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| Product | Description | |
|---|---|---|
| Native Rhodopseudomonas sphaeroides β-Hydroxybutyrate Dehydrogenase | In mammalian systems, β-hydroxybutyrate dehydrogenase is localized on the inner mitochondrial membrane and requires phosphatidyl choline for activity. In contrast, the enzyme from Pseudomonas is a soluble cytosolic enzyme that does not require a phospholipid allosteric activator. The enzyme is required for the utilization of ketone bodies as a source of metabolic energy. It catalyzes the oxidation of 3-hydroxybutyrate to acetoacetate, the first step in the conversion of ketone bodies to citric acid, which is then further metabolized via the tricarboxylic acid cycle (Krebs cycle). Applications: Suitable for the determination of acetoacetate and d (-)-3...nase; EC 1.1.1.30; 9028-38-0. Enzyme Commission Number: EC 1.1.1.30. CAS No. 9028-38-0. 3-HBDH. Activity: 250-750 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Rhodopseudomonas sphaeroides. 3-hydroxybutyrate dehydrogenase; 3-HBDH; NAD-β-hydroxybutyRate dehydrogenase; hydroxybutyRate oxidoreductase; β-hydroxybutyRate dehydrogenase; D-β-hydroxybutyRate dehydrogenase; D-3-hydroxybutyRate dehydrogenase; D-(-)-3-hydroxybutyRate dehydrogenase; β-hydroxybutyric acid dehydrogenase; 3-D-hydroxybutyRate dehydrogenase; β-hydroxybutyric dehydrogenase; EC 1.1.1.30; 9028-38-0. Cat No: NATE-0004. |  |
| Native Rhodothermus marinus Laminarinase/Lichenase | β-glucanases degrade β-1,4-glucans of cellulose, xyloglucan and β-1,4-xylan. β-Glucanase represents a group of carbohydrate enzymes which break down glycosidic bonds within beta-glucan. It forms the main constituent of fungal cell walls and could be a potential structural and storage polysaccharide of marine macro-algae. It has the ability to degrade fungal cell walls and may be involved in defense mechanism of plants against pathogenic fungi. Group: Enzymes. Synonyms: endo-1,3-β-D-glucanase; laminarinase; laminaranase; β-1,3-glucanase; β-1,3-1,4-glucanase; endo-1,3-β-glucanase; endo-β-1,3 (4)-glucanase; endo-β-1,3-1,4-glucanase; endo-β-(1?3)-D-glucanase; endo-1,3-1,4-β-D-glucanase; endo-β-(1-3)-D-glucan. Enzyme Commission Number: EC 3.2.1.6. CAS No. 62213-14-3. β-glucanase. Source: Rhodothermus marinus. EC 3.2.1.6; endo-1,3-β-D-glucanase; laminarinase; laminaranase; β-1,3-glucanase; β-1,3-1,4-glucanase; endo-1,3-β-glucanase; endo-β-1,3 (4)-glucanase; endo-β-1,3-1,4-glucanase; endo-β-(1?3)-D-glucanase; endo-1,3-1,4-β-D-glucanase; endo-β-(1-3)-D-glucanase; endo-β-1,3-glucanase IV; endo-1,3-β-D-glucanase; 1,3-(1,3; 1,4)-β-D-glucan 3 (4)-glucanohydrolase; endo-1,3 (4)-β-glucanase. Cat No: NATE-0376. | |
| Native Rhodothermus obamensis 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: This enzyme is useful for enzymatic determination of glucose or creatinine kinase activity when coupled with glucose-6-phosphate dehydrogenase. Group: Enzymes. Synonyms: hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Hexokinase. Mole weight: 140 kDa (gel filtration). Activity: 100 - 400 U/mg. Appearance: White to light grayish lyophilized powder. Storage: Storage at -20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Rhodothermus obamensis. hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase; EC 2.7.1.1. Cat No: NATE-1156. | |
| Native Rhodotorula glutinis Phenylalanine Ammonia-Lyase | Phenylalanine Ammonia-Lyase from Rhodotorula glutinis can be cleaved and inactivated by the proteases chymotrypsin, subtilisin, and trypsin. Applications: Phenylalanine ammonia-lyase has been used in a study to assess the effect of heat treatment on lignification of postharvest bamboo shoots. it has also been used in a study to investigate the effect of light on gene expression and podophyllotoxin biosynthesis in linum album cell culture. Group: Enzymes. Synonyms: phenylalanine ammonia-lyase; EC 4.3.1.24; phenylalanine deaminase; phenylalanine ammonium-lyase; PAL; L-phenylalanine ammonia-lyase; Phe ammonia-lyase; 9024-28-6. Enzyme Commission Number: EC 4.3.1.24. CAS No. 9024-28-6. PAL. Activity: 0.8-2.0 units/mg protein. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 60% glycerol, 3 mM Tris-HCl, pH 7.5, containing up to 0.5 M (NH4)2SO4. Source: Rhodotorula glutinis. phenylalanine ammonia-lyase; EC 4.3.1.24; phenylalanine deaminase; phenylalanine ammonium-lyase; PAL; L-phenylalanine ammonia-lyase; Phe ammonia-lyase; 9024-28-6. Cat No: NATE-0502. | |
| Native Rhus vernicifera Laccase | Laccase is a blue copper oxidase that reduces molecular oxygen to water. Laccase oxidizes polyphenols, methoxy-substituted phenols and diamines, but not tyrosine. Oxidation by laccase is an one-electron reaction that generates a free radical. Group: Enzymes. Synonyms: Laccases; EC 1.10.3.2; 80498-15-3; urishiol oxidase; urushiol oxidase; p-diphenol oxidase; benzenediol:oxygen oxidoreductase. Enzyme Commission Number: EC 1.10.3.2. CAS No. 80498-15-3. Laccase. Activity: > 50 units/mg solid. Storage: -20°C. Form: crude acetone powder. Source: Rhus vernicifera. Laccases; EC 1.10.3.2; 80498-15-3; urishiol oxidase; urushiol oxidase; p-diphenol oxidase; benzenediol:oxygen oxidoreductase. Cat No: NATE-0373. | |
| Native Rice α-Glucosidase | Alpha-glucosidase is a glucosidase located in the brush border of the small intestine that acts upon 1,4-alpha bonds. This is in contrast to beta-glucosidase. Alpha-glucosidase breaks down starch and disaccharides to glucose. Maltase, a similar enzyme that cleaves maltose, is nearly functionally equivalent. The enzyme catalyses the hydrolyzis of a-1.6 linked a-galactose residues from oligosaccharides. Group: Enzymes. Synonyms: 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. Enzyme Commission Number: EC 3.2.1.20. CAS No. 9001-42-7. α-Glucosidase. Source: Rice. 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. Cat No: NATE-0041. | |
| Native Russell's viper venom Factor V Activating Enzyme | Factor V activator for RVV contains fucose, mannose, galactose, glucosamine, and neuraminic acid. Factor V activating enzyme from RVV is an arginine esterase that is sensitive to diisopropyl fluorophosphate (DFP). Applications: Factor v activating enzyme from russells viper venom (rvv) is a single-chain glycoprotein that is involved in the rapid clotting of blood. factor v circulates in the blood as an inactive cofactor and must be activated by proteases such as factor v activating enzyme from rvv 1. this product may be useful in studying the blood coagulation cascade as well as the inherited deficiency called parahemophilia. Group: Enzymes. Synonyms: EC 3.4.21.95; Factor V Activating Enzyme; Snake venom factor V activator; 65522-14-7; Factor V activator. Enzyme Commission Number: EC 3.4.21.95. CAS No. 65522-14-7. Factor V activator. Activity: 20 units/mg protein. Storage: -20°C. Form: lyophilized powder; Stabilized in albumin and sodium chloride. Source: Russell's viper venom. EC 3.4.21.95; Factor V Activating Enzyme; Snake venom factor V activator; 65522-14-7; Factor V activator. Cat No: NATE-0249. | |
| Native Saccharomyces cerevisiae Adenosine-5'-triphosphate Sulfurylase | In enzymology, a sulfate adenylyltransferase (EC 2.7.7.4) is an enzyme that catalyzes the chemical reaction:ATP + sulfate<-> diphosphate + adenylyl sulfate. Thus, the two substRates of this enzyme are ATP and sulfate, whereas its two products are diphosphate and adenylyl sulfate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). This enzyme participates in 3 metabolic pathways:purine metabolism, selenoamino acid metabolism, and sulfur metabolism. Applications: Adenosine-5?-triphosphate sulfurylase (atp sulfurylase) may be used to study sulfur metabolism and h...s. Synonyms: ATP-sulfurylase; adenosine-5'-triphosphate sulfurylase; adenosinetriphosphate sulfurylase; adenylylsulfate pyrophosphorylase; ATP sulfurylase; sulfurylase; EC 2.7.7.4; 9012-39-9; Sulfate adenylate transferase. Enzyme Commission Number: EC 2.7.7.4. CAS No. 9012-39-9. ATP-sulfurylase. Activity: > 1.0 units/mg protein. Storage: -20°C. Form: lyophilized powder. Contains Citrate buffer salts. Source: Saccharomyces cerevisiae. ATP-sulfurylase; adenosine-5'-triphosphate sulfurylase; adenosinetriphosphate sulfurylase; adenylylsulfate pyrophosphorylase; ATP sulfurylase; sulfurylase; EC 2.7.7.4; 9012-39-9; Sulfate adenylate transferase. Cat No: NATE-0090. | |
| Native Saccharomyces cerevisiae Alcohol Dehydrogenase | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Applications: Alcohol dehydrogenase from sacchar...dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Activity: > 300 units/mg protein. Storage: -20°C. Form: Solids containing <2% Citrate buffer salts. Source: Saccharomyces cerevisiae. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Cat No: NATE-0035. | |
