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| Product | Description | |
|---|---|---|
| Exoenzyme C3 from Clostridium botulinum, Recombinant | Exoenzyme C3 transferase is an ADP ribosyl transferase that selectively ribosylates RhoA, RhoB and RhoC proteins on asparagine residue 41, rendering them inactive. It has extremely low affinity for other members of the Rho family such as Cdc42 and Rac1 and does therefore not affect these GTPases. Hence, C3 transferase is a very potent and useful reagent to specifically block RhoA/B/C signaling. Applications: Inhibition of rho activity in vivo by microinjection or pinocyctic uptake into cells. inhibition of rho activity in vitro. Group: Enzymes. Synonyms: Clostridium botulinum Exoenzyme C3; Exoenzyme C3; Exoenzyme C3 transferase; C3 transferase. Purity: >80% by SDS-P...2, 200 mM NaCl, 5% sucrose and 1% dextran. In order to maintain high biological activity of the protein, it is recommended that the protein solution be supplemented with DTT to 1 mM, aliquoted into "experiment sized" amounts, snap frozen in liquid nitrogen and stored at -70°C. The protein is stable for 6 months if stored at -70° C. Storage: The protein should not be exposed to repeated freeze-thaw cycles. The lyophilized protein is stable at 4°C desiccated (<10% humidity) for 1 year. Form: Lyophilized powder. Source: E. coli. Species: Clostridium botulinum. Clostridium botulinum Exoenzyme C3; Exoenzyme C3; Exoenzyme C3 transferase; C3 transferase. Cat No: NATE-0874. |  |
| 1,3-α-oligoglucan phosphorylase | The enzyme, isolated from the bacterium Clostridium phytofermentans, catalyses a reversible reaction. Substrates for the phosphorolytic reaction are α-1,3-linked oligoglucans with a polymerisation degree of 3 or more. Nigerose (i.e. 3-O-α-D-glucopyranosyl-D-glucopyranose) is not phosphorylyzed but can serve as substrate in the reverse direction (cf. EC 2.4.1.279, nigerose phosphorylase). Group: Enzymes. Enzyme Commission Number: EC 2.4.1.334. 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-2572; 1,3-α-oligoglucan phosphorylase; EC 2.4.1.334. Cat No: EXWM-2572. | |
| 4-hydroxybutanoyl-CoA dehydratase | Contains FAD and a [4Fe-4S] iron-sulfur cluster. The enzyme has been characterized from several microorganisms, including Clostridium kluyveri, where it participates in succinate fermentation, Clostridium aminobutyricum, where it participates in 4-aminobutyrate degradation, and Metallosphaera sedula, where it participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea. Group: Enzymes. Enzyme Commission Number: EC 4.2.1.120. 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-4961; 4-hydroxybutanoyl-CoA dehydratase; EC 4.2.1.120. Cat No: EXWM-4961. | |
| 4-hydroxyphenylacetate decarboxylase | The enzyme, from the strict anaerobe Clostridium difficile, can also use (3,4-dihydroxyphenyl)acetate as a substrate, yielding 4-methylcatechol as a product. The enzyme is a glycyl radical enzyme. Group: Enzymes. Synonyms: p-hydroxyphenylacetate decarboxylase; p-Hpd; 4-Hpd; 4-hydroxyphenylacetate carboxy-lyase. Enzyme Commission Number: EC 4.1.1.83. CAS No. 340137-18-0. 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-4832; 4-hydroxyphenylacetate decarboxylase; EC 4.1.1.83; 340137-18-0; p-hydroxyphenylacetate decarboxylase; p-Hpd; 4-Hpd; 4-hydroxyphenylacetate carboxy-lyase. Cat No: EXWM-4832. | |
| acrylyl-CoA reductase (NADH) | Contains FAD. The reaction is catalysed in the opposite direction to that shown. The enzyme from the bacterium Clostridium propionicum is a complex that includes an electron-transfer flavoprotein (ETF). The ETF is reduced by NADH and transfers the electrons to the active site. Catalyses a step in a pathway for L-alanine fermentation to propanoate. cf. EC 1.3.1.84, acrylyl-CoA reductase (NADPH). Group: Enzymes. Enzyme Commission Number: EC 1.3.1.95. 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-1365; acrylyl-CoA reductase (NADH); EC 1.3.1.95. Cat No: EXWM-1365. | |
| α(2-3,6,8) Neuraminidase from Clostridium perfringens, Recombinant | 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. Neuraminidase is the common name for acetyl-neuraminyl hydrolase (sialidase). this neuraminidase catalyzes the hydrolysis of α2-3, α2-6, and α2-8 linked n-acetyl-neuraminic acid residues from glycoproteins and oligosaccharides. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-ne. Purity: > 95% determined by SDS-PAGE. Neuraminidase. Mole weight: 43 kDa. Activity: ~225,000 units/mg. Storage: at -20°C. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C) and 5 mM Na2EDTA. Source: E. coli. Species: Clostridium perfringens. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α(2-3,6,8) Neuraminidase. Cat No: NATE-1277. | |
| α(2?3,6) Neuraminidase from Clostridium perfringens, Recombinant | Releases α(2-3,6)-linked sialic acid from oligosaccharides, glycoproteins, complex carbohydrates. Applications: Structural analysis of oligosaccharides; determining sialic acid linkage; glycoprotein deglycosylation; removing heterogeneity from glycoproteins. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase. Neuraminidase. Mole weight: ~41 kD. Activity: >10 U/ml (>40 U/mg). Storage: 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: Clostridium perfringens. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase. Cat No: NATE-0972. | |
| α-Galactosidase 27A 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: >90% by SDS-PAGE. GLA. Mole weight: 44.0 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: Clostridium cellulolyticum. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase; α-Galactosidase 27A. Cat No: NATE-1400. | |
| 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. | |
| β-acetylglucosaminidase 73A from Clostridium perfringens, Recombinant | This enzyme releases non-reducing terminal β1-2, β1-3, β1-4 and β1-6 linked N-acetylglucosamine from complex carbohydrates. When incubated with oligosaccharides at low concentrations (<50 mU/ml) the enzyme can differentiate between GlcNAcβ1-2Man, GlcNAcβ1-4Man and GlcNAcβ1-6Man linkages. Under such conditions, the enzyme cleaves essentially only β1-2 linked GlcNAc, with two provisos. Firstly, β1-2 GlcNAc is not hydrolyzed if the mannose to which it is substituted has a substitution at C-6. Thus, the enzyme is useful for the analysis of tri-antennary oligosaccharides. Secondly, if the β-linked mannose of th...etylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. Purity:>90% by SDS-PAGE. β-N-Acetylhexosaminidase. Mole weight: 24.6 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: Clostridium perfringens. beta-N-acetyl-D-hexosaminide; N-acetylhexosaminohydrolase; β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase; β-Acetylhexosaminidase; β-acetylglucosaminidase 73A. Cat No: NATE-1289. | |
