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| Product | Description | |
|---|---|---|
| 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. | |
| Native Swine Duodenum Mucopolysaccharide | It is mostly white or slightly yellow amorphous powder without odor. It is slightly salty in taste and hygroscopic. Applications: In theclinical, the treatment of coronary atherosclerosis heart disease. as alaboratory analysis reagent, is scientific research institutions widely used. Group: Others. Synonyms: Duodenum Mucopolysaccharide; Mucopolysaccharide; Glycosaminoglycans; GAGs; MPS. Appearance: White or slightly yellow amorphous powder. Storage: Sealed, Dark, at dry place. Source: Swine Duodenum. Species: Swine. Duodenum Mucopolysaccharide; Mucopolysaccharide; Glycosaminoglycans; GAGs; MPS. Cat No: PHAM-210. | |
| Native T4-infected Escherichia coli Polynucleotide Kinase | Polynucleotide kinase catalyses a "forward reaction" transfer of the γ-phosphate of ATP to the 5' hydroxyl terminus of single-and double-stranded nucleic acids (DNA and RNA) and 3'-nucleoside monophosphates. In exchange reactions containing ADP, the enzyme will catalyze the exchange of 5'-terminal phosphate groups and ATP. The 3'-phosphatase activity enables the enzyme to remove 3'-phosphoryl groups from phosphorylpolynucleotides. Applications: Suitable for: o sequencing or nucleic acid tagging (dna and rna) by 5?-end labeling o 5? phosphorylation of oligonucleotides o removal of 3?-phosphate groups from phosphorylpolynucleotides. Group: Enzymes. Synonyms: polynucleotide 5'-hydroxyl-kinase; EC 2.7.1.78; 37211-65-7; ATP:5'-dephosphopolynu. Enzyme Commission Number: EC 2.7.1.78. CAS No. 37211-65-7. PNK. Mole weight: mol wt 33 kDa. Activity: 10 units/μL. Storage: -20°C. Form: buffered aqueous glycerol solution. Source: T4-infected Escherichia coli. polynucleotide 5'-hydroxyl-kinase; EC 2.7.1.78; 37211-65-7; ATP:5'-dephosphopolynucleotide 5'-phosphatase; PNK; polynucleotide 5'-hydroxyl kinase (phosphorylating); 5'-hydroxyl polynucleotide kinase; 5'-hydroxyl polyribonucleotide kinase; 5'-hydroxyl RNA kinase; DNA 5'-hydroxyl kinase; DNA kinase; polynucleotide kinase; polynucleotide 5'-hydroxy-kinase. Cat No: NATE-0605. | |
| Native Thermoactinomyces intermedius 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. 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. Mole weight: ca. 380,000; Subunit molecular weight : ca. 40,000. Appearance: Ammonium sulphate suspension. Storage: Stable at 0 to 4 °C for at least six months (Do not freeze). Source: Thermoactinomyces intermedius. phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Cat No: NATE-1906. | |
| Native Thermoanaerobium brockii Alcohol Dehydrogenase, NADP+ dependent | Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an enzyme that in humans is encoded by the AKR1A1 gene. This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. This member, also known as aldehyde reductase, is involved in the reduction of biogenic and xenobiotic aldehydes and is present in virtually every tissue. Alternative splicing of this gene results in two transcript variants encoding the same protein. Applications: Alcohol dehydrogenase may be used to synthesize enantiomerically pure stereoisomers of chiral alcohols. it may...ase; AKR1A1; ALDR1; ALR; ARM; DD3; HEL-S-6; aldehyde reductase; aldo-keto reductase family 1 member A1; alcohol dehydrogenase (NADP+); aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.2. CAS No. 9028-12-0. ALR. Activity: 5-15 units/mg protein; 30-90 units/mg protein. Stability: -20°C. Form: lyophilized powder. Source: Thermoanaerobium brockii. EC 1.1.1.2; Aro | |
| Native Thermoanaerobium sp. Aromatic Alcohol Dehydrogenase, NADP+ dependent | Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an enzyme that in humans is encoded by the AKR1A1 gene. This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. This member, also known as aldehyde reductase, is involved in the reduction of biogenic and xenobiotic aldehydes and is present in virtually every tissue. Alternative splicing of this gene results in two transcript variants encoding the same protein. Group: Enzymes. Synonyms: EC 1.1.1.2; Aromatic Alcohol Dehydrogenase; Alcohol. Enzyme Commission Number: EC 1.1.1.2. CAS No. 9028-12-0. ALR. Activity: 1-5 units/mg solid. Stability: -20°C. Form: lyophilized powder. Source: Thermoanaerobium sp. EC 1.1.1.2; Aromatic Alcohol Dehydrogenase; Alcohol:NADP+ oxidoreductase; AKR1A1; ALDR1; ALR; ARM; DD3; HEL-S-6; aldehyde reductase; aldo-keto reductase family 1 member A1; alcohol dehydrogenase (NADP+); aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Cat No: NATE-0063. | |