| Native Saccharomyces cerevisiae α-Glucosidase | Alpha-glucosidase is a glucosidase located in the brush border of the small intestine that acts upon 1,4-alpha bonds. This is in contrast to beta-glucosidase. Alpha-glucosidase breaks down starch and disaccharides to glucose. Maltase, a similar enzyme that cleaves maltose, is nearly functionally equivalent. Protein determined by biuret. Applications: For the determination of α-amylase and the synthesis of various 1?-o-sucrose and 1-o-fructose esters. α-glucosidase is used for the determination of α-amylase and the synthesis of various 1?-o-sucrose and 1-o-fructose esters. it was also used in the measurement of glycosidase inhibition. Group: Enzymes. Synonyms: α-glucosidase; maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; α-glucopyranosidase; glucosidoinve. Enzyme Commission Number: EC 3.2.1.20. CAS No. 9001-42-7. α-Glucosidase. Mole weight: Mr ~63 kDa. Activity: 4-8 units/mg; > 10 units/mg protein (using p-nitrophenyl α-D-glucoside as substrate.). Storage: -20°C. Form: lyophilized powder. Source: Saccharomyces cerevisiae. α-glucosidase; maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; α-glucopyranosidase; glucosidoinvertase; α-D-glucosidase; α-glucoside hydrolase; α-1,4-glucosidase; EC 3.2.1.20; 9001-42-7. Cat No: NATE-0752. | |
| Native Saccharomyces cerevisiae Esterase | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: The compound is commonly used for the synthesis of biodiesel and biopolymers, as well as in the production of pharmaceuticals, agr ochemicals and flavor compounds. Group: Enzymes. Synonyms: EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; es. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: ~2 U/g. Storage: 2-8°C. Form: lyophilized powder. Source: Saccharomyces cerevisiae. EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase; 9016-18-6. Cat No: NATE-0240. | |
| Native Saccharomyces cerevisiae Glyoxalase I | Glyoxalase I is universally expressed and involved in the protection against cellular damage due to cytotoxic metabolites such as advanced glycation end products (AGEs). It is an integral component of the detoxification system, catalyzing the conversion of reactive, acyclic a-oxoaldehydes into the corresponding a-hydroxyacids in a glutathione-dependent manner. Glyoxalase detoxification system consists of glyoxalase (glo)-i and glo-ii. glo-i is a cytosolic, 42 kda, dimeric zn2+ metalloenzyme. Group: Enzymes. Synonyms: lactoylglutathione lyase; EC 4.4.1.5; methylglyoxalase; aldoketomutase; ketone-aldehyde mutase; glyoxylase I; (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing); 9033-12-9. Enzyme Commission Number: EC 4.4.1.5. CAS No. 9033-12-9. Glyoxalase I. Mole weight: 42 kDa. Activity: > 400 units/mg protein. Storage: 2-8°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol, 0.4 M (NH4)2SO4 and 0.002 M KH2PO4 pH 6.5. Source: Saccharomyces cerevisiae. lactoylglutathione lyase; EC 4.4.1.5; methylglyoxalase; aldoketomutase; ketone-aldehyde mutase; glyoxylase I; (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing); 9033-12-9. Cat No: NATE-0308. | |
| Native Saccharomyces cerevisiae 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. Group: Enzymes. Synonyms: hexokinase type IV glucokinase; hexokinase D; hexokinase type IV. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Hexokinase. Mole weight: ~ 54 kDa (monomer); ~110 kDa (dimer). Activity: Type I, > 350 units/mg protein; Type II, > 25 units/mg protein (biuret); Type III, > 130 units/mg protein (biuret). Storage: -20°C. Form: Type I, Lyophilized powder containing phosphate/Citrate pH approx. 7.0; Type II, Type III, Lyophilized powder containing approx. 15% sodium Citrate. Source: Saccharomyces cerevisiae. hexokinase type IV glucokinase; hexokinase D; hexokinase type IV; hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase; EC 2.7.1.1; 9001-51-8. Cat No: NATE-0342. | |
| Native Saccharomyces cerevisiae Invertase Glycoprotein Standard | Invertase is an enzyme that catalyzes the hydrolysis (breakdown) of sucrose (table sugar). The resulting mixture of fructose and glucose is called inverted sugar syrup. Related to invertases are sucrases. Invertases and sucrases hydrolyze sucrose to give the same mixture of glucose and fructose. Invertases cleave the O-C (fructose) bond, whereas the sucrases cleave the O-C (glucose) bond. Typically used in manufacturing confectionaries, dietary supplements, and other food grade applications. Applications: The invertase glycoprotein standard can be used to demonstrate n-glycosylation using pngase f with both in-solution and in-gel pr ocedures. the extent of deglycosylation can be assessed by mobility shift on sds-page gels. used in the production of confectionary foods and artificial honey. Group: Enzymes. Synonyms: EC 3.2.1.26; invertase; saccharase; glucosucrase; β-h-fructosidase; &bet. Enzyme Commission Number: EC 3.2.1.26. CAS No. 9001-57-4. Invertase. Storage: 2-8°C. Form: lyophilized powder. Source: Saccharomyces cerevisiae. EC 3.2.1.26; invertase; saccharase; glucosucrase; β-h-fructosidase; β-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase; β-fructofuranosidase; β-D-fructofuranoside fructohydrolase; 9001-57-4. Cat No: NATE-0359. | |
| Native Schizophyllum commune 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. Mole weight: approx. 130 kDa. Activity: GradeIII 2.0 U/mg-solid or more (containing approx. 20% of stabilizers). Stability: Store at -20°C. Appearance: Light brown amorphous powder, lyophilized. Source: Schizophyllum commune. 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-133. | |
| Native Serratia sp. Serrapeptase | Serrapeptase is a protein decomposition enzymes produced by bacteria serratia. Can decompose slow bradykinin, fibrin and fibrinogen. Applications: 1. as pharmaceutical raw materials manufacturing injection, oral agents, executive standard: ybh clinic? used for anti-inflammation, eliminate swelling. promote the dissolution of sputum, thick liquid to drain. promote the migration of antibiotics to lesion. 2. plant and animal protein hydrolysate powder (hap, hvp) production applications the flora and fauna of macromolecular protein hydrolysis into small molecular peptides or amino acids, to facilitate the effective absorption and utilization of protein. 3. the application of baki...y used in beer production, proteins can be ruled out "cold cloudy" phenomenon 7. application of textile industry processing of wool, and improve quality 8. application of leather industry made from the hair removal agent. 9. application of feed industry to improve protein utilization and lower costs. Group: Enzymes. Synonyms: Serratiopeptidase; Serratia E-15 protease; serralysin; serrapeptase; serratiapeptase; serratia peptidase; serratio peptidase; serrapeptidase. CAS No. 70851-98-8. Serrapeptase. Source: Serratia sp. Serratiopeptidase; Serratia E-15 protease; serralysin; serrapeptase; serratiapeptase; serratia peptidase; serratio peptidase; serrapeptidase. Cat No: PHAM-381. | |
| Native Sheep 6-Phosphogluconic Dehydrogenase | 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. Protein determined by biuret. 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; decarbo. Enzyme Commission Number: EC 1.1.1.44. CAS No. 9073-95-4. 6-Phosphogluconic Dehydrogenase. Activity: 2-10 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer. Source: Sheep liver. Species: Sheep. 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-0008. | |
| Native Sheep Cyclooxygenase 1 | COX-1 catalyzes the conversion of arachidonic acid to prostaglandin H2 (the first step in the biosynthesis of prostaglandins, thromboxanes, and prostacyclins). It is involved in the homeostatic role of eicosanoids and constitutively almost all animal tissues. Has an apparent KM of 8.3 μM for arachidonic acid. Group: Enzymes. Synonyms: COX-1; Constitutive cyclooxygenase; Prostaglandin H synthase 1; Prostaglandin endoperoxide synthase; EC 1.14.99.1; prostaglandin synthase; prostaglandin G/H synthase; (PG)H synthase; PG synthetase; prostaglandin synthetase; fatty acid cyclooxygenase; prostaglandin endoperoxide synthetase. Enzyme Commission Number: EC 1.14.99.1. CAS No. 9055-65-6. Purity: > 95% (SDS-PAGE). COX-1. Mole weight: dimer subunit mol wt 70 kDa. Activity: > 40,000 units/mg protein. Storage: -70°C. Form: aqueous solution. Solution in 80 mM Tris-HCl, pH 8, with 0.1% TWEEN 20 and 300 μM diethyldithiocarbamate. Source: Sheep. COX-1; Constitutive cyclooxygenase; Prostaglandin H synthase 1; Prostaglandin endoperoxide synthase; EC 1.14.99.1; prostaglandin synthase; prostaglandin G/H synthase; (PG)H synthase; PG synthetase; prostaglandin synthetase; fatty acid cyclooxygenase; prostaglandin endoperoxide synthetase. Cat No: NATE-0149. | |
| Native Sheep Hyaluronidase | Hyaluronidase degrades hyaluronan and has been found to be inappropriately regulated during cancer progression. These enzymes randomly cleave β-N-acetylhexosamine-[1?4] glycosidic bonds in hyaluronic acid, chondroitin, and chondroitin sulfates. Group: Enzymes. Synonyms: hyaluronoglucosaminidase; hyaluronidase; hyaluronoglucosidase; chondroitinase; chondroitinase I; hyaluronate 4-glycanohydrolase; EC 3.2.1.35; 37326-33-3. Enzyme Commission Number: EC 3.2.1.35. CAS No. 37326-33-3. Hyaluronidase. Mole weight: mol wt 55 kDa. Activity: Type I, > 1,500 units/mg solid; Type II, > 300 units/mg solid. Storage: -20°C. Form: Type I, lyophilized powder; Type II, Lyophilized powder containing lactose. Source: Sheep testes. Species: Sheep. hyaluronoglucosaminidase; hyaluronidase; hyaluronoglucosidase; chondroitinase; chondroitinase I; hyaluronate 4-glycanohydrolase; EC 3.2.1.35; 37326-33-3. Cat No: NATE-0348. | |
