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| Product | Description | |
|---|---|---|
| Ammonium Sulphate | White granular solid, soluble in water. Uses: fertilizer, flame retardant, food additive. Group: sulfate salt. Alternative Names: Sulfate of Ammonia. CAS No. 7783-20-2. |  |
| Ammonium Sulphate 7783-20-2 | Ammonium Sulphate - Surface Coatings. SUPPLIERS TO BUSINESS CUSTOMERS ONLY. |  North America & APAC |
| Ammonium Sulphate Crystal | Ammonium Sulphate Crystal - Agriculture Chemicals. SUPPLIERS TO BUSINESS CUSTOMERS ONLY. | North America & APAC |
| Ammonium sulphate,≥99.0%,AR | Ammonium sulphate,≥99.0%,AR is an inorganic sulfate salt used for molecular biology [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 7783-20-2. Pack Sizes: 250 mg; 500 mg. Product ID: HY-Y0261A. |  |
| Ammonium Sulphate Granular | Ammonium Sulphate Granular - Agriculture Chemicals. SUPPLIERS TO BUSINESS CUSTOMERS ONLY. | North America & APAC |
| Ammonium tetradecyl sulphate | Ammonium tetradecyl sulphate. CAS No. 52304-21-9. Pack Sizes: 1 kg. Product ID: CDC10-0420. Molecular formula: C14H33NO4S. Category: Cosmetic Surfactants. Product Keywords: Cosmetic Ingredients; Cosmetic Surfactants; Ammonium tetradecyl sulphate; CDC10-0420; 52304-21-9; C14H33NO4S; 257-834-5; 52304-21-9. Purity: 0.98. EC Number: 257-834-5. Boiling Point: 443.8°C at 760 mmHg. |  |
| Chondroitin sulphate hexasaccharide ammonium salt | Chondroitin sulphate hexasaccharide ammonium salt is a biomedical compound used for studying joint disorders, particularly osteoarthritand rheumatoid arthritis. Its anti-inflammatory effects and ability to promote cartilage regeneration make it an ideal component in pharmaceutical formulations targeting these conditions. Mole weight: 1488. |  |
| Chondroitin sulphate octasaccharide ammonium salt | | |
| Chondroitin sulphate tetrasaccharide ammonium salt | | |
| Dermatan sulphate decasaccharide ammonium salt | | |
| Dermatan sulphate hexasaccharide ammonium salt | | |
| Dermatan sulphate octasaccharide ammonium salt | | |
| Dermatan sulphate tetrasaccharide ammonium salt | | |
| Docosyltrimethylammonium methyl sulphate | This product is white flakes, soluble in water and ethanol, has good compatibility with cationic and non-ionic surfactants, and is stable below 100 °C. Good chemical stability, heat resistance, light resistance, pressure resistance, strong Acid and Alkali resistance. It has excellent thickening, emulsifying and softening properties. This product is used in hair care and shampoo products: conditioners, ointments, shampoos and other hair products softeners. Group: Heterocyclic organic compound. Alternative Names: Docosyltrimethylammonium methyl sulphate;1-Docosanaminium, N,N,N-trimethyl-, methyl sulfate;docosyl-triMethyl-azaniuM;Behenyl trimethyl ammonium methyl sulfate. CAS No. 81646-13-1. Molecular formula: C26H57NO4S. Mole weight: 479.80008. Purity: 0.96. IUPACName: docosyl(trimethyl)azanium; methyl sulfate. Canonical SMILES: CCCCCCCCCCCCCCCCCCCCCC[N+](C)(C)C. COS(=O)(=O)[O-]. ECNumber: 279-791-1. Catalog: ACM81646131. |  |
| Ethyldimethyl(octadecyl)ammonium ethyl sulphate | Heterocyclic Organic Compound. Alternative Names: ethyldimethyl(octadecyl)ammonium ethyl sulphate; Ethyldimethyl (octadecyl)ammoniumethylsulfat; N, N-Dimethyl-N-ethyl-N-octadecylammonium ethosulfate. CAS No. 110-07-6. Molecular formula: C24H53NO4S. Mole weight: 451.74692. Catalog: ACM110076. | |
| Ethylmethyldi(octadecyl)ammonium ethyl sulphate | Heterocyclic Organic Compound. Alternative Names: ethylmethyldi(octadecyl)ammonium ethyl sulphate;1-Octadecanaminium, N-ethyl-N-methyl-N-octadecyl-, ethyl sulfate;1-Octadecanaminium, N-ethyl-N-methyl-N-octadecyl-, ethyl sulfate (1:1);Einecs 233-834-0; Methyldistearylethylammonium ethosulfate. CAS No. 10378-14-0. Molecular formula: C41H87NO4S. Mole weight: 690.19878. Catalog: ACM10378140. | |
| Hexadecyltrimethyl Ammonium hydrogen sulphate | Hexadecyltrimethyl Ammonium hydrogen sulphate. Group: Biochemicals. Grades: Highly Purified. CAS No. 68214-07-3. Pack Sizes: 1g, 2g, 5g, 10g, 25g. Molecular Formula: C19H43NO4S. US Biological Life Sciences. |  Worldwide |
| Acetyl xylan esterase from Cellvibrio japonicus, Recombinant | In enzymology, an acetylxylan esterase (EC 3.1.1.72) is an enzyme that catalyzes a chemical reaction, the deacetylation of xylans and xylo-oligosaccharides. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. Group: Enzymes. Synonyms: Acetylxylan esterase; EC 3.1.1.72; 188959-24-2; 9000-82-2. Enzyme Commission Number: EC 3.1.1.72. CAS No. 188959-24-2;9000-82-2. Purity: > 95 % as judged by SDS-PAGE. Acetylxylan esterase. Mole weight: 39090.9 Da. Activity: 410.0 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Cellvibrio japonicus NCIMB 10462. Acetylxylan esterase; EC 3.1.1.72; 188959-24-2; 9000-82-2. Cat No: NATE-1194. |  |
| Acetyl xylan esterase from Clostridium thermocellum, Recombinant | In enzymology, an acetylxylan esterase (EC 3.1.1.72) is an enzyme that catalyzes a chemical reaction, the deacetylation of xylans and xylo-oligosaccharides. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. Group: Enzymes. Synonyms: Acetylxylan esterase; EC 3.1.1.72; 188959-24-2; 9000-82-2. Enzyme Commission Number: EC 3.1.1.72. CAS No. 188959-24-2;9000-82-2. Purity: > 95 % as judged by SDS-PAGE. Acetylxylan esterase. Mole weight: 37700 Da. Activity: 175 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Clostridium thermocellum. Acetylxylan esterase; EC 3.1.1.72; 188959-24-2; 9000-82-2. Cat No: NATE-1195. | |
| Alcohol dehydrogenase from E. coli, Recombinant | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Applications: High purity recombinant alcohol dehyd...l dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. Mole weight: ~ 38,642 Da. Activity: 6.7 U/mg protein at pH 8.5 and 25°C. Storage: Store at 4°C. Do not store the enzyme in presence of sodium azide. Form: In 3.2 M ammonium sulphate. Source: E. coli. 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-0803. | |
