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| Product | Description | |
|---|---|---|
| Native Aspergillus oryzae Diastase | A diastase is any one of a group of enzymes which catalyses the breakdown of starch into maltose. Alpha amylase degrades starch to a mixture of the disaccharide maltose, the trisaccharide maltotriose, which contains three α (1-4)-linked glucose residues, and oligosaccharides known as dextrins that contain the α (1-6)-linked glucose branches. Diastase was the first enzyme discovered. Today, diastase means any α-, β-, or γ-amylase (all of them hydrolases) that can break down carbohydrates. Group: Enzymes. Synonyms: 9000-92-4; Diastase. CAS No. 9000-92-4. Diastase. Activity: > 3500 U/g. Storage: 2-8°C. Form: powder. Source: Aspergillus oryzae. 9000-92-4; Diastase. Cat No: NATE-0190. |  |
| Native Aspergillus oryzae endo-Inulinase (food grade) | Inulinase hydrolyses inulin to produce oligosaccharides and liberate fructose. It also splits terminal fructose units in sucrose and raffinose. Applications: Food, beverage, alcohol fermentation, pharmaceutical preparation. Group: Enzymes. Synonyms: EC 3.2.1.7; inulinase; inulase; indoinulinase; endo-inulinase; exoinulinase; 2,1-β-D-fructan fructanohydrolase; 9025-67-6. Inulinase. Activity: 20,000u/g. Appearance: Light yellow powder. Storage: 4-10°C. Source: Aspergillus oryzae. EC 3.2.1.7; inulinase; inulase; indoinulinase; endo-inulinase; exoinulinase; 2,1-β-D-fructan fructanohydrolase; 9025-67-6. Cat No: NATE-1246. | |
| Native Aspergillus oryzae exo-Inulinase (food grade) | Inulinase hydrolyses inulin to produce oligosaccharides and liberate fructose. It also splits terminal fructose units in sucrose and raffinose. Applications: Food, beverage, alcohol fermentation, pharmaceutical preparation. Group: Enzymes. Synonyms: EC 3.2.1.80; fructan beta-fructosidase; beta-D-fructan fructohydrolase; EC 3.2.1.26; beta-fructofuranosidase; beta-D-fructofuranoside fructohydrolase; exo-inulinase. Inulinase. Activity: 20,000u/g. Appearance: Light yellow powder. Storage: 4-10°C. Source: Aspergillus oryzae. EC 3.2.1.80; fructan beta-fructosidase; beta-D-fructan fructohydrolase; EC 3.2.1.26; beta-fructofuranosidase; beta-D-fructofuranoside fructohydrolase; exo-inulinase. Cat No: NATE-1245. | |
| Native Aspergillus oryzae Lipase | Triacylglycerol lipase is an enzyme with system name triacylglycerol acylhydrolase. This enzyme catalyses the following chemical reaction:triacylglycerol + H2O<-> diacylglycerol + a carboxylate. Group: Enzymes. Synonyms: Triacylglycerol acylhydrolase; Triacylglycerol lipase. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Activity: ~50 U/mg. Appearance: White lyophilized powder. Storage: 2-8°C. Source: Aspergillus oryzae. 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-1608. | |
| Native Aspergillus oryzae Lipase (Solution) | Triacylglycerol lipase is an enzyme with system name triacylglycerol acylhydrolase. This enzyme catalyses the following chemical reaction:triacylglycerol + H2O<-> diacylglycerol + a carboxylate. Group: Enzymes. Synonyms: Lipolase 100L. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Activity: >100 U/mg. Storage: 2-8°C. Form: Solution. Source: Aspergillus oryzae. 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-1610. | |
| Native Aspergillus oryzae Nuclease S1 | Nuclease S1 isolated from Aspergillus oryzae exhibits endo-and exolytic hydrolytic activity for the phosphodiester bonds of single-stranded DNA and RNA yielding 5-phosphomononucleotide and 5-phosphooligonucleotide end-products. It is used to digest non-annealed polynucleotide tails and hairpin loops in RNA and DNA duplexes and can be used to convert superhelical DNA to the linear form. The nuclease s1 enzyme from aspergillus oryzae has the ability to degrade single-stranded oligonucleotides composed of either deoxynucleotides or ribonucleotides. Applications: Nuclease s1 from aspergillus oryzae has been used in a study to assess a bi ochemical method for mapping mutational...e S1 nuclease; EC 3.1.30.1; 37288-25-8. Enzyme Commission Number: EC 3.1.30.1. CAS No. 37288-25-8. Nuclease. Storage: -20°C. Form: Solution containing 30 mM sodium acetate, 50 mM NaCl, 1 mM ZnCl2, 50% glycerol, 2 mg/ml protein. Source: Aspergillus oryzae. endonuclease S1 (Aspergillus); single-stranded-nucleate endonuclease; deoxyribonuclease S1; deoxyribonuclease S1; nuclease S1; Neurospora crassa single-strand specific endonuclease; S1 nuclease; single-strand endodeoxyribonuclease; single-stranded DNA specific endonuclease; single-strand-specific endodeoxyribonuclease; single strand-specific DNase; Aspergillus oryzae S1 nuclease; EC 3.1.30.1; 37288-25-8. Cat No: NATE-0492. | |
| Native Aspergillus oryzae Phospholipase A1 | Phospholipase A1 is a phospholipase enzyme which removes the 1-acyl. Phospholipase A1 is an enzyme that resides in a class of enzymes called phospholipase that hydrolyze phospholipids into fatty acids. There are 4 classes, which are separated by the type of reaction they catalyze. In particular, phospholipase A1 (PLA1) specifically catalyzes the cleavage at the SN-1 position of phospholipids, forming a fatty acid and a lysophospholipid. Group: Enzymes. Synonyms: phospholipase A1; EC 3.1.1.32; phosphatidylcholine 1-acylhydrolase; PLA1. Enzyme Commission Number: EC 3.1.1.32. CAS No. 9043-29-2. PLA1. Form: liquid, > 10 KLU/G. Source: Aspergillus oryzae. phospholipase A1; EC 3.1.1.32; phosphatidylcholine 1-acylhydrolase; PLA1. Cat No: NATE-0582. | |
| Native Aspergillus oryzae Protease | Protease catabolizes proteins by hydrolysis of peptide bonds. Protease, from Aspergillus oryzae, contains both endoprotease and exopeptidase activities. Fungal protease/peptidase complex produced by submerged fermentation of a selected strain of aspergillus oryzae and contains both endoprotease and exopeptidase activities. Applications: Protease is an enzyme used to break down proteins by hydrolyzing peptide bonds. protease is used to degrade proteins, to study protease inhibitors and to study thermal inactivation kinetics. protease is used in nucleic acid isolation procedures in incubations. this product is a fungal protease/peptidase complex produced by submerged fermentation of a selected strain of aspergillus oryzae. it has been injected into flies with a nanoject apparatus for infection and survival experiments. the enzyme from creative enzymes has been used in the semi-purification of mouse colorectal mucins during protein digestion. Group: Enzymes. Synonyms: Protease; Flavourzyme. CAS No. 9001-92-7. Protease. Source: Aspergillus oryzae. Protease; Flavourzyme. Cat No: NATE-0631. | |
| Native Aspergillus oryzae Ribonuclease T1 | Ribonuclease T1 (RNase T1) from Aspergillus oryzae is an endoribonuclease that hydrolyzes after G residues. Cleavage occurs between the 3-phosphate group of a guanidine ribonucleotide and 5-hydroxyl of the adjacent nucleotide. The initial product is a 2:3 cyclic phosphate nucleoside that is hydrolyzed to the corresponding 3-nucleoside phosphate. It differs from Pancreatic RNase in that it attacks the guanine sites specifically to yield 3'-GMP and oligonucleotides with a 3'-GMP terminal group. Applications: Ribonuclease t1 (rnase t1) from aspergillus oryzae is used to digest denatured rna prior to sequencing and is used for protein folding studies. Group: Enzymes. Synonyms: Ribonuclease T1; EC 3.1.27.3; g. Enzyme Commission Number: EC 3.1.27.3. CAS No. 9026-12-4. Rnase. Activity: 300,000-600,000 units/mg protein. Storage: -20°C. Form: ammonium sulfate suspension; Suspension in 2.8 M (NH4)2SO4 solution. Source: Aspergillus oryzae. Ribonuclease T1; EC 3.1.27.3; guanyloribonuclease; Aspergillus oryzae ribonuclease; RNase N1; RNase N2; ribonuclease N3; ribonuclease U1; ribonuclease F1; ribonuclease Ch; ribonuclease PP1; ribonuclease SA; RNase F1; ribonuclease C2; binase; RNase Sa; guanyl-specific RNase; RNase G; RNase T1; ribonuclease guaninenucleotido-2'-transferase (cyclizing); ribonuclease N3; ribonuclease N1; 9026-12-4. Cat No: NATE-0658. | |