| Native Sheep Sorbitol Dehydrogenase | 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 dietary sorbitol, though sorbitol is known not to be absorbed as well in the intestine as its related compounds ...rogenase; glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase; L-iditol 2-dehydrogenase. Enzyme Commission Number: EC 1.1.1.14. CAS No. 9028-21-1. SDH. Activity: > 20 units/mg protein. Storage: -20°C. Form: lyophilized powder; Contains maltose. Source: Sheep liver. Species: Sheep. Sorbitol dehydrogenase; SDH; EC 1.1.1.14; 9028-21-1; 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; L-iditol 2-dehydrogenase. Cat No: NATE-0668. | |
| Native Silphium perfoliatum L. Superoxide Dismutase | Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice by preventing the conversion of NO to peroxynitrate, an inducer of apoptosis. Applications: Mainly used in health food, cosmetics, medical drugs, biochemical agents supporting raw materials and additives. Group: Enzymes. Synonyms: Superoxide dismutases; EC 1.15.1.1; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; Cu,Zn-SOD. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Mole weight: 32kD. Storage: at -4-25°C, dry, dark conditions for 3 years. Form: Light blue-green lyophilized powder. Source: Silphium perfoliatum L. Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; Cu,Zn-SOD. Cat No: NATE-1619. | |
| Native Sinapis alba (white mustard) seed Thioglucosidase | Myrosinases are present in many bacteria, fungi, and edible plants, including those of the Brassicaceae (Cruciferae) family. The enzyme hydrolyzes the S-glucosidic bond of a glucosinolate substrate to form an unstable aglycone that rearranges with the loss of sulfate primarily to the isothiocyanate, though thiocyanates and nitriles are also formed. Many of the isothiocyanate products of aliphatic and aromatic glucosinolates have cancer chemopreventive properties. Thioglucosidase research has f ocused mainly on the cruciferous crops due to their economic importance and cancer preventive benefits. Applications: Thioglucosidase has been used in a study to assess brassica species screening for glucosinolate content. thioglucosidase has also been used in a study to investigate a negative regulatory role for auxin in sulphate deficiency response in arabidopsis thaliana. Group: Enzymes. Synonyms: thioglucosidase; EC 3.2.1.147; myrosinase; sinigrinase; sinigrase; Glucosinolase; Thioglucoside glucohydrolase; 90. Enzyme Commission Number: EC 3.2.1.147. CAS No. 9025-38-1. Myrosinase. Activity: > 100 units/g solid. Storage: -20°C. Source: Sinapis alba (white mustard) seed. Species: Sinapis alba. thioglucosidase; EC 3.2.1.147; myrosinase; sinigrinase; sinigrase; Glucosinolase; Thioglucoside glucohydrolase; 9025-38-1. Cat No: NATE-0468. | |
| Native Snake Venom Carinactivase | Native Snake Venom Carinactivase. Group: Enzymes. Synonyms: CA-1; Prothrombin activator. Purity: > 90% (SDS-PAGE). Carinactivase. Mole weight: 55000. Stability: 1 year. Storage: at -20°CNote: Do not freeze. Form: Liquid, Solution in 50% glycerol (w/v). Source: Snake Venom. CA-1; Prothrombin activator; Carinactivase. Cat No: NATE-1605. | |
| Native Sphingomyelinase from Streptomyces sp. | Sphingomyelin phosphodiesterase is a hydrolase enzyme that is involved in sphingolipid metabolism reactions. SMase is a member of the DNase I superfamily of enzymes and is responsible for breaking sphingomyelin (SM) down into phosphocholine and ceramide. The activation of SMase has been suggested as a major route for the production of ceramide in response to cellular stresses. Applications: This enzyme is useful for enzymatic determination of sphingomyelin when coupled with alkaline phosphatase and choline oxidase. Group: Enzymes. Synonyms: Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; Smase. Enzyme Commission Number: EC 3.1.4.12. CAS No. 9031-54-3. SMase. Mole weight: 37.5 kDa (SDS-PAGE). Activity: > 500 U/mg. Stability: At least one year at ?20°C. Appearance: White to brownish amorphous powder?lyophilized. Storage: Storage at ?20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Streptomyces sp. Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; Smase. Cat No: NATE-1160. | |
| Native Spinach Aldolase | Fructose-bisphosphate aldolase (EC 4.1.2.13), often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate. Gluconeogenesis and the Calvin cycle, which are anabolic pathways, use the reverse reaction. Glycolysis, a catabolic pathway, uses the forward reaction. Aldolase is divided into two classes by mechanism. Protein determined by lowry. Group: Enzymes. Synonyms: aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Enzyme Commission Number: EC 4.1.2.13. CAS No. 9024-52-6. Aldolase. Activity: 0.3-1.0 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Spinach. aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Cat No: NATE-0049. | |
| Native Spinach D-Ribulose 1,5-Diphosphate Carboxylase | Ribulose-1,5-bisphosphate carboxylase/oxygenase, commonly known by the abbreviation RuBisCO, is an enzyme involved in the first major step of carbon fixation, a process by which atmospheric carbon dioxide is converted by plants to energy-rich molecules such as glucose. In chemical terms, it catalyzes the carboxylation of ribulose-1,5-bisphosphate (also known as RuBP). It is probably the most abundant protein on Earth. Applications: D-ribulose 1,5-diphosphate carboxylase from spinach has been used in a study to assess catalytic by-product formation and ligand binding by ribulose bisphosphate carboxylases from different phylogenies. d-ribulose 1,5-diphosphate carboxy...hate carboxylase/oxygenase; rubisco; 3-phospho-D-glyceRate carboxy-lyase (dimerizing; D-ribulose 1,5-bisphosphate-forming); 3-phospho-D-glyceRate carboxy-lyase (dimerizing); 9027-23-0. Enzyme Commission Number: EC 4.1.1.39. CAS No. 9027-23-0. RuBisCO. Activity: 0.01-0.1 unit/mg solid. Storage: -20°C. Form: partially purified powder. Source: Spinach. EC 4.1.1.39, D-ribulose 1,5-diphosphate carboxylase; D-ribulose-1,5-bisphosphate carboxylase; RuBP carboxylase; carboxydismutase; diphosphoribulose carboxylase; ribulose 1,5-bisphosphate carboxylase; ribulose 1,5-bisphosphate carboxylase/oxygenase; ribulose 1,5-diphosphate carboxylase; ribulose 1,5-diphosphate carboxylas | |
| Native Spinach Glutathione Reductase | Glutathione reductase (GR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the precess is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl proteases, ...PH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Enzyme Commission Number: EC 1.6.4.2. CAS No. 9001-48-3. GR. Mole weight: mol wt 118 kDa. Activity: 100-200 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4 mM, 10 mM potassium phosphate, pH 7.0. Source: Spinach. EC 1.6.4.2; 9001-48-3; Glutathione Reductase; GR; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Cat No: NATE-0318. | |
| Native Spinach Phosphoriboisomerase | Phosphoriboisomerase is responsible for the converstion of ribose 5-phosphate to ribulose 5-phosphate. Applications: Phosphoriboisomerase is used to study the ribulose monophosphate pathway. phosphoriboisomerase from spinach is used in enzyme assays to convert ribose 5-phosphate to ribulose 5-phosphate. Group: Enzymes. Synonyms: ribose-5-phosphate isomerase; phosphopentosisomerase; phosphoriboisomerase; ribose phosphate isomerase; 5-phosphoribose isomerase; D-ribose 5-phosphate isomerase; D-ribose-5-phosphate ketol-isomerase; EC 5.3.1.6; 9023-83-0. Enzyme Commission Number: EC 5.3.1.6. CAS No. 9023-83-0. Phosphoriboisomerase. Activity: > 75 units/mg protein (biuret). Storage: -20°C. Form: partially purified powder. Source: Spinach. ribose-5-phosphate isomerase; phosphopentosisomerase; phosphoriboisomerase; ribose phosphate isomerase; 5-phosphoribose isomerase; D-ribose 5-phosphate isomerase; D-ribose-5-phosphate ketol-isomerase; EC 5.3.1.6; 9023-83-0. Cat No: NATE-0561. | |
| Native Spinacia oleracea (Spinach) Ferredoxin-NADP+ Reductase | Ferredoxin-NADP+ reductase catalyzes the reversible conversion of reduced ferredoxin to oxidized ferredoxin during photosynthesis. Ferredoxin-NADP (H) reductase constitutes a family of hydrophilic FAD-containing monomeric enzymes that deliver NADPH or low potential one-electron donors to redox-based metabolisms in plastids, mitochondria, and bacteria. Applications: Ferredoxin-nadp+ reductase was used in in vitro ferredoxin-dependent desaturation of fatty acids in cyanobacterial thylakoid membranes. it was also used to regulate glyceraldehyde-3-phosphate dehydrogenase. Group: Enzymes. Synonyms: EC 1.18.1.2; ferredoxin-nicotinamide adenine dinucleotide phosphate reductase; ferredoxin-NADP+ reducta. Enzyme Commission Number: EC 1.18.1.2. CAS No. 9029-33-8. FNR. Activity: > 15 units/mg solid, secondary activity: > 10 units/mg solid NADPH diaphorase. Storage: -20°C. Form: lyophilized powder. Source: Spinacia oleracea (Spinach). EC 1.18.1.2; ferredoxin-nicotinamide adenine dinucleotide phosphate reductase; ferredoxin-NADP+ reductase; TPNH-ferredoxin reductase; ferredoxin-NADP+oxidoreductase; NADP+:ferredoxin oxidoreductase; ferredoxin-TPN reductase; ferredoxin-NADP+-oxidoreductase; NADPH:ferredoxin oxidoreductase; ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase; 9029-33-8; FNR. Cat No: NATE-0256. | |
