Creative Enzymes - Products
Enzyme manufacturing for life science research and medicines, food, alcohol, fabric, paper etc. Uses include: drug discovery, cancer and infectious disease research, microbiology and personalized medicine.
| Product | Description | |
|---|---|---|
| Na+-exporting ATPase | A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme from yeast is involved in the efflux of Na+, with one ion being exported per ATP hydrolysed. Group: Enzymes. Enzyme Commission Number: EC 7.2.2.3 (Formerly EC 3.6.3.7). Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4696; Na+-exporting ATPase; EC 3.6.3.7. Cat No: EXWM-4696. |  |
| Na+/K+-exchanging ATPase | A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This is a plasma membrane enzyme, ubiquitous in animal cells, that catalyses the efflux of three Na+ and influx of two K+ per ATP hydrolysed. It is involved in generating the plasma membrane electrical potential. Group: Enzymes. Enzyme Commission Number: EC 3.6.3.9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4698; Na+/K+-exchanging ATPase; EC 3.6.3.9. Cat No: EXWM-4698. | |
| N-alkylglycine oxidase | Isolated from the mold Cladosporium sp. G-10. Acts on N6-(carboxymethyl)lysine, 6-[(carboxymethy)amino]hexanoic acid, sarcosine and N-ethylglycine. It has negligible action on glycine (cf. EC 1.4.3.19 glycine oxidase). Group: Enzymes. Synonyms: N-carboxymethylalkylamine:oxygen oxidoreductase (decarboxymethylating). Enzyme Commission Number: EC 1.5.3.20. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1548; N-alkylglycine oxidase; EC 1.5.3.20; N-carboxymethylalkylamine:oxygen oxidoreductase (decarboxymethylating). Cat No: EXWM-1548. | |
| Nα-benzyloxycarbonylleucine hydrolase | Also acts on Nα-t-butoxycarbonyl-L-leucine, and, more slowly, on the corresponding derivatives of L-aspartate, L-methionine, L-glutamate and L-alanine. cf. EC 3.5.1.58 N-benzyloxycarbonylglycine hydrolase. Group: Enzymes. Synonyms: benzyloxycarbonylleucine hydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase IV; α-N-benzyloxycarbonyl-L-leucine urethanehydrolase. Enzyme Commission Number: EC 3.5.1.64. CAS No. 100630-47-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4454; Nα-benzyloxycarbonylleucine hydrolase; EC 3.5.1.64; 100630-47-5; benzyloxycarbonylleucine hydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase IV; α-N-benzyloxycarbonyl-L-leucine urethanehydrolase. Cat No: EXWM-4454. | |
| naphthalene 1,2-dioxygenase | This enzyme is a member of the ring-hydroxylating dioxygenase (RHD) family of bacterial enzymes that play a critical role in the degradation of aromatic compounds, such as polycyclic aromatic hydrocarbons. This enzyme comprises a multicomponent system, containing a reductase that is an iron-sulfur flavoprotein (FAD; EC 1.18.1.3, ferredoxin-NAD+ reductase), an iron-sulfur oxygenase, and ferredoxin. Requires Fe2+. Group: Enzymes. Synonyms: naphthalene dioxygenase; naphthalene oxygenase; NDO. Enzyme Commission Number: EC 1.14.12.12. CAS No. 9074-4-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0681; naphthalene 1,2-dioxygenase; EC 1.14.12.12; 9074-04-8; naphthalene dioxygenase; naphthalene oxygenase; NDO. Cat No: EXWM-0681. | |
| narbonolide synthase | The product, narbonolide, contains a 14-membered ring and is an intermediate in the biosynthesis of narbonomycin and pikromycin in the bacterium Streptomyces venezuelae. The enzyme also produces 10-deoxymethynolide (see EC 2.3.1.239, 10-deoxymethynolide synthase). The enzyme has 29 active sites arranged in four polypeptides (pikAI - pikAIV) with a loading domain, six extension modules and a terminal thioesterase domain. Each extension module contains a ketosynthase (KS), keto reductase (KR), an acyltransferase (AT) and an acyl-carrier protein (ACP). Not all active sites are used in the biosynthesis. Group: Enzymes. Synonyms: pikromycin PKS. Enzyme Commission Number: EC 2.3.1.240. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2189; narbonolide synthase; EC 2.3.1.240; pikromycin PKS. Cat No: EXWM-2189. | |
| nardilysin | Enzyme of 133 kDa from rat brain and testis. A homologue of pitrilysin containing the His-Phe-Leu-Glu-His zinc-binding sequence, and a highly acidic stretch of 71 residues. Unusually for a metalloendopeptidase, inhibited by bestatin, amastatin and N-ethylmaleimide. In peptidase family M16 (pitrilysin family). Group: Enzymes. Synonyms: N-arginine dibasic convertase; NRD-convertase. Enzyme Commission Number: EC 3.4.24.61. CAS No. 292850-69-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4344; nardilysin; EC 3.4.24.61; 292850-69-2; N-arginine dibasic convertase; NRD-convertase. Cat No: EXWM-4344. | |
| naringenin 7-O-methyltransferase | The enzyme is involved in the biosynthesis of the sakuranetin, an inducible defense mechanism of the plant Oryza sativa (Asian rice) against pathogen attack. Group: Enzymes. Synonyms: NOMT. Enzyme Commission Number: EC 2.1.1.232. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1835; naringenin 7-O-methyltransferase; EC 2.1.1.232; NOMT. Cat No: EXWM-1835. | |
| naringenin 8-dimethylallyltransferase | Requires Mg2+. This membrane-bound protein is located in the plastids. In addition to naringenin, the enzyme can prenylate several other flavanones at the C-8 position, but more slowly. Along with EC 1.14.13.103 (8-dimethylallylnaringenin 2'-hydroxylase) and EC 2.5.1.71 (leachianone G 2''-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway. Group: Enzymes. Synonyms: N8DT. Enzyme Commission Number: EC 2.5.1.70. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2808; naringenin 8-dimethylallyltransferase; EC 2.5.1.70; N8DT. Cat No: EXWM-2808. | |
| naringenin-chalcone synthase | In the presence of NADH and a reductase, 6'-deoxychalcone is produced. Group: Enzymes. Synonyms: chalcone synthase; flavanone synthase; 6'-deoxychalcone synthase; chalcone synthetase; DOCS; CHS. Enzyme Commission Number: EC 2.3.1.74. CAS No. 56803-04-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2254; naringenin-chalcone synthase; EC 2.3.1.74; 56803-04-4; chalcone synthase; flavanone synthase; 6'-deoxychalcone synthase; chalcone synthetase; DOCS; CHS. Cat No: EXWM-2254. | |