| Native Aspergillus oryzae Tannase | Tannase catalyzes the hydrolysis of tannic acid to produce gallic acid and glucose. Group: Enzymes. Synonyms: tannase; 9025-71-2; Tannin acyl Hydrolase. Enzyme Commission Number: EC 3.1.1.20. CAS No. 9025-71-2. Tannase. Mole weight: about 200,000. Activity: 30+ units/mg. Appearance: Grayish brown - brown, crystals - powder. Storage: Keep at 2-10 degrees C. Source: Aspergillus oryzae. tannase; 9025-71-2; Tannin acyl Hydrolase. Cat No: NATE-1078. | |
| Native Aspergillus restrictus Restrictocin | Restrictocin from Aspergillus restrictus is a ribosome-inactivating protein that acts by specifically cleaving rRNA. Approximately 70% of the protein is active restrictocin. Restrictocin shares a high degree of amino acid sequence homology with mitogillin, a ribotoxin that cleaves a single phosphodiester bond of the 29S rRNA of eukaryotic ribosomes. Restrictocin is thought to be activated during the process of secretion. Applications: Restrictocin from aspergillus restrictus is used to inhibit protein synthesis. it may be useful as a component of immunotoxins. this product is provided as a lyophilized powder. Group: Enzymes. Synonyms: Restrictocin; 1406-72-0. CAS No. 1406-72-0. Restrictocin. Storage: Store at -20°C. Form: Lyophilized powder. Source: Aspergillus restrictus. Restrictocin; 1406-72-0. Cat No: NATE-0865. | |
| Native Aspergillus saitoi α (1-2)-Mannosidase | α-Mannosidase is an acid hydrolase which is located in plant vacuoles and is thought to be involved with the turnover of N-linked glycoproteins. α-Mannosidase has been shown to inhibit the proliferation of B-lymphocytes. α-Mannosidase from Canavalia ensiformis is a tretamer composed of two subunits that each contain two components at 44 and 66 kDa. Group: Enzymes. Synonyms: α-mannosidase; α-D-mannosidase; p-nitrophenyl-α-mannosidase; α-D-mannopyranosidase; 1,2-α-mannosidase; 1,2-α-D-mannosidase; exo-α-mannosidase; EC 3.2.1.24; 9025-42-7; Mannosidase. Enzyme Commission Number: EC 3.2.1.24. CAS No. 9025-42-7. Mannosidase. Source: Aspergillus saitoi. α-mannosidase; α-D-mannosidase; p-nitrophenyl-α-mannosidase; α-D-mannopyranosidase; 1,2-α-mannosidase; 1,2-α-D-mannosidase; exo-α-mannosidase; EC 3.2.1.24; 9025-42-7; Mannosidase. Cat No: NATE-0436. | |
| Native Aspergillus sp. Catalase | Catalase is a common enzyme found in nearly all living organisms, where it functions to catalyze the decomposition of hydrogen peroxide to water and oxygen. Catalase has one of the highest turnover numbers of all enzymes; one molecule of catalase can convert millions of molecules of hydrogen peroxide to water and oxygen per second. Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. It contains four porphyrin heme (iron) groups that allow the enzyme to react with the hydrogen peroxide. The optimum pH for catalase is approximately 7, while the optimum temperature varies by species. Applications: Auxillary enzyme useful in many assay formulations. 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. 9001-0 5-2. Activity: 150,000 U/ml or more. Storage: -20°C. Form: Liquid. Source: Aspergillus sp. hydrogen-peroxide: hydrogen-peroxide oxidoreductase; equilase; caperase; optidase; catalase-peroxidase; CAT; EC 1.11.1.6; 9001-05-2; Catalase. Cat No: DIA-131. | |
| Native Aspergillus sp. Glucose Oxidase | The glucose oxidase enzyme (GOx) also known as notatin (EC number 1.1.3.4) is an oxido-reductase that catalyses the oxidation of glucose to hydrogen peroxide and D-glucono-δ-lactone. This enzyme is produced by certain species of fungi and insects and displays antibacterial activity when oxygen and glucose are present. Applications: This enzyme is useful for enzymatic determination of glucose, and for amylase-activity assay when coupled with α-glucosidase in clinical analysis. Group: Enzymes. Synonyms: EC 1.1.3.4; glucose oxyhydrase; corylophyline; penatin; glucose aerodehydrogenase; microcid; β-D-glucose oxidase; D-glucose oxidase; D-glucose-1-oxidase; β-D-glucose:quinone oxidoreductase; glucose oxyhydrase; deoxin-1; GOD; 9001-37-0; glucose oxidas. Enzyme Commission Number: EC 1.1.3.4. CAS No. 9001-37-0. Mole weight: approx. 153 kDa. Activity: 100U/mg-solid or more (containing approx. 50% of stabilizers). Appearance: Yellowish amorphous powder, lyophilized. Form: Freeze dried powder. Source: Aspergillus sp. EC 1.1.3.4; glucose oxyhydrase; corylophyline; penatin; glucose aerodehydrogenase; microcid; β-D-glucose oxidase; D-glucose oxidase; D-glucose-1-oxidase; β-D-glucose:quinone oxidoreductase; glucose oxyhydrase; deoxin-1; GOD; 9001-37-0; glucose oxidase enzyme; GOx; notatin; glucose oxidase. Cat No: DIA-193. | |
| Native Aspergillus sp. 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. CAS No. 80498-15-3. Laccase. Activity: > 1000 U/g. Storage: 2-8°C. Source: Aspergillus sp. Laccases; EC 1.10.3.2; 80498-15-3; urishiol oxidase; urushiol oxidase; p-diphenol oxidase; benzenediol:oxygen oxidoreductase. Cat No: NATE-1592. | |
| Native Aspergillus sp. Lipase (API) | This product is a lipase (TLL) from Thermomyces lanuginosus and it is produced by a submerged fermentation of Aspergillus sp.In opposition to most enzymes, lipases exhibit a wide specificity, recognizing very different substrates. This permits to use a determined lipases as a catalyst for very different reactions, and makes that lipases may be used in pharmaceuticals and drugs production, in energy (biodiesel) or food manufacture, etc. TLL enzyme is a basophilic and noticeably thermostable enzyme. Initially oriented toward the food industry, TLL has been used in many different industrial areas such as modification of fats and oils, production of biodiesel, production of fine chemicals (mainly in enatio/regioselective or specific processes), etc. This product is optimally designed for production of API. Group: Enzymes. Synonyms: EC 3.1.1.3; 9001-62-1; Lipase; Triacylglycerol acylhydrolase; Triacylglycerol lipase; butyrinase; . Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Activity: 100,000 unit/g. Appearance: dark brown liquid. Storage: Enzymes gradually lose activity over time depending on storage temperature and humidity. Cool and dry conditions are recommended. At lower temperatures the storage stability is increased. Extended storage and/or adverse conditions, including higher temperatures or high humidity, may lead to a | |
| Native Aspergillus sp. Lipase (immobilized) | This product is a lipase (TLL) from Thermomyces lanuginosus and it is produced by a submerged fermentation of Aspergillus sp.In opposition to most enzymes, lipases exhibit a wide specificity, recognizing very different substrates. This permits to use a determined lipases as a catalyst for very different reactions, and makes that lipases may be used in pharmaceuticals and drugs production, in energy (biodiesel) or food manufacture, etc. TLL enzyme is a basophilic and noticeably thermostable enzyme. Initially oriented toward the food industry, TLL has been used in many different industrial areas such as modification of fats and oils, production of biodiesel, production of fine chemicals (mainly in enatio/regioselective or specific processes), etc. This product is an immobilized non-specific lipase for production of specialty products and oleochemicals. Group: Enzymes. Synonyms: EC 3.1.1.3; 9001-62-1; Lipase; Triacylglycerol acylhydrolase; Triacylglycerol lipase; buty. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Activity: 100,000 unit/g. Appearance: dark brown liquid. Storage: Enzymes gradually lose activity over time depending on storage temperature and humidity. Cool and dry conditions are recommended. At lower temperatures the storage stability is increased. Extended storage and/or adverse conditions, including hig | |
| Native Aspergillus sp. Lysing Enzymes | Native Aspergillus sp. Lysing Enzymes. Group: Enzymes. Synonyms: Lysing Enzymes. Lysing Enzymes. Storage: 2-8°C. Form: powder (brown). Source: Aspergillus sp. Lysing Enzymes. Cat No: NATE-0427. | |