| β-D-galactosyl-(1?4)-L-rhamnose phosphorylase | The enzyme from Clostridium phytofermentans is also active towards towards β-D-galactosyl derivatives of L-mannose, L-lyxose, D-glucose, 2-deoxy-D-glucose, and D-galactose in this order. Differs from 1,3-β-galactosyl-N-acetylhexosamine phosphorylase (EC 2.4.1.211) in being active towards L-rhamnose and inactive towards N-acetyl hexosamine derivatives. Group: Enzymes. Synonyms: D-galactosyl-β1?4-L-rhamnose phosphorylase; GalRhaP. Enzyme Commission Number: EC 2.4.1.247. CAS No. 1236189-79-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2476; β-D-galactosyl-(1?4)-L-rhamnose phosphorylase; EC 2.4.1.247; 1236189-79-9; D-galactosyl-β1?4-L-rhamnose phosphorylase; GalRhaP. Cat No: EXWM-2476. | |
| bile-acid 7α-dehydratase | This enzyme, characterized from the gut bacterium Clostridium scindens (previously known as Eubacterium sp. strain VPI 12708), participates in the 7-dehydroxylation process associated with bile acid degradation. Group: Enzymes. Synonyms: baiE (gene name); 7α,12α-dihydroxy-3-oxochol-4-enoate hydro-lyase; 7α,12α-dihydroxy-3-oxochol-4-enoate hydro-lyase (12α-hydroxy-3-oxochola-4,6-dienoate-forming); BA7 α dehydratase. Enzyme Commission Number: EC 4.2.1.106. 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-4945; bile-acid 7α-dehydratase; EC 4.2.1.106; baiE (gene name); 7α,12α-dihydroxy-3-oxochol-4-enoate hydro-lyase; 7α,12α-dihydroxy-3-oxochol-4-enoate hydro-lyase (12α-hydroxy-3-oxochola-4,6-dienoate-forming); BA7 α dehydratase. Cat No: EXWM-4945. | |
| bile acid CoA-transferase | The enzyme, characterized from the gut bacterium Clostridium scindens, catalyses the last step in bile acid 7α-dehydroxylation, the removal of the CoA moiety from the products. By using a transferase rather than hydrolase, the bacteria conserve the thioester bond energy, saving ATP molecules. Clostridium scindens possesses two forms of the enzyme, encoded by the baiF and baiK genes. While the enzymes have a broad acceptor specificity and can use allocholate, ursodeoxycholate, and β-muricholate, the donor specificity is more strict. BaiF acts on lithocholoyl-CoA and deoxycholoyl-CoA, and BaiK acts only on the latter. Group: Enzymes. Synonyms: baiF (gene name); baiK (gene name); bile acid coenzyme A transferase. Enzyme Commission Number: EC 2.8.3.25. 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-3421; bile acid CoA-transferase; EC 2.8.3.25; baiF (gene name); baiK (gene name); bile acid coenzyme A transferase. Cat No: EXWM-3421. | |
| butyrate kinase | The enzyme from Clostridium sp. also acts, more slowly, on pentanoate and propanoate, and on some branched-chain fatty acids (cf. EC 2.7.1.14 sedoheptulokinase). Group: Enzymes. Enzyme Commission Number: EC 2.7.2.7. CAS No. 37278-14-1. 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-3178; butyrate kinase; EC 2.7.2.7; 37278-14-1. Cat No: EXWM-3178. | |
| Cellobiohydrolase 48A from Clostridium cellulolyticum, Recombinant | Cellulose 1,4-beta-cellobiosidase (non-reducing end) (EC 3.2.1.91, exo-cellobiohydrolase, beta-1,4-glucan cellobiohydrolase, beta-1,4-glucan cellobiosylhydrolase, 1,4-beta-glucan cellobiosidase, exoglucanase, avicelase, CBH 1, C1 cellulase, cellobiohydrolase I, cellobiohydrolase, exo-beta-1,4-glucan cellobiohydrolase, 1,4-beta-D-glucan cellobiohydrolase, cellobiosidase) is an enzyme with systematic name 4-beta-D-glucan cellobiohydrolase (non-reducing end). This enzyme catalyses the following chemical reaction: Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing [cellobiose] from the non-reducing ends of the chains. Group:... 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: Clostridium cellulolyticum. Cellulose 1,4-beta-cellobiosidase (non-reducing end); EC 3.2.1.91; exo-cellobiohydrolase; beta-1,4-glucan cellobiohydrolase; beta-1,4-glucan cellobiosylhydrolase; 1,4-beta-glucan cellobiosidase; exoglucanase; avicelase; CBH 1; C1 cellulase; cellobiohydrolase I; cellobiohydrolase; exo-beta-1,4-glucan cellobiohydrolase; 1,4-beta-D-glucan cellobiohydrolase; cellobiosidase; Cellobiohydrolase 48A. Cat No: NATE-1332. | |
| Cellobiohydrolase 48A from Clostridium thermocellum, Recombinant | Cellulose 1,4-beta-cellobiosidase (non-reducing end) (EC 3.2.1.91, exo-cellobiohydrolase, beta-1,4-glucan cellobiohydrolase, beta-1,4-glucan cellobiosylhydrolase, 1,4-beta-glucan cellobiosidase, exoglucanase, avicelase, CBH 1, C1 cellulase, cellobiohydrolase I, cellobiohydrolase, exo-beta-1,4-glucan cellobiohydrolase, 1,4-beta-D-glucan cellobiohydrolase, cellobiosidase) is an enzyme with systematic name 4-beta-D-glucan cellobiohydrolase (non-reducing end). This enzyme catalyses the following chemical reaction: Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing [cellobiose] from the non-reducing ends of the chains. Group: ...ge: 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: Clostridium thermocellum. Cellulose 1,4-beta-cellobiosidase (non-reducing end); EC 3.2.1.91; exo-cellobiohydrolase; beta-1,4-glucan cellobiohydrolase; beta-1,4-glucan cellobiosylhydrolase; 1,4-beta-glucan cellobiosidase; exoglucanase; avicelase; CBH 1; C1 cellulase; cellobiohydrolase I; cellobiohydrolase; exo-beta-1,4-glucan cellobiohydrolase; 1,4-beta-D-glucan cellobiohydrolase; cellobiosidase; Cellobiohydrolase 48A. Cat No: NATE-1331. | |
| Cellobiohydrolase 5A from Clostridium thermocellum, Recombinant | Cellulose 1,4-beta-cellobiosidase (non-reducing end) (EC 3.2.1.91, exo-cellobiohydrolase, beta-1,4-glucan cellobiohydrolase, beta-1,4-glucan cellobiosylhydrolase, 1,4-beta-glucan cellobiosidase, exoglucanase, avicelase, CBH 1, C1 cellulase, cellobiohydrolase I, cellobiohydrolase, exo-beta-1,4-glucan cellobiohydrolase, 1,4-beta-D-glucan cellobiohydrolase, cellobiosidase) is an enzyme with systematic name 4-beta-D-glucan cellobiohydrolase (non-reducing end). This enzyme catalyses the following chemical reaction: Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing [cellobiose] from the non-reducing ends of the chains. Group: ...rage: 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: Clostridium thermocellum. Cellulose 1,4-beta-cellobiosidase (non-reducing end); EC 3.2.1.91; exo-cellobiohydrolase; beta-1,4-glucan cellobiohydrolase; beta-1,4-glucan cellobiosylhydrolase; 1,4-beta-glucan cellobiosidase; exoglucanase; avicelase; CBH 1; C1 cellulase; cellobiohydrolase I; cellobiohydrolase; exo-beta-1,4-glucan cellobiohydrolase; 1,4-beta-D-glucan cellobiohydrolase; cellobiosidase; Cellobiohydrolase 5A. Cat No: NATE-1330. | |