| Native Sporosarcina sp. L-Phenylalanine Dehydrogenase | Phenylalanine dehydrogenase is a member of a large family of amino-acid dehydrogenases, which includes glutamate dehydrogenase, alanine dehydrogenase, leucine dehydrogenase, lysine EUR-dehydrogenase, and meso-a,EUR-diaminopimelate D-dehydrogenase. The three known gene sequences are octomers. It has a two-domain, three-dimensional structure. Applications: L-phenylalanine dehydrogenase is a nad+-dependent oxidoreductase that catalyzes the reversible, oxidative deamination of l-phenylalanine which results in its degradation. l-phenylalanine dehydrogenase is used to study phenylalanine metabolism and phenylalanine, tyrosine and tryptophan biosynthesis. Group: Enzymes. Synonyms: phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Enzyme Commission Number: EC 1.4.1.20. CAS No. 69403-12-9. PHD. Activity: > 6 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Sporosarcina sp. phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Cat No: NATE-0558. | |
| Native Staph aureus V8 Protease (Endoproteinase Glu-C) | Protease S. aureus V8 (Endoproteinase-Glu-C) specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acids. In the presence of ammonium, the enzyme specificity is limited to glutamic sites. It has a molecular weight of 27 kDa daltons and optimum pH's of 4.0 and 7.8 with hemoglobin as the substrate. Protease S. aureus V8 is inhibited by diisopropylfluorophosphate and monovalent anions such as F-, Cl-, CH3COO-and NO3. Enzyme activity is determined by the casein digestion assay described by Drapeau. Protease s. aureus v8 (endoproteinase-glu-c) specifically cleaves peptide bonds on the cooh-terminal side of either aspartic or glutamic acids. Group: Enzymes. Synonyms: EC 3.4.21.19; Staph aureus V8 Protease; Prot. Enzyme Commission Number: EC 3.4.21.19. CAS No. 137010-42-5. Purity: Chromatographically purified. V8 Protease. Mole weight: 27 kDa (Drapeau 1978). Activity: > 500 units per mg dry weight. Stability: Autolysis occurs at temperatures > 40°C. The enzyme is fully active in USP 0.2% SDS. Stable for 12 months at 2-8°C. Storage: Store at 2-8°C. Form: Lyophilized powder. Source: Staph aureus V8. EC 3.4.21.19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase. Cat No: NATE-0730. | |
| Native Staphylococcus aureus α-Hemolysin | α-Hemolysin is a 33 kDa extracellular protein secreted by most strains of pathogenic Staphylococcus aureus. It is selectively hemolytic and has a marked preference for rabbit red blood cells. It induces dermonecrosis, spastic muscle paralysis, and it is lethal for laboratory animals. The toxin must be in the monomeric form to initially bind to a membrane and specific receptors are not required for binding. Upon binding to biological membranes and/or artificial membranes, self-oligomerization occurs, resulting in ring structures (hexameric aggregates) believed to represent transmembrane pores, which are permeable to ions and small metabolites. Group: Enzymes. Synonyms: α-Hemolysin; 94716-94-6; α-Toxin. α-Hemolysin. Activity: > 10,000 units/mg protein. Storage: 2-8°C. Source: Staphylococcus aureus. α-Hemolysin; 94716-94-6; α-Toxin. Cat No: NATE-0753. | |
| Native Staphylococcus aureus Nuclease micrococcal | Micrococcal Nuclease is an endo-exonuclease that preferentially digests single-stranded nucleic acids. The rate of cleavage is 30 times greater at the 5' side of A or T than at G or C and results in the production of mononucleotides and oligonucleotides with terminal 3'-phosphates. The enzyme is also active against double-stranded DNA and RNA and all sequences will be ultimately cleaved. Applications: Nuclease from staphyl oc occus aureus has been used in a study to assess coagulase and heat-resistant strains found in animals. it has also been used in a study to investigate the expression characteristic of two genes in s. aureus that encode two thermostable nucleases. Group: Enzymes. Synonyms: Micrococcal Nuclease; EC 3.1.31.1; spleen endonuclease; thermonuclease; nuclease T; micrococcal endonuclease; nuclease T'; staphylococcal nucle. Enzyme Commission Number: EC 3.1.31.1. CAS No. 9013-53-0. MNase. Activity: 100-300 units/mg protein. Storage: -20°C. Source: Staphylococcus aureus. Micrococcal Nuclease; EC 3.1.31.1; spleen endonuclease; thermonuclease; nuclease T; micrococcal endonuclease; nuclease T'; staphylococcal nuclease; spleen phosphodiesterase; Staphylococcus aureus nuclease; Staphylococcus aureus nuclease B; ribonucleate (deoxynucleate) 3'-nucleotidohydrolase; 9013-53-0; Endonuclease micrococcal; MNase. Cat No: NATE-0452. | |
| Native Staphylococcus aureus Sphingomyelinase | Sphingomyelin phosphodiesterase is a hydrolase enzyme that is involved in sphingolipid metabolism reactions. SMase is a member of the DNase I superfamily of enzymes and is responsible for breaking sphingomyelin (SM) down into phosphocholine and ceramide. The activation of SMase has been suggested as a major route for the production of ceramide in response to cellular stresses. Group: Enzymes. Synonyms: Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; SMase. Enzyme Commission Number: EC 3.1.4.12. CAS No. 9031-54-3. SMase. Activity: 100-300 units/mg protein (Lowry). Storage: 2-8°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 0.25 M phosphate buffer, pH 7.5. Source: Staphylococcus aureus. Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; SMase. Cat No: NATE-0673. | |
| Native Staphylococcus aureus Staphopain A | Staphopains A and B are part of the staphylococcal proteolytic cascade (SPC) and may contribute to tissue invasion and metastatic infections of Staphylococcus aureus. Staphopain A, along with Staphopain B, may contribute to septic shock through the release of bradykinin and S-kinin from human kininogens. This activity required proteolytically-active Staphopain A and was augmented by Staphopain B. Staphopain a is inhibited by staphostatin a, e-64, and heavy metal ions such as hg2+ and ag+. staphopain a is also inhibited by plasma α2-macroglobulin but not by human cystatin c. staphopain a and staphopain b, members of the peptidase c47 family, are the major cysteine proteases secreted by s. aureus. Applications: Staphopain a was used for cleaving the n terminus of atypical chemokine receptor (ackr2) to suppress its ligand internalization activity in a study on the pivotal role of ackr2 in ligand binding, internalization and scavenging of inflammatory responses. Group: Enzymes. Synonyms: Staphopain; EC 3.4.2. Enzyme Commission Number: EC 3.4.22.48. CAS No. 347841-89-8. Staphopain. Mole weight: mol wt ~20 kDa by SDS-PAGE. Storage: -20°C. Form: lyophilized powder. Source: Staphylococcus aureus. Staphopain; EC 3.4.22.48; staphylopain; 347841-89-8; ScpA; Staphopain A; Staphylococcal cysteine proteinase A; Staphylopain A. Cat No: NATE-0666. | |
| Native Staphylococcus aureus Staphopain B | Staphopains A and B are part of the staphylococcal proteolytic cascade (SPC) and may contribute to tissue invasion and metastatic infections of Staphylococcus aureus. Staphopain A, along with Staphopain B, may contribute to septic shock through the release of bradykinin and S-kinin from human kininogens. This activity required proteolytically-active Staphopain A and was augmented by Staphopain B. Staphopain activity is inhbited by staphostatin b (sspc) and e-64. staphopain activity is stimulated by edta. staphopain a and staphopain b, members of the peptidase c47 family, are the major cysteine proteases secreted by s. aureus. Group: Enzymes. Synonyms: Staphopain; EC 3.4.22.48; staphylopain; 347841-89-8; Staphopain B; Staphylococcal cysteine proteinase B; Staphylopain B; sspB. Enzyme Commission Number: EC 3.4.22.48. CAS No. 347841-89-8. Purity: > 95% (SDS-PAGE). Staphopain. Mole weight: mol wt ~20 kDa by SDS-PAGE. Storage: -20°C. Source: Staphylococcus aureus. Staphopain; EC 3.4.22.48; staphylopain; 347841-89-8; Staphopain B; Staphylococcal cysteine proteinase B; Staphylopain B; sspB. Cat No: NATE-0683. | |
| Native Staphylococcus epidermidis D-Lactic Dehydrogenase | D-lactic dehydrogenase catalyzes the conversion of D-lactate into D-pyruvate while reducing NAD+ to NADH and H+. Applications: D-lactic dehydrogenase can be used to generate inhibitors of angiotensin converting enzyme by catalyzing the production of the intermediate (r)-2-hydroxy-4-phenylbutyric acid. d-lactic dehydrogenase has been used in a study to assess mechanisms of active transport in isolated membrane vesicles. it has also been used in a study to investigate β-galactoside transport in bacterial membrane preparations. 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: > 80 units/mg solid. Storage: -20°C. Form: Lyophilized powder containing primarily dextran. Source: Staphylococcus epidermidis. 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-0197. | |