| Native Thermococcus thioreducens Inorganic Pyrophosphatase | Pyrophosphatase (or inorganic pyrophosphatase) is an enzyme (EC 3.6.1.1) that catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. This is a highly exergonic reaction, and therefore can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The functionality of this enzyme plays a critical role in lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, and DNA synthesis,as well as other biochemical transformations. Group: Enzymes. Synonyms: Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. CAS No. 9024-82-2. Purity: ~ 90% (SDS PAGE). Inorganic pyrophosphatase. Mole weight: 20.9 kDa. Storage: at -20°C. Form: Lyophilized powder. Source: Thermococcus thioreducens. Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-1255. | |
| Native Thermococcus thioreducens Pyroglutamate Aminopeptidase | Pyroglutamate aminopetidase is an enzyme that digests proteins. This enzyme is specific for N-terminal pyroglutamic acids. It cleaves the N-terminal pyroglutamic acid from proteins and peptides prior to Edman degradation. The optimal temperature range is 95 to 100°C and the optimal pH range is 6.0 to 9.0. Group: Enzymes. Synonyms: pyroglutamyl-peptidase I; Pyroglutamate aminopeptidase; EC 3.4.19.3; 5-oxoprolyl-peptidase; pyrase; pyroglutamate aminopeptidase; pyroglutamyl aminopeptidase; L-pyroglutamyl peptide hydrolase; pyrrolidone-carboxyl peptidase; pyrrolidone-carboxylate peptidase; pyrrolidonyl peptidase; L-pyrrolidonecarboxylate peptidase; pyroglutamidase; pyrrolidonecarboxylyl peptidase; 9075-21-2. Purity: ~ 90% (SDS PAGE). Pyrase. Mole weight: 21.5 kDa. Activity: 20 U/mg. Storage: at -20°C. Form: Lyophilized powder. Source: Thermococcus thioreducens. pyroglutamyl-peptidase I; Pyroglutamate aminopeptidase; EC 3.4.19.3; 5-oxoprolyl-peptidase; pyrase; pyroglutamate aminopeptidase; pyroglutamyl aminopeptidase; L-pyroglutamyl peptide hydrolase; pyrrolidone-carboxyl peptidase; pyrrolidone-carboxylate peptidase; pyrrolidonyl peptidase; L-pyrrolidonecarboxylate peptidase; pyroglutamidase; pyrrolidonecarboxylyl peptidase; 9075-21-2. Cat No: NATE-1256. | |
| Native Thermomicrobia sp. Hesperidinase (Rhamnosidase B) | A Thermostable α-L-rhamnosidase that catalyzes the cleavage of the bond between terminal L (+)-rhamnose and the aglycone of rhamnose-containing glycosides. The enzyme is also very active on naringin. L-Rhamnose or its derivatives is a suitable chiral structural component and can be used for the synthesis of pharmaceutical products, plant protection agents and the preparation of fragrances in the foodstuffs and perfume industries. The enzyme catalyzes the cleavage of the bond between terminal l (+)-rhamnose and the aglycone of rhamnose-containing glycosides. hydrolysis of terminal non-reducing α-l-rhamnose residues in α-l-rhamnosides, naringin, hesperdin and rutin. Group: Enzymes. Synonyms: Hesperidinase; α-L-rhamnosidase T; α-L-rhamnosidase N; α-L-rhamnosidase. RhamA. Source: Thermomicrobia sp. Hesperidinase; α-L-rhamnosidase T; α-L-rhamnosidase N; α-L-rhamnosidase. Cat No: NATE-0341. | |
| Native Thermomicrobia sp. Naringinase (Rhamnosidase A) | A thermostable Alpha-L-Rhamnosidase (Naringinase, RhamA) that catalyzes the cleavage of the bond between terminal L (+)-rhamnose and the aglycone of rhamnose-containing glycosides. The enzyme is very active on naringin but has also substantial activity with hesperidin as substrate. Applications: Naringin is a source of bitter flavor in fruit juice and rhamnosidases with naringinase activity are frequently used for debittering citrus juice. other biotechnological applications include manufacture of prunin; manufacture of alpha-l-rhamnosidese fom natural glycosides; clarification of juices; enhancement of wine aromas by hydrolysis of terpenyl glycosides; conversion o...ural component and can be used for the synthesis of pharmaceutical products, plant protection agents and the preparation of fragrances in the foodstuffs and perfume industries. Group: Enzymes. Synonyms: glycoside hydrolase; RhamA; naringinase; hesperidinase; α-L-rhamnosidase A; α-L-rhamnosidase N; α-L-rhamnoside rhamnohydrolase; EC 3.2.1.40. Enzyme Commission Number: EC 3.2.1.40. CAS No. 37288-35-0. RhamA. Source: Thermomicrobia strain PRI-1686. Species: Thermomicrobia sp. glycoside hydrolase; RhamA; naringinase; hesperidinase; α-L-rhamnosidase A; α-L-rhamnosidase N; α-L-rhamnoside rhamnohydrolase; EC 3.2.1.40. Cat No: NATE-0653. | |
