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| Product | Description | |
|---|---|---|
| α(1-2,3) Mannosidase from Xanthomonas manihotis, Recombinant | 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. Α1-2,3 mannosidase is a highly specific exoglycosidase that catalyzes the hydrolysis of α1-2 and α1-3 linked d-mannopyranosyl residues from oligosaccharides. Group: Enzymes. Synonyms: alpha-D-mannosidase; alpha-mannosidase; alpha-D-mannoside mannohydrolase; α-D-Mannosidase; EC 3.2.1.24; 9025-42-7. Mannosidase. Mole weight: 90 kDa. Activity: 80,000 units/mg. Storage: 4°C. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C) and 1 mM Na2 EDTA. Source: E. coli. Species: Xanthomonas manihotis. alpha-D-mannosidase; alpha-mannosidase; alpha-D-mannoside mannohydrolase; α-D-Mannosidase; EC 3.2.1.24; 9025-42-7; α(1-2,3) Mannosidase. Cat No: NATE-1269. |  |
| α1-3,4,6 Galactosidase | α1-3,4,6 Galactosidase is a broad specificity exoglycosidase that catalyzes the hydrolysis of terminal, non-reducing α1-3, α1-4 and α1-6-linked galactose residues from oligosaccharides [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9025-35-8. Pack Sizes: 100 U; 500 U. Product ID: HY-P2871B. |  |
| α(1-3,4) Fucosidase from Sweet almond, Recombinant | 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. Α1-3,4 fucosidase, (also known as amf) is a broad specificity exoglycosidase that catalyzes the hydrolysis of α1-3 and α1-4 linked fucose residues from oligosaccharides and glycoproteins. Group: Enzymes. Synonyms: α-L-fucoside fucohydrolase; Alpha-Fucosidase; FUCA1; FUCA; EC 3.2.1.51. FUCA. Mole weight: 56000 daltons. Activity: 75,000 units/mg. Storage: 4°C. Form: 20 mM Tris-HCl (pH 7.5), 50 mM NaCl and 1 mM EDTA. Source: Pichia pastoris. Species: Sweet almond tree. α-L-fucoside fucohydrolase; Alpha-Fucosidase; FUCA1; FUCA; EC 3.2.1.51; α(1-3,4) Fucosidase. Cat No: NATE-1264. | |
| α(1-3,6) Galactosidase from Xanthomonas manihotis, 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). Α1-3,6 galactosidase is a highly specific exoglycosidase that catalyzes the hydrolysis of α1-3 and α1-6 linked d-galactopyranosyl residues from oligosaccharides. Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Purity: > 95% determined by SDS-PAGE. GLA. Mole weight: 70000 daltons. Activity: 137,000 units/mg. Storage: Recommended storage temperature is 4°C. Avoid repeated freeze/thaw cycles. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C) and 1 mM Na2EDTA. Source: E. coli. Species: Xanthomonas manihotis. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α(1-3,6) Galactosidase. Cat No: NATE-1279. | |
| α1-6 Mannosidase, Xanthomonas phaseoli | α1-6 Mannosidase, Xanthomonas phaseoli is a highly specific exoglycosidase that removes unbranched α1-6 linked mannose residues from oligosaccharides [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9025-42-7. Pack Sizes: 500 U. Product ID: HY-P2950A. | |
| β1-3,4,6 Galactosidase | β1-3,4,6 Galactosidase is a broad specificity exoglycosidase that catalyzes the hydrolysis of terminal, non-reducing β1-3 β1-4 and β1-6 linked galactose residues from oligosaccharides, with β1-6 linked galactose residues at a slower rate [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9031-11-2. Pack Sizes: 100 U; 200 U ; 1 KU. Product ID: HY-P2869E. | |
| β1-3 Galactosidase | β1-3 Galactosidase is a highly specific exoglycosidase that catalyzes the hydrolysis of terminal β1-3-linked galactose from oligosaccharides and glycoprotein substrates, at a much lower rate, β1-6 linked galactose residues from oligosaccharides [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9031-11-2. Pack Sizes: 500 U. Product ID: HY-P2869A. | |
| β1-4 Galactosidase, E. coli | β1-4 Galactosidase, E. coli is a highly specific exoglycosidase that catalyzes the hydrolysis of terminal, non-reducing β1-4 linked galactose residues from oligosaccharides [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9031-11-2. Pack Sizes: 100 U. Product ID: HY-P2869B. | |
| β(1-4)-Galactosidase from Bacteroides fragilis, Recombinant | 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. Β1-4 galactosidase is a highly specific exoglycosidase that catalyzes the hydrolysis of β1-4 linked d-galactopyranosyl residues from oligosaccharides. 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. β-gal. Mole weight: 94000 daltons. Activity: 50,000 units/mg. Storage: at -20°C. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C) and 1 mM Na2EDTA. Source: E. coli. Species: Bacteroides fragilis. 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; β(1-4)-Galactosidase. Cat No: NATE-1278. | |