| Native Staphylococcus staphylolyticus Lysostaphin | Lysostaphin is a Staphylococcus simulans metalloendopeptidase. It can function as an antimicrobial against Staphylococcus aureus. Lysostaphin is a 27 KDa glycylglycine endopeptidase, an antibacterial enzyme which is capable of cleaving the crosslinking pentaglycin bridges in the cell wall of Staphylococci. Group: Enzymes. Synonyms: Lysostaphin; EC 3.4.24.75; glycyl-glycine endopeptidase; 9011-93-2. Enzyme Commission Number: EC 3.4.24.75. CAS No. 9011-93-2. Lysostaphin. Activity: Type I, > 2,000 units/mg protein; Type II, > 500 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Staphylococcus staphylolyticus. Lysostaphin; EC 3.4.24.75; glycyl-glycine endopeptidase; 9011-93-2. Cat No: NATE-0429. | |
| Native Streptococcus faecalis L-Phenylalanine decarboxylase | In enzymology, a phenylalanine decarboxylase (EC 4.1.1.53) is an enzyme that catalyzes the chemical reaction:L-phenylalanine<-> phenylethylamine + CO2. Hence, this enzyme has one substrate, L-phenylalanine, and two products, phenylethylamine and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. This enzyme participates in phenylalanine metabolism. It employs one cofactor, pyridoxal phosphate. Group: Enzymes. Synonyms: phenylalanine decarboxylase; L-phenylalanine decarboxylase; aromatic L-amino acid decarboxylase; L-phenylalanine carboxy-lyase; EC 4.1.1.53; 9075-72-3. Enzyme Commission Number: EC 4.1.1.53. CAS No. 9075-72-3. L-Phenylalanine decarboxylase. Activity: > 5 units/g solid. Storage: -20°C. Form: Dried cells from which activity can be extracted. Source: Streptococcus faecalis. phenylalanine decarboxylase; L-phenylalanine decarboxylase; aromatic L-amino acid decarboxylase; L-phenylalanine carboxy-lyase; EC 4.1.1.53; 9075-72-3. Cat No: NATE-0415. | |
| Native Streptococcus faecalis L-Tyrosine Decarboxylase | In enzymology, a tyrosine decarboxylase (EC 4.1.1.25) is an enzyme that catalyzes the chemical reaction:L-tyrosine<-> tyramine + CO2. Hence, this enzyme has one substrate, L-tyrosine, and two products, tyramine and carbon dioxide. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. This enzyme participates in tyrosine metabolism and alkaloid biosynthesis. It employs one cofactor, pyridoxal phosphate. Applications: L-tyrosine decarboxylase from strept oc occus faecalis has been used in a study to isolate and identify the carbonyl-active site of diamine oxidase by gas chromatographic mass spectrometry. l-tyrosine decarboxylase from strept oc occus faecalis has also been used in a study to investigate the adsorption of strept oc occus faecalis on diatomite carriers for use in biotransformations. Group: Enzymes. Synonyms: tyrosine decarboxylase; EC 4.1.1.25; L-tyrosine decarboxylase; L-(-)-tyrosine apodecarboxylase; L-tyrosine carboxy-lyase; 9002-09-9. Enzyme Commission Number: EC 4.1.1.25. CAS No. 9002-9-9. L-Tyrosine Decarboxylase. Activity: > 0.1 unit/mg solid. Storage: -20°C. Source: Streptococcus faecalis. tyrosine decarboxylase; EC 4.1.1.25; L-tyrosine decarboxylase; L-(-)-tyrosine apodecarboxylase; L-tyrosine carboxy-lyase; 9002-09-9. Cat No: NATE-0421. | |
| Native Streptococcus faecalis L-Tyrosine Decarboxylase Apoenzyme | In enzymology, a tyrosine decarboxylase (EC 4.1.1.25) is an enzyme that catalyzes the chemical reaction:L-tyrosine<-> tyramine + CO2. Hence, this enzyme has one substrate, L-tyrosine, and two products, tyramine and carbon dioxide. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. This enzyme participates in tyrosine metabolism and alkaloid biosynthesis. It employs one cofactor, pyridoxal phosphate. Applications: L-tyrosine decarboxylase apoenzyme from strept oc occus faecalis has been used in a study to purify and characterize tyrosine decarboxylase and aromatic-l-amino-acid decarboxylase. l-tyrosine decarboxylase apoenzyme from strept oc occus faecalis has also been used in a study to investigate the stereospecificity of sodium borohydride reduction of tyrosine decarboxylase. Group: Enzymes. Synonyms: tyrosine decarboxylase; EC 4.1.1.25; L-tyrosine decarb. Enzyme Commission Number: EC 4.1.1.25. CAS No. 9002-9-9. L-Tyrosine Decarboxylase. Activity: <0.005 unit/mg solid (without pyridoxal 5-phosphate),> 0.05 unit/mg solid (with excess pyridoxal 5-phosphate). Storage: -20°C. Source: Streptococcus faecalis. tyrosine decarboxylase; EC 4.1.1.25; L-tyrosine decarboxylase; L-(-)-tyrosine apodecarboxylase; L-tyrosine carboxy-lyase; 9002-09-9. Cat No: NATE-0420. | |
| Native Streptococcus faecalis Ornithine Transcarbamylase | Ornithine transcarbamylase (OTC) is an enzyme that catalyzes the reaction between carbamoyl phosphate (CP) and ornithine (Orn) to form citrulline (Cit) and phosphate (Pi). In plants and microbes, OTC is involved in arginine (Arg) biosynthesis, whereas in mammals it is located in the mitochondria and is part of the urea cycle. Group: Enzymes. Synonyms: Ornithine transcarbamylase; EC 2.1.3.3; citrulline phosphorylase; ornithine transcarbamylase; OTC; OTCase; carbamylphosphate-ornithine transcarbamylase; L-ornithine carbamoyltransferase; L-ornithine carbamyltransferase; L-ornithine transcarbamylase; ornithine carbamyltransferase; 9001-69-8. Enzyme Commission Number: EC 2.1.3.3. CAS No. 9001-69-8. OTC. Activity: > 600 units/mg protein. Storage: -20°C. Form: Lyophilized powder contains Tris buffer salts. Source: Streptococcus faecalis. Ornithine transcarbamylase; EC 2.1.3.3; citrulline phosphorylase; ornithine transcarbamylase; OTC; OTCase; carbamylphosphate-ornithine transcarbamylase; L-ornithine carbamoyltransferase; L-ornithine carbamyltransferase; L-ornithine transcarbamylase; ornithine carbamyltransferase; 9001-69-8. Cat No: NATE-0499. | |
| Native Streptococcus hemolyticus Streptokinase | Streptokinase (SK) is an enzyme secreted by several species of streptococci that can bind and activate human plasminogen. SK is used as an effective and inexpensive thrombolysis medication in some cases of myocardial infarction (heart attack) and pulmonary embolism. Streptokinase belongs to a group of medications known as fibrinolytics, and complexes of streptokinase with human plasminogen can hydrolytically activate other unbound plasminogen by activating through bond cleavage to produce plasmin. Streptokinase from β-hemolytic streptococcus (lancefield group c). Applications: Streptokinase is commonly used as a thrombolytic agent in the therapy of ischemic stroke. this therapy carries the important risk of intracerebral hemorrhage. streptokinase is also used in the treatment of complicated parapneumonic effusions and empyema where adverse reactions, allergic type, are rare. Group: Enzymes. Synonyms: St. Enzyme Commission Number: EC 3.4.99.0. CAS No. 9002-1-1. SK. Activity: > 3,500 units/mg solid. Appearance: Appearance (Color): Conforms to Requirements Off-White to Light Yellow to Light Beige. Form: Lyophilized powder containing ~50% total protein by biuret and sodium glutamate. Total protein composed of enzyme protein and human serum albumin. Source: Streptococcus hemolyticus. Streptokinase; SK; EC 3.4.99.0. Cat No: PHAM-261. | |
| Native Streptococcus pneumoniae α (2?3) Neuraminidase | 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: neuraminidase; 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. Neuraminidase. Storage: 2-8°C. Form: buffered aqueous solution. Solution in 50 mM sodium phosphate, pH 7.5. Source: Streptococcus pneumoniae. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Cat No: NATE-0757. | |
| Native Streptococcus pneumoniae β(1-4)-Galactosidase | The enzyme releases non-reducing terminal β(1-4)-linked galactose from oligosaccharides and glycoproteins. This specificity is only evident at enzyme concentrations < 100mU/ml. At higher concentrations, hydrolysis of β(1-3)-linked galactose occurs. Applications: Due to its high selectivity the enzyme is an extremely useful reagent for the identification of non-reducing terminal β(1-4)-linked galactose residues. as such the enzyme has been extensively used for detailed structural analysis in conjunction with broader specificity bovine testes β-galactosidase or jack bean β-galactosidase. Group: Enzymes. Synonyms: β-galactosidase; beta-gal; β-gal; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. β-gal. Mole weight: 220-247 kD. Form: 20 mM Tris-HCl, 25 mM NaCl (pH 7.5). Source: Streptococcus pneumoniae. β(1-4)-Galactosidase; β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. Cat No: NATE-0974. | |
| Native Streptococcus pyogenes Streptolysin O | Streptolysin O possesses a single polypeptide chain with a molecular weight of f62 kDa. Streptolysin O binds to membrane cholesterol and oligomerizes to create a ring structure that consists of 45 to 50 units. The ring structure inserts into the membrane to make a large pore (25 to 30 nm), which DNA, RNA, peptides and proteins may pass. It is thiol-activated. It is inhibited by allicin, an active component of garlic. Applications: Permeabilizes membranes to permit cellular uptake of large or charged molecules. streptolysin o is a toxin secreted by streptococcus pyogenes and is a prototype member of poreforming bacterial cytolysins. it is used permeabilize cell membranes to permit cellular uptake of large or charged molecules. it is used to study macromolecule delivery. it is a potential anticancer agent and is used to study suicide cancer gene therapy. Group: Enzymes. Synonyms: Streptolysin O; 98072-47-0; SLO. CAS No. 98072-47-0. SLO. Mole weight: 69 kDa. Storage: 2-8°C. Form: lyophilized powder. Source: Streptococcus pyogenes. Streptolysin O; 98072-47-0; SLO. Cat No: NATE-0671. | |