| Native Thermostable Fungi Catalase for Semiconductor Process | Catalase is an enzyme that presents in the cells of plants, animals and aerobic (oxygen requiring) bacteria. It promotes the conversion of hydrogen peroxide, a powerful and harmful oxidizing agent, into water and molecular oxygen. It is widely used for removal of H2O2 in textile industry, semiconductor and HPPO factory. It saves time and energy and is environmental-friendly. The dosage of this product is 0.01-0.05g/L, and the processing time is 5-20 minutes. Group: Enzymes. Synonyms: hydrogen-peroxide: hydrogen-peroxide oxidoreductase; equilase; caperase; optidase; catalase-peroxidase; CAT; EC 1.11.1.6; 9001-05-2; Catalase. Enzyme Commission Number: EC 1.11.1.6. CAS No. 9001-5-2. CAT. Activity: > 350,000 unit/ml (at pH 7.0). Appearance: brown to dark brown liquid. Storage: avoid a direct ray of light and keep cool. Source: Thermostable Fungi. hydrogen-peroxide: hydrogen-peroxide oxidoreductase; equilase; caperase; optidase; catalase-peroxidase; CAT; EC 1.11.1.6; 9001-05-2; Catalase. Pack: 225 kg drum. Cat No: NATE-1748. | |
| Native Thermostable Fungi Catalase for Textile Process | Catalase is an enzyme that presents in the cells of plants, animals and aerobic (oxygen requiring) bacteria. It promotes the conversion of hydrogen peroxide, a powerful and harmful oxidizing agent, into water and molecular oxygen. It is widely used for removal of H2O2 in textile industry, semiconductor and HPPO factory. It saves time and energy and is environmental-friendly. The dosage of this product is 0.01-0.05g/L, and the processing time is 5-20 minutes. Group: Enzymes. Synonyms: hydrogen-peroxide: hydrogen-peroxide oxidoreductase; equilase; caperase; optidase; catalase-peroxidase; CAT; EC 1.11.1.6; 9001-05-2; Catalase. Enzyme Commission Number: EC 1.11.1.6. CAS No. 9001-5-2. CAT. Activity: > 350,000 unit/ml (at pH 7.0). Appearance: brown to dark brown liquid. Storage: avoid a direct ray of light and keep cool. Source: Thermostable Fungi. hydrogen-peroxide: hydrogen-peroxide oxidoreductase; equilase; caperase; optidase; catalase-peroxidase; CAT; EC 1.11.1.6; 9001-05-2; Catalase. Pack: 20 kg, 200 kg drum and 1 ton bulk. Cat No: NATE-1747. | |
| Native Thermotoga neopolitana 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. Applications: The enzyme may be used for hydrolysis of various glycosides such as polyphenol glycosides including naturally occurring antioxid...ntiobiase; cellobiase; emulsin; elaterase; aryl-β-glucosidase; β-D-glucosidase; arbutinase; amygdalinase; p-nitrophenyl β-glucosidase; primeverosidase; amygdalase; linamarase; salicilinase; β-1,6-glucosidase. Enzyme Commission Number: EC 3.2.1.6. CAS No. 62213-14-3. β-Glucosidase. Source: Thermotoga neopolitana. 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-0771. | |
| Native Thermus brockianus α-Galactosidase | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Protein determined by biuret. Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. GLA. Activity: 40-80 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 2.8 M (NH4)2SO4 solution. Source: Thermus brockianus. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Cat No: NATE-0290. | |
| Native Thermus brockianus β-Galactosidase | β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. SubstRates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. The enzyme hydrolyses terminal, non-reducing b-d-galactose residues in b-d-galactosides. Group: Enzymes. Synonyms: Beta-Galactosidase; Galactosidase; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. CAS No. 9031-11-2. β-gal. Source: Thermus brockianus. Beta-Galactosidase; Galactosidase; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Cat No: NATE-0298. | |
| Native Thermus flavus Lipase | Triacylglycerol lipase is an enzyme with system name triacylglycerol acylhydrolase. This enzyme catalyses the following chemical reaction:triacylglycerol + H2O<-> diacylglycerol + a carboxylate. The product is a crude preparation containing a mixture of intracellular lipases and is supplied as a lyophilized powder. Group: Enzymes. Synonyms: Triacylglycerol acylhydrolase; Triacylglycerol lipase. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Activity: >3.0 units/g. Stability: 2 years. Storage: 2-8°C. Form: Lyophilized powder. Source: Thermus flavus. EC 3.1.1.3; lipase; triglyceride lipase; tributyrase; butyrinase; glycerol ester hydrolase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969-4-9; Meito MY 30; Tweenesterase; GA 56; capalase L; triglyceride hydrolase; triolein hydrolase; tween-hydrolyzing esterase; amano CE; cacordase; triglyceridase; triacylglycerol ester hydrolase; amano P; amano AP; PPL; glycerol-ester hydrolase; GEH; meito Sangyo OF lipase; hepatic lipase; lipazin; post-heparin plasma protamine-resistant lipase; salt-resistant post-heparin lipase; heparin releasable hepatic lipase; amano CES; amano B; tributyrase; triglyceride lipase; liver lipase; hepatic monoacylglycerol acyltransferase; 9001-62-1. Cat No: NATE-1614. | |