| Native Aspergillus sp. Viscozyme L | Multi-enzyme complex containing a wide range of carbohydrases, including arabanase, cellulase, β-glucanase, hemicellulase, and xylanase. Cell wall degrading enzyme complex from aspergillus sp., lysing enzyme from aspergillus sp. Applications: Viscozyme l was shown to be an effective enzyme for the extraction of polyphenols from unripe apples. Group: Enzymes. Synonyms: Viscozyme L; Cell Wall Degrading Enzyme Complex from Aspergillus sp.; Lysing Enzyme from Aspergillus sp. Viscozyme L. Source: Aspergillus sp. Viscozyme L; Cell Wall Degrading Enzyme Complex from Aspergillus sp.; Lysing Enzyme from Aspergillus sp. Cat No: NATE-0731. | |
| Native Avian myeloblastosis virus AMV-Reverse Transcriptase | A Reverse transcriptase (RT) is an enzyme used to geneRate complementary DNA (cDNA) from an RNA template, a process termed reverse transcription. It is mainly associated with retroviruses. However, non-retroviruses also use RT (for example, the hepatitis B virus, a member of the Hepadnaviridae, which are dsDNA-RT viruses, while retroviruses are ssRNA viruses). RT inhibitors are widely used as antiretroviral drugs. RT activities are also associated with the replication of chromosome ends (telomerase) and some mobile genetic elements (retrotransposons). Applications: Amv reverse transcriptase synthesizes dna complementary (cdna) to rna templates. a dna primer complementary to the rna template and a divalent cation, either mg or mn, are required for initiation of transcription. this enzyme is commonly used to make cdnas from mrna for eventual cloning or for use as probes. Group: Enzymes. Synonyms: DNA nucleotidyltransferase (RNA-directed); reverse transcripta. Enzyme Commission Number: EC 2.7.7.49. CAS No. 9068-38-6. RT. Storage: -70°C. Source: Avian myeloblastosis virus. DNA nucleotidyltransferase (RNA-directed); reverse transcriptase; revertase; RNA-dependent deoxyribonucleate nucleotidyltransferase; RNA revertase; RNA-dependent DNA polymerase; RNA-instructed DNA polymerase; RT; EC 2.7.7.49; 9068-38-6. Cat No: NATE-0073. | |
| Native Bacillus amyloliquefaciens α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. this product is from bacillus amyloliquefaciens and is supplied as a liquid. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. α-amylase from bacillus amy...ng sugars, which are then used for ethanol fermentation by saccharomyces cerevisiae fncc 3012. the enzyme catalyzes amylolysis of gelatinised waxy maize starch to produce reducing sugars. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Mole weight: 55 kDa. Activity: > 250 units/g. Form: liquid. Source: Bacillus amyloliquefaciens. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0741. | |
| Native Bacillus amyloliquefaciens Protease | Bacterial protease produced by submerged fermentation of a selected strain of Bacillus amyloliquefaciens. Secretion of protease by Bacillus amyloliquefaciens can be inhibited by treatment with the fatty acid synthetase inhibitor cerulenin. Bacterial protease produced by submerged fermentation of a selected strain of bacillus amyloliquefaciens. secretion of protease by bacillus amyloliquefaciens can be inhibited by treatment with the fatty acid synthetase inhibitor cerulenin. Applications: Protease from bacillus amyloliquefaciens has been used for the unhairing of hides and skins. it has also been used in a study to investigate peptide bond formation using the carbamoylmethyl ester as the acyl donor. Group: Enzymes. Synonyms: Protease; Neutrase. CAS No. 9001-92-7. Protease. Form: liquid, > 0.8 U/g. Source: Bacillus amyloliquefaciens. Protease; Neutrase. Cat No: NATE-0632. | |
| Native Bacillus cereus β-lactamase Blend | β--lactamase inactivates β-lactam antibiotics by breaking open the β-lactam ring. Applications: Useful for assaying penicillins and cephalosporins. Group: Enzymes. Synonyms: β-lactamase; penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase; EC 3.5.2.6; 9073-60-3. Enzyme Commission Number: EC 3.5.2.6. CAS No. 9073-60-3. β-Lactamase. Storage: at -20°C. Ok to freeze. Form: Lyophilized Powder. Source: Bacillus cereus 569/H9. β-lactamase; penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase; EC 3.5.2.6; 9073-60-3. Cat No: NATE-1628. | |
| Native Bacillus cereus L-Leucine Dehydrogenase | In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction:L-leucine + H2O + NAD+<-> 4-methyl-2-oxopentanoate + NH3 + NADH + H+. The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis. Group: Enzymes. Synonyms: leucine dehydrogenase; L-leucine dehydrogenase; L-leucine:NAD+ oxidoreductase (deaminating); LeuDH; EC 1.4.1.9; 9082-71-7. Enzyme Commission Number: EC 1.4.1.9. CAS No. 9082-71-7. Leucine dehydrogenase. Activity: 60-120 units/mg protein (Lowry). Storage: -20°C. Form: lyophilized powder. Source: Bacillus cereus. leucine dehydrogenase; L-leucine dehydrogenase; L-leucine:NAD+ oxidoreductase (deaminating); LeuDH; EC 1.4.1.9; 9082-71-7. Cat No: NATE-0391. | |
| Native Bacillus cereus Penicillinase | Penicillinase specifically catalyzes the hydrolysis of β-lactam ring of penicillin. Applications: Used in the production of penicillin. Group: Enzymes. Synonyms: EC 3.5.2.6; β-lactamase; penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase; 9073-60-3. Enzyme Commission Number: EC 3.5.2.6. CAS No. 9073-60-3. Mole weight: Mr ~30 kDa. Storage: -20°C. Source: Bacillus cereus. EC 3.5.2.6; β-lactamase; penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase; 9073-60-3. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0542. | |
| Native Bacillus cereus Phospholipase C | Phospholipase C is an enzyme with system name phosphatidylcholine cholinephosphohydrolase. This enzyme catalyses the following chemical reaction: a phosphatidylcholine + H2O<-> 1, 2-diacyl-sn-glycerol + phosphocholine. The bacterial enzyme is a zinc protein. It also acts on sphingomyelin and phosphatidylinositol. Native phospholipase c (ec 3.1.4.3) was purified from bacillus cereus. Applications: Useful for enzymatic determination of lecithin. Group: Enzymes. Synonyms: Phospholipase C; EC 3.1.4.3; lipophosphodiesterase I; Clostridium welchii alpha-toxin; Clostridium oedematiens beta-and gamma-toxins; lipophosphodiesterase C; phosphatidase C; heat-labile hemolysin; alpha-toxin. Enzyme Commission Number: EC 3.1.4.3. CAS No. 9001-86-9. Phospholipase C. Activity: > 30 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: Bacillus cereus. Phospholipase C; EC 3.1.4.3; lipophosphodiesterase I; Clostridium welchii alpha-toxin; Clostridium oedematiens beta-and gamma-toxins; lipophosphodiesterase C; phosphatidase C; heat-labile hemolysin; alpha-toxin. Cat No: DIA-163. | |
| Native Bacillus cereus 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. Applications: Sphingomyelinase has been used in a study to assess the interaction of actin with the hiv-1 accessory protein nef. sphingomyelinase has also been used in a study to investigate x-ray scattering as a quality-control tool for liposomal drug-delivery systems. 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 units/mg protein. Storage: 2-8°C. Form: Type I, buffered aqueous glycerol solution, Solution in 50% glycerol containing 50 mM Tris-HCl, pH 7.5; Type II, Lyophilized powder containing potassium phosphate buffer salts and stabilizer. Source: Bacillus cereus. Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; SMase. Cat No: NATE-0672. | |
| Native Bacillus circulans β-Galactosidase | β-Galactosidase (EC 3.2.1.23) preparation derived from Bacillus circulans. The enzyme catalyzes the hydrolysis of lactose and the galactosyl transfer reaction. In the galactosyl transfer reaction, it is advantageous to react at high temperature because of the low solubility of lactose. Group: Enzymes. Synonyms: β-Galactosidase; beta-gal; β-gal; GLB; 9031-11-2; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Enzyme Commission Number: EC 3.2.1.23. CAS No. 9031-110-2. β-gal. Activity: > 4,000 unit/g. Appearance: Yellow-light brown, powder. Storage: store under cool and dry condition. Source: Bacillus circulans. β-Galactosidase; beta-gal; β-gal; GLB; 9031-11-2; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Pack: 5 kg, powder. Cat No: NATE-1745. | |