| Native Streptococcus thermophilus Glycerol 3-phosphate 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: Gpo has been used for sensitive metabolite assays of starch and lipid synthesis, pyrophosphate, atp, adp, and most glycolytic i...3-phosphate Oxidase; 9046-28-0; sn-Glycerol 3-phosphate:oxygen 2-oxidoreductase; L-Glycerol 3-phosphate Oxidase; GPO. Enzyme Commission Number: EC 1.1.3.21. CAS No. 9046-28-0. Glycerol-3-phosphate oxidase. Activity: > 35 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Streptococcus thermophilus. EC 1.1.3.21; glycerol phosphate oxidase; glycerol-1-phosphate oxidase; glycerol phosphate oxidase; L-α-glycerophosphate oxidase; α-glycerophosphate oxidase; L-α-glycerol-3-phosphate oxidase; Glycerol 3-phosphate Oxidase; 9046-28-0; sn-Glycerol 3-phosphate:oxygen 2-oxidoreductase; L-Glycerol 3-phosphate Oxidase; GPO. Cat No: NATE-0316. | |
| Native Streptolysin O from Escherichia coli | Streptolysin O possesses a single polypeptide chain with a molecular weight of f62 kDa. Streptolysin O binds to membrane cholesterol and oligomerizes to create a ring structure that consists of 45 to 50 units. The ring structure inserts into the membrane to make a large pore (25 to 30 nm), which DNA, RNA, peptides and proteins may pass. It is thiol-activated. It is inhibited by allicin, an active component of garlic. Streptolysin-o is one of several toxic immunogenic exoenzymes produced by most strains of group a and many strains of groups c and g, β-hemolytic streptococci. the o in the name stands for oxygenlabile; the other related toxin being oxygen-stable streptolysin-s. the main function of streptolysin o is to cause hemolysis (the breaking open of red blood cells) in particular, beta-hemolysis. Applications: Used in the formulation of anti-streptolysin o (aso) assays which are used in the diagnosis of group a streptococcal based illnesses. Group: Enzymes. Synonyms: Streptolysin O; 98072-47-0; SLO. Enzyme Commission Number: EC.3.2.2.5. CAS No. 9032-65-9. Purity: > 90%. SLO. Appearance: Clear to slightly cloudy solution. Source: Escherichia coli. Streptolysin O; 98072-47-0; SLO. Cat No: NATE-1161. | |
| Native Streptomyces canus Glycerokinase | 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. Group: Enzymes. Synonyms: EC 2.7.1.30; glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase; 9030-66-4. Enzyme Commission Number: EC 2.7.1.30. CAS No. 9030-66-4. GK. Activity: 10-30 units/mg protein (biuret). Storage: -20°C. Form: lyophilized powder. Source: Streptomyces canus. EC 2.7.1.30; glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase; 9030-66-4. Cat No: NATE-0289. | |
| Native Streptomyces chromofuscus Phospholipase D | Phospholipase D is a phospholipid hydrolyzing enzyme and an important component of receptor-mediated signal transduction responses and regulated secretion. Hydrolyzes the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid. Phospholipase D is involved in conferring drought susceptibility in peanuts, which increases the risk of aflatoxin contamination. Group: Enzymes. Synonyms: Phospholipase D; EC 3.1.4.4; lipophosphodiesterase II; lecithinase D; choline phosphatase; PLD; 9001-87-0. Enzyme Commission Number: EC 3.1.4.4. CAS No. 9001-87-0. PLD. Mole weight: mol wt ~60 kDa. Activity: Type I, > 50,000 units/mL; Type II, > 150 units/mg solid. Storage: -20°C. Form: Type I, buffered aqueous glycerol solution; Solution in 100 mM Tris/HCl, pH 8.0, 10% glycerol (v/v), and 0.1% Triton X-100 (w/v); Type II, lyophilized powder. Source: Streptomyces chromofuscus. Phospholipase D; EC 3.1.4.4; lipophosphodiesterase II; lecithinase D; choline phosphatase; PLD; 9001-87-0. Cat No: NATE-0596. | |
| Native Streptomyces fulvissimus TU-6 Labiase | Labiase from Streptomyces fulvissimus is an enzyme preparation useful for the lysis of many Gram-positive bacteria such as Lactobacillus, Aerococcus and, Streptococcus. Labiase contains β-N-acetyl-D-glucosaminidase and lysozyme activity. Applications: Labiase from streptomyces fulvissimus is an enzyme preparation useful for the lysis of many gram-positive bacteria such as lactobacillus, aerococcus and, streptococcus. labiase contains β-n-acetyl-d-glucosaminidase and lysozyme activity. ph optimum for activity: ph ~4 ph optimum for stability: ph 4-8. Group: Enzymes. Synonyms: Labiase. Labiase. Activity: > 10.0 units/g solid. Storage: 2-8°C. Source: Streptomyces fulvissimus TU-6. Labiase. Cat No: NATE-0369. | |
| Native Streptomyces globisporus ATCC 21553 Mutanolysin | Mutanolysin is an N-acetylmuramidase. Like lysozyme, it is a muralytic enzyme that cleaves the β-N-acetylmuramyl-(1?4)-N-acetylglucosamine linkage of the bacterial cell wall polymer peptidoglycan-polysaccharide. Its carboxy terminal moieties are involved in the recognition and binding of unique cell wall polymers. Mutanolysin lyses Listeria and other Gram-positive bacteria such as Lactobacillus and Lactococcus. Mutanolysin from streptomyces globisporus consists of two main lytic enzymes and may be a useful agent for dental caries control. Applications: Mutanolysin has been used in a study to assess lysing and generating protoplasts of dairy streptococci. it ha...es gentle cell lysis for the isolation of easily degradable biomolecules and rna from bacteria. it has been used in the formation of spheroplasts for isolation of dna. provides gentle cell lysis for the isolation of easily degradable biomolecules and rna from bacteria. it has been used in the formation of spheroplasts for isolation of dna. Group: Enzymes. Synonyms: Mutanolysin; 55466-22-3. CAS No. 55466-22-3. Mutanolysin. Mole weight: 23 kDa. Activity: > 4000 units/mg protein (biuret). Storage: -20°C. Form: lyophilized powder containing Ficoll and sodium succinate buffer salts. Source: Streptomyces globisporus ATCC 21553. Mutanolysin; 55466-22-3. Cat No: NATE-0464. | |
| Native Streptomyces griseus Aminopeptidase I | Aminopeptidase I from S. griseus has a fairly broad specificity, being able to remove the N-terminal residue of most proteins, except where the penultimate residue is an imino acid. It contains two Zn2+ binding sites. Aminopeptidase I from S. griseus is inhibited by 1,10-phenanthroline and is activated six-fold by Ca2+, which also stabilizes it against heat inactivation. This monomeric zinc metalloprotein has an isoelectric point (pI) of 5.4. Applications: Aminopeptidase i from streptomyces griseus may be used as a reagent for the analysis of protein structure and as a model for studies of proteolytic enzyme activation by calcium ions. it may be used as a reagent in the assay of endoprotease activities with a synthetic substrate in a two-stage assay. the lyophilized powder also contains calcium acetate. Group: Enzymes. Synonyms: aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I; EC 3.4.11.22; 9031-94-1; Aminopeptidase I. Enzyme Commission Number: EC 3.4.11.22. CAS No. 9031-94-1. Aminopeptidase I. Activity: > 200 units/mg protein. Storage: -20°C. Form: lyophilized powder. Contains calcium acetate. Source: Streptomyces griseus. aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I; EC 3.4.11.22; 9031-94-1; Aminopeptidase I. Cat No: NATE-0070. | |
| Native Streptomyces griseus Chitinase | Chitinase is an extracellular enzyme complex that degrades chitin and has a molecular mass of approximately 30 kDa. Chitin is degraded to N-acetyl-D-glucosamine in 2 enzymatic reactions. Firstly, chitobiose units are removed from chitin by chitodextrinase-chitinase. The second reaction involves N-acetyl-glucosaminidase-chitobiase, which cleaves the disaccharide to its monomer subunits (that comprise of N-acetyl-D-glucosamine). Applications: Chitinase from streptomyces griseus has been used to study the effect of the allosamidin on the regulatory system for chitinase production. it has also been used to study the enrichment of chitinolytic microorganisms. this enrichment wa...;-glucosaminidase; β-1,4-poly-N-acetyl glucosamidinase; poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase; (1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase; EC 3.2.1.14. Enzyme Commission Number: EC 3.2.1.14. CAS No. 9001-6-3. Chitinase. Activity: > 200 units/g solid. Storage: -20°C. Form: lyophilized powder (essentially salt free). Source: Streptomyces griseus. Chitinase; chitodextrinase; 1,4-β-poly-N-acetylglucosaminidase; poly-β-glucosaminidase; β-1,4-poly-N-acetyl glucosamidinase; poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase; (1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase; EC 3.2.1.14. Cat No: NATE-0123. | |