| Cellobiohydrolase 9A from Clostridium thermocellum, Recombinant | Cellulose 1,4-beta-cellobiosidase (non-reducing end) (EC 3.2.1.91, exo-cellobiohydrolase, beta-1,4-glucan cellobiohydrolase, beta-1,4-glucan cellobiosylhydrolase, 1,4-beta-glucan cellobiosidase, exoglucanase, avicelase, CBH 1, C1 cellulase, cellobiohydrolase I, cellobiohydrolase, exo-beta-1,4-glucan cellobiohydrolase, 1,4-beta-D-glucan cellobiohydrolase, cellobiosidase) is an enzyme with systematic name 4-beta-D-glucan cellobiohydrolase (non-reducing end). This enzyme catalyses the following chemical reaction: Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing [cellobiose] from the non-reducing ends of the chains. Group: ...rage: 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: Clostridium thermocellum. Cellulose 1,4-beta-cellobiosidase (non-reducing end); EC 3.2.1.91; exo-cellobiohydrolase; beta-1,4-glucan cellobiohydrolase; beta-1,4-glucan cellobiosylhydrolase; 1,4-beta-glucan cellobiosidase; exoglucanase; avicelase; CBH 1; C1 cellulase; cellobiohydrolase I; cellobiohydrolase; exo-beta-1,4-glucan cellobiohydrolase; 1,4-beta-D-glucan cellobiohydrolase; cellobiosidase; Cellobiohydrolase 9A. Cat No: NATE-1329. | |
| cellulose 1,4-β-cellobiosidase (reducing end) | Some exocellulases, most of which belong to the glycoside hydrolase family 48 (GH48, formerly known as cellulase family L), act at the reducing ends of cellulose and similar substrates. The CelS enzyme from Clostridium thermocellum is the most abundant subunit of the cellulosome formed by the organism. It liberates cellobiose units from the reducing end by hydrolysis of the glycosidic bond, employing an inverting reaction mechanism. Different from EC 3.2.1.91, which attacks cellulose from the non-reducing end. Group: Enzymes. Synonyms: CelS; CelSS; endoglucanase SS; cellulase SS; cellobiohydrolase CelS; Cel48A. Enzyme Commission Number: EC 3.2.1.176. Cellulose 1,4-beta-cellobiosidase. 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-3859; cellulose 1,4-β-cellobiosidase (reducing end); EC 3.2.1.176; CelS; CelSS; endoglucanase SS; cellulase SS; cellobiohydrolase CelS; Cel48A. Cat No: EXWM-3859. | |
| Chitinase 18A from Clostridium thermocellum, Recombinant | Chitosanase catalyzes the endohydrolysis of β (1,4) linkages between N-acetyl-D-glucosamine and D-glucosamine residues in partially deacetylated chitosan. Chitosanase from Streptomyces griseus is capable of hydrolyzing both chitosan and carboxymethyl cellulose. It is used for the lysis of cell walls of fungi belonging to the group Mucorales. It is found in several types of microorganisms. Group: Enzymes. Synonyms: Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase. Enzyme Commission Number: EC 3.2.1.14. Purity: >90% by SDS-PAGE. Chitosanase. Mole weight: 43.9 kDa. Activity: 25 U/mg. 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: Clostridium thermocellum. Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase; Chitosanase 18A. Cat No: NATE-1379. | |
| Chitinase from Clostridium thermocellum, Recombinant | Chitinase is an extracellular enzyme complex that degrades chitin and has a molecular mass of approximately 30 kDa. Chitin is degraded to N-acetyl-D-glucosamine in 2 enzymatic reactions. Firstly, chitobiose units are removed from chitin by chitodextrinase-chitinase. The second reaction involves N-acetyl-glucosaminidase-chitobiase, which cleaves the disaccharide to its monomer subunits (that comprise of N-acetyl-D-glucosamine). Group: Enzymes. Synonyms: Chitinase; chitodextrinase; 1,4-β-poly-N-acetylglucosaminidase; poly-β-glucosaminidase; β-1,4-poly-N-acetyl glucosamidinase; poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase; (1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase; EC 3.2.1.14. Enzyme Commission Number: EC 3.2.1.14. Purity: > 80 % as judged by SDS-PAGE. Chitinase. Mole weight: 43927.1 Da. Activity: 25 U/mg. Storage: Store at -20°C (shipped at room temperature). Form: Glycerol/buffer solution. Source: Clostridium thermocellum ATCC 27405. Chitinase; chitodextrinase; 1,4-β-poly-N-acetylglucosaminidase; poly-β-glucosaminidase; β-1,4-poly-N-acetyl glucosamidinase; poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase; (1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase; EC 3.2.1.14. Cat No: NATE-1201. | |
| cinnamoyl-CoA:phenyllactate CoA-transferase | 3-Phenylproprionate is a better CoA acceptor than (R)-phenyllactate in vitro. The enzyme from Clostridium sporogenes is specific for derivatives of 3-phenylpropionate and 4-phenylbutyrate. Group: Enzymes. Synonyms: FldA. Enzyme Commission Number: EC 2.8.3.17. CAS No. 289682-21-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3412; cinnamoyl-CoA:phenyllactate CoA-transferase; EC 2.8.3.17; 289682-21-9; FldA. Cat No: EXWM-3412. | |
| clostridial aminopeptidase | A secreted enzyme from Clostridium histolyticum, requiring Mn2+ or Co2+. Group: Enzymes. Synonyms: Clostridium histolyticum aminopeptidase. Enzyme Commission Number: EC 3.4.11.13. CAS No. 59680-69-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4009; clostridial aminopeptidase; EC 3.4.11.13; 59680-69-2; Clostridium histolyticum aminopeptidase. Cat No: EXWM-4009. | |
| clostripain | From the bacterium Clostridium histolyticum. It requires Ca2+ ions and is inhibited by EDTA. Type example of peptidase family C11. Group: Enzymes. Synonyms: clostridiopeptidase B; clostridium histolyticum proteinase B; α-clostridipain; clostridiopeptidase. Enzyme Commission Number: EC 3.4.22.8. CAS No. 9028-00-6. Kallikrein. 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-4249; clostripain; EC 3.4.22.8; 9028-00-6; clostridiopeptidase B; clostridium histolyticum proteinase B; α-clostridipain; clostridiopeptidase. Cat No: EXWM-4249. | |
| Clostripain | Clostripain (Clostridiopeptidase B) is a proteolytic enzyme isolated from Clostridium histolyticum with esterase, amidase and protease activities and is a highly specific carboxypeptide targeting arginine key protease [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Clostridiopeptidase B. CAS No. 9028-00-6. Pack Sizes: 1 mg. Product ID: HY-P2895. |  |