| Native Bacillus fastidiosus Uricase | The enzyme urate oxidase (UO), or uricase or factor-independent urate hydroxylase, absent in humans, catalyzes the oxidation of uric acid to 5-hydroxyisourate: Uric acid + O2 + H2O ? 5-hydroxyisourate + H2O2 ? allantoin + CO2. Urate:oxygen oxidoreductase produced in microorganism has a molecular mass of approximately 34 kda. Group: Enzymes. Synonyms: urate oxidase; uric acid oxidase; uricase; uricase; urate: oxygen oxidoreductase; EC 1.7.3.3; uricase II; UO. Enzyme Commission Number: EC 1.7.3.3. CAS No. 9002-12-4. UO. Activity: 15 U/mg. Appearance: White to off-white powder. Storage: -20°C. Form: Freeze dried powder. Source: Bacillus fastidiosus. urate oxidase; uric acid oxidase; uricase; uricase; urate: oxygen oxidoreductase; EC 1.7.3.3; uricase II; UO. Cat No: DIA-173. | |
| Native Bacillus licheniformis Alkaline Protease | Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Subtilisin a is a member of the serine s8 endoproteinase family. it has broad specificity with a preference for a large uncharged residue in the p1 position. it hydrolyzes native and denatured proteins, and is active under alkaline conditions. Applications: The enzyme has been used to optimize release of all mitochondrial populations from homogenized ventricular tissue of rat heart.1 it has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax...ex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; triCorn proteinase; triCorn protease; EC 3.4.25.1. Enzyme Commission Number: EC 3.4.25.1. CAS No. 140879-24-9. Alkaline Protease. Mole weight: 27 Kda. Activity: 7.0-14.0 units/mg. Form: lyophilized powder. Source: Bacillus licheniformis. ingensin; macropain; multicatalytic endopeptidase complex; prosome; multicatalytic proteinase (complex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; triCorn proteinase; triCorn protease; EC 3.4.25.1. Cat No: NATE-0444. | |
| Native Bacillus licheniformis α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. this product is from bacillus licheniformis and is type xii-a. α-amylase, from creative enzymes, has been used in various plant studies, such as metabolism studies in arabidopsis. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Activity: Type XII-A, saline solution, > 500 units/mg protein (biuret); Type B, liquid. Source: Bacillus licheniformis. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0742. | |
| Native Bacillus licheniformis Keratinase (feed grade) | Keratinase is a particular class of extracellular proteolytic inducible enzyme with the capability of degrading insoluble keratin substrates. It is important for hydrolyzing hair, feather, and collagen in sewage system during waste water treatment. It is also useful in food industry, animal feed preparation etc. Insoluble feather keratin from poultry industry may be converted by enzymatic hydrolysis to glues, feedstuffs, fertilizers, films or used for the production of rare amino acids serine, cysteine and proline. Group: Enzymes. Synonyms: KerA; Keratinolytic protease; EC 3.4.21. Enzyme Commission Number: EC 3.4.21. Keratinase. Form: Powder. Source: Bacillus licheniformis. Keratinase; KerA; Keratinase from Bacillus licheniformis; Keratinolytic protease; EC 3.4.21. Cat No: FEED-0001. | |
| Native Bacillus licheniformis NADH Oxidase | NADH Oxidase from Bacillus licheniformis was shown to display hydrogen peroxide-forming activity. Nadh oxidase is a surface enzyme with increased oxidative activity in polymorphonuclear leukocytes during phagocytosis. Applications: Nadh oxidase from bacillus licheniformis has been used in a study to assess nitrogen assimilation by bacillus licheniformis growing in chemostat cultures. it has also been used in a study to investigate the role of glutamate dehydrogenase in ammonia assimilation in bacillus macerans. Group: Enzymes. Synonyms: NADH Oxidase; 9032-21-7. CAS No. 9032-21-7. NADH Oxidase. Activity: > 35 units/mg protein. Form: lyophilized powder. Source: Bacillus licheniformis. NADH Oxidase; 9032-21-7. Pack: vial of > 15 units. Cat No: NATE-0473. | |
| Native Bacillus licheniformis Protease | Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Protease is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. It is active in some organic solvents such as dry octane. The enzyme is found to be stable at ph 8-10, retaining activity of up to 90% for 24 hours. it shows maximum activity at temperatures between 55-60°c. Applications: The product has been used with other enzymes for in situ proteolysis to produce crystals suitable for structure determi...f bacillus licheniformis. it is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. Group: Enzymes. Synonyms: Protease; 9014-01-1; Subtilisin A; EC 3.4.21.62; Alcalase. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9001-92-7. Protease. Mole weight: Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 KDa. Activity: Type VIII, 7-15 units/mg solid; Type I, > 2.4 U/g. Form: Type VIII, lyophilized powder; Type I, aqueous solution. Source: Bacillus licheniformis. Protease; 9014-01-1; Subtilisin A; EC 3.4.21.62; Alcalase. Cat No: NATE-0633. | |
| Native Bacillus licheniformis Proteinase | Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 kda. Applications: The enzyme from creative enzymes has been used to optimize release of all mit ochondrial populations from homogenized ventricular tissue of rat heart. it has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax-embedded liver specimens for detecting human and viral dna. this is a proteolytic enzyme isolated from th...ls to study the silencing of cardiac mit ochondrial nhe1. Group: Enzymes. Synonyms: protease; peptidase; proteinase; EC 3.4.21.62; 9014-01-1; Alkaline Protease; Protease from Bacillus licheniformis; Proteinase from Bacillus licheniformis; Subtilo peptidase A. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9001-92-7. Purity: crystallization. Proteinase. Mole weight: 27 KDa. Activity: 7.0-14.0 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Bacillus licheniformis. protease; peptidase; proteinase; EC 3.4.21.62; 9014-01-1; Alkaline Protease; Protease from Bacillus licheniformis; Proteinase from Bacillus licheniformis; Subtilo peptidase A. Cat No: NATE-0639. | |
| Native Bacillus megaterium Diaphorase (NADH) | In enzymology, a NADPH dehydrogenase is an enzyme that catalyzes In enzymology, a NAD (P)H dehydrogenase (quinone) (EC 1.6.5.2) is an enzyme that catalyzes the chemical reaction NAD (P)H + H+ + a quinone<-> NAD (P)+ + a hydroquinone. The 4 substrates of this enzyme are NADH, NADPH, H+, and quinone, whereas its 3 products are NAD+, NADP+, and hydroquinone. Native diaphorase (ec 1.6.5.2) was purified from bacillus megaterium. Applications: Useful for enzymatic determination of reduced nad. Group: Enzymes. Synonyms: EC 1.6.99.3; cytochrome c reductase; type 1 dehydrogenase; beta-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydr. Enzyme Commission Number: EC 1.6.99.3. CAS No. 9079-67-8. Diaphorase. Activity: 30-60 U/mg. Appearance: Yellow dried powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus megaterium. EC 1.6.99.3; cytochrome c reductase; type 1 dehydrogenase; beta-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine dinucleotide dehydrogenase; diphosphopyridine diaphorase; DPNH diaphorase; NADH diaphorase; NADH hydrogenase; NADH oxidoreductase; NADH-menadione oxidoreductase; reduced diphosphopyridine nucleotide diaphorase; Beta-NADH dehydrogenase dinucleotide. Cat No: DIA-142. | |