| Naringin | Naringin. Applications: 1.anti-inflammatory, anti-viral, anti-mutation, anti-carcinogen. 2.hypotensive activity, function as urogastrone, alleviating pain.3.tranquilizing, lowering blood viscosity , reduce the emerge of the thrombus. Group: Others. Synonyms: Naringin; 10236-47-2. CAS No. 10236-47-2. Purity: 98%, HPLC. Mole weight: C27H32O14; 580.53. Appearance: light white powder. Storage: 24 months with original packing under 18°C. Store in cool dry place,avoid sunlight and high temperature. Source: Extracted from the fruit of Citrus paradisi. Naringin; 10236-47-2; plant extract. Pack: 1kg, 5kg, 10kg aluminum foil vacuum bag; or 20kg, 25kg Fiber Drum. Cat No: EXTW-206. | |
| Native 6-phospho-D-gluconate dehydrogenase from E. coli | In enzymology, a phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) is an enzyme that catalyzes the chemical reaction:6-phospho-D-gluconate + NADP+<-> D-ribulose 5-phosphate + CO2 + NADPH. Thus, the two substRates of this enzyme are 6-phospho-D-gluconate and NADP+, whereas its 3 products are D-ribulose 5-phosphate, CO2, and NADPH. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. Applications: Determination of d-gluconate and d-glucono-δ-lactone in foodstaffs. Group: Enzymes. Synonyms: 6-Phosphogluconic Dehydrogenase; phosphogluconic acid dehydrogenase; 6-phosphogluconic dehydrogenase; 6-phosphogluconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase; EC 1.1.1.44; p. Enzyme Commission Number: EC 1.1.1.44. CAS No. 9073-95-4. 6-Phosphogluconic Dehydrogenase. Activity: > 150 UI/ml, > 45 U/mg. Storage: 4°C. Form: Suspension in Ammonium Sulphate. Source: E. coli. 6-Phosphogluconic Dehydrogenase; phosphogluconic acid dehydrogenase; 6-phosphogluconic dehydrogenase; 6-phosphogluconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase; EC 1.1.1.44; phosphogluconate dehydrogenase; decarboxylating; 9073-95-4. Cat No: NATE-1167. | |
| Native Abalone β-Glucuronidase | β-glucuronidase catalyzes the breakdown of complex carbohydrates. In humans it converts conjugated bilirubin into the unconjugated form, making bilirubin suitable for reabsorption. Group: Enzymes. Synonyms: β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase; EC 3.2.1.31; 9001-45-0; β-D-glucuronoside glucuronosohydrolase; GUSB. Enzyme Commission Number: EC 3.1.2.31. CAS No. 9001-45-0. GUSB. Activity: 1,500,000-3,000,000 units/g solid or > 100,000 units/mL. Form: lyophilized powder, Supplied as a lyophilized powder containing citric acid or aqueous solution, Supplied as an aqueous solution containing 0.85% NaCl and 0.02% sodium azide. Source: Abalone. β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase; EC 3.2.1.31; 9001-45-0; β-D-glucuronoside glucuronosohydrolase; GUSB. Cat No: NATE-0328. | |
| Native Abalone Sulfatase | Sulfatases EC 3.1.6.1 are enzymes of the esterase class that catalyze the hydrolysis of sulfate esters. These may be found on a range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. In the latter case the resultant N-sulfates can also be termed sulfamates. Sulfatases play important roles in the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodelling sulfated glycosaminoglycans in the extracellular space. Together with sulfotransferases, sulfatases form the major catalytic machinery for the synthesis and breakage of sulfa...ne conjugates from hamster embryo fibroblasts. Group: Enzymes. Synonyms: EC 3.1.6.1; 9016-17-5; sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; arylsulfatase. Enzyme Commission Number: EC 3.1.6.1. CAS No. 9016-17-5. Sulfatases. Activity: 20-40 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Abalone entrails. Species: Abalone. EC 3.1.6.1; 9016-17-5; sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; arylsulfatase. Cat No: NATE-0685. | |
| Native Acetyl esterase from Microbial | Catalyzed reaction: Hydrolysis of acetyl esters. Known substrates: Acetylated xylan, ethyl acetate, cephalosporin C and derivatives. Applications: Desacetylation of β-lactam antibiotics; broad range esterase; desacethylation of other substartes. Group: Enzymes. Synonyms: Acetyl esterase (Lyophilized); Acetyl esterase; EC 3.1.1.72. Enzyme Commission Number: EC 3.1.1.72. Acetylxylan esterase. Activity: > 50 U/mg of powder. Storage: Store at -20°C. Form: Lyophilized. Source: Microbial. Acetyl esterase (Lyophilized); Acetyl esterase; EC 3.1.1.72. Cat No: NATE-1169. | |
| Native Achromobacter lyticus Achromopeptidase | Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase) is an enzyme. This enzyme catalyses the following chemical reaction:Preferential cleavage:Lys-, including-Lys-Pro-. This enzyme is isolated from Achromobacter lyticus. Group: Enzymes. Synonyms: Achromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; EC 3.4.21.50; 123175-82-6; Lysyl endopeptidase. Enzyme Commission Number: EC 3.4.21.50. CAS No. 123175-82-6. Achromopeptidase. Storage: -20°C. Form: lyophilized powder, Protein ~5 % by biuret, 300-600 units/mg solid. Source: Achromobacter lyticus. Achromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; EC 3.4.21.50; 123175-82-6; Lysyl endopeptidase. Cat No: NATE-0021. | |
| Native Acid Phosphatase from Microbial | 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: Hydrolysis of phosphate monoesters. Group: Enzymes. Synonyms: 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. Enzyme Commission Number: EC 3.1.3.2. CAS No. 9001-77-8. Apase. Activity: > 40 U/mg; > 100 U/ml. Storage: 4°C. Form: Suspension in Ammonium Sulphate. Source: Microbial. 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-1170. | |
| Native Acremonium sp. Ascorbate Oxidase | In enzymology, a L-ascorbate oxidase (EC 1.10.3.3) is an enzyme that catalyzes the chemical reaction:2 L-ascorbate + O2<-> 2 dehydroascorbate + 2 H2O. Thus, the two substRates of this enzyme are L-ascorbate and O2, whereas its two products are dehydroascorbate and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor with oxygen as acceptor. This enzyme participates in ascorbate metabolism. It employs one cofactor, copper. Applications: This enzyme is useful for avoidance from interference of ascorbic acid on diagnostic assay such as blood, uric acid, tg, tc and creatinine. Group: Enzymes. Synonyms: ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; L-ascorbate:O2 oxidoreductase;. Enzyme Commission Number: EC 1.10.3.3. CAS No. 9029-44-1. AAO. Mole weight: 80 kDa?gel filtration?. Activity: > 200 U/mg. Appearance: Light blue amorphous powder, lyophilized. Storage: Storage at ?20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Acremonium sp. ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; L-ascorbate:O2 oxidoreductase; AA oxidase; EC 1.10.3.3; L-ascorbate oxidase. Cat No: NATE-0864. | |