| α-2,3/2,6-Sialyltransferase from Pasteurella multocida, recombinant | α-2,3/2,6-Sialyltransferase from Pasteurella multocida, recombinant. Group: Enzymes. Synonyms: Alpha-2,3/2,6-sialyltransferase/sialidase; β-galactoside α-2,6-sialyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-1,4-N-acety. Enzyme Commission Number: EC 2.4.99.1, 2.4.99.4, 3.2.1.-. Purity: > 95 % as judged by SDS-PAGE. α-Sialyltransferase. Mole weight: 46240.5 Da. Storage: 4°C. Form: Supplied in 3.2 M ammonium sulphate. Source: Pasteurella multocida. Alpha-2,3/2,6-sialyltransferase/sialidase; β-galactoside α-2,6-sialyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine α-2,6-N-acetylneuraminyltransferase; β-galactoside α-2,3-sialyltransferase; CMP-N-acetylneuraminate:β-D-galactoside α-2,3-N-acetylneuraminyl-transferase; CMP-N-acetylneuraminate:β-D-galactoside α-(2?3)-N-acetylneuraminyl-transferase; beta-galactoside alpha-2,6-sialyltransferase; CMP-N-acetylneuraminate:beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine alpha-2,6-N-acetylneuraminyltransferase; beta-galactoside alpha-2,3-sialyltransferase; CMP-N-acetylneuraminate:beta-D-galactoside alpha-2,3-N-acetylneuraminyl-transferase; CMP-N-acetylneuraminate:beta-D-galactoside alpha-(2?3)-N-acetylneuraminyl-transferase. Cat No: NATE-1921 | |
| α-Amylase from Bacillus subtilis, Recombinant | 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. 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. 9000-90-2. Purity: > 95 % as judged by SDS-PAGE. α-Amylase. Mole weight: 72550.6 Da. Activity: 4449.51 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Bacillus subtilis subsp. subtilis str. 168. 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-1172. | |
| α-Amylase from Bacteroides fragilis, Recombinant | 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. 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. 9000-90-2. Purity: > 95 % as judged by SDS-PAGE. α-Amylase. Mole weight: 59099.7 Da. Activity: 36.25 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Bacteroides fragilis NCTC 9343. 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-1173. | |
| α-Amylase from Escherichia coli, Recombinant | 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. 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. 9000-90-2. Purity: > 95 % as judged by SDS-PAGE. α-Amylase. Mole weight: 60459.5 Da. Activity: 23.61 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. W3110. 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-1174. | |
| α-Galactosidase from Clostridium cellulolyticum, Recombinant | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. Purity: > 95 % as judged by SDS-PAGE. GLA. Mole weight: 64179.5 Da. Activity: 186.7 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Clostridium cellulolyticum H10. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Cat No: NATE-1176. | |
| α-Glucosidase from Escherichia coli, Recombinant | Glycoside hydrolases (also called glycosidases or glycosyl hydrolases) assist in the hydrolysis of glycosidic bonds in complex sugars. They are extremely common enzymes with roles in nature including degradation of biomass such as cellulose and hemicellulose, in anti-bacterial defense strategies (e.g., lysozyme), in pathogenesis mechanisms (e.g., viral neuraminidases) and in normal cellular function (e.g., trimming mannosidases involved in N-linked glycoprotein biosynthesis). Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds. Group: Enzymes. Synonyms: Alpha-glucosidase; EC 3.2.1.20; maltase; glucoinvertase; glucosidosucra. Enzyme Commission Number: EC 3.2.1.20. CAS No. 9001-42-7. Purity: > 95 % as judged by SDS-PAGE. α-Glucosidase. Mole weight: 72992.3 Da. Activity: 34.1 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. W3110. 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; glycosidases; glycosyl hydrolases; α-Glucosidase. Cat No: NATE-1177. | |
| α-Glucuronidase from Cellvibrio japonicus, Recombinant | In enzymology, an alpha-glucuronidase (EC 3.2.1.139) is an enzyme that catalyzes the chemical reaction: an alpha-D-glucuronoside + H2O <-> an alcohol + D-glucuronate. Thus, the two substrates of this enzyme are alpha-D-glucuronoside and H2O, whereas its two products are alcohol and D-glucuronate. This enzyme belongs to the family of hydrolases, to be specific those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is alpha-D-glucosiduronate glucuronohydrolase. This enzyme is also called alpha-glucosiduronase. Group: Enzymes. Synonyms: EC 3.2.1.139; alpha-D-glucosiduronate glucuronohydrolase; alpha-glucosiduronase. Enzyme Commission Number: EC 3.2.1.139. CAS No. 37259-81-7. Purity: > 95 % as judged by SDS-PAGE. α-Glucuronidase. Mole weight: 97904.6 Da. Activity: 27.72 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Cellvibrio japonicus NCIMB 10462. EC 3.2.1.139; alpha-D-glucosiduronate glucuronohydrolase; alpha-glucosiduronase. Cat No: NATE-1178. | |
| α-Glucuronidase from Opitutus terrae PB90-1, Recombinant | In enzymology, an alpha-glucuronidase (EC 3.2.1.139) is an enzyme that catalyzes the chemical reaction: an alpha-D-glucuronoside + H2O <-> an alcohol + D-glucuronate. Thus, the two substrates of this enzyme are alpha-D-glucuronoside and H2O, whereas its two products are alcohol and D-glucuronate. This enzyme belongs to the family of hydrolases, to be specific those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is alpha-D-glucosiduronate glucuronohydrolase. This enzyme is also called alpha-glucosiduronase. Group: Enzymes. Synonyms: EC 3.2.1.139; alpha-D-glucosiduronate glucuronohydrolase; alpha-glucosiduronase. Enzyme Commission Number: EC 3.2.1.139. CAS No. 37259-81-7. Purity: > 95 % as judged by SDS-PAGE. α-Glucuronidase. Mole weight: 82809.8 Da. Activity: 21.12 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Opitutus terrae PB90-1. EC 3.2.1.139; alpha-D-glucosiduronate glucuronohydrolase; alpha-glucosiduronase. Cat No: NATE-1179. | |