| Native Thermus flavus Malic Dehydrogenase | Malic dehydrogenase (MDH) exists as two isoforms within eukaryotic cells, one that is expressed in the mitochondria and functions in the TCA cycle and one in the cytoplasm that converts malate from the mitochondria back into oxaloacetate. Malic dehydrogenase from thermus flavus is stable and active at 90 oc. Applications: Malic dehydrogenase has been used in a study to assess electron transport chain activity in mit ochondria from human skeletal muscle. it has also been used in a study to investigate activities of enzymes and ammonia in serum of rats with fluoride hyperglycemia. Group: Enzymes. Synonyms: malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic deh. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Activity: > 50 units/mg solid. Storage: -20°C. Form: lyophilized powder; Contains dextran. Source: Thermus flavus. 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-specific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; EC 1.1.1.37; 9001-64-3. Cat No: NATE-0448. | |
| Native Thermus thermophilus Lipase | Triacylglycerol lipase is an enzyme with system name triacylglycerol acylhydrolase. This enzyme catalyses the following chemical reaction:triacylglycerol + H2O<-> diacylglycerol + a carboxylate. The product is a crude preparation containing a mixture of intracellular lipases and is supplied as a lyophilized powder. Group: Enzymes. Synonyms: Triacylglycerol acylhydrolase; Triacylglycerol lipase. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Activity: >3.0 units/g. Stability: 2 years. Storage: 2-8°C. Form: Lyophilized powder. Source: Thermus thermophilus. EC 3.1.1.3; lipase; triglyceride lipase; tributyrase; butyrinase; glycerol ester hydrolase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969-4-9; Meito MY 30; Tweenesterase; GA 56; capalase L; triglyceride hydrolase; triolein hydrolase; tween-hydrolyzing esterase; amano CE; cacordase; triglyceridase; triacylglycerol ester hydrolase; amano P; amano AP; PPL; glycerol-ester hydrolase; GEH; meito Sangyo OF lipase; hepatic lipase; lipazin; post-heparin plasma protamine-resistant lipase; salt-resistant post-heparin lipase; heparin releasable hepatic lipase; amano CES; amano B; tributyrase; triglyceride lipase; liver lipase; hepatic monoacylglycerol acyltransferase; 9001-62-1. Cat No: NATE-1613. | |
| Native Torula yeast 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). Group: Enzymes. Synonyms: EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Activity: 300-600 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 2.6 M (NH4)2SO4 solution, pH 7.5. Source: Torula yeast. EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase; 9001-40-5. Cat No: DIA-322. | |
| Native Trametes versicolor 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: > 0.5 units/mg. Storage: 2-8°C. Form: powder; light brown. Source: Trametes versicolor. Laccases; EC 1.10.3.2; 80498-15-3; urishiol oxidase; urushiol oxidase; p-diphenol oxidase; benzenediol:oxygen oxidoreductase. Cat No: NATE-0374. | |
| Native Transketolase from Thermophillic bacteria | Transketolase is highly specific for ketol donor substrates and is stereospecific and enantioselective to hydroxyaldehyde substrates with an (R) configuration. It specifically catalyzes the irreversible transfer of one ketol unit from α-hydroxypyruvic acid to an aldehyde to produce a D-threo (3S,4R)ketose. Applications: This enzyme is a potential candidate for biocatalysis, suitable for pharmaceutical development / manufacturing. asymmetric c-c bond formation, ketol donor d-xylulose-5-phosphate may be substituted by hydroxypyruvate; preparation of ketose sugars such as fructose analogs, azasugars and fluorogenic substrates. Group: Enzymes. Synonyms: Transketolase; EC 2.2.1.1; 9014-48-6; glycolaldehydetransferase; Glycolaldehyde Transferase. Enzyme Commission Number: EC 2.2.1.1. CAS No. 9014-48-6. Transketolase. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. Transketolase; EC 2.2.1.1; 9014-48-6; glycolaldehydetransferase; Glycolaldehyde Transferase. Cat No: NATE-1162. | |
| Native Trichoderma harzianum Lysing Enzymes | Native Trichoderma harzianum Lysing Enzymes. Contains β-glucanase, cellulase, protease, and chitinase activities. Applications: Used for yeast spheroplast transformation by hydrolyzing poly (1-3)-glucose of the yeast cell wall glucan. also used to retrieve dna plugs from agarose gels. Group: Enzymes. Synonyms: Lysing Enzymes; Glucanex. Lysing Enzymes. Form: lyophilized powder. Source: Trichoderma harzianum. Lysing Enzymes; Glucanex. Cat No: NATE-0428. | |