| Native Actinobacillus sp. Creatinase | In enzymology, a creatinase (EC 3.5.3.3) is an enzyme that catalyzes the chemical reaction:creatine + H2O? sarcosine + urea. Thus, the two substrates of this enzyme are creatine and H2O, whereas its two products are sarcosine and urea. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. Creatinase accelerates the conversion reaction of creatine and water molecule to sarcosine and urea. It always acts in homodimer state and is induced by choline chloride. Applications: Creatinase mixed with sarcosine oxidase may be used to determine the level of creatine in different ph, temperature, enzyme ratio, and buffer concentration. it may also be used to determine the plasma creatinine level by using a centrifugal analyser. Group: Enzymes. Synonyms: Creatine amidinohydrolase; creatinase; 37340-58-2; EC 3.5.3.3. Enzyme Commission Number: EC 3.5.3.3. CAS No. 37340-58-2. Mole weight: mol wt ~100 kDa. Activity: 6.0 U/mg-solid or more. Storage: -20°C. Form: Lyophilized powder containing sugars and EDTA as stabilizers. Source: Actinobacillus sp. Creatine amidinohydrolase; creatinase; 37340-58-2; EC 3.5.3.3. Cat No: NATE-0160. | |
| Native Aerobacter aerogenes Sulfatase | Sulfatases EC 3.1.6.1 are enzymes of the esterase class that catalyze the hydrolysis of sulfate esters. These may be found on a range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. In the latter case the resultant N-sulfates can also be termed sulfamates. Sulfatases play important roles in the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodelling sulfated glycosaminoglycans in the extracellular space. Together with sulfotransferases, sulfatases form the major catalytic machinery for the synthesis and breakage o...17-5; sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; arylsulfatase. Enzyme Commission Number: EC 3.1.6.1. CAS No. 9016-17-5. Sulfatases. Activity: 2-5 units/mg protein (biuret), 10-20 units/mL. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 0.01 M Tris, pH 7.5. Source: Aerobacter aerogenes. EC 3.1.6.1; 9016-17-5; sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; arylsulfatase. Cat No: NATE-0686. | |
| Native Aerococcuss viridans Lactate Oxidase | Native Aerococcuss viridans Lactate Oxidase. Native lactate oxidase (ec 1.13.12.4) was purified from aerococcuss viridans. Group: Enzymes. Synonyms: lactate 2-monooxygenase; EC 1.13.12.4; (S)-lactate: oxygen 2-oxidoreductase (decarboxylating); lactate oxidative decarboxylase; lactate oxidase; lactic oxygenase; lactate oxygenase; lactic oxidase; L-lactate monooxygenase; lactate monooxygenase; L-lactate-2-monooxygenase. Enzyme Commission Number: EC 1.13.12.4. CAS No. 9028-72-2. Lactate oxidase. Activity: > 20 U/mg. Appearance: Yellowish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Aerococcuss viridans. lactate 2-monooxygenase; EC 1.13.12.4; (S)-lactate: oxygen 2-oxidoreductase (decarboxylating); lactate oxidative decarboxylase; lactate oxidase; lactic oxygenase; lactate oxygenase; lactic oxidase; L-lactate monooxygenase; lactate monooxygenase; L-lactate-2-monooxygenase. Cat No: DIA-156. | |
| Native Aerococcuss viridans Pyruvate oxidase | In enzymology, a pyruvate oxidase (EC 1.2.3.3) is an enzyme that catalyzes the chemical reaction: pyruvate + phosphate + O2 <-> acetyl phosphate + CO2 + H2O2. The 3 substrates of this enzyme are pyruvate, phosphate, and O2, whereas its 3 products are acetyl phosphate, CO2, and H2O2. Native pyruvate oxidase (ec 1.2.3.3) was purified from aerococcuss viridans. Applications: Useful for enzymatic determination of ast and alt. Group: Enzymes. Synonyms: pyruvate oxidase; EC 1.2.3.3; pyruvate: oxygen 2-oxidoreductase (phosphorylating); pyruvic oxidase; phosphate-dependent pyruvate oxidase. Enzyme Commission Number: EC 1.2.3.3. CAS No. 9001-96-1. Pyruvate oxidase. Activity: > 25 U/mg. Appearance: Yellowish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Aerococcuss viridans. pyruvate oxidase; EC 1.2.3.3; pyruvate: oxygen 2-oxidoreductase (phosphorylating); pyruvic oxidase; phosphate-dependent pyruvate oxidase. Cat No: DIA-169. | |
| Native Aerococcus viridans 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. Group: Enzymes. Synonyms: 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-phosph. Enzyme Commission Number: EC 1.1.3.21. CAS No. 9046-28-0. Glycerol-3-phosphate oxidase. Activity: > 70 units/mg solid. Storage: -20°C. Form: Lyophilized powder containing sucrose. Source: Aerococcus viridans. 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-0314. | |
| Native Aeromonas proteolytica Aminopeptidase | Aminopeptidase from Aeromonas proteolytica is a metalloenzyme, which contains 2 atoms of Zn2+ in a single polypeptide with an approximate molecular weight of 29.5 kDa as determined by sedimentation. This enzyme has a high degree of stability, being stable even at tempeRatures of 70°C for several hours. Partial inactivation occurs in 8 M urea. Maximum stability and activity are between pH 8.0-8.5. Aminopeptidase from Aeromonas proteolytica can function as an esterase. Applications: Aminopeptidases are a family of widely distributed proteases, which may be used to study many significant biological processes such as protein maturation, hormone production, and peptide digestion. the enzyme has been used to measure the kinetic rate constant for the binding of bestatin, a general protease inhibitor, to aminopeptidase. Group: Enzymes. Synonyms: Aminopeptidase; 37288-67-8; EC 3.4.11.10; Aeromonas proteolytica aminopeptidase. Enzyme Commission Number: EC 3.4.11.10. CAS No. 37288-67-8. Aminopeptidase. Storage: -20°C. Form: lyophilized powder, 50-150 units/mg protein. Source: Aeromonas proteolytica. Aminopeptidase; 37288-67-8; EC 3.4.11.10; Aeromonas proteolytica aminopeptidase. Cat No: NATE-0071. | |
| Native Agaricus bisporus 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. Applications: Laccase is polyphenol oxidase found in many plants, fungi and microorganisms. laccases may be useful in enzymatic biofuel systems, teeth whitening, textile dyeing, and in other applications that require the removal of oxygen. 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: > 4 units/mg. Storage: -20°C. Form: powder; deep brown. Source: Agaricus bisporus. Laccases; EC 1.10.3.2; 80498-15-3; urishiol oxidase; urushiol oxidase; p-diphenol oxidase; benzenediol:oxygen oxidoreductase. Cat No: NATE-0370. | |