| Native Bacillus polymyxa Dispase | Dispase is a protease which cleaves fibronectin, collagen IV, and to a lesser extent collagen I. It is found in some bacteria and can be isolated from culture filtrates of Bacillus polymyxa. It can be extracted, purified, and used in research. It can be particularly useful to separate embryonic epithelia and mesenchyme. Dispase II is specific for the cleavage of Leucine-Phenylalanine bonds. Dispase is often used to digest adhering primary cells in culture, since this treatment turned out to be milder than trypsin digestion. Applications: Dispase is a protease which cleaves fibronectin, collagen iv, and to a lesser extent collagen i. it is found in some bacteria and can be iso...d used in research. it can be particularly useful to separate embryonic epithelia and mesenchyme. dispase ii is specific for the cleavage of leucine-phenylalanine bonds. dispase is often used to digest adhering primary cells in culture, since this treatment turned out to be milder than trypsin digestion (sinclair et al., 2013). a recent article also finds that dispase can digest serine-phenylalanine. Group: Enzymes. Synonyms: Dispase; 42613-33-2; Proteinase; Bacillus polymyxa neutral. CAS No. 42613-33-2. Dispase. Activity: ~0.4 unit/mg solid. Storage: 2-8°C. Form: powder. Source: Bacillus polymyxa. Dispase; 42613-33-2; Proteinase; Bacillus polymyxa neutral. Cat No: NATE-0193. | |
| Native Bacillus polymyxa Dispase I | Dispase I is a rapid, effective, gentle and neutral protease that can separate intact epidermis from the dermis. It can also separate intact epithelial sheets in culture from the substratum. The enzyme preserves the viability of the epithelial cells while cleaving the basement membrane zone region. It can also be used to prevent clumping in suspension cultures. This protease cleaves fibronectin and type IV collagen, but not laminin, type V collagen, serum albumin, or transferrin. It hydrolyzes N-terminal peptide bonds of non-polar amino acid residues. It preferentially attacks denatured and intercellular proteins with exposed hydrophobic amino acid residues. Ca2+, Mg2+, Mn2+...e i has also been used in a study to investigate a dityrosine-based substrate for a protease assay. dispase i has been used in lung digestion and processing for flow staining, as well as for cd4 cell isolation in mice. the enzyme has also been used to digest excised wounds and a small amount of surrounding skin for the detection of gfp+ (green fluorescence protein) cells. this study to investigated the effect of differentiation and angiogenesis of bone marrow-derived mesenchymal stem cells on wound healing. it has also been used to remove the epidermis during the isolation of dermal fibroblasts from mice. Group: Enzymes. Synonyms: Dispase I; Dispase; 42613-33-2; Protease fro | |
| Native Bacillus polymyxa Dispase II | Dispase II is a neutral protease that hydrolyzes the N-terminal peptide bonds of non-polar amino acid residues. It may be used for separating many tissues and cells grown in vitro. The enzyme is very gentle and does not damage cell membranes. It can also be used to prevent clumping in suspension cultures. This protease cleaves fibronectin and type IV collagen, but not laminin, type V collagen, serum albumin, or transferrin. Dispase II is specific for the cleavage of Leucine-Phenylalanine bonds. Ca2+, Mg2+, Mn2+, Fe2+, Fe3+ and Al3+ activate the enzyme. EDTA, EGTA, Hg2+ and other heavy metals inhibit the enzyme activity. The enzyme contains 1g-atom of zinc per g-mol of purif... it has been used in the treatment of rat heart pieces during the isolation of mitochondria from rat heart. it has also been used for the isolation of dental pulp stem cells (dpscs) by enzymatic hydrolysis. these cells have been compared with dpscs isolated by explant method to analyse their stem cell and differentiation properties. Group: Enzymes. Synonyms: Dispase II; Dispase; 42613-33-2; Protease from Bacillus polymyxa. CAS No. 42613-33-2. Dispase. Activity: > 0.5 units/mg solid. Storage: 2-8°C. Form: lyophilized powder containing calcium acetate and milk sugar. Source: Bacillus polymyxa. Dispase II; Dispase; 42613-33-2; Protease from Bacillus polymyxa. Cat No: NATE-0192. | |
| Native Bacillus polymyxa Neutral Protease (Dispase) | Neutral protease (Dispase) is a non-mammalian animal origin free (AOF) metallo, neutral protease. Its mild proteolytic action makes the enzyme especially suitable for the preparation of primary cells and secondary (subcultivation) cell culture, since it is gentle on cell membranes. This protease is also used as a secondary enzyme in cell isolation and tissue dissociation applications, commonly used with collagense. Chromatographically purified. a lyophilized powder. Applications: Tissue disaggregation and subcultivation; prevention of unwanted cell clumping; preparation of cells for culture; separation of intact epidermis from dermis and intact epithelial sheet in c...se; Neutral Protease (Dispase). Enzyme Commission Number: EC 3.4.24.28. CAS No. 9001-92-7. Purity: Chromatographically purified. Neutral Protease. Mole weight: 32.5 kDa. Activity: > 4 units per mg dry weight. Stability: Stable at 2-8°C for 12 months. Aliquot and Store at -20°C after reconstitution with water or commonly used balanced salt solutions or media. Storage: Store at 2-8°C. Form: lyophilized powder. Source: Bacillus polymyxa. Bacillolysin; EC 3.4.24.28; Bacillus metalloendopeptidase; Bacillus subtilis neutral proteinase; anilozyme P 10; Bacillus metalloproteinase; Bacillus neutral proteinase; megateriopeptidase; Neutral Protease (Dispase). Cat No: NATE-0482. | |
| Native Bacillus pumilus Bilirubin Oxidase/Laccase | In enzymology, a bilirubin oxidase (EC 1.3.3.5) is an enzyme that catalyzes the chemical reaction 2 bilirubin + O2<-> 2 biliverdin + 2 H2O. Thus, the two substrates of this enzyme are bilirubin and O2, whereas its two products are biliverdin and H2O. This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in porphyrin and chlorophyll metabolism. Group: Enzymes. Synonyms: bilirubin oxidase M-1; EC 1.3.3.5; 80619-01-8; Bilirubin:oxygen oxidoreductase; Bilirubin Oxidase. Purity: ~ 90% (SDS PAGE). Bilirubin Oxidase. Mole weight: 61 kDa. Storage: at -20°C. Form: Lyophilized powder. Source: Bacillus pumilus. bilirubin oxidase M-1; EC 1.3.3.5; 80619-01-8; Bilirubin:oxygen oxidoreductase; Bilirubin Oxidase. Cat No: NATE-1257. | |
| Native Bacillus sp. Amylase, Maltogenic | Glucan 1,4-alpha-maltohydrolase (EC 3.2.1.133, maltogenic alpha-amylase, 1,4-alpha-D-glucan alpha-maltohydrolase) is an enzyme with system name 4-alpha-D-glucan alpha-maltohydrolase. This enzyme catalyses the following chemical reaction:hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains. This enzyme acts on starch and related polysaccharides and oligosaccharides. Applications: Maltogenic amylases (mase) are commonly used in the starch industry. they are used to hydrolyze starch, pullulan and cyclodextrin and to make novel carbohydrates. Group: Enzymes. Synonyms: Glucan 1,4-alpha-maltohydrolase; EC 3.2.1.133; maltogenic alpha-amylase; 1,4-alpha-D-glucan alpha-maltohydrolase; Glucan 1,4-α-maltohydrolase, Maltogenic Amylase, Novamyl 1000BG. Enzyme Commission Number: EC 3.2.1.133. CAS No. 160611-47-2. α-Amylase. Storage: 2-8°C. Source: Bacillus sp. Glucan 1,4-alpha-maltohydrolase; EC 3.2.1.133; maltogenic alpha-amylase; 1,4-alpha-D-glucan alpha-maltohydrolase; Glucan 1,4-α-maltohydrolase, Maltogenic Amylase, Novamyl 1000BG. Cat No: NATE-0074. | |
| Native Bacillus sp Chitosanase | Chitosanase is a powdered chitosanase preparation made by submerged fermentation of a selected strain of the bacterium Bacillus sp. The enzyme catalyzes the breakdown of chitosan, a partially or completely de-acetylated derivative of chitin (β-1,4 homopolymer of N-acetyl glucosamine). Applications: Chitosanase can be used for hydrolyzing chitosan(degree of de-acetylatin: 40?100%). especially, it can be used for the production of chitosan oligosaccharides from chitosan, which have a variety of biological activities such as immuno-stimulating activity, anti-tumor activity, anti-microbial activity, etc. 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. Mole weight: 45,000Da estimated by SDS-PAGE. Activity: 35,000U/g. Appearance: White or light yellow colored, freeze-dried powder. Storage: The product should be stored in a cool, dry environment with temperatures below 4°C. Source: Bacillus sp. Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase. Cat No: NATE-1746. | |