| Ammonium alum | Ammonium alum. Group: Electrolytes. Alternative Names: ALUMINUM AMMONIUM SULFATE, 12-HYDRATE; ALUMINUM AMMONIUM SULFATE DODECAHYDRATE; ALUMINUM AMMONIUM SULPHATE, DODECHYDRATE; ALUMINUM AMMONIUM SULPHATE HYDRATED; AMMONIUM ALUM; AMMONIUM ALUMINUM SULFATE DODECAHYDRATE; AMMONIUM ALUM SULFATE DODECAHYDRATE; AMMONIUM A. CAS No. 7784-26-1. Product ID: aluminum azanium disulfate dodecahydrate. Molecular formula: 453.33. Mole weight: AlH28< / sub>NO20< / sub>S2< / sub>. [NH4+]. O. O. O. O. O. O. O. O. O. O. O. O. [O-]S(=O)(=O)[O-]. [O-]S(=O)(=O)[O-]. [Al+3]. WZUKKIPWIPZMAS-UHFFFAOYSA-K. 96%. |  |
| Ammonium iron(II)sulfate | Ammonium iron(II)sulfate. Group: other glass and ceramic materials. Alternative Names: ammoniumironsulfate; ammoniumironsulfate(2:2:1); diammoniumferroussulfate; diammoniumironbis(sulphate); diammoniumironsulfate; ferrousdiammoniumdisulfate; Sulfuricacid, ammoniumiron(2+)salt(2:2:1); sulfuricacid, ammoniumiron(2++)salt(2:2:1). CAS No. 10045-89-3. Molecular formula: 284.05. Mole weight: FeH8< / sub>N2< / sub>O8< / sub>S2< / sub>. | |
| Ammonium iron(II)sulfate | Heterocyclic Organic Compound. Alternative Names: ammoniumironsulfate; ammoniumironsulfate(2:2:1); diammoniumferroussulfate; diammoniumironbis(sulphate); diammoniumironsulfate; ferrousdiammoniumdisulfate; Sulfuricacid, ammoniumiron(2+)salt(2:2:1); sulfuricacid, ammoniumiron(2++)salt(2:2:1). CAS No. 10045-89-3. Molecular formula: FeH8N2O8S2. Mole weight: 284.05. Catalog: ACM10045893. | |
| Ammonium iron(II) sulfate hexahydrate | Ammonium iron(II) sulfate hexahydrate. Uses: Used as analytical standard. Group: Electrolytes. Alternative Names: DI-AMMONIUM IRON(II) SULPHATE 6-HYDRATE; IRON(II) AMMONIUM SULFATE; IRON(II) AMMONIUM SULFATE HEXAHYDRATE; FERROUS AMMONIUM SULFATE; FERROUS AMMONIUM SULFATE, 6-HYDRATE; FERROUS AMMONIUM SULFATE HEXAHYDRATE; FERROUS AMMONIUM SULPHATE 6H2O; FERROUS AMMONIUM SULPH. CAS No. 7783-85-9. Molecular formula: 392.14. Mole weight: (NH4)2Fe(SO4)2 · 6H2O. | |
| Ammonium iron(II) sulfate hexahydrate | Used as analytical standard. Group: Metal & ceramic materials. Alternative Names: DI-AMMONIUM IRON(II) SULPHATE 6-HYDRATE;IRON(II) AMMONIUM SULFATE;IRON(II) AMMONIUM SULFATE HEXAHYDRATE;FERROUS AMMONIUM SULFATE;FERROUS AMMONIUM SULFATE, 6-HYDRATE;FERROUS AMMONIUM SULFATE HEXAHYDRATE;FERROUS AMMONIUM SULPHATE 6H2O;FERROUS AMMONIUM SULPH. CAS No. 7783-85-9. Molecular formula: (NH4)2Fe(SO4)2 · 6H2O. Mole weight: 392.14. Catalog: ACM7783859. | |
| Arabinoxylan arabinofuranohydrolase from Bacillus subtilis, Recombinant | Alpha-N-arabinofuranosidase is an enzyme with system name alpha-L-arabinofuranoside arabinofuranohydrolase. This enzyme catalyses the following chemical reaction: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. The enzyme acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Group: Enzymes. Synonyms: non-reducing end alpha-L-arabinofuranosidase; alpha-L-arabinofuranoside non-reducing end alpha-L-arabinofuranosidase; EC 3.2.1.55; arabinosidase; alpha-arabinosidase; alpha-L-arabinosida. Enzyme Commission Number: EC 3.2.1.55. CAS No. 9067-74-7. Purity: > 95 % as judged by SDS-PAGE. α-L-Arabinofuranosidase. Mole weight: 53852.8 Da. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Bacillus subtilis subsp. subtilis str. 168. non-reducing end alpha-L-arabinofuranosidase; alpha-L-arabinofuranoside non-reducing end alpha-L-arabinofuranosidase; EC 3.2.1.55; arabinosidase; alpha-arabinosidase; alpha-L-arabinosidase; alpha-arabinofuranosidase; polysaccharide alpha-L-arabinofuranosidase; alpha-L-arabinofuranoside hydrolase; L-arabinosidase; alpha-L-arabinanase; Alpha-N-arabinofuranosidase; α-L-Arabinofuranosidase. Cat No: NATE-1199. | |
| Arginase from Human, Recombinant | Arginase (EC 3.5.3.1, arginine amidinase, canavanase, L-arginase, arginine transamidinase) is a manganese-containing enzyme. The reaction catalyzed by this enzyme is:arginine + H2O ? ornithine + urea. It is the final enzyme of the urea cycle. It is ubiquitous to all domains of life. Group: Enzymes. Synonyms: Arginase; arginine amidinase; canavanase; L-arginase; arginine transamidinase; EC 3.5.3.1. Enzyme Commission Number: EC 3.5.3.1. CAS No. 9000-96-8. Purity: >95% as judged by SDS-PAGE. Arginase. Mole weight: 35 kDa. Activity: 390 U/mg protein, 1950 U/ml. Storage: Arginase should be stored at 4 °C or and will remain stable up to 3 years if stored as specified. Form: 3.2 M ammonium sulphate. Source: E. coli. Species: Human liver. Arginase; arginine amidinase; canavanase; L-arginase; arginine transamidinase; EC 3.5.3.1. Cat No: NATE-1572. | |
| β-Glucosidase from Bacteroides fragilis, Recombinant | Beta-glucosidase is a glucosidase enzyme that acts upon β1->4 bonds linking two glucose or glucose-substituted molecules (i.e., the disaccharide cellobiose). It is one of the cellulases, enzymes involved in the decomposition of cellulose and related polysaccharides; more specifically, an exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of glucose. Group: Enzymes. Synonyms: EC 3.2.1.21; gentiobiase; cellobiase; emulsin; elaterase; aryl-beta-glucosidase; beta-D-glucosidase; beta-glucoside glucohydrolase; arbutinase; amygdalinase; p-nitrophenyl beta-glucosidase; primeverosidase; amygdalase; linamarase; salicilinase; beta-1,6-. Enzyme Commission Number: EC 3.2.1.21. CAS No. 9001-42-7. Purity: > 95 % as judged by SDS-PAGE. β-Glucosidase. Mole weight: 83500.1 Da. Activity: 27.7 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Bacteroides fragilis NCTC 9343. EC 3.2.1.21; gentiobiase; cellobiase; emulsin; elaterase; aryl-beta-glucosidase; beta-D-glucosidase; beta-glucoside glucohydrolase; arbutinase; amygdalinase; p-nitrophenyl beta-glucosidase; primeverosidase; amygdalase; linamarase; salicilinase; beta-1,6-glucosidase. Cat No: NATE-1181. | |