| Collagenase AF-1 GMP Grade | Collagenase AF-1 GMP Grade, often in combination with Neutral Protease AF GMP Grade, is suitable for the dissociation of sensitive cells from several tissues, such as pancreas, liver and dental pulp. It has been shown to be highly effective for the isolation of islets of Langerhans from human pancreas intended for transplantation. Applications: Collagenase af-1 gmp grade is suitable for cell isolation from several tissue types intended for clinical applications. it is often used in combination with neutral protease af gmp grade. Group: Enzymes. Synonyms: Collagenase AF-1; Collagenase; Collagenase AF-1 GMP; Collagenase GMP. Enzyme Commission Number: EC 3.4.24.3. CAS No. 9001-12-1. Collagenase. Activity: ≥ 3.00 U/mg. Storage: 2 to 8 °C. Form: Lyophilized powder. Source: Clostridium histolyticum. Collagenase AF-1; Collagenase; Collagenase AF-1 GMP; Collagenase GMP. Cat No: NATE-1919. | |
| Collagenase I, from Clostridium histolyticum | Collagenases are enzymes that break the peptide bonds in collagen. Collagenases are derived from the Clostridium histolyticum. Collagenases (Type I) are proteolytic enzymes that break peptide bonds in collagen and can be used for tissue digestion and dissociation. Uses: Scientific research. Group: Signaling pathways. CAS No. 9001-12-1. Pack Sizes: 25 mg; 50 mg; 100 mg. Product ID: HY-O0004. | |
| Collagenase NB 6 from Clostridium histolyticum (GMP Grade) | Collagenases from Clostridium histolyticum are proteolytic enzymes that cleave peptide bonds in the triple helical collagen molecule of human or animal tissue in situ. For this reason collagenases are widely used for isolation of various cell types by tissue dissociation. Applications: Collagenase nb 6 gmp grade is suitable for cell isolation from various tissue types intended for clinical applications. if a research or sterile product is required, collagenase nb 4 standard grade or collagenase nb 5 sterile grade, respectively, are recommended. both products have comparable enzymatic activities to collagenase nb 6 gmp grade. Group: Enzymes. Synonyms: Collagenase NB 6; Collagenase NB; Collagenase. Enzyme Commission Number: EC 3.4.24.3. CAS No. 9001-12-1. Collagenase. Mole weight: 70 000 - 120 000 (collagenases). Activity: ≥ 0.100 U/mg. Storage: 2 to 8 °C. Form: Lyophilized powder. Source: Clostridium histolyticum. Collagenase NB 6; Collagenase NB; Collagenase. Cat No: NATE-1918. | |
| Collagenase/Neutral Protease Blend (GMP Grade) | NATE-1917 is an avian and mammalian tissue-free Collagenase and neutral protease enzyme blend produced under GMP quality conditions. Applications: Nate-1917 is specifically designed for stem cell isolation from human and other adipose tissue with following advantages:o a single, sterile, ready-to-use vial containing both collagenase and neutral protease can digest up to 280g of adipose tissue with best-in-class gmp quality and shelf life of up to 72 months.o currently included in ide applications approved by the u.s. fda for alopecia, chronic heart failure, hamstring injuries, osteoarthritis of the knee, and hand manifestations of scleroderma.o research protocols are a...sociation of nucleated cells from adipose tissue.o produced using avian and mammalian tissue-free raw materials, aseptic processes and sterile filtration under gmp guidelines to assure the lowest levels of impurities and stringent quality standards. Group: Enzymes. Synonyms: Collagenase/Neutral Protease Blend; GMP, Collagenase/Neutral Protease Blend; Collagenase; Neutral Protease; GMP. Collagenase. Stability: 48 months at -15 to -25° C. Appearance: White lyophilizate. Source: Clostridium histolyticum/Bacillus polymyxa. Collagenase/Neutral Protease Blend; GMP, Collagenase/Neutral Protease Blend; Collagenase; Neutral Protease; GMP. Pack: 1 vial, 35 mg. Cat No: NATE-1917. | |
| D-psicose 3-epimerase | The enzyme is highly specific for D-psicose and shows very low activity with D-tagatose (cf. EC 5.1.3.31, D-tagatose 3-epimerase). The enzyme from the bacterium Clostridium scindens requires Mn2+, whereas the enzymes from the bacteria Clostridium cellulolyticum, Clostridium sp. BNL1100, and Clostridium bolteae require Co2+ as optimum cofactor. The enzyme from Ruminococcus sp. is not dependent on the presence of metal ions, but its activity is enhanced by Mn2+. Group: Enzymes. Synonyms: DPEase (ambiguous). Enzyme Commission Number: EC 5.1.3.30. 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-5417; D-psicose 3-epimerase; EC 5.1.3.30; DPEase (ambiguous). Cat No: EXWM-5417. | |
| endo-α-N-acetylgalactosaminidase | The enzyme catalyses the liberation of Gal-(1?3)-β-GalNAc α-linked to serine or threonine residues of mucin-type glycoproteins. EngBF from the bacterium Bifidobacterium longum specifically acts on core 1-type O-glycan to release the disaccharide Gal-(1?3)-β-GalNAc. The enzymes from the bacteria Clostridium perfringens, Enterococcus faecalis, Propionibacterium acnes and Alcaligenes faecalis show broader specificity (e.g. they can also release the core 2 trisaccharide Gal-(1?3)-β-(GlcNAc-(1?6)-β)-GalNAc or the core 3 disaccharide GlcNAc-(1?3)-β-GalNAc). The enzyme may play an important role in the degradation and utilization of mucins having co...alactosaminohydrolase. Enzyme Commission Number: EC 3.2.1.97. CAS No. 59793-96-3. O-Glycosidase. 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-3960; endo-α-N-acetylgalactosaminidase; EC 3.2.1.97; 59793-96-3; endo-α-acetylgalactosaminidase; endo-α-N-acetyl-D-galactosaminidase; mucinaminylserine mucinaminidase; D-galactosyl-3-(N-acetyl-α-D-galactosaminyl)-L-serine mucinaminohydrolase; endo-α-GalNAc-ase; glycopeptide α-N-acetylgalactosaminidase; D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase. Cat No: EXWM-3960. | |
| 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. | |
| methylenetetrahydrofolate reductase (ferredoxin) | An iron-sulfur flavoprotein that also contains zinc. The enzyme from Clostridium formicoaceticum catalyses the reduction of methylene blue, menadione, benzyl viologen, rubredoxin or FAD with 5-methyltetrahydrofolate and the oxidation of reduced ferredoxin or FADH2 with 5,10-methylenetetrahydrofolate. However, unlike EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H], there is no activity with NAD(P)H. Group: Enzymes. Synonyms: 5,10-methylenetetrahydrofolate reductase. Enzyme Commission Number: EC 1.5.7.1. 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-1558; methylenetetrahydrofolate reductase (ferredoxin); EC 1.5.7.1; 5,10-methylenetetrahydrofolate reductase. Cat No: EXWM-1558. | |
