylglucosamine leads to its separation from the mitochondrial outer membrane, resulting in activation of NLRP3 inflammasome [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9001-51-8. Pack Sizes: 1 KU. Product ID: HY-P2776. | |
| Laccase, Microorganisms | Laccase, Microorganisms (Denilite IIS) is a multi-copper oxidase (MCOs), which widely exists in microorganisms, plants and fungi, and can catalyze the oxidation of one electron of various phenolic compounds. Laccase can promote the oxidative coupling of single lignin, which plays an important role in the formation and biodegradation of lignin, and also has the potential to cross-link food polymers [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Denilite IIS. CAS No. 80498-15-3. Pack Sizes: 100 mg; 500 mg; 1 g. Product ID: HY-P2890. | |
| Lactate oxidase, Microorganism | Lactate oxidase (EC 1.13.12.4) belongs to a group of FMN-dependent enzymes and they catalyze a conversion of lactate to pyruvate with a release of hydrogen peroxide. Lactate oxidase can be used in the detection of Lactate [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9028-72-2. Pack Sizes: 100 U; 500 U. Product ID: HY-134757. | |
| Leucine dehydrogenase from Microorganism | In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction: L-leucine + H2O + NAD+ ? 4-methyl-2-oxopentanoate + NH3 + NADH + H+. The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis. Group: Enzymes. Synonyms: EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH. Enzyme Commission Number: EC 1.4.1.9. CAS No. 9082-71-7. Mole weight: 43 kDa (SDS-PAGE). Activity: >500U/mg protein. Storage: Store at -20°C. Form: White powder, lyophilized. Source: Microorganism. EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH; LEDH. Cat No: NATE-1715. | |
| Leucine dehydrogenase, Microorganism | Leucine dehydrogenase, Microorganism (EC 1.4.1.9) can be purified from Bacillus spheroides. Leucine dehydrogenase catalyzed the oxidative deamination of L-leucine, L-valine, L-isoleucine, L-norvaline, L-alpha-aminobutyrate, and L-norleucine, and the reductive amination of their keto analogues [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: LDH, EC 1.4.1.9. CAS No. 9082-71-7. Pack Sizes: 1 KU; 100 U; 200 U. Product ID: HY-P2768. | |
| Lichenase, Microorganism | Lichenase, Microorganism (endo-1,3:1,4-β-D-Glucanase) is a specific, endo-(1-3),(1-4)-β-D-glucan 4-glucanohydrolase. Lichenase, Microorganism solubilizes β-glucans from cereal grains and gives gluco-oligosaccharides (GOS). Lichenase, Microorganism can be used in the degradation of polysaccharides in the cell walls [1] [2]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: endo-1,3:1,4-β-D-Glucanase. CAS No. 37288-51-0. Pack Sizes: 5 KU; 10 KU; 50 KU. Product ID: HY-E70013. | |
| L-Lactate dehydrogenase, Microorganism | L-Lactate dehydrogenase, Microorganism (LAD) is a redox enzyme. L-Lactate dehydrogenase catalyzes the reduction of pyruvate to L-lactate by NADH in vivo with absolute enantiospecificity [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: LAD. CAS No. 9001-60-9. Pack Sizes: 5 mg; 10 mg; 25 mg. Product ID: HY-P2807. | |
| Malic dehydrogenase, microorganism | Malate dehydrogenase (EC 1.1.1.37) (MDH) catalyzes the mutual conversion of oxaloacetate and malate, and is associated with the oxidation/reduction of dinucleotide coenzymes [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: MDH; EC 1.1.1.37. CAS No. 9001-64-3. Pack Sizes: 1 KU; 10 KU. Product ID: HY-P2809. | |
| Native Glutamine Synthetase from Microorganism | Glutamine synthetase (GS) (EC 6.3.1.2) is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine: Glutamate + ATP + NH3 ? Glutamine + ADP + phosphate. Glutamine Synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration. The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites. Group: Enzymes. Synonyms: Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase. Enzyme Commission Number: EC 6.3.1.2. CAS No. 9023-70-5. GS. Mole weight: ca. 900 kDa. Activity: > 7 U/mg lyophilizate. Appearance: Light yellow lyophilizate. Storage: at -20°C. Source: Microorganism. Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase. Cat No: DIA-411. | |
| 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 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. | |
| Neuraminidase from Microorganism | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Group: Enzymes. Synonyms: sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Enzyme Commission Number: EC 3.2.1.18. CAS No. 9001-67-6. Mole weight: 52 kDa (SDS-PAGE). Activity: >300U/mg protein. Storage: Store at -20°C. Form: White powder, lyophilized. Source: Microorganism. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; NRH. Cat No: NATE-1716. | |
| Neuraminidase, Microorganism | Neuraminidase, Microorganism (Exo-α-sialidase) is an exosialidase, is often used in biochemical studies. Neuraminidase cleaves α-ketosidic linkage between the sialic (N-acetylneuraminic) acid and an adjacent sugar residue. Neuraminidase, derived from mucosal pathogens, is a virulence factor that modifies the host's response to infection [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Exo-α-sialidase. CAS No. 9001-67-6. Pack Sizes: 5 U; 10 U. Product ID: HY-P2988. | |
| Peptidase, microorganism | Peptidase (IMPa) (Erepsin) is catalytically active enzyme that cleaves peptide bonds in proteins and peptides by hydrolysis [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Erepsin; Peptidase (IMPa). CAS No. 9031-96-3. Pack Sizes: 5 g. Product ID: HY-E70017. | |
| Phosphoenolpyruvate carboxylase, Microorganism | Phosphoenolpyruvate carboxylase, Microorganism (PEPC) is a carbon dioxide fixing enzyme that in an irreversible manner and in the presence of Mg 2+ , converts phosphoenolpyruvate and bicarbonate into oxaloacetate and inorganic phosphorus. Phosphoenolpyruvate carboxylase catalyses the primary assimilation of CO(2) in Crassulacean acid metabolism plants. Phosphoenolpyruvate carboxylase plays a major role in setting the day-night pattern of metabolism in plants [1] [2]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: PEPC. CAS No. 9067-77-0. Pack Sizes: 100 U; 500 U. Product ID: HY-E70015. | |
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