| Native Trichoderma longibrachiatum β-Glucanase | β-glucanases degrade β-1,4-glucans of cellulose, xyloglucan and β-1,4-xylan. β-Glucanase represents a group of carbohydrate enzymes which break down glycosidic bonds within beta-glucan. It forms the main constituent of fungal cell walls and could be a potential structural and storage polysaccharide of marine macro-algae. It has the ability to degrade fungal cell walls and may be involved in defense mechanism of plants against pathogenic fungi. Applications: Β-glucanase was used as a cellulase enzyme in the combined biological and chemical pretreatment method for lignocellulosic ethanol production from energy cane. it was also used in the enz...-(1,3; 1,4)-β-D-glucan 3 (4)-glucanohydrolase; EC 3.2.1.6. Enzyme Commission Number: EC 3.2.1.6. CAS No. 62213-14-3. β-glucanase. Form: powder. contains maltodextrin, silica and sodium benzoate. Source: Trichoderma longibrachiatum. endo-1,3-β-D-glucanase; laminarinase; laminaranase; β-1,3-glucanase; β-1,3-1,4-glucanase; endo-1,3-β-glucanase; endo-β-1,3 (4)-glucanase; endo-β-1,3-1,4-glucanase; endo-β-(1?3)-D-glucanase; endo-1,3-1,4-β-D-glucanase; endo-β-(1-3)-D-glucanase; endo-β-1,3-glucanase IV; endo-1,3-β-D-glucanase; 1,3-(1,3; 1,4)-β-D-glucan 3 (4)-glucanohydrolase; EC 3.2.1.6. Cat No: NATE-0768. | |
| Native Trichoderma longibrachiatum endo-1,4-β-Xylanase | Xylanase is the name given to a class of enzymes which degrade the linear polysaccharide beta-1,4-xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls. As such, it plays a major role in micro-organisms thriving on plant sources for the degradation of plant matter into usable nutrients. Xylanases are produced by fungi, bacteria, yeast, marine algae, protozoans, snails, crustaceans, insect, seeds, etc., (mammals do not produce xylanases). Group: Enzymes. Synonyms: EC 3.2.1.8; endo-(1?4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-β-xylan xylanohydrolase; β-xylanase; β-1,4-xylan xylanohydrolase; endo-1,4-β-xylanase; β-D-xylanase; endo-1,4. Enzyme Commission Number: EC 3.2.1.8. CAS No. 9025-57-4. Xylanase. Activity: > 1.0 units/mg solid. Storage: Room temp. Source: Trichoderma longibrachiatum. EC 3.2.1.8; endo-(1?4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-β-xylan xylanohydrolase; β-xylanase; β-1,4-xylan xylanohydrolase; endo-1,4-β-xylanase; β-D-xylanase; endo-1,4-β-xylanase. Cat No: NATE-0735. | |
| Native Trichoderma reesei Cellulase | Cellulase refers to a family of enzymes which act in concert to hydrolyze cellulose. Trichoderma reesei has an extensively studied cellulase enzyme complex. This complex converts crystalline, amorphous, and chemically derived celluloses quantitatively to glucose. Applications: Digestive tablets removal or softening of cellulose in food preparation protoplast preparation from plants various manufacturing processes. Group: Enzymes. Synonyms: endo-1,4-β-D-glucanase; β-1,4-glucanase; β-1,4-endoglucan hydrolase; celluase A; cellulosin AP; endoglucanase D; alkali cellulase; cellulase A 3; celludextrinase; 9.5 cellulase; avicelase; pancellase SS; 1,4-(1,3; 1,4)-β-D-glucan 4-glucanohydrolase; EC 3.2.1.4. Enzyme Commission Number: EC 3.2.1.4. CAS No. 9012-54-8. Cellulase. Activity: Type 1 > 25 units per mg dry weight; Type 2 > 45 units per mg dry weight. Storage: 2-8°C. Form: Lyophilized powder. Source: Trichoderma reesei ATCC26921. endo-1,4-β-D-glucanase; β-1,4-glucanase; β-1,4-endoglucan hydrolase; celluase A; cellulosin AP; endoglucanase D; alkali cellulase; cellulase A 3; celludextrinase; 9.5 cellulase; avicelase; pancellase SS; 1,4-(1,3; 1,4)-β-D-glucan 4-glucanohydrolase; EC 3.2.1.4. Cat No: NATE-0120. | |
| Native Trichoderma sp. Cellulase | Cellulase is any of several enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis, the decomposition of cellulose and of some related polysaccharides; specifically, the hydrolysis of the 1,4-beta-D-glycosidic linkages in cellulose, hemicellulose, lichenin, and cereal beta-D-glucans. Cellulases break down the cellulose molecule into monosaccharides ("simple sugars") such as beta-glucose, or shorter polysaccharides and oligosaccharides. The name is also used for any naturally occurring mixture or complex of various such enzymes, that act serially or synergistically to decompose cellulosic material. Applications: Cellulases are enzymes that hydro...-glucanase; β-1,4-endoglucan hydrolase; celluase A; cellulosin AP; endoglucanase D; alkali cellulase; cellulase A 3; celludextrinase; 9.5 cellulase; avicelase; pancellase SS; 1,4-(1,3; 1,4)-β-D-glucan 4-glucanohydrolase; EC 3.2.1.4. Enzyme Commission Number: EC 3.2.1.4. CAS No. 9012-54-8. Cellulase. Activity: > 5,000 units/g solid. Storage: 2-8°C. Source: Trichoderma sp. endo-1,4-β-D-glucanase; β-1,4-glucanase; β-1,4-endoglucan hydrolase; celluase A; cellulosin AP; endoglucanase D; alkali cellulase; cellulase A 3; celludextrinase; 9.5 cellulase; avicelase; pancellase SS; 1,4-(1,3; 1,4)-β-D-glucan 4-glucanohydrolase; EC 3.2.1.4. Cat No: NATE-0119. | |