| Native Streptomyces griseus Chitosanase | Chitosanase catalyzes the endohydrolysis of β (1,4) linkages between N-acetyl-D-glucosamine and D-glucosamine residues in partially deacetylated chitosan. Chitosanase from Streptomyces griseus is capable of hydrolyzing both chitosan and carboxymethyl cellulose. It is used for the lysis of cell walls of fungi belonging to the group Mucorales. It is found in several types of microorganisms. Applications: Chitosanase from streptomyces griseus has been used in a study to assess the effect of chitin sources on production of chitinase and chitosanase. chitosanase from streptomyces griseus has also been used in a study to investigate the effective production of chitinase an...cete aphanomyces euteiches, a major parasite of legume plants. it has also been used for the enzymatic hydrolysis of the fully de-n-acetylated chitosan to get chitosan oligomer mixtures during the preparation of biocompatible chitosan-alginate gel. Group: Enzymes. Synonyms: Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase. Enzyme Commission Number: EC 3.2.1.132. CAS No. 51570-20-8. Chitosanase. Activity: >50 units/mg protein (Bradford). Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Streptomyces griseus. Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase. Cat No: NATE-0125. | |
| Native Streptomyces griseus Pronase | Pronase is a mixture of several nonspecific endo- and exoproteases that digest proteins down to single amino acids. Applications: Use pronase to completely hydrolyze proteins in research applications. pronase is used for the degradation of proteins during the isolation of dna and rna, such as in the extraction of phage dna or the isolation of plasmid dna. it is not necessary to let pronase self-digest prior to use. it is also used in histochemistry and cell culture for tissue dissociation in conjunction with collagenase and trypsin, and for the production of glycopeptides from purified glycoproteins. Group: Enzymes. Synonyms: non-specific protease. Enzyme Commission Number: EC 3.4.24.4. CAS No. 70851-98-8. Pronase. Activity: ~7.0 units/mg protein (at 40°C with casein as the substrate, pH 7.5, equivalent to approximately 1270 PU/mg or approximately 25 PUK/mg.). Storage: 2-8°C. Form: Lyophilized powder. Source: Streptomyces griseus. non-specific protease; Pronase; EC 3.4.24.4. Cat No: NATE-0997. | |
| Native Streptomyces griseus Protease | Protease from Streptomyces griseus is a mixture of at least three proteolytic activities including an extracellular serine protease. In general, serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid. Collected from culture broth of s. griseus and purified by successive column procedures. a mixture of at least three proteolytic activities including an extracellular serine protease. in general, serine proteases display a wide range of substrate specifici...de aldehydes and serine proteases. protease is typically used in nucleic acid isolation procedures in incubations of 0.5-3.0 hours supplemented with 0.2% sodium dodecyl sulfate and 10 mm edta. the enzyme from creative enzymes has been used for the digestion and analysis of antithrombin-heparin complexes. it has also been used for the isolation of enzyme-resistant starch. this enzyme is more active at a higher ph range than the known alkaline protease, showing the proteolytic activity even in 0.2n naoh solution. this enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein. Group: Enzymes. Synonyms: Protease; 9036-06-0; Actinase E, Pro | |
| Native Streptomyces hyalurolyticus Hyaluronidase | Hyaluronidase degrades hyaluronan and has been found to be inappropriately regulated during cancer progression. These enzymes randomly cleave β-N-acetylhexosamine-[1?4] glycosidic bonds in hyaluronic acid, chondroitin, and chondroitin sulfates. Group: Enzymes. Synonyms: hyaluronoglucosaminidase; hyaluronidase; hyaluronoglucosidase; chondroitinase; chondroitinase I; hyaluronate 4-glycanohydrolase; EC 3.2.1.35; 37326-33-3. Enzyme Commission Number: EC 3.2.1.35. CAS No. 37326-33-3. Hyaluronidase. Activity: Type I, > 1,500 units/mg solid; Type II, > 300 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Streptomyces hyalurolyticus. hyaluronoglucosaminidase; hyaluronidase; hyaluronoglucosidase; chondroitinase; chondroitinase I; hyaluronate 4-glycanohydrolase; EC 3.2.1.35; 37326-33-3. Pack: ampule of 300 × units. Cat No: NATE-0349. | |
| Native Streptomyces sp. Alkalophilic proteinase | Native Streptomyces sp. Alkalophilic proteinase. Applications: This enzyme is more active at a higher ph range than the known alkaline protease, showing the proteolytic activity even in 0.2n naoh solution. this enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein. Group: Enzymes. Synonyms: Alkalophilic proteinase; EC 3.4.21.-. Enzyme Commission Number: EC 3.4.21.-. Alkalophilic proteinase. Mole weight: approx. 50 kDa. Activity: Grade ? 20U/mg-solid or more. Stability: Stable at-20?C for at least one year. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Streptomyces sp. Alkalophilic proteinase; EC 3.4.21.-. Cat No: DIA-183. | |
| Native Streptomyces sp. 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. Applications: Cholesterol oxidase from streptomyces has been used in a study to assess the relationship between the micellar structure of model bile and the activity of esterase. cholesterol oxidase from streptomyces has also been used in a study to investigate the effects of sphingomyelin degradation on cell cholesterol oxidizability and steady-state distribution between the cell ...ton boll weevil. chod has also been used as a molecular probe to elucidate cellular membrane structures. Group: Enzymes. Synonyms: EC 1.1.3.6, 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. Mole weight: mol wt ~34 kDa. Activity: > 20 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing bovine serum albumin and sugars as stabilizers. Source: Streptomyces sp. EC 1.1.3.6, cholesterol-O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase; 9028-76-6. Cat No: NATE-0128. | |
| Native Streptomyces sp. Phospholipase D | Phospholipase D (PLD) is glycerophospholipid-specific. It is markedly less active on sphingomyelins and lysophospholipids. Phospholipase D hydrolyzes the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid. Applications: Phospholipase d (pld) has been used to hydrolyze the phosphate bonds of phospholipids and sphingomyelin to yield the corresponding phosphatidic acid. it has also been used to study metabolic labeling and direct imaging of choline phospholipids in vivo by measuring propargyl-cho incorporation. furthermore, pld has been used in purification and kinetic studies. the enzyme has been used in the translocation of sphingosine kinase 1 (sk1) to membrane fractions under in vitro conditions. it has also been used to produce phosphatidic acid (pa) from phosphatidylcholine (pc) in hl60 permeabilized cells. Group: Enzymes. Synonyms: phospholipase D; lipophosphodiesterase II; lecithinase D;. Enzyme Commission Number: EC 3.1.4.4. CAS No. 9001-87-0. PLD. Activity: > 150 units/mg solid. Storage: -20°C. Form: Type VII, lyophilized powder. Source: Streptomyces sp. phospholipase D; lipophosphodiesterase II; lecithinase D; choline phosphatase; phosphatidylcholine phosphatidohydrolase; EC 3.1.4.4; 9001-87-0; PLD. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0597. | |
| Native Streptomyces violaceoruber 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. Applications: Phospholipase a 2 is an enzyme used to hydrolyze phospholipids. it is used to study the release of arachidonic acid from various cell types such as neutrophils, gastric mucosal cells and kidney cells. 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: > 10 units/mg solid. Storage: -20°C. Form: Lyophilized powder containing mannitol and Tris buffer. Source: Streptomyces violaceoruber. Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Cat No: NATE-0588. | |
| Native Sweet almond β-Glucosidase | Beta-glucosidase is a glucosidase enzyme that acts upon β1->4 bonds linking two glucose or glucose-substituted molecules (i.e., the disaccharide cellobiose). It is one of the cellulases, enzymes involved in the decomposition of cellulose and related polysaccharides; more specifically, an exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of glucose. Applications: This enzyme is useful for structural investigations of carbohydrates and for the enzymatic determination of α-amylase when coupled with α-glucosidase in clinical analysis. Group: Enzymes. Synonyms: EC 3.2.1.21; gentiobiase; cellobiase; emulsin; elaterase; aryl-beta-glucosidase; beta-D-glucosidase; beta-glucoside gl. Enzyme Commission Number: EC 3.2.1.21. CAS No. 9001-22-3. Mole weight: approx. 110 kDa. Activity: 10U/mg-solid or more (containing approx. 50% of BSA). Appearance: Light yellow amorphous powder, lyophilized. Form: Freeze dried powder. Source: Sweet almond. EC 3.2.1.21; gentiobiase; cellobiase; emulsin; elaterase; aryl-beta-glucosidase; beta-D-glucosidase; beta-glucoside glucohydrolase; arbutinase; amygdalinase; p-nitrophenyl beta-glucosidase; primeverosidase; amygdalase; linamarase; salicilinase; beta-1,6-glucosidase. Cat No: DIA-195. | |