| Native Bacillus sp. 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). Native glucose-6-phosphate dehydrogenase (ec 1.1.1.49) was purified from bacillus sp. Applications: Useful for enzymatic determination of glucose or atp when coupled with hexokinase. Group: Enzymes. Synonyms: Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosph. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Mole weight: 104 kDa dalton (two subunits of approx. 55 kDa). Activity: > 200 U/mg. Appearance: White/off white powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus sp. Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; GPD. Cat No: DIA-143. | |
| Native Bacillus sp. Glutamine synthetase | Glutamine synthetase (GS) (EC 6.3.1.2) is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine: Glutamate + ATP + NH3 ? Glutamine + ADP + phosphate. Glutamine Synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration. The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites. Native glutamine synthetase (ec 6.3.1.2) was purified from bacillus sp. Applications: Useful for the determination of ammonia and atp in clinical analysis. Group: Enzymes. Synonyms: Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase. Enzyme Commission Number: EC 6.3.1.2. CAS No. 9023-70-5. GS. Activity: > 15 U/mg. Appearance: White to pale brown powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus sp. Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase. Cat No: DIA-155. | |
| Native Bacillus sphaericus 12α-Hydroxysteroid Dehydrogenase | In enzymology, a 12alpha-hydroxysteroid dehydrogenase (EC 1.1.1.176) is an enzyme that catalyzes the chemical reaction:3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + NADP+<-> 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate + NADPH + H+. Thus, the two substrates of this enzyme are 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate and NADP+, whereas its 3 products are 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme is involved in a metabolic pathway that degrades bile acids into cholesterol. Group: Enzymes. Synonyms: EC 1.1.1.176; 61642-40-8; 12α Hydroxysteroid Dehydrogenase; 12alpha-hydroxy steroid dehydrogenase; NAD+-dependent. Enzyme Commission Number: EC 1.1.1.176. CAS No. 61642-40-8. 12α-Hydroxysteroid Dehydrogenase. Activity: 150-350 units/mg protein (Lowry). Storage: -20°C. Form: lyophilized powder. Source: Bacillus sphaericus. EC 1.1.1.176; 61642-40-8; 12α Hydroxysteroid Dehydrogenase; 12alpha-hydroxy steroid dehydrogenase; NAD+-dependent 12alpha-hydroxysteroid dehydrogenase; NADP+-12alpha-hydroxysteroid dehydrogenase; 12-α-Hydroxysteroid Dehydrogenase; 12alpha-hydroxysteroid:NADP+ 12-oxidoreductase. Cat No: NATE-0001. | |
| Native Bacillus sp. 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-phosphotransferase. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Hexokinase. Mole weight: 68 kDa (gel filtration). Activity: More than 250 U/mg solid. Appearance: White amorphous powder, lyophilized. Storage: Storage at -20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Bacillus sp. hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase; EC 2.7.1.1. Cat No: NATE-1157. | |
| Native Bacillus sp. Leucine dehydrogenase | In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction: L-leucine + H2O + NAD+ <-> 4-methyl-2-oxopentanoate + NH3 + NADH + H+. The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis. Applications: This enzyme is useful for enzyme determination of l-leucine and the activity of leucine amino-peptidase. Group: Enzymes. Synonyms: EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH. Enzyme Commission Number: EC 1.4.1.9. CAS No. 9082-71-7. Leucine dehydrogenase. Mole weight: 245 kDa. Activity: Grade? 20U/mg-solid or more (containing approx. 70% of stabilizers). Stability: Stable at-20°C for at least one year. Appearance: White amorphous powder, lyophilized. Source: Bacillus sp. EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH. Cat No: DIA-209. | |
| Native Bacillus sp. Monoglyceride Lipase | In enzymology, an acylglycerol lipase (EC 3.1.1.23) is an enzyme that catalyzes a chemical reaction that uses water molecules to break the glycerol monoesters of long-chain fatty acids. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. This enzyme participates in glycerolipid metabolism. Is an enzyme produced by microorganisms. this product shall be used for a diagnostics reagent. Applications: Useful for enzymatic determiantion of triglyceride. Group: Enzymes. Synonyms: EC 3.1.1.23; acylglycerol lipase; glycerol-ester acylhydrolase; monoacylglycerol lipase; monoacylglycerolipase; monoglyceride lipase; monoglyceride hydrolase; fatty acyl monoester lipase; monoacylglycerol hydrolase; monoglyceridyllipase; monoglyceridase. Enzyme Commission Number: EC 3.1.1.23. CAS No. 9040-75-9. Monoglyceride lipase. Mole weight: 20 kDa (gel filtration). Activity: > 20 U/mg. Appearance: White powder. Storage: Storage at-20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Bacillus sp. EC 3.1.1.23; acylglycerol lipase; glycerol-ester acylhydrolase; monoacylglycerol lipase; monoacylglycerolipase; monoglyceride lipase; monoglyceride hydrolase; fatty acyl monoester lipase; monoacylglycerol hydrolase; monoglyceridyllipase; monoglyceridase. Cat No: NATE-0455. | |
| Native Bacillus sp. Purine Nucleoside Phosphorylase | Purine nucleoside phosphorylase (also known as PNPase) is an enzyme (EC 2.4.2.1) involved in purine metabolism. PNP metabolizes adenosine into adenine, inosine into hypoxanthine, and guanosine into guanine, in each case creating ribose phosphate. NP encodes the enzyme purine nucleoside phosphorylase that together with adenosine deaminase (ADA) serves a key role in purine catabolism, referred to as the salvage pathway. Mutations in either enzyme result in a severe combined immunodeficiency (SCID). Confusingly, the same abbreviation (PNPase), is also used for another, otherwise unrelated, enzyme, namely Polynucleotide Phosphorylase. Purine nucleoside phosphorylase produced in microorganism has a molecular mass of 32 kda. Applications: Useful for enzymatic determination of inorganic phosphate. Group: Enzymes. Synonyms: inos. Enzyme Commission Number: EC 2.4.2.1. CAS No. 9030-21-1. PNPase. Activity: > 500U/mL. Appearance: Colourless to light brown solution. Storage: -20°C. Form: Liquid. Source: Bacillus sp. inosine phosphorylase; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase; purine ribonucleoside phosphorylase; purine-nucleoside: phosphate ribosyltransferase; EC 2.4.2.1. Cat No: DIA-164. | |
| Native Bacillus sp. Pyroglutamate Aminopeptidase | Pyroglutamate aminopetidase is an enzyme that digests proteins. Applications: Pyroglutamate aminopetidase is used to digest proteins for subsequent analysis, such as amino acid sequencing. pyroglutamate aminopeptidase is used to hydrolyze and activate various prodrugs. 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. Enzyme Commission Number: EC 3.4.19.3. CAS No. 9075-21-2. Pyrase. Activity: > 0.11 units/mg protein. Storage: -20°C. Source: Bacillus sp. 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-0647. | |
| Native Bacillus sp. Sarcosine Oxidase | Sarcosine oxidase is an enzyme (EC 1.5.3.1) that catalyzes the oxidative demethylation of sarcosine to yield glycine, H2O2, 5,10-CH2-tetrahydrofolate in a reaction requiring H4-tetrahydrofolate and oxygen. Corynebacterial sarcosine oxidase is a heterotetramer and is produced as an inducible enzyme when Corynebacterium sp.is grown with sarcosine as source of carbon and energy. Monomeric sarcosine oxidase (msox) is a flavoenzyme that catalyzes the oxidative demethylation of sarcosine (n-methylglycine) to yield glycine, formaldehyde, and hydrogen peroxide. monomeric sarcosine oxidase can oxidize other secondary amino acids such as n-methyl-l-alanine, n-ethylglycine, and l-proline. Applications: Sarcosine oxidase has been used in a study as part of a multienzyme cascade, that when immobilized constructed amperometric biosensors. sarcosine oxidase has also been used in a study to investigate oxidation of amines by flavoproteins. Group: Enzymes. Synonyms: Sarcosine oxidase; EC 1.5.3.1; 9029-22-5; sarcosine:oxygen oxidoreductase (demethylating). Enzyme Commission Number: EC 1.5.3.1. CAS No. 9029-22-5. SAO. Activity: 25-50 units/mg solid. Storage: -20°C. Form: lyophilized powder; No stabilizers added. Source: Bacillus sp. Sarcosine oxidase; EC 1.5.3.1; 9029-22-5; sarcosine:oxygen oxidoreductase (demethylating). Cat No: NATE-0664. | |