| Native Trichoderma sp. Laminarinase | 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-gluc. Enzyme Commission Number: EC 3.2.1.6. CAS No. 62213-14-3. β-glucanase. Activity: 100-400 units/g solid. Storage: 2-8°C. Form: powder. Source: Trichoderma sp. EC 3.2.1.6; endo-1,3-beta-D-glucanase; laminarinase; beta-1,3-glucanase; beta-1,3-1,4-glucanase; endo-1,3-beta-glucanase; endo-beta-1,3 (4)-glucanase; endo-beta-1,3-1,4-glucanase; endo-beta-(1->3)-D-glucanase; endo-1,3-1,4-beta-D-glucanase; endo-beta-(1-3)-D-glucanase; endo-beta-1,3-glucanase IV; 1,3-(1,3, 1,4)-beta-D-glucan 3 (4)-glucanohydrolase; 1,3-[1,3; 1,4]-β-D-Glucan 3 (4)-glucanohydrolase; Endo-1,3 (4)-β-glucanase. Cat No: NATE-0377. | |
| Native Trichoderma sp. Mutanase | This product is a mutanase preparation derived from Trichoderma sp. The enzyme catalyzes the hydrolysis of α-1,3 Glucan(Mutan), which is main substance of dental plaque. Applications: 1.conventional dental care products(tooth paste, antiseptic mouthwash, etc.) contain dextranase (α-1,6 glucanase). so, dextran can be easily decomposed by conventional dental care products.2.however, mutan, the main structure of dental plaque which is water-insoluble, can not be decomposed by dextranase and remains in the mouth.3.mutanase can decompose dental plaque mutan. so, it can be applied to dental care products. Group: Enzymes. Synonyms: endo-1,3-α-glucanase; endo-(1?3)-α-glucanase; cariogenase; cariogenanase; endo-1,3-α-D-glucanase; 1,3(1,3;1,4)-α-D-glucan 3-glucanohydrolase. Enzyme Commission Number: EC 3.2.1.59. CAS No. 9075-84-7. Activity: > 1,000 unit/g (at 45 °C, pH 5.0.). Appearance: Yellow-light brown, powder. Storage: store under cool and dry condition. Source: Trichoderma sp. endo-1,3-α-glucanase; endo-(1?3)-α-glucanase; cariogenase; cariogenanase; endo-1,3-α-D-glucanase; 1,3(1,3;1,4)-α-D-glucan 3-glucanohydrolase. Pack: 10 L, 20 L LDPE bottle (Liquid); Available in both liquid and powdered forms. Cat No: NATE-1751. | |
| Native Trichoderma viride 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 trichoderma viride has been used in a study to investigate the differential release of high mannose structural isoforms by fungal and bacterial endo-β-n-acetylglucosaminidases. chitinase from trichoderma viride has al...glucosaminidase; 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. Enzyme Commission Number: EC 3.2.1.14. CAS No. 9001-6-3. Chitinase. Activity: > 600 units/g solid. Storage: -20°C. Form: lyophilized powder. Source: Trichoderma viride. 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-0124. | |
| Native Trichoderma viride Lysine Oxidase | In enzymology, a L-lysine oxidase (EC 1.4.3.14) is an enzyme that catalyzes the chemical reaction:L-lysine + O2 + H2O<-> 6-amino-2-oxohexanoate + NH3 + H2O2. The 3 substrates of this enzyme are L-lysine, O2, and H2O, whereas its 3 products are 6-amino-2-oxohexanoate, NH3, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. This enzyme participates in lysine degradation. Group: Enzymes. Synonyms: L-lysine α-oxidase; L-lysyl-α-oxidase; L-lysine oxidase; EC 1.4.3.14; 70132-14-8. Enzyme Commission Number: EC 1.4.3.14. CAS No. 70132-14-8. Lysine Oxidase. Activity: 20-60 units/mg protein. Storage: 2-8°C. Form: lyophilized powder; Contains phosphate buffer salts and stabilizer. Source: Trichoderma viride. L-lysine α-oxidase; L-lysyl-α-oxidase; L-lysine oxidase; EC 1.4.3.14; 70132-14-8. Cat No: NATE-0426. | |
| Native Tritirachium album limber Proteinase K | Proteinase K (PROK) is a serine protease with broad specificity towards aliphatic, aromatic and other hydrophobic amino acids. PROK has a molecular weight of 27,000 daltons and is Ca2+ dependent. It is not inactivated by metal ion chelating agents such as EDTA, sulfhydryl reagents, PCMB, TLCK, or TPCK. It also retains activity in 0.5% SDS. It can be inhibited by PMSF or DFP. Applications: Useful for the proteolytic inactivation of nucleases during the isolation of dna and rna. removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease a. reported useful for the isolation of hepatic, yeast, and mung bean mit ochondria determination of enzyme l o...oteinase; Tritirachium album proteinase K; endopeptidase K; 39450-01-6; protease K. Enzyme Commission Number: EC 3.4.21.64. CAS No. 39450-01-6. Purity: Purified to remove DNase and RNase. Proteinase K. Mole weight: 27 kDa. Activity: Type I, > 20 units per mg dry weight; Type II, > 400 u/ml. Storage: Powder: 2-8°C; Liquid: -20°C. Form: Type I, powder; Type II, Liquid in 20mg/ml in 10mM Tris-HCl, 1mM calcium acetate, pH 7.5 containing 50% glycerol. Source: Tritirachium album limber. Proteinase K; EC 3.4.21.64; Tritirachium alkaline proteinase; Tritirachium album serine proteinase; Tritirachium album proteinase K; endopeptidase K; 39450-01-6; protease K. Cat No: NATE-0637. | |