| microbial collagenase | Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum. Class I has forms α (68 kDa), β (115 kDa) and γ (79 kDa); class II has Δ (100 kDa), ε (110 kDa) and ζ (125 kDa). The two classes are immunologically crossreactive, but have significantly different sequences, and different specificities such that their actions on collagen are complementary. The enzymes also act as peptidyl-tripeptidases. Variants of the enzyme have been purified from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio, Vibrio B-30 (ATCC 21250) and V. alginolyticu...ase-8; matirx metalloproteinase-18; interstitial collagenase. Enzyme Commission Number: EC 3.4.24.3. CAS No. 9001-12-1. Collagenase. 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-4311; microbial collagenase; EC 3.4.24.3; 9001-12-1; Clostridium histolyticum collagenase; clostridiopeptidase A; collagenase A; collagenase I; Achromobacter iophagus collagenase; collagenase; aspergillopeptidase C; nucleolysin; azocollase; metallocollagenase; soycollagestin; Clostridium histolyticum proteinase A; clostridiopeptidase II; MMP-8; clostridiopeptidase I; collagen peptidase; collagen protease; collagenase MM | |
| NAD(P)+ transhydrogenase (ferredoxin) | The iron-sulfur flavoprotein complex, isolated from the bacterium Clostridium kluyveri, couples the exergonic reduction of NADP+ with reduced ferredoxin and the endergonic reduction of NADP+ with NADH. Group: Enzymes. Synonyms: NADH-dependent reduced ferredoxin:NADP+ oxidoreductase. Enzyme Commission Number: EC 1.6.1.4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1577; NAD(P)+ transhydrogenase (ferredoxin); EC 1.6.1.4; NADH-dependent reduced ferredoxin:NADP+ oxidoreductase. Cat No: EXWM-1577. | |
| 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 Clostridium botulinum ADP-ribosyltransferase C3 | ADP-ribosyltransferase C3 from Clostridium botulinum ribosylates rho in eukaryotes in the presence of NAD. The ADP-ribosylating exoenzyme forms a single major 25 kDA (approx.) band with SDS electrophoresis. The enzyme labels 21-24 kDa proteins in tissues such as the human platelet membranes. Applications: Adp-ribosyltransferase c3 from clostridium botulinum may be used to study cellular signaling and g protein expression. Group: Enzymes. Synonyms: ADP-ribosyltransferase C3; 58319-92-9; Botulinum neurotoxin C3; C3 Exoenzyme; C3 Exotoxin; C3 Transferase. CAS No. 58319-92-9. C3 Transferase. Storage: 2-8°C. Source: Clostridium botulinum. ADP-ribosyltransferase C3; 58319-92-9; Botulinum neurotoxin C3; C3 Exoenzyme; C3 Exotoxin; C3 Transferase. Cat No: NATE-0095. | |
| Native Clostridium histolyticum Clostripain | Clostripain from Clostridium histolyticum is composed of two polypeptide chains, with molecular masses of 41.7 kDa and 15.4 kDa. Clostripain has a highly restricted substRate specificity for Arg-Xaa peptide bonds. Therefore, clostripain has been explored as a potential enzyme for protein sequencing purposes. It has also been studied as a catalyst for condensation of pharmaceutically important peptides containing Arg-Pro bonds. The isoelectric point of the enzyme is 4.8-4.9 (at 8°C), and optimum pH is 7.4~7.8 (against α-benzoyl-arginine ethyl ester). Group: Enzymes. Synonyms: clostridiopeptidase B; clostridium histolyticum proteinase B; α-clostridipain; clostridiopeptidase; Endoproteinase Arg-C; EC 3.4.22.8; 9028-00-6. Enzyme Commission Number: EC 3.4.22.8. CAS No. 9028-00-6. Kallikrein. Activity: > 20 units/mg solid. Storage: 2-8°C. Form: lyophilized powder. Source: Clostridium histolyticum. clostridiopeptidase B; clostridium histolyticum proteinase B; α-clostridipain; clostridiopeptidase; Endoproteinase Arg-C; EC 3.4.22.8; 9028-00-6. Cat No: NATE-0143. | |
| Native Clostridium histolyticum Collagenase | Collagenases are endopeptidases that digest native collagen in the triple helix region. Collagens are the major fibrous component of animal extracellular connective tissue. Bacterial collagenases differ from vertebrate collagenases in that they exhibit broader substrate specificity (Peterkofsky 1982, Birkedal-Hansen 1987). Unlike animal collagenases that split collagen in its native triple-helical conformation (Woolley et al. 1975, Gross et al. 1974), bacterial collagenase is unique because it can degrade both water-insoluble native collagens and water-soluble denatured ones. It can attack almost all collagen types, and is able to make multiple cleavages within triple h...ations needing to avoid introduction of animal derived pathogens into bioprocessing procedures. Group: Enzymes. Synonyms: EC 3.4.24.3; Collagenase; Clostridiopeptidase A; Clostridium histolyticum collagenase; collagenase A; collagenase I; Achromobacter iophagus collagenase; aspergillopeptidase C; nucleolysin; Collagenase, Type 1; Collagenase, Type 2; Collagenase, Type 3; Collagenase, Type 4; Collagenase, Type 5. Enzyme Commission Number: EC 3.4.24.3. CAS No. 9001-12-1. Collagenase. Mole weight: 68 to 130 kDa. Activity: Type 1 > 125 units per mg; Type 2 > 125 units per mg; Type 3 > 100 units per mg; Type 4 > 160 units per mg; Type 5 > 450 units per mg. Stability: This pro | |
| Native Clostridium kluyveri Diaphorase | Native Clostridium kluyveri Diaphorase. Applications: Diaphorase from clostridium kluyveri, or lipoyl dehydrogenase, has been used in a study to assess the protein-protein interactions in assembly of lipoic acid on the 2-oxoacid dehydrogenases of aerobic metabolism. lipoyl dehydrogenase has also been used in a study to investigate the redox regulation of tyrosine nitration and 3-nitrotyrosine reduction by antioxidants. Group: Enzymes. Synonyms: dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxidoreductase (NADH); lipoamide reductase; lipo. Enzyme Commission Number: EC 1.8.1.4. CAS No. 9001-18-7. Diaphorase. Activity: 3.0-20.0 units/mg protein (biuret). Storage: Store at -20°C. Form: Lyophilized powder. Source: Clostridium kluyveri. dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxidoreductase (NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate dehydrogenase; lipoic acid dehydrogenase; lipoyl dehydrogenase; dihydrolipoyl dehydrogenase; EC 1.8.1.4; 9001-18-7; Lipoamide Dehydrogenase. Cat No: NATE-0875. | |
| Native Clostridium perfringens (C. welchII) Choloylglycine Hydrolase | Choloylglycine hydrolase (EC 3.5.1.24) is an N-terminal nucleophilic (Ntn) hydrolase that catalyzes the hydrolysis of amide bonds, libeRates the glycine/taurine moiety from the steroid core and eventually yields unconjugated bile acids. Agents that oxidize thiol groups (e.g., p-mercuribenzoate, iodoacetamide, Hg2+, Cu2+, and Cd2+) have been shown to strongly inhibit bile salt hydrolase (BSH) activity in Clostridium perfringens. Applications: The enzyme from creative enzymes has been used in the analysis of bile samples in various studies. Group: Enzymes. Synonyms: EC 3.5.1.24; glycocholase; bile salt hydrolase; choloyltaurine hydrolase; 3α,7α,12α-trihydroxy-5β-cholan-24-oylglycine amidohydrolase; 37289-07-9. Enzyme Commission Number: EC 3.5.1.24. CAS No. 37289-07-9. Choloylglycine Hydrolase. Activity: > 100 units/mg protein. Storage: -20°C. Form: lyophilized powder. Partially purified lyophilized powder containing buffer salts and stabilizer. Source: Clostridium perfringens (C. welchII). EC 3.5.1.24; glycocholase; bile salt hydrolase; choloyltaurine hydrolase; 3α,7α,12α-trihydroxy-5β-cholan-24-oylglycine amidohydrolase; 37289-07-9. Cat No: NATE-0129. | |