| Native Alcaligenes faecalis 3-Hydroxybutyrate Dehydrogenase | In mammalian systems, β-hydroxybutyrate dehydrogenase is localized on the inner mitochondrial membrane and requires phosphatidyl choline for activity. In contrast, the enzyme from Pseudomonas is a soluble cytosolic enzyme that does not require a phospholipid allosteric activator. The enzyme is required for the utilization of ketone bodies as a source of metabolic energy. It catalyzes the oxidation of 3-hydroxybutyrate to acetoacetate, the first step in the conversion of ketone bodies to citric acid, which is then further metabolized via the tricarboxylic acid cycle (Krebs cycle). Is an enzyme produced by microorganisms. this product shall be used for a diag...Enzyme Commission Number: EC 1.1.1.30. CAS No. 9028-38-0. 3-HBDH. Mole weight: 60±5 kDa (TSK G-3000SW); 30±5 kDa (SDS-PAGE). Activity: > 1,500 U/mg. Appearance: White powder. Storage: -20°C. Form: Freeze dried powder. Source: Alcaligenes faecalis. 3-hydroxybutyrate dehydrogenase; 3-HBDH; NAD-β-hydroxybutyRate dehydrogenase; hydroxybutyRate oxidoreductase; β-hydroxybutyRate dehydrogenase; D-β-hydroxybutyRate dehydrogenase; D-3-hydroxybutyRate dehydrogenase; D-(-)-3-hydroxybutyRate dehydrogenase; β-hydroxybutyric acid dehydrogenase; 3-D-hydroxybutyRate dehydrogenase; β-hydroxybutyric dehydrogenase; EC 1.1.1.30; 9028-38-0. Cat No: NATE-0005. | |
| Native Alcaligenes sp. Choline Oxidase | In enzymology, a choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes the chemical reaction: choline + O2<-> betaine aldehyde + H2O2. Thus, the two substrates of this enzyme are choline and O2, whereas its two products are betaine aldehyde and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. Applications: This enzyme is useful for enzymatic determination of phospholipids when coupled with phospholipase d and for choline esterase-activity in clinical analysis. Group: Enzymes. Synonyms: choline oxidase; EC 1.1.3.17. Enzyme Commission Number: EC 1.1.3.17. CAS No. 9028-67-5. Choline Oxidase. Mole weight: approx. 95 kDa. Activity: GradeIII 10U/mg-solid or more (containing approx. 20% of stabilizers). Stability: Stable at-20°C for at least 6 months. Appearance: Yellowish amorphous powder, lyophilized. Form: Freeze dried powder. Source: Alcaligenes sp. choline oxidase; EC 1.1.3.17. Cat No: DIA-184. | |
| Native Alcohol dehydrogenase | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. The enzyme is an alcohol dehydrogenase most active on n-butanol but with low activity on ethanol. Group: Enzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcoh. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Cat No: NATE-0034. | |
| Native Alginate Lyase | In enzymology, a poly (beta-D-mannuronate) lyase (EC 4.2.2.3) is an enzyme that catalyzes the chemical reaction:Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their ends. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. This enzyme participates in fructose and mannose metabolism. Applications: Alginate lyase is used to break down alginate or alginic acid and to reduce viscosity. it is useful during follicle isolation, encapsulation, and culture. Group: Enzymes. Synonyms: alginate lyase I; alginate lyase; alginase I; alginase II; alginase; poly (β-D-1,4-mannuronide) lyase; EC 4.2.2.3; 9024-15-1. Enzyme Commission Number: EC 4.2.2.3. CAS No. 9024-15-1. Alginate lyase. Activity: > 10,000 units/g solid. Storage: 2-8°C. Form: powder. alginate lyase I; alginate lyase; alginase I; alginase II; alginase; poly (β-D-1,4-mannuronide) lyase; EC 4.2.2.3; 40591-57-9. Cat No: NATE-0050. | |
| Native Almond α (1-3,4) Fucosidase | Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the FUCA1 gene. Alpha-Fucosidase is an enzyme that breaks down fucose. Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fucosidase with accumulation of fucose in the tissues. Different phenotypes include clinical features such as neurologic deterioration, growth retardation, visceromegaly, and seizures in a severe early form; coarse facial features, angiokeratoma corporis diffusum, spasticity and delayed psychomotor development in a longer surviving form; and an unusual spondylometaphyseoepiphyseal dysplasia in yet another form. Group: Enzymes. Synonyms: α ...buffer supplied with the enzyme, >85% of the original activity is observed after two months at 2-8°C. In the buffer solution at 37°C, the half-life is approximately 80 hours. Storage: Shipped on ice pack for next day delivery. Store at -20°C. Store lyophilized enzyme at-20°C. Enzyme reconstituted with the provided reaction buffer is stable at 2-8°C for at least two months and may be stored at-20°C for at least six months. Avoid repeated freeze/thaw cycles. Form: Lyophilized from 50 mM sodium acetate, 3 mg/ml bovine serum albumin (pH 5.0). Source: Almond meal. Species: Almond. α (1-3,4) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA. Cat No: NATE-0260. | |
| Native Almonds β-Glucosidase | β-glucosidase is involved in the hydrolysis of β-glycosidic bonds connecting carbohydrate residues in β-D-glycosides. They convert cellobiose and cellooligosaccharides produced by the endo and exoglucanases to glucose. Applications: Β-glucosidase is also used in the synthesis of glucosides and fucosides with various potential applications in pharmaceutical, cosmetic and detergent industries, hydrolytic removal of aglycone moiety from flavonoid and isoflavonoid glycosides, flavor enhancement of fruit juices and wine, and biosynthesis of oligosaccharides. Group: Enzymes. Synonyms: β-glucosidase; gentiobiase; cellobiase; emulsin; elaterase; aryl-β-glucosidase; β-D-glucosidase; β-glucoside glucohydrolase; arbutinase; amygdalinase; p-nitrophenyl β-glucosidase; primeverosida. Enzyme Commission Number: EC 3.2.1.31. CAS No. 9001-22-3. β-Glucosidase. Mole weight: Mr ~135 kDa. Activity: 10-30 units/mg solid; > 2 units/mg solid. Storage: 2-8°C. Form: lyophilized powder. Source: Almonds. β-glucosidase; gentiobiase; cellobiase; emulsin; elaterase; aryl-β-glucosidase; β-D-glucosidase; β-glucoside glucohydrolase; arbutinase; amygdalinase; p-nitrophenyl β-glucosidase; primeverosidase; amygdalase; linamarase; salicilinase; β-1,6-glucosidase; EC 3.2.1.31; 9001-22-3. Cat No: NATE-0769. | |
| Native Almonds Glycopeptidase A | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Group: Enzymes. Synonyms: EC 3.5.1.52; glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; 83534-39-8; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. PNGase F. Activity: > 0.05 unit/mL. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 50 mM Citrate-phosphate buffer, pH 5.0, and BSA. Source: Almonds. EC 3.5.1.52; glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; 83534-39-8; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase. Cat No: NATE-0600. | |