| Native Tritirachium album Proteinase K | Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments:pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA. Applications: Proteinase k is useful for the proteolytic inactivation of nucleases during the isolation of dna and rna. it is used for the removal of endotoxins bo... used to facilitate the access of probes to rrna using fish techniques to detect pathogenic staphylococcus aureus. useful for the proteolytic inactivation of nucleases during the isolation of dna and rna. removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease a. reported useful for the isolation of hepatic, yeast, and mung bean mitochondria determination of enzyme localization on membranes treatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling. digestion of proteins from brain tissue samples for prions in transmissible spongiform encephalopathies (tse) research. Group: Enzymes. Synonyms: Tritirachiu | |
| Native Vaccinia virus Topoisomerase I | Topoisomerase I relaxes supercoiled DNA molecules. The enzyme initiates transient breakages and rejoins of phosphodiester bonds in superhelical turns of closed-circular DNA. Enzyme activity is independent of right-and left-handed superhelices. Applications: Enzyme activity is increased in the presence of 2.5 mm mg2+. topoisomerase i from vaccinia virus can be used for studying pivotal biological pr ocess such as-replication, transcription, recombination as well as dna structure and topology which includes chromatin reconstitution in vitro and the degree of supercoiling of dna. additionally, the product helps in relaxing the dna coils and exposes the restriction sites which...me; swivelase; ω-protein; deoxyribonucleate topoisomerase; topoisomerase; type I DNA topoisomerase; DNA topoisomerase; TOPO I. Enzyme Commission Number: EC 5.99.1.2. CAS No. 80449-01-0. TOPO I. Mole weight: mol wt 32 kDa. Storage: -20°C. Form: buffered aqueous solution; Solution in 50 mM Tris HCl, pH 7.5, containing 100 mM NaCl, 1 mM EDTA, 1 mM DTT, 0.1% Triton X-100, and 50% glycerol. Source: Vaccinia virus. Topoisomerase I; EC 5.99.1.2; type I DNA topoisomerase; untwisting enzyme; relaxing enzyme; nicking-closing enzyme; swivelase; ω-protein; deoxyribonucleate topoisomerase; topoisomerase; type I DNA topoisomerase; DNA topoisomerase; TOPO I. Cat No: NATE-0708. | |
| Native Versatile Peroxidase from Bjerkandera adusta | Versatile peroxidase (EC 1.11.1.16, VP, hybrid peroxidase, polyvalent peroxidase) is an enzyme with systematic name reactive-black-5:hydrogen-peroxide oxidoreductase. This enzyme catalyses the following chemical reaction: (1) Reactive Black 5 + H2O2 ? oxidized Reactive Black 5 + 2 H2O (2) donor + H2O2 ? oxidized donor + 2 H2O Versatile peroxidase is a hemoprotein. Group: Enzymes. Synonyms: EC 1.11.1.16; VP; hybrid peroxidase; polyvalent peroxidase. Enzyme Commission Number: EC 1.11.1.16. CAS No. 114995-15-2;42613-30-9. Versatile Peroxidase. Stability: 12 months. Storage: store at -20 °C. Form: Freeze-dried brown-coloured amorphous powder, no stabilizing agent added. Source: Bjerkandera adusta. EC 1.11.1.16; VP; hybrid peroxidase; polyvalent peroxidase. Cat No: NATE-1580. | |
| Native Vibrio cholerae 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. At least four mammalian sialidase homologs have been described in the...say of neuraminidase. 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. Activity: Type I, 1-5 units/mg protein (Lowry, using NAN-lactose); Type II, 8-24 units/mg protein (Lowry, using NAN-lactose); Type III, > 1.5 units/mg protein. Storage: 2-8°C. Form: Type I, buffered aqueous solution; Aqueous solution, pH 5.5, containing 0.15 M NaCl and 4 mM CaCl2; Type II, buffered aqueous solution, Solution in 50 mM sodium acetate, pH 5.5, containing 0.15 M sodium chloride and 4 mM calcium chloride; Type III, sterile filte | |