| β-Glucosidase from Rhizobium etli, Recombinant | Beta-glucosidase is a glucosidase enzyme that acts upon β1->4 bonds linking two glucose or glucose-substituted molecules (i.e., the disaccharide cellobiose). It is one of the cellulases, enzymes involved in the decomposition of cellulose and related polysaccharides; more specifically, an exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of glucose. Group: Enzymes. Synonyms: EC 3.2.1.21; gentiobiase; cellobiase; emulsin; elaterase; aryl-beta-glucosidase; beta-D-glucosidase; beta-glucoside glucohydrolase; arbutinase; amygdalinase; p-nitrophenyl beta-glucosidase; primeverosidase; amygdalase; linamarase; salicilinase; beta-1,6-glucosidase. Enzyme Commission Number: EC 3.2.1.21. CAS No. 9001-42-7. Purity: > 95 % as judged by SDS-PAGE. β-Glucosidase. Mole weight: 53741.8 Da. Activity: 159.5 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Rhizobium etli CFN 42. EC 3.2.1.21; gentiobiase; cellobiase; emulsin; elaterase; aryl-beta-glucosidase; beta-D-glucosidase; beta-glucoside glucohydrolase; arbutinase; amygdalinase; p-nitrophenyl beta-glucosidase; primeverosidase; amygdalase; linamarase; salicilinase; beta-1,6-glucosidase. Cat No: NATE-1183. | |
| β-Mannosidase from Bacteroides fragilis, Recombinant | Beta-mannosidase is an enzyme with system name beta-D-mannoside mannohydrolase. This enzyme catalyses the following chemical reaction:Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. This gene encodes a member of the glycosyl hydrolase 2 family. The encoded protein localizes to the lysosome where it is the final exoglycosidase in the pathway for N-linked glycoprotein oligosaccharide catabolism. Mutations in this gene are associated with beta-mannosidosis, a lysosomal storage disease that has a wide spectrum of neurological involvement. Group: Enzymes. Synonyms: β-mannosidase; mannanase; mannase; β-D-mannosidase; β-mannoside mannohydrolase; exo-β-D-mannanase; EC 3.2.1.25; 9025-43-8. Enzyme Commission Number: EC 3.2.1.25. CAS No. 9025-43-8. Purity: > 95 % as judged by SDS-PAGE. β-Mannosidase. Mole weight: 100520.1 Da. Activity: 5.32 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Bacteroides fragilis NCTC 9343. β-mannosidase; mannanase; mannase; β-D-mannosidase; β-mannoside mannohydrolase; exo-β-D-mannanase; EC 3.2.1.25; 9025-43-8. Cat No: NATE-1185. | |
| β-Mannosidase from Bacteroides thetaiotaomicron, Recombinant | Beta-mannosidase is an enzyme with system name beta-D-mannoside mannohydrolase. This enzyme catalyses the following chemical reaction:Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. This gene encodes a member of the glycosyl hydrolase 2 family. The encoded protein localizes to the lysosome where it is the final exoglycosidase in the pathway for N-linked glycoprotein oligosaccharide catabolism. Mutations in this gene are associated with beta-mannosidosis, a lysosomal storage disease that has a wide spectrum of neurological involvement. Group: Enzymes. Synonyms: β-mannosidase; mannanase; mannase; β-D-mannosidase; β-mannoside mannohydrolase; exo-β-D-mannanase; EC 3.2.1.25; 9025-43-8. Enzyme Commission Number: EC 3.2.1.25. CAS No. 9025-43-8. Purity: > 95 % as judged by SDS-PAGE. β-Mannosidase. Mole weight: 96040.16 Da. Activity: 10.62 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Bacteroides thetaiotaomicron VPI-5482. β-mannosidase; mannanase; mannase; β-D-mannosidase; β-mannoside mannohydrolase; exo-β-D-mannanase; EC 3.2.1.25; 9025-43-8. Cat No: NATE-1186. | |
| β-Mannosidase from Cellvibrio japonicus, Recombinant | Beta-mannosidase is an enzyme with system name beta-D-mannoside mannohydrolase. This enzyme catalyses the following chemical reaction:Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. This gene encodes a member of the glycosyl hydrolase 2 family. The encoded protein localizes to the lysosome where it is the final exoglycosidase in the pathway for N-linked glycoprotein oligosaccharide catabolism. Mutations in this gene are associated with beta-mannosidosis, a lysosomal storage disease that has a wide spectrum of neurological involvement. Group: Enzymes. Synonyms: β-mannosidase; mannanase; mannase; β-D-mannosidase; β-mannoside mannohydrolase; exo-β-D-mannanase; EC 3.2.1.25; 9025-43-8. Enzyme Commission Number: EC 3.2.1.25. CAS No. 9025-43-8. Purity: > 95 % as judged by SDS-PAGE. β-Mannosidase. Mole weight: 48581.4 Da. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Cellvibrio japonicus NCIMB 10462. β-mannosidase; mannanase; mannase; β-D-mannosidase; β-mannoside mannohydrolase; exo-β-D-mannanase; EC 3.2.1.25; 9025-43-8. Cat No: NATE-1187. | |
| β-Mannosidase from Cellvibrio mixtus, Recombinant | Beta-mannosidase is an enzyme with system name beta-D-mannoside mannohydrolase. This enzyme catalyses the following chemical reaction:Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. This gene encodes a member of the glycosyl hydrolase 2 family. The encoded protein localizes to the lysosome where it is the final exoglycosidase in the pathway for N-linked glycoprotein oligosaccharide catabolism. Mutations in this gene are associated with beta-mannosidosis, a lysosomal storage disease that has a wide spectrum of neurological involvement. Group: Enzymes. Synonyms: β-mannosidase; mannanase; mannase; β-D-mannosidase; β-mannoside mannohydrolase; exo-β-D-mannanase; EC 3.2.1.25; 9025-43-8. Enzyme Commission Number: EC 3.2.1.25. CAS No. 9025-43-8. Purity: > 95 % as judged by SDS-PAGE. β-Mannosidase. Mole weight: 50300 Da. Activity: 40 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Cellvibrio mixtus. β-mannosidase; mannanase; mannase; β-D-mannosidase; β-mannoside mannohydrolase; exo-β-D-mannanase; EC 3.2.1.25; 9025-43-8. Cat No: NATE-1188. | |
| β-Xylosidase from Bacillus subtilis, Recombinant | Releases reducing sugars from birchwood xylan (X0502), also catalyzes the hydrolysis of 4-methylumbelliferyl-β-D-cellobioside and 4-methylumbelliferyl-β-D-glucopyranoside. This enzyme does not possess endo-xylanase, arabinoxylanase or β-glucanase activities. β-Xylosidase undergoes post-translation glycosylation which has been shown to be critical for its proper activity and stability. Deglycosylation altered the the optimum temperature and pH for activity and decreased its thermostability. Group: Enzymes. Synonyms: β-Xylosidase; β-Xylosidase, thermostable; 9025-53-0. Enzyme Commission Number: EC 3.2.1.37. CAS No. 9025-53-0. Purity: > 95 % as judged by SDS-PAGE. β-Xylosidase. Mole weight: 64909.6 Da. Activity: 20.67 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Bacillus subtilis subsp. subtilis str. 168. β-Xylosidase; β-Xylosidase, thermostable; 9025-53-0. Cat No: NATE-1190. | |