| Native Clostridium sp. Diaphorase | Native Clostridium sp. Diaphorase. Applications: This enzyme is useful for colorimetric determination of nad(p)h and many dehydrogenases when coupled with various dyes which act as hydrogen acceptors from nad(p)h. Group: Enzymes. Synonyms: Diaphorase; EC 1.6.99.-. Enzyme Commission Number: EC 1.6.99.-. Diaphorase. Mole weight: 24 kDa. Activity: Grade? 30U/mg-solid or more (containing approx. 15% of stabilizers). Stability: Stable at-20°C for at least one year. Appearance: Yellowish amorphous powder, lyophilized. Form: Freeze dried powder. Source: Clostridium sp. Diaphorase; EC 1.6.99.-. Cat No: DIA-187. | |
| Neutral Protease AF GMP Grade | Neutral Protease AF GMP Grade is manufactured according to cGMP guidelines using a production process completely free of animal-based components. In this way the introduction of any potential animal-derived pathogen is excluded. Neutral Protease AF GMP Grade is chromatographically purified and largely free from collagenolytic activity (PZ U) as well as endotoxins. The absence of any animal-derived ingredients and thorough microbial analysis provide the highest possible safety. Applications: Neutral protease af gmp grade is suitable for cell isolation from several tissue types for clinical applications. it is often used in combination with collagenase af-1 gmp grade. Group: Enzymes. Synonyms: Neutral Protease AF GMP Grade; Neutral Protease AF; Neutral Protease; Protease. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9001-92-7. Protease. Mole weight: 34 000. Activity: ≥ 0.50 U/mg. Storage: 2 to 8 °C. Form: Lyophilized powder. Source: Clostridium histolyticum. Neutral Protease AF GMP Grade; Neutral Protease AF; Neutral Protease; Protease. Cat No: NATE-1920. | |
| nicotinate dehydrogenase | A flavoprotein containing non-heme iron. The enzyme is capable of acting on a variety of nicotinate analogues to varying degrees, including pyrazine-2-carboxylate, pyrazine 2,3-dicarboxylate, trigonelline and 6-methylnicotinate. The enzyme from Clostridium barkeri also possesses a catalytically essential, labile selenium that can be removed by reaction with cyanide. Group: Enzymes. Synonyms: nicotinic acid hydroxylase; nicotinate hydroxylase. Enzyme Commission Number: EC 1.17.1.5. CAS No. 9059-3-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1083; nicotinate dehydrogenase; EC 1.17.1.5; 9059-03-4; nicotinic acid hydroxylase; nicotinate hydroxylase. Cat No: EXWM-1083. | |
| nigerose phosphorylase | The enzymes from Clostridium phytofermentans is specific for nigerose, and shows only 0.5% relative activity with kojibiose (cf. EC 2.4.1.230, kojibiose phosphorylase). Group: Enzymes. Synonyms: cphy1874 (gene name). Enzyme Commission Number: EC 2.4.1.279. 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-2511; nigerose phosphorylase; EC 2.4.1.279; cphy1874 (gene name). Cat No: EXWM-2511. | |
| Pectin acetylesterase from Clostridium thermocellum, Recombinant | Pectin acetylesterase catalyses the hydrolysis of acetate from acetylated pectins. Group: Enzymes. Synonyms: Pectinacetylesterase; PAE. Enzyme Commission Number: EC 3.1.1.-. Purity: > 95 % as judged by SDS-PAGE. PAE. Mole weight: 23800 Da. Activity: 100 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Clostridium thermocellum. Pectinacetylesterase; PAE; Pectin acetylesterase. Cat No: NATE-1224. | |
| phospholipase C | The bacterial enzyme, which is a zinc protein, also acts on sphingomyelin and phosphatidylinositol; that from seminal plasma does not act on phosphatidylinositol. Group: Enzymes. Synonyms: lipophosphodiesterase I; lecithinase C; Clostridium welchii α-toxin; Clostridium oedematiens β- and γ-toxins; lipophosphodiesterase C; phosphatidase C; heat-labile hemolysin; α-toxin. Enzyme Commission Number: EC 3.1.4.3. CAS No. 9001-86-9. Phospholipase C. 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-3718; phospholipase C; EC 3.1.4.3; 9001-86-9; lipophosphodiesterase I; lecithinase C; Clostridium welchii α-toxin; Clostridium oedematiens β- and γ-toxins; lipophosphodiesterase C; phosphatidase C; heat-labile hemolysin; α-toxin. Cat No: EXWM-3718. | |
| phytochromobilin:ferredoxin oxidoreductase | Catalyses the two-electron reduction of biliverdin IX&alpha. Can use [2Fe-2S] ferredoxins from a number of sources as acceptor but not the [4Fe-4S] ferredoxin from Clostridium pasteurianum. The isomerization of (3Z)-phytochromobilin to (3E)-phytochromobilin is thought to occur prior to covalent attachment to apophytochrome in the plant cell cytoplasm. Flavodoxins can be used instead of ferredoxin. Group: Enzymes. Synonyms: HY2; PPhi B synthase; phytochromobilin synthase. Enzyme Commission Number: EC 1.3.7.4. CAS No. 138263-99-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1399; phytochromobilin:ferredoxin oxidoreductase; EC 1.3.7.4; 138263-99-7; HY2; PPhi B synthase; phytochromobilin synthase. Cat No: EXWM-1399. | |
| (R)-2-hydroxyglutaryl-CoA dehydratase | The enzymes from the bacteria Acidaminococcus fermentans and Clostridium symbiosum are involved in the fermentation of L-glutamate. The enzyme contains [4F-4S] clusters, FMNH2 and riboflavin. It must be activated by an activator protein. Once activated, it can catalyse many turnovers. Group: Enzymes. Synonyms: hgdAB (gene names). Enzyme Commission Number: EC 4.2.1.167. 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-5008; (R)-2-hydroxyglutaryl-CoA dehydratase; EC 4.2.1.167; hgdAB (gene names). Cat No: EXWM-5008. | |
| Reducing-end cellobiohydrolase 48A from Clostridium stercorarium, Recombinant | Cellulose 1,4-beta-cellobiosidase (reducing end) (EC 3.2.1.176, CelS, CelSS, endoglucanase SS, cellulase SS, cellobiohydrolase CelS, Cel48A) is an enzyme with systematic name 4-beta-D-glucan cellobiohydrolase (reducing end). This enzyme catalyses the following chemical reaction: Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and similar substrates, releasing cellobiose from the reducing ends of the chains. The CelS enzyme from Clostridium thermocellum is the most abundant subunit of the cellulosome formed by the organism. Group: Enzymes. Synonyms: Cellulose 1,4-beta-cellobiosidase (reducing end); EC 3.2.1.176; CelS; CelSS; endoglucanase SS; cellulase SS; cellobiohydrolas. Enzyme Commission Number: EC 3.2.1.176. Purity: >50% by SDS-PAGE. Cellulose 1,4-beta-cellobiosidase. Mole weight: 73.5 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: Clostridium stercorarium. Cellulose 1,4-beta-cellobiosidase (reducing end); EC 3.2.1.176; CelS; CelSS; endoglucanase SS; cellulase SS; cellobiohydrolase CelS; Cel48A; 4-beta-D-glucan cellobiohydrolase (reducing end); Reducing-end cellobiohydrolase 48A. Cat No: NATE-1326. | |