| Native Almonds Mandelonitrile Lyase | In enzymology, a mandelonitrile lyase is an enzyme that catalyzes the chemical reaction:mandelonitrile<-> hydrogen cyanide + benzaldehyde. Hence, this enzyme has one substrate, mandelonitrile, and two products, hydrogen cyanide and benzaldehyde. This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. This enzyme participates in cyanoamino acid metabolism. It has 2 cofactors:flavin, and flavoprotein. Mandelonitrile lyase is a cyanogenic enzyme. Applications: Mandelonitrile lyase from almonds has been used in a study to assess the apoplastic antioxidant system in prunus. it has also been used in a study to investigate screening for new hydroxynitrilases from plants. Group: Enzymes. Synonyms: mandelonitrile lyase; EC 4.1.2.10; (R)-oxynit. Enzyme Commission Number: EC 4.1.2.10. CAS No. 9024-43-5. PhaMDL. Activity: 80-240 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 50 mM imidazole, 2.8 M (NH4)2SO4, pH 6.0. Source: Almonds. mandelonitrile lyase; EC 4.1.2.10; (R)-oxynitrilase; oxynitrilase; D-oxynitrilase; D-α-hydroxynitrile lyase; mandelonitrile benzaldehyde-lyase; PaHNL; AtHNL; PhaMDL; (R)-HNL; (R)-PeHNL; (R)-hydroxynitrile lyase; R-selective hydroxynitrile lyase; R-selective HNL; (R)-(+)-mandelonitrile lyase; 9024-43-5. Cat No: NATE-0557. | |
| Native α-1,2-Fucosidase solution | Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the FUCA1 gene. Alpha-Fucosidase is an enzyme that breaks down fucose. Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fucosidase with accumulation of fucose in the tissues. Different phenotypes include clinical features such as neurologic deterioration, growth retardation, visceromegaly, and seizures in a severe early form; coarse facial features, angiokeratoma corporis diffusum, spasticity and delayed psychomotor development in a longer surviving form; and an unusual spondylometaphyseoepiphyseal dysplasia in yet another form. Group: Enzymes. Synonyms: α-1,2-Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA; 9037-65-4. Enzyme Commission Number: EC 3.2.1.51. CAS No. 9037-65-4. FUCA. Activity: > 0.4 units/mg protein. Storage: 2-8°C. Form: buffered aqueous solution, Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl. α-1,2-Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA; 9037-65-4. Pack: vial of 0.004 unit. Cat No: NATE-0259. | |
| Native α-Glucosidase from Bacillus stearothermophilus | Alpha-glucosidase is a glucosidase located in the brush border of the small intestine that acts upon 1,4-alpha bonds. This is in contrast to beta-glucosidase. Alpha-glucosidase breaks down starch and disaccharides to glucose. Maltase, a similar enzyme that cleaves maltose, is nearly functionally equivalent. Α-glucosidase hydrolyzes carbohydrates by acting on 1,4-α linkages. inhibition of α-glucosidase is a prominent target in the management of non-insulin-dependent diabetes mellitus. Applications: Α-glucosidase is potential enzyme for the biosynthesis of complex carbohydrates. Group: Enzymes. Synonyms: Alpha-glucosidase; EC 3.2.1.20; maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; alpha-glucopyranosidase; glucosidoinvertase; alpha-D-glucosidase; alpha-glucoside hydrolase; alpha-1,4-glucosidase; al. Enzyme Commission Number: EC 3.2.1.20. CAS No. 9001-42-7. α-Glucosidase. Activity: >50 units/mg. Storage: 2-8°C. Form: Lyophilized powder containing potassium phosphate buffer salt. Source: Bacillus stearothermophilus. Alpha-glucosidase; EC 3.2.1.20; maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; alpha-glucopyranosidase; glucosidoinvertase; alpha-D-glucosidase; alpha-glucoside hydrolase; alpha-1,4-glucosidase; alpha-D-glucoside glucohydrolase. Cat No: NATE-1163. | |
| Native α-lytic protease | Alpha-lytic protease (aLP) is an alternative specificity protease for proteomics applications. This protease cleaves after T, A, S, and V residues. It geneRates peptides of similar average length as trypsin. aLP was first isolated from the myxobacterium Lysobacter enzymogenes. The pro-form of aLP is 397 amino acids long. In its mature form, aLP is 198 amino acids long. Its tertiary structural core resembles those of pancreatic serine proteases. Group: Enzymes. Synonyms: Alpha-lytic protease; myxobacter α-lytic proteinase; α-lytic proteinase; α-lytic protease; Mycobacterium sorangium α-lytic proteinase; Myxobacter 495 α-lytic proteinase; Alp. α-LP. Storage: -70°C. Form: Supplied as a solution in 10 mM sodium acetate buffer, pH 5.0. Alpha-lytic protease; myxobacter α-lytic proteinase; α-lytic proteinase; α-lytic protease; Mycobacterium sorangium α-lytic proteinase; Myxobacter 495 α-lytic proteinase; Alp. Cat No: NATE-0052. | |
| Native Arachis hypogaea (peanut) 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. Phospholipase d is a phospholipid hydrolyzing enzyme and an important component of receptor-mediated signal transduction responses and regulated secretion. Applications: Research has shown adp-ribosylation factor regulation of phospholipase d is important in the release of nascent secretory vesicles from the trans-golgi network. it has also been used in a study to investigate stimulation of na+-ca2+ exchange activity in canine cardiac sarcolemmal vesicals. 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. Activity: > 60 units/mg protein. Storage: -20°C. Form: Partially purified, lyophilized powder containing buffer salts. Source: Arachis hypogaea (peanut). Phospholipase D; EC 3.1.4.4; lipophosphodiesterase II; lecithinase D; choline phosphatase; PLD; 9001-87-0. Cat No: NATE-0594. | |
| Native Arthrobacter globiformis Choline oxidase | In enzymology, a choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes the chemical reaction choline + O2<-> betaine aldehyde + H2O2. Thus, the two substrates of this enzyme are choline and O2, whereas its two products are betaine aldehyde and H2O2. Native choline oxidase (ec 1.1.3.17) was purified from arthrobacter globiformis. Group: Enzymes. Synonyms: choline oxidase; EC 1.1.3.17; choline: oxygen 1-oxidoreductase. Enzyme Commission Number: EC 1.1.3.17. CAS No. 9028-67-5. Choline Oxidase. Activity: 8-20 U/mg. Appearance: Yellow amorphous powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Arthrobacter globiformis. choline oxidase; EC 1.1.3.17; choline: oxygen 1-oxidoreductase. Cat No: DIA-139. | |