| β-Xylosidase from Lactobacillus brevis, Recombinant | Releases reducing sugars from birchwood xylan (X0502), also catalyzes the hydrolysis of 4-methylumbelliferyl-β-D-cellobioside and 4-methylumbelliferyl-β-D-glucopyranoside. This enzyme does not possess endo-xylanase, arabinoxylanase or β-glucanase activities. β-Xylosidase undergoes post-translation glycosylation which has been shown to be critical for its proper activity and stability. Deglycosylation altered the the optimum temperature and pH for activity and decreased its thermostability. Group: Enzymes. Synonyms: β-Xylosidase; β-Xylosidase, thermostable; 9025-53-0. Enzyme Commission Number: EC 3.2.1.37. CAS No. 9025-53-0. Purity: > 95 % as judged by SDS-PAGE. β-Xylosidase. Mole weight: 63608.3 Da. Activity: 26.76 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Lactobacillus brevis ATCC 367. β-Xylosidase; β-Xylosidase, thermostable; 9025-53-0. Cat No: NATE-1191. | |
| β-Xylosidase from Opitutus terrae, Recombinant | Releases reducing sugars from birchwood xylan (X0502), also catalyzes the hydrolysis of 4-methylumbelliferyl-β-D-cellobioside and 4-methylumbelliferyl-β-D-glucopyranoside. This enzyme does not possess endo-xylanase, arabinoxylanase or β-glucanase activities. β-Xylosidase undergoes post-translation glycosylation which has been shown to be critical for its proper activity and stability. Deglycosylation altered the the optimum temperature and pH for activity and decreased its thermostability. Group: Enzymes. Synonyms: β-Xylosidase; β-Xylosidase, thermostable; 9025-53-0. Enzyme Commission Number: EC 3.2.1.37. CAS No. 9025-53-0. Purity: > 95 % as judged by SDS-PAGE. β-Xylosidase. Mole weight: 81101.4 Da. Activity: 31.35 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Opitutus terrae PB90-1. β-Xylosidase; β-Xylosidase, thermostable; 9025-53-0. Cat No: NATE-1192. | |
| Diammonium phosphate sulfate | Heterocyclic Organic Compound. Alternative Names: diammonium phosphate sulphate;Ammonium phosphate sulfate ((NH4)2(H2PO4)(HSO4));Ammonium phosphate sulfate ((NH4)2H3(PO4)(SO4)). CAS No. 12593-60-1. Molecular formula: H11N2O8PS. Mole weight: 212.119421. Catalog: ACM12593601. | |
| Dioleoylamidoethyl hydroxyethylmonium methosulfate | Leveling agent in cationic dyes, antistatic agent, softening agent in textile, fiber, leather. Group: Oil fieldtextile industry. Alternative Names: (2-Hydroxyethyl)methylbis(2-((1-oxooctadec-9-enyl)amino)ethyl)ammonium, (9Z)-, methyl sulphate. CAS No. 92888-37-4. Molecular formula: C44H87N3O7S. Mole weight: 802.24. IUPACName: 2-Hydroxyethyl-methyl-bis[2-(octadec-9-enoylamino)ethyl]azanium;methyl sulfate. Canonical SMILES: CCCCCCCCC=CCCCCCCCC (=O)NCC[N+] (C) (CCNC (=O)CCCCCCCC=CCCCCCCCC)CCO. COS (=O) (=O)[O-]. Catalog: ACM92888374. | |
| endo-1,4-β-Xylanase from Clostridium thermocellum, Recombinant | Xylanase is the name given to a class of enzymes which degrade the linear polysaccharide beta-1,4-xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls. As such, it plays a major role in micro-organisms thriving on plant sources for the degradation of plant matter into usable nutrients. Xylanases are produced by fungi, bacteria, yeast, marine algae, protozoans, snails, crustaceans, insect, seeds, etc., (mammals do not produce xylanases). Group: Enzymes. Synonyms: EC 3.2.1.8; endo-(1?4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-&. Enzyme Commission Number: EC 3.2.1.8. CAS No. 9025-57-4. Purity: > 95 % as judged by SDS-PAGE. Xylanase. Mole weight: 39474.6 Da. Activity: 2500 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Clostridium thermocellum. EC 3.2.1.8; endo-(1?4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-β-xylan xylanohydrolase; β-xylanase; β-1,4-xylan xylanohydrolase; endo-1,4-β-xylanase; β-D-xylanase; endo-1,4-β-xylanase. Cat No: NATE-1202. | |
| Endo-arabinanase from Streptomyces coelicolor, Recombinant | Arabinan endo-1,5-alpha-L-arabinanase is an enzyme with system name 5-alpha-L-arabinan 5-alpha-L-arabinanohydrolase. This enzyme catalyses the following chemical reaction: Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans. This enzyme is most active on linear 1,5-alpha-L-arabinan. Group: Enzymes. Synonyms: EC 3.2.1.99; endo-exo-Arabinanase; endo-1,5-alpha-L-arabinanase; endo-alpha-1,5-arabanase; endo-arabanase; 1,5-alpha-L-arabinan 1,5-alpha-L arabinanohydrolase. Enzyme Commission Number: EC 3.2.1.99. Purity: > 80 % as judged by SDS-PAGE. endo-1,5-α-Arabinanase. Mole weight: 33858.2 Da. Activity: 16.05 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Streptomyces coelicolor. EC 3.2.1.99; endo-exo-Arabinanase; endo-1,5-alpha-L-arabinanase; endo-alpha-1,5-arabanase; endo-arabanase; 1,5-alpha-L-arabinan 1,5-alpha-L arabinanohydrolase. Cat No: NATE-1205. | |
| Endo-β-N-acetylglucosaminidase from Clostridium perfringens, Recombinant | An Endoglycosidase is an enzyme that releases oligosaccharides from glycoproteins or glycolipids. It may also cleave polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common. It breaks the glycosidic bonds between two sugar monomer in the polymer. It is different from exoglycosidase that it does not do so at the terminal residue. Hence, it is used to release long carbohydrates from conjugated molecules. If an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. An endoglycosidase cleaves, giving a polymeric product. Group: Enzymes. Synonyms: Endoglycosidase; Endo-β-N-acetylglucosaminidase; EC 3.2.1.96; 231-791-2. Enzyme Commission Number: EC 3.2.1.96. CAS No. 37278-88-9. Purity: > 95 % as judged by SDS-PAGE. Endo-β-N-acetylglucosaminidase. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Clostridium perfringens. Endoglycosidase; Endo-β-N-acetylglucosaminidase; EC 3.2.1.96; 231-791-2. Cat No: NATE-1203. | |