| rubredoxin-NAD+ reductase | Requires FAD. The enzyme from Clostridium acetobutylicum reduces rubredoxin, ferricyanide and dichlorophenolindophenol, but not ferredoxin or flavodoxin. The reaction does not occur when NADPH is substituted for NADH. Contains iron at the redox centre. Group: Enzymes. Synonyms: rubredoxin reductase; rubredoxin-nicotinamide adenine dinucleotide reductase; dihydronicotinamide adenine dinucleotide-rubredoxin reductase; reduced nicotinamide adenine dinucleotide-rubredoxin reductase; NADH-rubredoxin reductase; rubredoxin-NAD reductase; NADH: rubredoxin oxidoreductase; DPNH-rubredoxin reductase; NADH-rubredoxin oxidoreductase. Enzyme Commission Number: EC 1.18.1.1. CAS No. 9032-27-3. 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-1106; rubredoxin-NAD+ reductase; EC 1.18.1.1; 9032-27-3; rubredoxin reductase; rubredoxin-nicotinamide adenine dinucleotide reductase; dihydronicotinamide adenine dinucleotide-rubredoxin reductase; reduced nicotinamide adenine dinucleotide-rubredoxin reductase; NADH-rubredoxin reductase; rubredoxin-NAD reductase; NADH: rubredoxin oxidoreductase; DPNH-rubredoxin reductase; NADH-rubredoxin oxidoreductase. Cat No: EXWM-1106. | |
| (S)-citramalyl-CoA lyase | Requires Mg2+ ions for activity. The enzyme from the bacterium Clostridium tetanomorphum is a component of EC 4.1.3.22, citramalate lyase. It also acts on (3S)-citramalyl thioacyl-carrier protein. The enzyme from the bacterium Chloroflexus aurantiacus also has the activity of EC 4.1.3.24, malyl-CoA lyase. It has no activity with (3R)-citramalyl-CoA (cf. EC 4.1.3.46, (R)-citramalyl-CoA lyase). Group: Enzymes. Synonyms: citramalyl coenzyme A lyase (ambiguous); (+)-CMA-CoA lyase; (3S)-citramalyl-CoA pyruvate-lyase; Mcl (ambiguous); citramalyl-CoA lyase (ambiguous). Enzyme Commission Number: EC 4.1.3.25. CAS No. 37290-68-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4905; (S)-citramalyl-CoA lyase; EC 4.1.3.25; 37290-68-9; citramalyl coenzyme A lyase (ambiguous); (+)-CMA-CoA lyase; (3S)-citramalyl-CoA pyruvate-lyase; Mcl (ambiguous); citramalyl-CoA lyase (ambiguous). Cat No: EXWM-4905. | |
| short-chain-enoyl-CoA hydratase | The enzyme from the bacterium Clostridium acetobutylicum is part of the central fermentation pathway and plays a key role in the production of both acids and solvents. It is specific for short, C4-C6, chain length substrates and exhibits an extremely high turnover number for crotonyl-CoA. cf. EC 4.2.1.17, enoyl-CoA hydratase and EC 4.2.1.74, long-chain-enoyl-CoA hydratase. Group: Enzymes. Synonyms: 3-hydroxybutyryl-CoA dehydratase; crotonase; crt (gene name). Enzyme Commission Number: EC 4.2.1.150. 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-4991; short-chain-enoyl-CoA hydratase; EC 4.2.1.150; 3-hydroxybutyryl-CoA dehydratase; crotonase; crt (gene name). Cat No: EXWM-4991. | |
| succinyl-CoA-D-citramalate CoA-transferase | The enzyme, purified from the bacterium Clostridium tetanomorphum, can also accept itaconate as acceptor, with lower efficiency. Group: Enzymes. Synonyms: Sct. Enzyme Commission Number: EC 2.8.3.20. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3416; succinyl-CoA-D-citramalate CoA-transferase; EC 2.8.3.20; Sct. Cat No: EXWM-3416. | |
| 7α-hydroxysteroid dehydrogenase | Catalyses the oxidation of the 7α-hydroxy group of bile acids and alcohols both in their free and conjugated forms. The Bacteroides fragilis and Clostridium enzymes can also utilize NADP+. Group: Enzymes. Synonyms: 7α-hydroxy steroid dehydrogenase; 7α-HSDH. Enzyme Commission Number: EC 1.1.1.159. CAS No. 39361-64-3. 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-0062; 7α-hydroxysteroid dehydrogenase; EC 1.1.1.159; 39361-64-3; 7α-hydroxy steroid dehydrogenase; 7α-HSDH. Cat No: EXWM-0062. | |
| 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. | |
| α-Mannosidase 125A from Clostridium perfringens, 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. Group: Enzymes. Synonyms: alpha-D-mannosidase; alpha-mannosidase; alpha-D-mannoside mannohydrolase; α-D-Mannosidase; EC 3.2.1.24; 9025-42-7. Enzyme Commission Number: EC 3.2.1-. Purity: >90% by SDS-PAGE. Mannosidase. Mole weight: 51.8 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: Clostridium perfringens. alpha-D-mannosidase; alpha-mannosidase; alpha-D-mannoside mannohydrolase; α-D-Mannosidase; EC 3.2.1.-; α-Mannosidase 125A. Cat No: NATE-1472. | |
| aminoimidazolase | Requires Fe2+. This enzyme forms part of the xanthine-degradation pathway in some bacteria. The product of the reaction, imidazol-4-one, can be converted non-enzymically into formiminoglycine. An enzyme has been identified in Clostridium cylindrosporum that can perform this hydrolysis reaction. Group: Enzymes. Synonyms: 4-aminoimidazole hydrolase;4-aminoimidazole deaminase. Enzyme Commission Number: EC 3.5.4.8. CAS No. 9025-17-6. 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-4576; aminoimidazolase; EC 3.5.4.8; 9025-17-6; 4-aminoimidazole hydrolase;4-aminoimidazole deaminase. Cat No: EXWM-4576. | |
| Amylase 126A from Clostridium perfringens, 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: >90% by SDS-PAGE. α-Amylase. Mole weight: 40.4 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: Clostridium perfringens. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A; Amylase 126A. Cat No: NATE-1302. | |
| Arabinofuranosidase 43A from Clostridium stercorarium, 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-a. Enzyme Commission Number: EC 3.2.1.55 & EC 3.2.1.37. CAS No. 9067-74-7. Purity: >90% by SDS-PAGE. α-L-Arabinofuranosidase. Mole weight: 39.1 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: Clostridium stercorarium. 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; Arabinofuranosidase 43A. Cat No: NATE-1314. | |
| Arabinofuranosidase 43A from Streptomyces avermitilis, 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-arabinofuranosid. Enzyme Commission Number: EC 3.2.1.-. CAS No. 9067-74-7. Purity: >90% by SDS-PAGE. α-L-Arabinofuranosidase. Mole weight: 36.4 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: Clostridium stercorarium. 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; Arabinofuranosidase 43A. Cat No: NATE-1315. | |