| Native Arthrobacter globiformis Uricase | The enzyme urate oxidase (UO) catalyzes the oxidation of uric acid to 5-hydroxyisourate:Uric acid + O2 + H2O ? 5-hydroxyisourate + H2O2 ? allantoin + CO2. Group: Enzymes. Synonyms: uric acid oxidase; uricase; uricase II; urate oxidase; factor-independent urate hydroxylase; EC 1.7.3.3; 9002-12-4; UO. Enzyme Commission Number: EC 1.7.3.3. CAS No. 9002-12-4. UO. Mole weight: 4 × ~32 KDa (tetramer). Activity: 15-30 units/mg protein (biuret). Storage: -20°C. Form: lyophilized powder. Source: Arthrobacter globiformis. uric acid oxidase; uricase; uricase II; urate oxidase; factor-independent urate hydroxylase; EC 1.7.3.3; 9002-12-4; UO. Cat No: NATE-0729. | |
| Native Arthrobacter luteus Lyticase | Lyticase hydrolyzes poly-β (1?3)-glucose such as yeast cell wall glucan. Applications: Yeast cells are difficult to disrupt because the cell walls may form capsules or resistant spores. dna can be extracted from yeast by using lysing enzymes such as lyticase, chitinase, zymolase, and gluculase to induce partial spheroplast formation; spheroplasts are subsequently lysed to release dna. lyticase is preferred to digest cell walls of yeast and generate spheroplasts from fungi for transformation. reported to be useful for lysis of ashbya, candida, debaryomyces, eremothecium, endomyces, hansenula, hanseniaspora, kloeckera, kluyveromyces, lipomyces, metschikowia, pichia, pullularia, torulopsis, saccharomyces, saccharomycopsis, saccharomycodes, and schwanniomyces species. Group: Enzymes. Synonyms: Lyticase; 37340-57-1. CAS No. 37340-57-1. Lyticase. Activity: > 200 units/mg solid; > 1,500 units/mg protein; > 2,000 units/mg protein, Protein > 20 % by biuret. Storage: 2-8°C. Form: lyophilized powder. Source: Arthrobacter luteus. Lyticase; 37340-57-1. Cat No: NATE-0431. | |
| Native Arthrobacter luteus Zymolyase | Native Arthrobacter luteus Zymolyase. Group: Enzymes. Synonyms: Zymolyase. Zymolyase. Activity: 20U/mg. Stability: Stable for one year at 4°C. Storage: -20°C. Form: Lyophilized powder. Source: Arthrobacter luteus. Zymolyase. Cat No: NATE-0739. | |
| Native Arthrobacter sp. acyl-CoA oxidase | In enzymology, an acyl-CoA oxidase (EC 1.3.3.6) is an enzyme that catalyzes the chemical reaction acyl-CoA + O2<-> trans-2, 3-dehydroacyl-CoA + H2O2. Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2, 3-dehydroacyl-CoA and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in 3 metabolic pathways: fatty acid metabolism, polyunsaturated fatty acid biosynthesis, and ppar signaling pathway. It employs one cofactor, FAD. Native acyl-coa oxidase (ec 1.3.3.6) was purified from arthrobacter sp. Group: Enzymes. Synonyms: acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; and fatty acyl-coenzyme A oxidase. Enzyme Commission Number: EC 1.3.3.6. CAS No. 61116-22-1. Acyl-CoA oxidase. Activity: > 20 U/mg. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Yellowish Freeze dried powder. Source: Arthrobacter sp. acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; and fatty acyl-coenzyme A oxidase. Cat No: DIA-121. | |
| Native Arthrobacter sp. Tyramine Oxidase | Amine oxidases (AO) are enzymes that catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. There are two classes of amine oxidases: flavin-containing (EC 1.4.3.4) and copper-containing (EC 1.4.3.6). Copper-containing AO act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor: RCH2NH2 + H2O + O2 <-> RCHO + NH3 + H2O2. The 3 substrates of this enzyme are primary amines (RCH2NH2), H2O, and O2, whereas its 3 products are RCHO, NH3, and H2O2. Native tyramine oxidase (ec 1.4.3.4) was purified from arthrobacter sp. Applications: Useful for enzymatic determiantion of leucine aminopeptidase. Group: Enzymes. Synonyms: Tyramine Oxidase; TOD; EC 1.4.3.6. Enzyme Commission Number: EC 1.4.3.6. CAS No. 9001-53-0. Tyramine Oxidase. Activity: > 3 U/mg. Appearance: White to light brown powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Arthrobacter sp. Tyramine Oxidase; TOD; EC 1.4.3.6. Cat No: DIA-158. | |
| Native Arthrobacter ureafaciens α (2?3,6,8,9) 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. Applications: Neuraminidase is an important deglycosyl... resulting in partial or complete o-deglycosylation. sds-page and maldi-tof ms are typically utilized in purification, structural analysis, and sequencing process. these techniques also remove heterogeneity and charge from the glycoprotein. 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: Lyophilized powder. Source: Arthrobacter ureafaciens. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Cat No: NATE-0756. | |
| Native Aspergillus aculeatus Pectinase | Pectinase is an active pectolytic enzyme preparation that is produced by a selected strain of Aspergillus aculeatus. It contains mainly pectintranseliminase, polygalacturonase and pectinesterase, along with small amounts of hemicellulases and cellulases. Pectinase hydrolyzes pectin, which is a component of the cell wall. They may attack methyl-esterified pectin or de-esterified pectin. Fungal protease/peptidase complex produced by submerged fermentation of a selected strain of aspergillus oryzae and contains both endoprotease and exopeptidase activities. Applications: Pectinase from aspergillus aculeatus is used in plant protoplast preparation to digest cell wall prior to organelle isolation. it has been used to conduct partial saccharification of sugars. pectinases are used to study their role in the invasion of plant tissues using phytopathogens, as well as various food processing and plant biotechnology applications. the enzyme from creative enzymes has been used to determine the content of quercetin produced and also to evaluate its rutinase activity. Group: Enzymes. Synonyms: Pectinase. CAS No. 9032-75-1. Pectinase. Activity: > 500 U/g. Form: aqueous solution. Source: Aspergillus aculeatus. Pectinase. Cat No: NATE-0534. | |
| Native Aspergillus ficuum Tannase | Tannase catalyzes the hydrolysis of tannic acid to produce gallic acid and glucose. Group: Enzymes. Synonyms: tannase; 9025-71-2; Tannin acyl Hydrolase. CAS No. 9025-71-2. Tannase. Activity: > 150 U/g. Storage: 2-8°C. Form: powder; white. Source: Aspergillus ficuum. tannase; 9025-71-2; Tannin acyl Hydrolase. Pack: 1 g in glass bottle; 250 mg in glass bottle. Cat No: NATE-0690. | |