| Feruloyl esterase from Acetivibrio cellulolyticus, Recombinant | In enzymology, a feruloyl esterase (EC 3.1.1.73) is an enzyme that catalyzes the chemical reaction: feruloyl-polysaccharide + H2O rightleftharpoons ferulate + polysaccharide. Thus, the two substrates of this enzyme are feruloyl-polysaccharide and H2O, whereas its two products are ferulate and polysaccharide. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. Group: Enzymes. Synonyms: feruloyl esterase; ferulic acid esterase (FAE); hydroxycinnamoyl esterase; hemicellulase accessory enzyme; cinnamoyl ester hydrolase (cinnAE); EC 3.1.1.73; 4-hydroxy-3-methoxycinnamoyl-sugar hydrolase. Enzyme Commission Number: EC 3.1.1.73. CAS No. 134712-49-5. Purity: > 95 % as judged by SDS-PAGE. Feruloyl esterase. Mole weight: 32631.3 Da. Activity: 1.169 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Acetivibrio cellulolyticus. feruloyl esterase; ferulic acid esterase (FAE); hydroxycinnamoyl esterase; hemicellulase accessory enzyme; cinnamoyl ester hydrolase (cinnAE); EC 3.1.1.73; 4-hydroxy-3-methoxycinnamoyl-sugar hydrolase. Cat No: NATE-1204. | |
| Galactose dehydrogenase from recombinant E. coli | In enzymology, a galactose 1-dehydrogenase (EC 1.1.1.48) is an enzyme that catalyzes the chemical reaction: D-galactose + NAD+ rightleftharpoons D-galactono-1,4-lactone + NADH + H+. Thus, the two substrates of this enzyme are D-galactose and NAD+, whereas its 3 products are D-galactono-1,4-lactone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in galactose metabolism. Group: Enzymes. Synonyms: D-galactose:NAD+ 1-oxidoreductase; D-galactose dehydrogenase; beta-galactose dehydrogenase; NAD+-dependent D-galactose dehydrogenase; galactose 1-dehydrogenase; EC 1.1.1.48; Galactose dehydrogenase. Enzyme Commission Number: EC 1.1.1.48. CAS No. 9028-54-0. Galactose dehydrogenase. Mole weight: ca. 33,800. Activity: more than 80 U/mg protein. Stability: Stable at 4 °C for at least one year. Storage: Store at 4 to 10 °C (Do not freeze). Form: Ammonium sulphate suspension. Source: E. coli. D-galactose:NAD+ 1-oxidoreductase; D-galactose dehydrogenase; beta-galactose dehydrogenase; NAD+-dependent D-galactose dehydrogenase; galactose 1-dehydrogenase; EC 1.1.1.48; Galactose dehydrogenase. Cat No: NATE-1931. | |
| Glucokinase from Escherichia coli, Recombinant | Glucokinase (EC 2.7.1.2) is an enzyme that facilitates phosphorylation of glucose to glucose-6-phosphate. Glucokinase occurs in cells in the liver, pancreas, gut, and brain of humans and most other vertebrates. In each of these organs it plays an important role in the regulation of carbohydrate metabolism by acting as a glucose sensor, triggering shifts in metabolism or cell function in response to rising or falling levels of glucose, such as occur after a meal or when fasting. Mutations of the gene for this enzyme can cause unusual forms of diabetes or hypoglycemia. Group: Enzymes. Synonyms: EC 2.7.1.2; glucokinase; glucokinase (phosphorylating); 9001-36-9; GCK; FGQTL3; GK; GLK; HHF3; HK4; HKIV; HXKP; LGLK; MODY2. Enzyme Commission Number: EC 2.7.1.2. CAS No. 9001-36-9. Purity: >95% as judged by SDS-PAGE. GCK. Mole weight: 35 kDa. Activity: 5.8 U/mg protein, 98.6 U/ml. Storage: Glucokinase should be stored at 4 °C, remaining stable up to 3 years under these storage conditions. Form: 3.2 M ammonium sulphate. Source: E. coli. Species: Escherichia coli. EC 2.7.1.2; glucokinase; glucokinase (phosphorylating); 9001-36-9; GCK; FGQTL3; GK; GLK; HHF3; HK4; HKIV; HXKP; LGLK; MODY2. Cat No: NATE-1571. | |
| Glucose-6-phosphate Dehydrogenase from E. coli, Recombinant | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Group: Enzymes. Synonyms: EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate . Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Mole weight: ~ 56,770. Activity: 172 U/mg. Stability: > 2 years. Storage: 4°C. Form: In 3.2 M ammonium sulphate. Source: E. coli. Species: E. coli. EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase; 9001-40-5. Cat No: DIA-407. | |
| Glutathione reductase from E. coli, Recombinant | Glutathione reductase (GR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the precess is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl prote...e; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Enzyme Commission Number: EC 1.8.1.7. CAS No. 9001-48-3. Purity: >95% as judged by SDS-PAGE. GR. Mole weight: 49.5 kDa. Activity: 35 U/mg protein, 98 U/ml. Storage: Glutathione reductase should be stored at 4 °C or and will remain stable up to 3 years if stored as specified. Form: 3.2 M ammonium sulphate. Source: E. coli. Species: E. coli. GR; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Cat No: NATE-1574. | |
| Glycogen branching enzyme from Bacillus subtilis, Recombinant | Glycogen branching enzyme is an enzyme that adds branches to the growing glycogen molecule during the synthesis of glycogen, a storage form of glucose. More specifically, during glycogen synthesis, a glucose 1-phosphate molecule reacts with uridine triphosphate (UTP) to become UDP-glucose, an activated form of glucose. The activated glucosyl unit of UDP-glucose is then transferred to the hydroxyl group at the C-4 of a terminal residue of glycogen to form an α-1,4-glycosidic linkage, a reaction catalyzed by glycogen synthase. Importantly, glycogen synthase can only catalyze the synthesis of α-1,4-glycosidic linkages. Since glycogen is a readily mobil...;-1,4-glucan-6-glycosyltransferase; starch branching enzyme; 1,4-α-D-glucan:1,4-α-D-glucan 6-α-D-(1,4-α-D-glucano)-transferase. Enzyme Commission Number: EC 2.4.1.18. CAS No. 9001-97-2. Purity: > 95 % as judged by SDS-PAGE. Glycogen branching enzyme. Mole weight: 77485.4 Da. Activity: 38.04 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Bacillus subtilis subsp. subtilis str. 168. Branching enzyme, amylo-(1,4?1,6)-transglycosylase; Q-enzyme; α-glucan-branching glycosyltransferase; amylose isomerase; enzymatic branching factor; branching glycosyltransferase; enzyme Q; gluc | |