| Arabinofuranosidase 43B from Clostridium thermocellum, 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-arabinofuranosi. Enzyme Commission Number: EC 3.2.1.55. CAS No. 9067-74-7. Purity: >90% by SDS-PAGE. α-L-Arabinofuranosidase. Mole weight: 36.2 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: Clostridium thermocellum. 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; Arabinofuranosidase 43B. Cat No: NATE-1316. | |
| Arabinofuranosidase 51A from Clostridium thermocellum, 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; alp. Enzyme Commission Number: EC 3.2.1.55. CAS No. 9067-74-7. Purity: >90% by SDS-PAGE. α-L-Arabinofuranosidase. Mole weight: 58.7 kDa. Activity: 125 U/mg. 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: Clostridium thermocellum. 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; Arabinofuranosidase 51A. Cat No: NATE-1324. | |
| Arabinoxylanase 5A from Clostridium thermocellum, Recombinant | A group of enzymes that catalyze the hydrolysis of alpha- or beta-xylosidic linkages. Group: Enzymes. Synonyms: arabinoxylanase; EC 3.2.1.-. Enzyme Commission Number: EC 3.2.1.-. Purity: >90% as judged by SDS-PAGE. Arabinoxylanase. Mole weight: 94.5 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: Clostridium thermocellum. arabinoxylanase; EC 3.2.1.-. Cat No: NATE-1517. | |
| β-1,3-Glucanase from Clostridium thermocellum, Recombinant | Glucan endo-1,3-beta-D-glucosidase is an enzyme with system name 3-beta-D-glucan glucanohydrolase. This enzyme catalyses the following chemical reaction:Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. This enzyme is marginally active on mixed-link (1->3,1->4)-beta-D-glucans. Group: Enzymes. Synonyms: endo-1,3-β-glucanase; laminarinase; laminaranase; oligo-1,3-glucosidase; endo-1,3-β-glucanase; callase; β-1,3-glucanase; kitalase; 1,3-β-D-glucan 3-glucanohydrolase; endo-(1,3)-β-D-gl. Enzyme Commission Number: EC 3.2.1.39. CAS No. 9025-37-0. Purity: > 95 % as judged by SDS-PAGE. Glucanase. Mole weight: 82262.8 Da. Activity: 1500 U/mg. Storage: Store at -20°C (shipped at room temperature). Form: Supplied in 35 mM HEPES buffer, pH 7.8, containing 750 mM NaCl, 5 mM imidazole, 2.5 mM CaCl2, 0.02 % (w/v) sodium azide and 25 % (v/v) glycerol. Source: Clostridium thermocellum ATCC 27405. endo-1,3-β-glucanase; laminarinase; laminaranase; oligo-1,3-glucosidase; endo-1,3-β-glucanase; callase; β-1,3-glucanase; kitalase; 1,3-β-D-glucan 3-glucanohydrolase; endo-(1,3)-β-D-glucanase; (1?3)-β-glucan 3-glucanohydrolase; endo-1,3-β-D-glucanase; endo-1,3-β-glucosidase; 1,3-β-D-glucan glucanohydrolase; EC 3.2.1.39; 9044-93-3. Cat No: NATE-1180. | |
| β-Glucosidase 1A from Clostridium cellulovorans, 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; ar. Enzyme Commission Number: EC 3.2.1.21. CAS No. 9001-22-3. Purity: >90% by SDS-PAGE. β-Glucosidase. Mole weight: 53.6 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: Clostridium cellulovorans. 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; β-Glucosidase 1A. Cat No: NATE-1434. | |
| β-Glucosidase from Clostridium thermocellum, 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; arbutinas. Enzyme Commission Number: EC 3.2.1.21. CAS No. 9001-42-7. Purity: > 95 % as judged by SDS-PAGE. β-Glucosidase. Mole weight: 52700 Da. Activity: 33 U/mg. Storage: Store at -20°C (shipped at room temperature). Form: Supplied in 35 mM HEPES buffer, pH 7.8, containing 750 mM NaCl, 5 mM imidazole, 3.5 mM CaCl2, 0.02 % (w/v) sodium azide and 25 % (v/v) glycerol. Source: Clostridium thermocellum DSM 1237. 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-1182. | |
| β-Mannanase 26B from Clostridium cellulovorans, Recombinant | Mannan endo-1,4-beta-mannosidase is an enzyme with system name 4-beta-D-mannan mannanohydrolase. This enzyme catalyses the following chemical reaction: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans. Group: Enzymes. Synonyms: endo-1,4-β-mannanase; endo-β-1,4-mannase; β-mannanase B; β-1, 4-mannan 4-mannanohydrolase; endo-β-mannanase; β-D-mannanase; mannan endo-1,4-β-mannosidase; 1,4-β-D-mannan mannanohydrolase; EC 3.2.1.78. Enzyme Commission Number: EC 3.2.1.78. CAS No. 37288-54-3. Purity: >90% by SDS-PAGE. endo-1,4 β-Mannanase. Mole weight: 39.8 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: Clostridium cellulovorans. endo-1,4-β-mannanase; endo-β-1,4-mannase; β-mannanase B; β-1, 4-mannan 4-mannanohydrolase; endo-β-mannanase; β-D-mannanase; mannan endo-1,4-β-mannosidase; 1,4-β-D-mannan mannanohydrolase; EC 3.2.1.78; β-Mannanase 26B. Cat No: NATE-1462. | |
| β-Mannanase 26C from Clostridium thermocellum, Recombinant | Mannan endo-1,4-beta-mannosidase is an enzyme with system name 4-beta-D-mannan mannanohydrolase. This enzyme catalyses the following chemical reaction: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans. Group: Enzymes. Synonyms: endo-1,4-β-mannanase; endo-β-1,4-mannase; β-mannanase B; β-1, 4-mannan 4-mannanohydrolase; endo-β-mannanase; β-D-mannanase; mannan endo-1,4-β-mannosidase; 1,4-β-D-mannan mannanohydrolase; EC 3.2.1.78. Enzyme Commission Number: EC 3.2.1.78. CAS No. 37288-54-3. Purity: >90% by SDS-PAGE. endo-1,4 β-Mannanase. Mole weight: 42.0 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: Clostridium thermocellum. endo-1,4-β-mannanase; endo-β-1,4-mannase; β-mannanase B; β-1, 4-mannan 4-mannanohydrolase; endo-β-mannanase; β-D-mannanase; mannan endo-1,4-β-mannosidase; 1,4-β-D-mannan mannanohydrolase; EC 3.2.1.78; β-Mannanase 26C. Cat No: NATE-1460. | |
| β-Mannanase 5A from Clostridium cellulovorans, Recombinant | Mannan endo-1,4-beta-mannosidase is an enzyme with system name 4-beta-D-mannan mannanohydrolase. This enzyme catalyses the following chemical reaction: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans. Group: Enzymes. Synonyms: endo-1,4-β-mannanase; endo-β-1,4-mannase; β-mannanase B; β-1, 4-mannan 4-mannanohydrolase; endo-β-mannanase; β-D-mannanase; mannan endo-1,4-β-mannosidase; 1,4-β-D-mannan mannanohydrolase; EC 3.2.1.78. Enzyme Commission Number: EC 3.2.1.78. CAS No. 37288-54-3. Purity: >50% by SDS-PAGE. endo-1,4 β-Mannanase. Mole weight: 38.8 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: Clostridium cellulovorans. endo-1,4-β-mannanase; endo-β-1,4-mannase; β-mannanase B; β-1, 4-mannan 4-mannanohydrolase; endo-β-mannanase; β-D-mannanase; mannan endo-1,4-β-mannosidase; 1,4-β-D-mannan mannanohydrolase; EC 3.2.1.78; β-Mannanase 5A. Cat No: NATE-1461. | |
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