| Native Bacillus sp. Uricase | The enzyme urate oxidase (UO), or uricase or factor-independent urate hydroxylase, absent in humans, catalyzes the oxidation of uric acid to 5-hydroxyisourate: Uric acid + O2 + H2O ? 5-hydroxyisourate + H2O2 ? allantoin + CO2. Applications: This enzyme is useful for enzymatic determination of uric acid in clinical analysis. Group: Enzymes. Synonyms: urate oxidase; uric acid oxidase; uricase; uricase; urate: oxygen oxidoreductase; EC 1.7.3.3; uricase II. UO. Mole weight: approx.150,000. Activity: Grade? 1.5U/mg-solid or more. Stability: Stable at -20°C for at least 6 months. Appearance: White amorphous powder, lyophilized. Source: Bacillus sp. urate oxidase; uric acid oxidase; uricase; uricase; urate: oxygen oxidoreductase; EC 1.7.3.3; uricase II. Cat No: DIA-276. | |
| Native Bacillus stearothermophilius NAD Synthetase | In enzymology, a NAD+ synthase (EC 6.3.1.5) is an enzyme that catalyzes the chemical reaction:ATP + deamido-NAD+ + NH3<-> AMP + diphosphate + NAD+. The 3 substrates of this enzyme are ATP, deamido-NAD+, and NH3, whereas its 3 products are AMP, diphosphate, and NAD+. This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). This enzyme participates in nicotinate and nicotinamide metabolism and nitrogen metabolism. Is an enzyme produced by microorganisms. this product shall be used for a diagnostics reagent. Applications: Useful for enzymatic determination of atp, ammonia, urea or creatinine. it is also suitable for enzymatic cycling method. Group: Enzymes. Synonyms: EC 6.3.1.5; 9032-69-3; NAD+ synthetase; NAD+ synthase; nicotinamide adenine dinucleotide synthetase; diphosp. Enzyme Commission Number: EC 6.3.1.5. CAS No. 9032-69-3. NAD Synthetase. Mole weight: 50 kDa (gel filtration); 25 kDa (SDS-PAGE). Activity: > 1 U/mg. Appearance: White powder. Storage: Storage at-20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Bacillus stearothermophilius. EC 6.3.1.5; 9032-69-3; NAD+ synthetase; NAD+ synthase; nicotinamide adenine dinucleotide synthetase; diphosphopyridine nucleotide synthetase. Cat No: NATE-0471. | |
| Native Bacillus stearothermophilus Acetate Kinase | In molecular biology, acetate kinase (EC 2.7.2.1), which is predominantly found in micro-organisms, facilitates the production of acetyl-CoA by phosphorylating acetate in the presence of ATP and a divalent cation. Short-chain fatty acids (SCFAs) play a major role in carbon cycle and can be utilized as a source of carbon and energy by bacteria. The enzyme is important in the process of glycolysis, enzyme levels being increased in the presence of excess glucose. The growth of a bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme is involved in excretion of excess carbohydRate. A related enzyme, butyRate kinase, ... acetate kinase from creative enzymes. this [32p]-acetyl phosphate was used to label bldm, bldm d-54n or bldm d-54a loci during the study of the effect of bldm gene on streptomyces coelicolor development. Group: Enzymes. Synonyms: Acetate kinase (phosphorylating); Acetic kinase; Acetokinase; EC 2.7.2.1; 9027-42-3; Acetate kinase. Enzyme Commission Number: EC 2.7.2.1. CAS No. 9027-42-3. Acetate kinase. Activity: 400-1,200 units/mg solid. Storage: 2-8°C. Form: lyophilized powder. Contains potassium phosphate buffer. Source: Bacillus stearothermophilus. Acetate kinase (phosphorylating); Acetic kinase; Acetokinase; EC 2.7.2.1; 9027-42-3; Acetate kinase. Cat No: NATE-0016. | |
| Native Bacillus stearothermophilus Alanine Dehydrogenase | L-Alanine dehydrogenase is a stereospecific dehydrogenase that catalyzes the reversible deamination of L-alanine to pyruvate and ammonium. It is important for the generation of pyruvate during sporulation. Applications: The enzyme is useful for determination of l-alanine. Group: Enzymes. Synonyms: L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. Mole weight: ca. 230,000; Subunit molecular weight : ca. 38,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Bacillus stearothermophilus. L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Cat No: NATE-1899. | |
| Native Bacillus stearothermophilus Alanine Racemase | Alanine racemase is involved in alanine, aspartate and D-alanine metabolism. 3-Fluoro-D-alanine and D-Cycloserine are known to inhibit alanine racemase. Alanine racemase monomer is composed of two domains, an eight-stranded α/β barrel at the N-terminus and a C-terminal domain. The N-terminus includes residues 1-240, whereas the C-terminal comprises of the β-strand (residues 241-388). One molecule of pyridoxalphosphate (PLP) is present as the cofactor in each subunit. Applications: Alanine racemase is used to convert l-alanine into d-alanine. alanine racemase, from creative enzymes, has been used to isomerize l-[u-14c]alanine to a racemic mixture of l/d-[14c]alanine. Group: Enzymes. Synonyms: Alanine Racemase; EC 5.1.1.1; 9024-06-0; L-alanine racemase. Enzyme Commission Number: EC 5.1.1.1. CAS No. 9024-06-0. Alanine Racemase. Mole weight: Mr 78 kDa (2 subunits 39 kDa each). Activity: > 10 Iunits/mg solid. Storage: -20°C. Form: lyophilized powder. Lyophilized from 50 mM phosphate buffer, pH 7.5. Source: Bacillus stearothermophilus. Alanine Racemase; EC 5.1.1.1; 9024-06-0; L-alanine racemase. Cat No: NATE-0045. | |
| Native Bacillus stearothermophilus Diaphorase 1 | Diaphorase catalyzes the reaction of a reduced di- or tri-phosphopyridine nucleotide hydrogen donor with a hydrogen acceptor, usually a dye in the leucoform. Applications: The enzyme is useful for the measurement of various dehydrogenase reactions in visible spectral range. Group: Enzymes. Synonyms: Diaphorase 1; Di-1; EC 1.6.99 -. Enzyme Commission Number: EC 1.6.99.-. Diaphorase. Mole weight: ca. 30,000. Appearance: Lyophilized. Storage: Stable at -20 to 5 °C for at least one year. Source: Bacillus stearothermophilus. Diaphorase 1; Di-1; EC 1.6.99 -. Cat No: NATE-1901. | |
| Native Bacillus stearothermophilus 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; esterase A; se. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 0.2 units/mg. Storage: 2-8°C. Source: Bacillus stearothermophilus. 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-0234. | |
| Native Bacillus stearothermophilus Fructose-6-phosphate Kinase | Fructose-1,6-bisphosphatase (FBP) is an important enzyme in glucose metabolism. It catalyzes the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate. Fructose-6-phosphate kinase converts fructose-6-phosphate into fructose 1,6-bisphophate in the rate limiting step of the glycolysis cycle. Bacillus stearothermophilus phosphofructokinase (bspfk) is a homotetramer that is allosterically inhibited by phosphoenolpyruvate (pep), which binds along one dimer-dimer interface. Applications: Fructose-6-phosphate kinase from bacillus stearothermophilus was shown to interact with neuronal nitric oxide synthase (nnos) causing a defect in glycolytic metabolism and increased fatigability in dystrophic muscle. Group: Enzymes. Sy. Enzyme Commission Number: EC 2.7.1.11. CAS No. 9001-80-3. FBP. Activity: > 50 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing phosphate buffer salt. Source: Bacillus stearothermophilus. EC 2.7.1.11; phosphohexokinase; phosphofructokinase I; phosphofructokinase (phosphorylating); 6-phosphofructose 1-kinase; ATP-dependent phosphofructokinase; D-fructose-6-phosphate 1-phosphotransferase; fructose 6-phosphate kinase; fructose 6-phosphokinase; nucleotide triphosphate-dependent phosphofructokinase; phospho-1,6-fructokinase; PFK; 9001-80-3. Cat No: NATE-0252. | |