| Glycogen branching enzyme from Bacteroides fragilis, Recombinant | Glycogen branching enzyme is an enzyme that adds branches to the growing glycogen molecule during the synthesis of glycogen, a storage form of glucose. More specifically, during glycogen synthesis, a glucose 1-phosphate molecule reacts with uridine triphosphate (UTP) to become UDP-glucose, an activated form of glucose. The activated glucosyl unit of UDP-glucose is then transferred to the hydroxyl group at the C-4 of a terminal residue of glycogen to form an α-1,4-glycosidic linkage, a reaction catalyzed by glycogen synthase. Importantly, glycogen synthase can only catalyze the synthesis of α-1,4-glycosidic linkages. Since glycogen is a readily mobi...1,4-glucan-6-glycosyltransferase; starch branching enzyme; 1,4-α-D-glucan:1,4-α-D-glucan 6-α-D-(1,4-α-D-glucano)-transferase. Enzyme Commission Number: EC 2.4.1.18. CAS No. 9001-97-2. Purity: > 95 % as judged by SDS-PAGE. Glycogen branching enzyme. Mole weight: 81104.6 Da. Activity: 50.88 U/mg (pH 7.0; 3.3 mg/mL starch). Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate, containing 0.5 M imidazole and 0.5 M NaCl, pH ~ 6.8. Source: Bacteroides fragilis NCTC 9343. Branching enzyme, amylo-(1,4?1,6)-transglycosylase; Q-enzyme; α-glucan-branching glycosyltransferase; amylose isomerase; enzym | |
| Glycogen branching enzyme from Escherichia coli, Recombinant | Glycogen branching enzyme is an enzyme that adds branches to the growing glycogen molecule during the synthesis of glycogen, a storage form of glucose. More specifically, during glycogen synthesis, a glucose 1-phosphate molecule reacts with uridine triphosphate (UTP) to become UDP-glucose, an activated form of glucose. The activated glucosyl unit of UDP-glucose is then transferred to the hydroxyl group at the C-4 of a terminal residue of glycogen to form an α-1,4-glycosidic linkage, a reaction catalyzed by glycogen synthase. Importantly, glycogen synthase can only catalyze the synthesis of α-1,4-glycosidic linkages. Since glycogen is a readily mobili...;-1,4-glucan-6-glycosyltransferase; starch branching enzyme; 1,4-α-D-glucan:1,4-α-D-glucan 6-α-D-(1,4-α-D-glucano)-transferase. Enzyme Commission Number: EC 2.4.1.18. CAS No. 9001-97-2. Purity: > 95 % as judged by SDS-PAGE. Glycogen branching enzyme. Mole weight: 88157.0 Da. Activity: 15.44 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. W3110. Branching enzyme, amylo-(1,4?1,6)-transglycosylase; Q-enzyme; α-glucan-branching glycosyltransferase; amylose isomerase; enzymatic branching factor; branching glycosyltransferase; enzyme Q; glucos | |
| Hyaluronate lyase from Streptococcus equi, Recombinant | Hyaluronate lyase degrades hyaluronate using an elimination reaction to break glycosidic linkages yielding unsaturated disaccharide products. Group: Enzymes. Synonyms: hyaluronidase; glucuronoglycosaminoglycan lyase; spreading factor; mucinase; 37259-53-3; EC 4.2.2.1; hyaluronate lyase. Enzyme Commission Number: EC 4.2.2.1. CAS No. 37259-53-3. Purity: > 95 % as judged by SDS-PAGE. Hyaluronate Lyase. Mole weight: 38447.1 Da. Activity: 4.6 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Streptococcus equi 4047. hyaluronidase; glucuronoglycosaminoglycan lyase; spreading factor; mucinase; 37259-53-3; EC 4.2.2.1; hyaluronate lyase. Cat No: NATE-1210. | |
| Hyaluronate lyase from Streptomyces coelicolor, Recombinant | Hyaluronate lyase degrades hyaluronate using an elimination reaction to break glycosidic linkages yielding unsaturated disaccharide products. Group: Enzymes. Synonyms: hyaluronidase; glucuronoglycosaminoglycan lyase; spreading factor; mucinase; 37259-53-3; EC 4.2.2.1; hyaluronate lyase. Enzyme Commission Number: EC 4.2.2.1. CAS No. 37259-53-3. Purity: > 95 % as judged by SDS-PAGE. Hyaluronate Lyase. Mole weight: 82914.2 Da. Activity: 8.1 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Streptomyces coelicolor A3(2). hyaluronidase; glucuronoglycosaminoglycan lyase; spreading factor; mucinase; 37259-53-3; EC 4.2.2.1; hyaluronate lyase. Cat No: NATE-1211. | |
| Invertase from S. cerevisiae, Recombinant | Invertase is an enzyme that catalyzes the hydrolysis (breakdown) of sucrose (table sugar). The resulting mixture of fructose and glucose is called inverted sugar syrup. Related to invertases are sucrases. Invertases and sucrases hydrolyze sucrose to give the same mixture of glucose and fructose. Invertases cleave the O-C(fructose) bond, whereas the sucrases cleave the O-C(glucose) bond. Group: Enzymes. Synonyms: EC 3.2.1.26; saccharase; glucosucrase; beta-h-fructosidase; beta-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase; beta-fructofuranosidase. Enzyme Commission Number: EC 3.2.1.26. CAS No. 9001-57-4. Purity: >95% as judged by SDS-PAGE. Invertase. Mole weight: 60.64 kDa. Activity: 7600 U/ml. Storage: Invertase should be stored at 4 °C or and will remain stable up to 3 years if stored as specified. Form: 3.2 M ammonium sulphate. Source: E. coli. Species: S. cerevisiae. EC 3.2.1.26; saccharase; glucosucrase; beta-h-fructosidase; beta-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase; beta-fructofuranosidase. Cat No: NATE-1573. | |
| Isoamylase from Escherichia coli, Recombinant | Isoamylase is an enzyme with system name glycogen 6-alpha-D-glucanohydrolase. This enzyme catalyses the following chemical reaction:Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins. This enzyme also readily hydrolyses amylopectin. Group: Enzymes. Synonyms: EC 3.2.1.68; debranching enzyme; glycogen alpha-1,6-glucanohydrolase; isoamylase. Enzyme Commission Number: EC 3.2.1.68. CAS No. 9067-73-6. Purity: > 95 % as judged by SDS-PAGE. Isoamylase. Mole weight: 77396.8 Da. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. W3110. EC 3.2.1.68; debranching enzyme; glycogen alpha-1,6-glucanohydrolase; isoamylase. Cat No: NATE-1212. | |
| L-Lactate Dehydrogenase from Porcine, Recombinant | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: High purity l-lactate dehydrogenase (porcine) for use in research, biochemical enzyme assays and in vitro diagnostic analysis. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L- (+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. Activity: ~ 330 U/mg. Storage: > 2 years at 4°C. Form: In 3.2 M ammonium sulphate. Source: Porcine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L- (+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-1105. | |