| β-Mannosidase 1A from Pyrococcus furiosus, 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. 37288-54-3. Purity: >90% by SDS-PAGE. β-Mannosidase. Mole weight: 61.1 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Pyrococcus furiosus. β-mannosidase; mannanase; mannase; β-D-mannosidase; β-mannoside mannohydrolase; exo-β-D-mannanase; EC 3.2.1.25; 9025-43-8; β-Mannosidase 1A. Cat No: NATE-1470. | |
| 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-Mannosidase from Streptomyces coelicolor, 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. β-Mannosidase. Mole weight: 56179.6 Da. Source: Streptomyces coelicolor A3(2). 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-1189. | |
| β-N-Acetylhexosaminidase, Streptococcus pneumoniae | β-N-Acetylhexosaminidase (EC 3.2.1.52) is an exoglycosidase that catalyzes the hydrolysis of terminal non-reducing β-N-acetylgalactosamine and glucosamine residues in oligosaccharides for epigenetic applications [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9012-33-3. Pack Sizes: 5 U; 10 U. Product ID: HY-P2866. | |
| Endo-β-N-acetylglucosaminidase from Arthrobacter protophormia, 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: min 95% by SDS-PAGE. Endo-β-N-acetylglucosaminidase. Mole weight: 69 kDa. Source: E. coli. Species: Arthrobacter protophormia. Endoglycosidase; Endo-β-N-acetylglucosaminidase; EC 3.2.1.96; 231-791-2; Endo-A; Endo-β-N-Acetylglucosaminidase A. Cat No: NATE-1493. | |
| 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. | |
| Endoglycosidase F1 from Elizabethkingia miricola, 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 endoglycosida...ules. 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 F1; Endo-β-N-acetylglucosaminidase F1; Endoglycosidase F1 from Chryseobacterium meningosepticum; Endoglycosidase F1 from Elizabethkingia meningoseptica; Endoglycosidase F1 from Flavobacterium meningosepticum; Endoglycosidase F1; EC 3.2.1.96; 231-791-2. Enzyme Commission Number: EC 3.2.1.96. CAS No. 231-791-2. Endo-β-N-acetylglucosaminidase. Activity: > 16 U/mg, buffered aqueous solution. Storage: 2-8°C. Form: buf | |
| Endoglycosidase F2 from Elizabethkingia miricola, 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: EC 3.2.1.96; Elizabethkingia miricola; Endo-β-N-acetylglucosaminidase F2; Endo F2; Endoglycosidase F2 from Chryseobacterium meningosepticum; Endoglycosidase F2 from Elizabethkingia meningoseptica; Endoglyco. Enzyme Commission Number: EC 3.2.1.96. CAS No. 37278-88-9. Endo-β-N-acetylglucosaminidase. Activity: 20 units/mg. Storage: -20°C. Form: Aseptically filled solution in 10 mM sodium acetate, 25 mM sodium chloride, pH 4.5. Source: E. coli. Species: Elizabethkingia miricola. EC 3.2.1.96; Elizabethkingia miricola; Endo-β-N-acetylglucosaminidase F2; Endo F2; Endoglycosidase F2 from Ch | |
| Endoglycosidase F3 from Elizabethkingia miricola, 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 F3; Elizabethkingia miricola; Endo-β-N-. Enzyme Commission Number: EC 3.2.1.96. CAS No. 231-791-2. Endo-β-N-acetylglucosaminidase. Activity: 30 U/mg. Storage: 2-8°C. Form: Aseptically filled solution in 20 mM Tris-HCl, pH 7.5. Source: E. coli. Species: Elizabethkingia miricola. Endoglycosidase F3; Elizabethkingia miricola; Endo-β-N-acetylglucosaminidase F3; Endoglycosidase F3 from Elizabethkingia (Chryseobacterium/Flavobacterium) meningosepticum; EC 3.2.1.96; 231-791-2; Endo F3. Pack: Supplied with 5× Reaction Buffer, 250 mM sodium acetate, pH 4.5. Cat No: NATE-0216. | |
| Native Bovine β(1-3,4)-Galactosidase | Hydrolyzes non-reducing terminal galactose β(1-3) and β(1-4) linkages. Can be used in conjunction with other β-galactosidases for exoglycosidase sequencing. Applications: The enzyme has applications in the analysis of a wide variety of glycoconjugates. it is particularly useful for ensuring the complete removal of β(1-3) and β(1-4)-linked non-reducing terminal galactose residues of oligosaccharides. gal β(1-6) glcnac is hydrolyzed more slowly, however this linkage is not normally encountered in native complex glycans. this activity towards β(1-3) and β(1-4)-linked galactose contrasts with that of our other β-galactosidases whi...tose residues. Group: Enzymes. Synonyms: β-galactosidase; beta-gal; β-gal; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. β-gal. Mole weight: ~68 kD. Form: 20 mM sodium Citrate phosphate, 150 mM NaCl (pH 4.0). Source: Bovine testis. Species: Bovine. β(1-3,4)-Galactosidase; β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. Cat No: NATE-0973. | |
