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| Product | Description | |
|---|---|---|
| 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. | |
| 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. | |
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