| Native Aspergillus genus Acylase I | In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Group: Enzymes. Synonyms: aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. CAS No. 9012-37-7. ACY1. Storage: 0-10°C. Source: Aspergillus genus. aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-1593. | |
| Native Aspergillus japonicus Pectolyase | Pectolyase catalyzes the eliminative cleavage of a-(1-4)-Dgalacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-a-D-galact-4-enuronosyl groups at their non-reducing ends. It contain two types of pectinase, endopolygalacturonase, endo-pectin lyase and a maceration stimulating factora. Applications: Used in plant protoplast preparation to digest cell wall prior to organelle isolation. pectolyase p5936 (pel1) is a natural mixed pectolyase produced by the fungus aspergillus japonicus used to digest components (endopolygalacturonate and pectin) of plant cell walls. treatment of cell walls with pectolyase can be used to destablilize the cell walls for organelle isolation or to modify the elasticity of the cell walls. Group: Enzymes. Synonyms: polygalacturonase; pectin depolymerase; pectinase; endopolygalacturonase; pectolase;. Enzyme Commission Number: EC 3.2.1.15. CAS No. 9033-35-6. Pectinase. Activity: > 0.3 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Aspergillus japonicus. polygalacturonase; pectin depolymerase; pectinase; endopolygalacturonase; pectolase; pectin hydrolase; pectin polygalacturonase; endo-polygalacturonase; poly-α-1,4-galacturonide glycanohydrolase; endogalacturonase; endo-D-galacturonase; poly (1,4-α-D-galacturonide) glycanohydrolase; EC 3.2.1.15; PEL1. Cat No: NATE-0540. | |
| Native Aspergillus melleus Acylase I | In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Enzyme activity: the optimum temperature is 40-45 oc, the optimum ph is 8.0 (stable form ph 6-10). the enzyme is activated by cocl2 in the range of 10-4 to 10-3 m. Group: Enzymes. Synonyms: aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; . Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. ACY1. Activity: >0.5 units/mg. Storage: 2-8°C. Form: powder. Source: Aspergillus melleus. aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-0029. | |
| Native Aspergillus melleus Proteinase | A protease (also called peptidase or proteinase) is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in animals, plants, bacteria, archaea and viruses. Applications: Proteinase is an enzyme used to break down proteins by hydrolyzing peptide bonds. proteinase is used to degrade proteins, to study proteinase inhibitors and to study thermal inactivation kinetics. proteinase is used in nucleic acid isolation procedures in incubations. it is used to study proteinase-activated receptors, such as the transducers of proteinase-mediated signaling in inflammation and the immune response. it is from aspergillus melleus and has been used to non-specifically degraded xylanase from streptomyces halstedii. Group: Enzymes. Synonyms: Protease; peptidase; proteinase; 9001-92-7. CAS No. 9001-92-7. Proteinase. Activity: > 3 units/mg solid. Storage: 2-8°C. Source: Aspergillus melleus. Protease; peptidase; proteinase; 9001-92-7. Cat No: NATE-0638. | |
| Native Aspergillus niger Amyloglucosidase | Glucan 1,4-alpha-glucosidase is an enzyme located on the brush border of the small intestine with system name 4-alpha-D-glucan glucohydrolase. This enzyme catalyses the following chemical reaction:Hydrolysis0 of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. Most forms of the enzyme can rapidly hydrolyse 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4. Stabilized with glucose. Applications: Amyloglucosidase from aspergillus niger is used to hydrolyze α-d-glucosides. it may be used in the brewing of beer and in the production of bread and juices. amyloglucosidase has been used to hydrolyze glycogen into glucose monomers in order to study lipid accumulation in skeletal muscle. Group: Enzymes. Synonyms: glucoamylase; amyloglucosidase; γ-amylase; lysosomal α-glucosidase; acid maltase; exo-1,4-α-glucosidase; g. Enzyme Commission Number: EC 3.2.1.3. CAS No. 9032-08-0. Glucoamylase. Activity: > 300 U/mL. Form: aqueous solution. Source: Aspergillus niger. glucoamylase; amyloglucosidase; γ-amylase; lysosomal α-glucosidase; acid maltase; exo-1,4-α-glucosidase; glucose amylase; γ-1,4-glucan glucohydrolase; acid maltase; 1,4-α-D-glucan glucohydrolase; EC 3.2.1.3; 9032-08-0. Cat No: NATE-0075. | |
| Native Aspergillus niger 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. Group: Enzymes. Synonyms: endo-1,3-β-D-glucanase; laminarinase; laminaranase; β-1,3-glucanase; β-1,3-1,4-glucanase; endo-1,3-β-glucanase; endo-β-1,3 (4)-glucanase; endo-β-1,3-1,4-glucanase; endo-β-(1?3)-D-glucanase; endo-1,3-1,4-β-D-glucanase; endo-&. Enzyme Commission Number: EC 3.2.1.6. CAS No. 9074-98-0. β-glucanase. Activity: ~1 units/mg. Storage: 2-8°C. Form: powder. Source: Aspergillus niger. 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; 9074-98-0. Cat No: NATE-0766. | |
| Native Aspergillus niger Cellobiase | Cellobiase enzyme preparation obtained by submerged fermentation of an Aspergillus niger microorganism. The cellobiase hydrolyzes cellobiose to glucose. Cellobiase enzyme preparation obtained by submerged fermentation of an aspergillus niger microorganism. the cellobiase hydrolyzes cellobiose to glucose. Applications: Cellobiase from aspergillus niger has been used in a study to assess the targeted antifungal delivery system of a β-glucosidase sensitive nystatin-star poly (ethylene glycol) conjugate. cellobiase from aspergillus niger has also been used in a study to investigate the influence of substrate particle size and wet oxidation on physical surface structures and enzymatic hydrolysis of wheat straw. Group: Enzymes. Synonyms: Novozyme 188; Cellobiase. CAS No. 9033-6-1. Cellobiase. Activity: > 250 units/g. Storage: 2-8°C. Form: liquid. Source: Aspergillus niger. Novozyme 188; Cellobiase. Cat No: NATE-0117. | |
| Native Aspergillus niger 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. The fda recognizes cellulase from a. niger as ...;-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: > 0.3 units/mg solid. Storage: 2-8°C. Form: powder. Source: Aspergillus niger. 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-0118. | |