| Macrolide glycosyltransferase from Streptomyces lividans, Recombinant | UDP glycosyltransferases (UGT) are a superfamily of enzymes that catalyzes the addition of the glycosyl group from a UTP-sugar to a small hydrophobic molecule. Group: Enzymes. Synonyms: UDP-glucose: oleandomycin β-glucosyltransferase; UDP-glucose: tylosin β-glucosyltransferase; UDP-glucose: erythromycin β-glucosyltransferase; Macrolide glycosyltransferase; Oleandomycin glycosyltransferase. Enzyme Commission Number: EC 2.4.1.-. Purity: > 95 % as judged by SDS-PAGE. Macrolide glycosyltransferase. Mole weight: 45551.4 Da. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Streptomyces lividans DSMZ 46482. UDP-glucose: oleandomycin β-glucosyltransferase; UDP-glucose: tylosin β-glucosyltransferase; UDP-glucose: erythromycin β-glucosyltransferase; Macrolide glycosyltransferase; Oleandomycin glycosyltransferase. Cat No: NATE-1214. | |
| Maltooligosyl trehalose trehalohydrolase from Bradyrhizobium sp., Recombinant | 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase (EC 3.2.1.141, malto-oligosyltrehalose trehalohydrolase) is an enzyme with system name 4-alpha-D-((1->4)-alpha-D-glucano)trehalose glucanohydrolase (trehalose-producing).This enzyme catalyses the following chemical reaction: hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-[(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-alpha-D-glucan. Group: Enzymes. Synonyms: 4-α-D-{(1?4)-α-D-Glucano}trehalose trehalohydrolase; 4-α-D-(1,4-α-D-glucano)trehalose glucanohydrolase (trehalose-producing); 4-alpha-D. Enzyme Commission Number: EC 3.2.1.141. CAS No. 170780-50-4. Purity: > 95 % as judged by SDS-PAGE. Maltooligosyl trehalose trehalohydrolase. Mole weight: 69634.7 Da. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Bradyrhizobium sp. BTAi1. 4-α-D-{(1?4)-α-D-Glucano}trehalose trehalohydrolase; 4-α-D-(1,4-α-D-glucano)trehalose glucanohydrolase (trehalose-producing); 4-alpha-D-{(1?4)-alpha-D-glucano}trehalose trehalohydrolase; 4-alpha-D-(1,4-alpha-D-glucano)trehalose glucanohydrolase (trehalose-producing); Malto-oligosyltrehalose trehalohydrolase; EC 3.2.1.141; Maltooligosyl trehalose trehalohydrolase. Cat No: NATE-1215. | |
| Mannosylglycerate synthase from Rhodothermus marinus, Recombinant | Mannosylglycerate synthase (EC 2.4.1.269) is an enzyme with system name GDP-mannose:D-glycerate 2-alpha-D-mannosyltransferase. This enzyme catalyses the following chemical reaction: GDP-mannose + D-glycerate <-> GDP + 2-O-(alpha-D-mannopyranosyl) -D-glycerate. Depending on conditions mannosylglycerate synthase is more or less specific for the GDP-mannose and D-glycerate. Group: Enzymes. Synonyms: GDP-Man:mannosylglycerate synthase; α-mannosyltransferase; GDP-mannose:D-glycerate 2-alpha-D-mannosyltransferase. Enzyme Commission Number: EC 2.4.1.-. Purity: > 95 % as judged by SDS-PAGE. Mannosylglycerate synthase. Mole weight: 47190.6 Da. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Rhodothermus marinus DSM 4252. GDP-Man:mannosylglycerate synthase; α-mannosyltransferase; GDP-mannose:D-glycerate 2-alpha-D-mannosyltransferase; Mannosylglycerate synthase; EC 2.4.1.-. Cat No: NATE-1216. | |
| NAD Kinase from Human, Recombinant | NAD kinase catalyzes the transfer of a phosphate group from ATP to NAD+ to generate NADP+, which in its reduced form acts as an electron donor for biosynthetic reactions. NADP+ is an essential coenzyme in metabolism and provides reducing power to biosynthetic processes such as fatty acid biosynthesis. Group: Enzymes. Synonyms: NADK; Poly (P)/ATP NAD Kinase; EC 2.7.1.23. CAS No. 9032-66-0. Purity: > 95% determined by SDS-PAGE. NADK. Mole weight: ~50 kDa (monomer). Human full length NAD kinase (aa 1-446) is fused at the N-terminus to a His-tag. Activity: > 1U/mg. Appearance: Liquid. Storage: at -20°C. Form: 1 mg/ml of ammonium sulphate suspension. Source: E. coli. Species: Human. NADK; Poly (P)/ATP NAD Kinase; EC 2.7.1.23; NAD Kinase. Cat No: NATE-1283. | |
| 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 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 Penicillium citrinum Nuclease P1 | Nuclease P1 from Penicillium citrinum is a zinc-dependent endonuclease that exhibits increased activity in the presence of low concentrations of urea. Applications: Nuclease p1 from penicillium citrinum has been used in a study to assess crystal structures using ammonium sulphate or polyethylene glycol 4000 as a precipitating agent. it has also been used in a study to investigate a method for the direct sequence analysis 20-25 nucleotides from the terinini of 5? or 3? end group labeled rna. nuclease p1 is used to improve the sensitivity of a 32p-labeling method for the detection of dna adducts. the enzyme has an optimal temperature of approximately 70 oc, but for a long incubation, a temperature below 60 oc is more suitable. it is stable in the ph range of 5-8. Group: Enzymes. Synonyms: Endonuclease P1; EC 3.1.30.1; 54576-84-0; Nuclease P1; P1 nuclease. Enzyme Commission Number: EC 3.1.30.1. CAS No. 54576-84-0. Nuclease. Mole weight: 42-50 kDa. Activity: > 200 units/mg protein (E1%/280, 3?-5?-Phosphodiesterase). Storage: 2-8°C. Form: lyophilized powder. Source: Penicillium citrinum. Endonuclease P1; EC 3.1.30.1; 54576-84-0; Nuclease P1; P1 nuclease. Pack: vial of > 250 units (using RNA substrate). Cat No: NATE-0491. | |
| Native Thermoactinomyces intermedius Phenylalanine Dehydrogenase | Phenylalanine dehydrogenase is a member of a large family of amino-acid dehydrogenases, which includes glutamate dehydrogenase, alanine dehydrogenase, leucine dehydrogenase, lysine EUR-dehydrogenase, and meso-a,EUR-diaminopimelate D-dehydrogenase. The three known gene sequences are octomers. It has a two-domain, three-dimensional structure. Group: Enzymes. Synonyms: phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Enzyme Commission Number: EC 1.4.1.20. CAS No. 69403-12-9. PHD. Mole weight: ca. 380,000; Subunit molecular weight : ca. 40,000. Appearance: Ammonium sulphate suspension. Storage: Stable at 0 to 4 °C for at least six months (Do not freeze). Source: Thermoactinomyces intermedius. phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Cat No: NATE-1906. | |
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