| Native Helix pomatia β-Mannosidase | 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. β-Mannosidase. Activity: 5-30 units/mL. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.0 M (NH4)2SO4 containing 10 mM sodium acetate, pH approx. 4.0. Source: Helix pomatia. 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-0778. | |
| Native Mouse Endoproteinase Arg-C | 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: EC 3.4.21.35; glandular kallikrein; pancreatic kallikrein; submandibular. Enzyme Commission Number: EC 3.4.21.35. CAS No. 82047-85-6. Kallikrein. Storage: -20°C. Form: lyophilized powder. Source: Mouse submaxillary gland. Species: Mouse. EC 3.4.21.35; glandular kallikrein; pancreatic kallikrein; submandibular kallikrein; submaxillary kallikrein; kidney kallikrein; urinary kallikrein; kallikrein; salivary kallikrein; kininogenin; kininogenase; callicrein; glumorin; padreatin; padutin; kallidinogenase; bradykininogenase; depot-padutin; urokallikrein; dilminal D; onokrein P; 82047-85-6. Pack: vial of 5 μg. Cat No: NATE-0218. | |
| N-Glycanase (EDTA-Free) from Elizabethkingia meningoseptica, Recombinant | N-Glycanase (EDTA-Free) from Elizabethkingia meningoseptica, Recombinant. Group: Enzymes. Synonyms: N-Glycanase. Purity: The absence of exoglycosidase contaminants was confirmed by extended incubations with the corresponding pNP or MU-glycosides. No protease activity was detectable after incubation of the enzyme with 0.2 mg resorufin-labeled casein for ~18 hours at 37°C according to the method described by Twining. N-Glycanase. Mole weight: ~35 kDa daltons. Activity: > 10 U/mg. Stability: Extended incubations may be performed at 25°C rather than 37°C to promote stability of the N-Glycanase. Storage: Shipped on ice pack for next day delivery. Store enzyme at 2-8°C or -20°C, but avoid repeated freeze-thawing. Form: A sterile-filtered solution in 20 mM Tris-HCl, 50 mM NaCl (pH 7.5). Source: E. coli. Species: Elizabethkingia meningoseptica. N-Glycanase. Cat No: NATE-0483. | |
| O-Glycanase from Streptococcus pneumoniae, Recombinant | O-Glycanase from Streptococcus pneumoniae, Recombinant. The enzyme is inactivated with sulfhydryl reagents such as p-chloro-mercuribenzene sulfonic acid and transition metals such as mn2+ or zn2+. the enzyme is also inhibited with 1 mm edta. in a highly purified form, o-glycanase adsorbs to glass surfaces and is inactivated or gives variable activities. assays with purified substrates should be carried out in polypropylene vessels, and transfer of the enzyme solutions with glass pipettes should be avoided. the purified enzyme, as formulated, is stable at 2-8°c but about 30% of its activity is lost with a single freeze-thaw cycle. the enzyme activity is not signific...Glycanase. Purity: O-Glycanase is free of contaminating endo-and exoglycosidase activity. No protease activity was detectable after incubation of the enzyme with 0.2 mg resorufin-labeled casein for ~18 hours at 37°C according to the method described by Twining. The production host strain has been extensively tested and does not produce any detectable glycosidases. O-Glycanase. Mole weight: ~180 kDa daltons. Activity: > 12 U/mg. Storage: Shipped on cold pack for next day delivery. Store at 2-8°C. DO NOT FREEZE. Form: A sterile-filtered solution in 20 mM Tris-HCl, 25 mM NaCl (pH 7.5). Source: E. coli. Species: Streptococcus pneumoniae. O-Glycanase. Cat No: NATE-0496. | |
| xylan 1,4-β-xylosidase | Also hydrolyses xylobiose. Some other exoglycosidase activities have been found associated with this enzyme in sheep liver. Group: Enzymes. Synonyms: xylobiase; β-xylosidase; exo-1,4-β-xylosidase; β-D-xylopyranosidase; β-xylosidase; β-xylosidase; exo-1,4-xylosidase; exo-1,4-β-D-xylosidase; 1,4-β-D-xylan xylohydrolase. Enzyme Commission Number: EC 3.2.1.37. CAS No. 9025-53-0. β-Xylosidase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3899; xylan 1,4-β-xylosidase; EC 3.2.1.37; 9025-53-0; xylobiase; β-xylosidase; exo-1,4-β-xylosidase; β-D-xylopyranosidase; β-xylosidase; β-xylosidase; exo-1,4-xylosidase; exo-1,4-β-D-xylosidase; 1,4-β-D-xylan xylohydrolase. Cat No: EXWM-3899. | |
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