| Native Aspergillus niger 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. Glucose oxidase from aspergillus niger is a dimer consisting of 2 equal subunits with a molecular mass of 80 kda each. each subunit contains one flavin adenine dinulceotide moiety and one iron. the enzyme is a glycoprotein containing ~16% neutral sugar and 2% amino sugars. the enzyme also contains 3 cysteine residues and 8 potential sites for n-linked ...xidase oxidizes β-d-glucose to d-gluconolactate and hydrogen peroxide, horseradish peroxidase is often used as the coupling enzyme for glucose determination. although glucose oxidase is specific for β-d-glucose, solutions of d-glucose can be quantified as α-d-glucose will mutorotate to β-d-glucose as the β-d-glucose is consumed by the enzymatic reaction. Applications: Glucose oxidase is widely used in the food and pharmaceutical industries as well as a major component of glucose biosensors. Group: Enzymes. Synonyms: EC 1.1.3.4; glucose oxyhydrase; corylophyline; penatin; glucose aerodehydrogenase; microcid; β-D-glucose oxidase; D-glucose oxi | |
| Native Aspergillus niger Glucosidase | Glucosidase catalyzes the hydrolysis of α-1,4 linkages with a substrate preference for maltose, maltotriose and maltotetraose. Reactivity with large polysaccharides like dextrin and starch have also been described. Group: Enzymes. Synonyms: EC 3.2.1-; 9033-06-1; Glucosidase; Cellobiase. Enzyme Commission Number: EC 3.2.1-. CAS No. 9001-22-3. β-Glucosidase. Activity: > 750 U/g. Storage: 2-8°C. Form: powder; gray-brown. Source: Aspergillus niger. EC 3.2.1-; 9033-06-1; Glucosidase; Cellobiase. Cat No: NATE-0306. | |
| Native Aspergillus niger Inulinase | Inulinase hydrolyses inulin to produce oligosaccharides and liberate fructose. It also splits terminal fructose units in sucrose and raffinose. Group: Enzymes. Synonyms: EC 3.2.1.7; inulinase; inulase; indoinulinase; endo-inulinase; exoinulinase; 2,1-β-D-fructan fructanohydrolase; 9025-67-6. Enzyme Commission Number: EC 3.2.1.7. CAS No. 9025-67-6. Inulinase. Activity: Type I, ~25 units/mg. Storage: 2-8°C. Form: Type I, lyophilized powder, brown-gray; Type II, aqueous glycerol solution, Supplied as a solution in 20% Glycerol and 20% Sorbitol. Source: Aspergillus niger. EC 3.2.1.7; inulinase; inulase; indoinulinase; endo-inulinase; exoinulinase; 2,1-β-D-fructan fructanohydrolase; 9025-67-6. Cat No: NATE-0356. | |
| Native Aspergillus niger 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: Lipase AP6. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Mole weight: ~ 45,000. Activity: ~200 U/g. Storage: 2-8°C. Form: Powder (fine). Source: Aspergillus niger. 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-1607. | |
| Native Aspergillus niger Nitrate Reductase (NAD[P]H) | Nitrate reductase (NAD (P)H) is an enzyme with system name nitrite:NAD (P)+ oxidoreductase. This enzyme catalises the following chemical reaction:nitrite + NAD (P)+ + H2O<-> nitrate + NAD (P)H + H+. Nitrate reductase is an iron-sulfur molybdenum flavoprotein. Group: Enzymes. Synonyms: nitrate reductase [NAD (P)H]; Nitrate reductases; assimilatory nitrate reductase; assimilatory NAD (P)H-nitrate reductase; NAD (P)H bispecific nitrate reductase; nitrate reductase (reduced nicotinamide adenine dinucleotide (phosphate)); nitrate reductase NAD (P)H; NAD (P)H-nitrate reductase; nitrate reductase [NAD (P)H2]; NAD (P)H2:nitrate oxidoreductase; 9029-27-0; EC 1.7.1.2. Enzyme Commission Number: EC 1.7.1.2. CAS No. 9029-27-0. Nitrate reductase. Activity: > 300 units/g solid. Storage: -20°C. Form: lyophilized powder. Source: Aspergillus niger. nitrate reductase [NAD (P)H]; Nitrate reductases; assimilatory nitrate reductase; assimilatory NAD (P)H-nitrate reductase; NAD (P)H bispecific nitrate reductase; nitrate reductase (reduced nicotinamide adenine dinucleotide (phosphate)); nitrate reductase NAD (P)H; NAD (P)H-nitrate reductase; nitrate reductase [NAD (P)H2]; NAD (P)H2:nitrate oxidoreductase; 9029-27-0; EC 1.7.1.2. Cat No: NATE-0484. | |
| Native Aspergillus niger Pectinase | Pectolytic enzyme preparation produced from a selected strain of Aspergillus niger:contains mainly pectintranseliminase, polygalacturonase, and pectinesterase and small amounts of hemicellulases and cellulases. Pectinases hydrolyses pectin, which is a component of the cell wall. They may attack methyl-esterified pectin or de-esterified pectin. It is a source of pectinase activity, also containing cellulase and hemicellulase activities.Pectinase catalyzes the random hydrolysis of a-(1-4)-Dgalactosiduronic linkages in pectin and other galacturonans. Applications: Used in plant protoplast preparation to digest cell wall prior to organelle isolation. petctinase is an enzyme from...galacturonide glycanohydrolase; endogalacturonase; endo-D-galacturonase; poly (1,4-α-D-galacturonide) glycanohydrolase; polygalacturonase; EC 3.2.1.15; 9032-75-1. Enzyme Commission Number: EC 3.2.1.15. CAS No. 9032-75-1. Pectinase. Activity: > 5 units/mg protein (Lowry). Storage: 2-8°C. Form: Solution in 40% glycerol. Source: Aspergillus niger. Pectinase; pectin depolymerase; endopolygalacturonase; pectolase; pectin hydrolase; pectin polygalacturonase; endo-polygalacturonase; poly-α-1,4-galacturonide glycanohydrolase; endogalacturonase; endo-D-galacturonase; poly (1,4-α-D-galacturonide) glycanohydrolase; polygalacturonase; EC 3.2.1.15; 9032-75-1. Cat No: NA | |
| Native Aspergillus oryzae 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. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. amylases from aspergillus oryzae are commonly used as baking additives to prevent staling in the baking industry, clarify haze from fruit juices and alcoholic beverages, and to produce glucose and maltose syrup products. 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: Mr ~51 kDa. Activity: > 150 units/mg protein (biuret); ~1.5 units/mg; ~30 units/mg. Storage: -20°C. Form: powder containing dextrin. Source: Aspergillus oryzae. 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-0740. | |
| Native Aspergillus oryzae β-Galactosidase | β-galactosidase 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. Applications: Β-galactosidase was used for reversed-phase (rp) adsorption. it was also used in the hydrolysis of whey lactose. Group: Enzymes. Synonyms: 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. Enzyme Commission Number: EC 3.2.1.23. CAS No. 9031-11-2. β-gal. Storage: -20°C. Source: Aspergillus oryzae. 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: DIA-220. | |
| 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. | |
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