| Native Sweet almonds β-Glucosidase | β-glucosidase is a glucosidase enzyme located in on the brush border of the small intestine that acts upon β1->4 bonds linking two glucose or glucose-substituted molecules (i.e., the disaccharide cellobiose). It is one of the cellulases, enzymes involved in the decomposition of cellulose and related polysaccharides; more specifically, an exocellulase with specificity for a variety of beta-D-glycoside substRates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of glucose. Beta-glucosidase isolated from sweet almonds is used in the determination of alpha-amylase and in carbohydrate structure research. creative enzyme...9001-22-3. β-Glucosidase. Activity: > 1000 U/mg. Storage: Store desiccated at-15°C or below. Allow to come to room temperature before opening. Before returning to storage, redesiccate under vacuum over silica gel for a minimum of four hours. Re-seal before returning to-15°C or below. Form: A freeze-dried material. Source: Sweet almonds. β-glucosidase; glycoside hydrolase; β-D-glucoside glucohydrolase; EC 3.2.1.6; gentiobiase; cellobiase; emulsin; elaterase; aryl-β-glucosidase; β-D-glucosidase; arbutinase; amygdalinase; p-nitrophenyl β-glucosidase; primeverosidase; amygdalase; linamarase; salicilinase; β-1,6-glucosidase. Cat No: NATE-0770. | |
| Native Sweet potato β-Amylase | β-Amylase hydrolyzes the α-(1,4) glucan linkages in polysaccharides of three or more α-(1,4) linked D-glucose units. Natural substrates such as starch and glycogen are broken down into glucose and maltose. Pure, crystalline β-amylase preparation consists of four isoenzymes with different isoelectric points. The enzyme polymerizes very rapidly through the sulfhydryl groups in the absence of reducing agents. p-Chloromercuribenzoate inhibits the polymerization and the enzymatic activity. The reducing agents mercaptoethanol or dithiothreitol can completely restore the activity. Applications: Β-amylase is used to hydrolyze α bonds of α-linke...ng and removing staphylococcus aureus biofilms. the enzyme has also been used to prepare β-limit dextrin from waxy maize starch. Group: Enzymes. Synonyms: saccharogen amylase; glycogenase; β amylase, β-amylase; 1,4-α-D-glucan maltohydrolase; EC 3.2.1.2; 9000-91-3. Enzyme Commission Number: EC 3.2.1.2. CAS No. 9000-91-3. β-Amylase. Mole weight: 127.5. Activity: > 750 units/mg protein (E1%/280). Storage: 2-8°C. Form: ammonium sulfate suspension. Crystalline suspension in 2.3 M (NH4)2SO4. Source: Sweet potato. saccharogen amylase; glycogenase; β amylase, β-amylase; 1,4-α-D-glucan maltohydrolase; EC 3.2.1.2; 9000-91-3. Cat No: NATE-0762. | |
| Native Sweet Potato Non-Prostatic Acid Phosphatase | Acid phosphatase is a phosphatase, a type of enzyme, used to free attached phosphoryl groups from other molecules during digestion. It can be further classified as a phosphomonoesterase. Acid phosphatase is stored in lysosomes and functions when these fuse with endosomes, which are acidified while they function; therefore, it has an acid pH optimum. This enzyme is present in many animal and plant species. Different forms of acid phosphatase are found in different organs, and their serum levels are used to evaluate the success of the surgical treatment of prostate cancer. In the past, they were also used to diagnose this type of cancer. Group: Enzymes. Synonyms: Acid Phosphatase; acid phosphomonoesterase; phosphomonoesterase; glycerophosphatase; acid monophosphatase; acid phosphohydrolase; acid phosphomonoester hydrolase; uteroferrin; acid nucle. Enzyme Commission Number: EC 3.1.3.2. CAS No. 9001-77-8. Purity: Purified. Mole weight: 110 kDa. Activity: > 30 U/mg solid. Storage: 2-8°C. Form: Lyophilized. Source: Sweet Potato. Acid Phosphatase; acid phosphomonoesterase; phosphomonoesterase; glycerophosphatase; acid monophosphatase; acid phosphohydrolase; acid phosphomonoester hydrolase; uteroferrin; acid nucleoside diphosphate phosphatase; orthophosphoric-monoester phosphohydrolase (acid optimum); EC 3.1.3.2; ACP. Cat No: NATE-0025. | |
| Native Swine (Bovine) Ribonuclease | Pancreatic Ribonuclease (RNase I) catalyzes cleavage of the phosphodiester bond between the 5'-ribose of a nucleotide and the phosphate group attached to the 3'-ribose of an adjacent pyrimidine nucleotide forming a 2',3'-cyclic phosphate which may then be hydrolyzed to the corresponding 3'-nucleoside phosphate. Ribonuclease A has a molecular weight of 13,700 daltons. It operates in an optimum pH range of 7.0-7.5. The high purity Ribonuclease is purified by re-crystallization, and then by Ion Exchange Chromatography and ultra-filtration. Applications: As a laboratory analysis reagent, is scientific research institutions widely used. Group: Enzymes. Synonyms: RNase; RNase I; RNase A; pancreatic RNase; ribonuclease I; endo. Rnase. Mole weight: 13.7 kDa. Activity: No less than 50Kunitz units/mg, calculated on the dried basis. Appearance: White or pale yellow lyophilized powder. Storage: Sealed, Dark, at temperature 2-8 centigrade. Source: Bovine (Swine) Pancrease. Species: Swine (Bovine). RNase; RNase I; RNase A; pancreatic RNase; ribonuclease I; endoribonuclease I; ribonucleic phosphatase; alkaline ribonuclease; ribonuclease; gene S glycoproteins; Ceratitis capitata alkaline ribonuclease; SLSG glycoproteins; gene S locus-specific glycoproteins; S-genotype-assocd; glycoproteins; ribonucleate 3'-pyrimidino-oligonucleotidohydrolase. Cat No: PHAM-240. | |
| Native Swine (Bovine) Trypsin-Chymotrypsin 1: 1 | Trypsin-Chymotrypsin is the co-crystal of Chymotrypsin and Trypsin so it has the properties of both. The activity of hydrolyzing casein is as much as Chymotrypsin. But the activity of its Chemotrypsin to hydrolyze N-Benzoyl-L-tyrosine ethyl ester?BTEE?is three times higher than Chemotrypsin.The activity of hydrolyze ester bond similar to that of Trypsin. It is stable when dry and easy to be inactivated in solutions. The optimum pH is 7.0-8.0. The high purity Trypsin-Chymotrypsin is purified by re-crystallization, and then by Ion Exchange Chromatography and ultra-filtration. Applications: 1. as pharmaceutical raw materials for antibacterial, anti-inflammatory, clinical. 2. as analytical reagents used in scientific research institutions. Group: Enzymes. Synonyms: Trypsin-Chymotrypsin 1: 1. Trypsin-Chymotrypsin. Activity: Trypsin: 1000 ~1100 USP units/mg, powder; Chymotrypsin 1000 ~1100 USPunits/mg, powder. Appearance: White or almost white powder. Storage: Sealed, Dark, at temperature 2-8°C. Form: Powder. Source: Swine (Bovine) pancreas. Species: Swine (Bovine). Trypsin-Chymotrypsin 1: 1. Cat No: PHAM-378. | |
| Native Swine (Bovine) Trypsin-Chymotrypsin 1: 250 | Trypsin-Chymotrypsin is the co-crystal of Chymotrypsin and Trypsin so it has the properties of both. The activity of hydrolyzing casein is as much as Chymotrypsin. But the activity of its Chemotrypsin to hydrolyze N-Benzoyl-L-tyrosine ethyl ester?BTEE?is three times higher than Chemotrypsin.The activity of hydrolyze ester bond similar to that of Trypsin. It is stable when dry and easy to be inactivated in solutions. The optimum pH is 7.0-8.0. The high purity Trypsin-Chymotrypsin is purified by re-crystallization, and then by Ion Exchange Chromatography and ultra-filtration. Applications: 1. as a laboratory analysis reagent, is scientific research institutions widely used. 2. animal cell culture of tissue processing. Group: Enzymes. Synonyms: Trypsin-Chymotrypsin 1: 250. Trypsin-Chymotrypsin. Activity: Trypsin > 2400 USP units/mg, powder; Chymotrypsin < 75 USP units/mg, powder. Appearance: White or almost white powder. Storage: Sealed, Dark, at temperature 2-8°C. Form: Powder. Source: Swine (Bovine) pancreas. Species: Swine (Bovine). Trypsin-Chymotrypsin 1: 250. Cat No: PHAM-379. | |
| Native Swine (Bovine) Trypsin-Chymotrypsin 6: 1 | Trypsin-Chymotrypsin is the co-crystal of Chymotrypsin and Trypsin so it has the properties of both. The activity of hydrolyzing casein is as much as Chymotrypsin. But the activity of its Chemotrypsin to hydrolyze N-Benzoyl-L-tyrosine ethyl ester?BTEE?is three times higher than Chemotrypsin.The activity of hydrolyze ester bond similar to that of Trypsin. It is stable when dry and easy to be inactivated in solutions. The optimum pH is 7.0-8.0. The high purity Trypsin-Chymotrypsin is purified by re-crystallization, and then by Ion Exchange Chromatography and ultra-filtration. Applications: 1. in the clinical, the treatment of various inflammatory, inflammatory edema, hematoma, postoperative adhesion, ulcer, thrombus and so on and have a certain effect to chronic bronchitis asthma, gastritis, cervicitis, pelvic inflammatory disease, suppurative otitis media, prostatitis, thrombophlebitis and cerebral thrombosis. 2. application in modern industrial fields, such as senior leather depilation, softener. Group: Enzymes. Synonyms: . Trypsin-Chymotrypsin. Activity: Trypsin > 2400 USP units/mg, powder; Chymotrypsin > 400 USP units/mg, powder. Appearance: White or almost white powder. Storage: Sealed, Dark, at temperature 2-8°C. Form: Powder. Source: Swine (Bovine) pancreas. Species: Swine (Bovine). Trypsin-Chymotrypsin 6: 1. Cat No: PHAM-380. | |
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