| Native Vibrio fischeri (Photobacterium f) Luciferase | In enzymology, an alkanal monooxygenase (FMN-linked) (EC 1.14.14.3) is an enzyme that catalyzes the chemical reaction:RCHO + reduced FMN + O2<-> RCOOH + FMN + H2O + hnu. The 3 substrates of this enzyme are RCHO, reduced FMN, and O2, whereas its 4 products are RCOOH, FMN, H2O, and hn. 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 reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor. Applications: Luciferase from vibrio fischeri has been used in a s...; aldehyde monooxygenase; luciferase; Vibrio fischeri luciferase; alkanal,reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing); alkanal,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing); EC 1.14.14.3; 9014-00-0. Enzyme Commission Number: EC 1.13.12.7. CAS No. 9014-00-0. Luciferase. Form: lyophilized powder. Source: Vibrio fischeri (Photobacterium f). alkanal monooxygenase (FMN); bacterial luciferase; aldehyde monooxygenase; luciferase; Vibrio fischeri luciferase; alkanal,reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing); alkanal,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing); EC 1.14.14.3; 9014-00-0. Cat No: NATE-0423. | |
| Native Vibrio sp. Lysophospholipase | In enzymology, a lysophospholipase (EC 3.1.1.5) is an enzyme that catalyzes the chemical reaction: 2-lysophosphatidylcholine + H2O <-> glycerophosphocholine + a carboxylate. Thus, the two substrates of this enzyme are 2-lysophosphatidylcholine and H2O, whereas its two products are glycerophosphocholine and carboxylate. Native lysophospholipase (ec 3.1.1.5) was purified from vibrio sp. Applications: Useful for the enzymatic determination of lysolecithin. Group: Enzymes. Synonyms: lysophospholipase; EC 3.1.1.5; 2-lysophosphatidylcholine acylhydrolase; lecithinase B; lysolecithinase; phospholipase B. Enzyme Commission Number: EC 3.1.1.5. CAS No. 9001-85-8. Lysophospholipase. Activity: > 20.0 U/mg. Appearance: White to brownish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Vibrio sp. lysophospholipase; EC 3.1.1.5; 2-lysophosphatidylcholine acylhydrolase; lecithinase B; lysolecithinase; phospholipase B. Cat No: DIA-157. | |
| Native Wheat Carboxypeptidase W | Carboxypeptidase D can refer to one of several enzymes. A family of serine carboxypeptidases (i.e. enzymes that use an active site serine residue) includes (EC 3.4.16.6, cereal serine carboxypeptidase II, Saccharomyces cerevisiae KEX1 gene product, carboxypeptidase Kex1, gene KEX1 serine carboxypeptidase, KEX1 carboxypeptidase, KEX1 proteinase, KEX1DELTAp, CPDW-II, serine carboxypeptidase, Phaseolus proteinase) is an enzyme. This enzyme has an optimal pH of 4.5-6.0, is inhibited by diisopropyl fluorophosphate. Applications: Carboxypeptidase w from wheat has been used in a study to assess the proteolytic activities in dormant rye (secale cereale l.) grain. carboxypeptidase w from wheat has also been used in a study to investigate the structure determination of the human protective protein. Group: Enzymes. Synonyms: Carboxypeptidase W; 9046-67-7; EC 3.4.16.6; carboxypeptidase D; cereal. Enzyme Commission Number: EC 3.4.16.6. CAS No. 9046-67-7. CPDW-II. Activity: > 50 units/mg protein. Storage: -20°C. Source: Wheat. Carboxypeptidase W; 9046-67-7; EC 3.4.16.6; carboxypeptidase D; cereal serine carboxypeptidase II; Saccharomyces cerevisiae KEX1 gene product; carboxypeptidase Kex1; gene KEX1 serine carboxypeptidase; KEX1 carboxypeptidase; KEX1 proteinase; KEX1DELTAp; CPDW-II; serine carboxypeptidase (misleading); Phaseolus proteinase. Cat No: NATE-0154. | |
| Native Wheat germ Acid Phosphatase | Acid phosphatases (APase) are a family of enzymes that non-specifically catalyze the hydrolysis of monoesters and anhydrides of phosphoric acid to produce inorganic phosphate at an optimum pH of 4 to 7. Acid phosphatase from potatoes is a 111 kDa diner consisting of two subunits at 41 and 35 kDa. This phosphatase has also been shown to cleave DNA. Applications: Acid phosphatase (apase) non-specifically catalyzes the hydrolysis of monoesters and anhydrides of phosphoric acid to produce inorganic phosphate. it is used to study the production, transport, and recycling of phosphate and the metabolic and energy transduction pr ocesses of the cell. this product is from wheat germ and has been used to determine the effect of phosphatase treatment on 3f3/2 staining. Group: Enzymes. Synonyms: acid phosphatase; 9001-77-8; acid phosphomonoesterase; phosphomon. Enzyme Commission Number: EC 3.1.3.2. CAS No. 9001-77-8. Mole weight: 58 kDa (gel filtration). Activity: > 1 unit/mg. Storage: -20°C. Form: lyophilized powder. Source: Wheat germ. acid phosphatase; 9001-77-8; 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; APase. Cat No: NATE-0084. | |
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