| Native Bacillus stearothermophilus Glucokinase | Glucokinase (EC 2.7.1.2) is an enzyme that facilitates phosphorylation of glucose to glucose-6-phosphate. Glucokinase occurs in cells in the liver, pancreas, gut, and brain of humans and most other vertebrates. In each of these organs it plays an important role in the regulation of carbohydrate metabolism by acting as a glucose sensor, triggering shifts in metabolism or cell function in response to rising or falling levels of glucose, such as occur after a meal or when fasting. Mutations of the gene for this enzyme can cause unusual forms of diabetes or hypoglycemia. Group: Enzymes. Synonyms: EC 2.7.1.2; glucokinase; glucokinase (phosphorylating); 9001-36-9; GCK; FGQTL3; GK; GLK; HHF3; HK4; HKIV; HXKP; LGLK; MODY2. Enzyme Commission Number: EC 2.7.1.2. CAS No. 9001-36-9. GCK. Activity: > 300 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Bacillus stearothermophilus. EC 2.7.1.2; glucokinase; glucokinase (phosphorylating); 9001-36-9; GCK; FGQTL3; GK; GLK; HHF3; HK4; HKIV; HXKP; LGLK; MODY2. Cat No: NATE-0282. | |
| Native Bacillus stearothermophilus 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: > 75 units/mg protein (biuret). Storage: 2-8°C. Form: buffered aqueous solution; Stabilized solution in Tris buffer, pH 7.3. Source: Bacillus stearothermophilus. EC 2.7.1.30; glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase; 9030-66-4. Cat No: NATE-0286. | |
| Native Bacillus stearothermophilus 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. Applications: Inorganic pyrophosphatase (ppase) is a ubiquitous enzyme catalyzing the reaction ppi + h2o ? 2pi. it plays an important role in protein, rna, and dna synthesis. Group: Enzymes. Synonyms: Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Enzyme Commission Number: EC 3.6.1.1. CAS No. 9024-82-2. Inorganic pyrophosphatase. Activity: 15-25 units/mg protein (biuret). Storage: 2-8°C. Form: lyophilized powder. Source: Bacillus stearothermophilus. Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-0353. | |
| Native Bacillus stearothermophilus Leucine Dehydrogenase | In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction: L-leucine + H2O + NAD+ <-> 4-methyl-2-oxopentanoate + NH3 + NADH + H+. The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis. Applications: The enzyme is useful for determination of l-leucine, l-valine or l-isoleucine. Group: Enzymes. Synonyms: EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH. Enzyme Commission Number: EC 1.4.1.9. CAS No. 9082-71-7. Leucine dehydrogenase. Mole weight: ca. 300,000; Subunit molecular weight : ca. 49,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Bacillus stearothermophilus. EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH. Cat No: NATE-1905. | |
| Native Bacillus stearothermophilus Myokinase | Adenylate kinase (EC 2.7.4.3) (also known as ADK or myokinase) is a phosphotransferase enzyme that catalyzes the interconversion of adenine nucleotides, and plays an important role in cellular energy homeostasis. Myokinase is an enzyme that can be found in skeletal muscle and acts as a phosphotransferase agitator. Applications: Myokinase from bacillus stearothermophilus has been used in a study to assess its thermostability grown in a temperature range from 37 oc to 60 oc. Group: Enzymes. Synonyms: Adenylate kinase; EC 2.7.4.3; ADK; myokinase; 9013-02-9; Adenylic kinase; Adenylokinase. Enzyme Commission Number: EC 2.7.4.3. CAS No. 9013-2-9. Myokinase. Activity: > 150 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts, pH 8.5. Source: Bacillus stearothermophilus. Adenylate kinase; EC 2.7.4.3; ADK; myokinase; 9013-02-9; Adenylic kinase; Adenylokinase. Cat No: NATE-0036. | |
| Native Bacillus stearothermophilus Phosphofructokinase | Phosphofructokinase is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis. The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes. One enzyme that utilizes this reaction is phosphofructokinase (PFK), which catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the glycolytic pathway. PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains) and as an octomer in yeast (where there are 4 alpha-(PFK1) and 4 beta-chains (PFK2), the latter, like the mammalian monomers, possessing 2 ...cs reagent. Applications: Useful for enzymatic determiantion of fructose-6-phosphate. Group: Enzymes. Synonyms: PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Enzyme Commission Number: EC 2.7.1.11. CAS No. 9001-80-3. PFK. Mole weight: 72 kDa (gel filtration); 35 kDa (SDS-PAGE). Activity: > 250 U/mg. Appearance: White to pale yellow powder. Storage: Storage at-20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Bacillus stearothermophilus. PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Cat No: NATE-0551. | |
| Native Bacillus stearothermophilus Phosphoglucose isomerase | Glucose-6-phosphate isomerase is an enzyme that catalyzes the conversion of glucose-6-phosphate into fructose 6-phosphate in the second step of glycolysis. The human variant of this enzyme is encoded by the GPI gene. Native glucose-6-phosphate isomerase (ec 5.3.1.9) was purified from bacillus stearothermophilus. Group: Enzymes. Synonyms: Glucose-6-phosphate isomerase; phosphoglucose isomerase; phosphohexose isomerase; EC 5.3.1.9; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase. Enzyme Commission Number: EC 5.3.1.9. CAS No. 9001-41-6. PGI. Activity: > 250 U/mg. Appearance: White powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus stearothermophilus. Glucose-6-phosphate isomerase; phosphoglucose isomerase; phosphohexose isomerase; EC 5.3.1.9; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase. Cat No: DIA-162. | |
| Native Bacillus stearothermophilus Phosphotransacetylase | Phosphotransacetylase converts CoA to acetyl CoA. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. This enzyme participates in 3 metabolic pathways:taurine and hypotaurine metabolism, pyruvate metabolism, and propanoate metabolism. Applications: Phosphotransacetylase, from bacillus stearothermophilus, is used to convert coa to acetyl coa. phosphotransacetylase (pta) is used to study transport systems for acetate. it is used to study metabolic pathways in various bacterium. Group: Enzymes. Synonyms: phosphate acetyltransferase; phosphotransacetylase; phosphoacylase; PTA; EC 2.3.1.8; 9029-91-8. Enzyme Commission Number: EC 2.3.1.8. CAS No. 9029-91-8. PTA. Activity: > 3,000 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized powder containing potassium phosphate. Source: Bacillus stearothermophilus. phosphate acetyltransferase; phosphotransacetylase; phosphoacylase; PTA; EC 2.3.1.8; 9029-91-8. Cat No: NATE-0641. | |
| Native Bacillus stearothermophilus Polynucleotide Phosphorylase | Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity. It is also involved in mRNA processing and degradation in bacteria, plants, and humans. Applications: The enzyme is useful for the preparation of polyribonucleotide. Group: Enzymes. Synonyms: PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Enzyme Commission Number: EC 2.7.7.8. CAS No. 9014-12-4. Polynucleotide phosphorylase. Mole weight: 300,000 - 340,000; Subunit molecular weight : ca. 85,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Bacillus stearothermophilus. PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Cat No: NATE-1908. | |
| Native Bacillus stearothermophilus Pyruvate Kinase | Pyruvate kinase is an enzyme involved in glycolysis. It catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to ADP, yielding one molecule of pyruvate and one molecule of ATP. Applications: Pyruvate kinase from bacillus stearothermophilus has been used in a study to assess evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon. 1 it has also been used in a study to investigate the importance of the lys221 active site for pyruvate kinase activity. Group: Enzymes. Synonyms: Pyruvate kinase; EC 2.7.1.40; 9001-59-6; phosphoenolpyruvate kinase; phosphoenol transphosphorylase; pyruvate kinase (phosphorylating); fluorokinase; fluorokinase (phosphorylating); pyruvic kinase; pyruvate phosphotransferase; ATP:pyruvate 2-O-phosphotransferase. Enzyme Commission Number: EC 2.7.1.40. CAS No. 9001-59-6. Pyruvate Kinase. Activity: 100-300 units/mg protein. Stability: 2-8°C. Form: lyophilized powder. Source: Bacillus stearothermophilus. EC 2.7.1.40; 9001-59-6; Pyruvate kinase. Cat No: NATE-0649. | |
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