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| Product | Description | |
|---|---|---|
| Glycogen branching enzyme from Bacillus subtilis, Recombinant | Glycogen branching enzyme is an enzyme that adds branches to the growing glycogen molecule during the synthesis of glycogen, a storage form of glucose. More specifically, during glycogen synthesis, a glucose 1-phosphate molecule reacts with uridine triphosphate (UTP) to become UDP-glucose, an activated form of glucose. The activated glucosyl unit of UDP-glucose is then transferred to the hydroxyl group at the C-4 of a terminal residue of glycogen to form an α-1,4-glycosidic linkage, a reaction catalyzed by glycogen synthase. Importantly, glycogen synthase can only catalyze the synthesis of α-1,4-glycosidic linkages. Since glycogen is a readily mobil...;-1,4-glucan-6-glycosyltransferase; starch branching enzyme; 1,4-α-D-glucan:1,4-α-D-glucan 6-α-D-(1,4-α-D-glucano)-transferase. Enzyme Commission Number: EC 2.4.1.18. CAS No. 9001-97-2. Purity: > 95 % as judged by SDS-PAGE. Glycogen branching enzyme. Mole weight: 77485.4 Da. Activity: 38.04 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Bacillus subtilis subsp. subtilis str. 168. Branching enzyme, amylo-(1,4?1,6)-transglycosylase; Q-enzyme; α-glucan-branching glycosyltransferase; amylose isomerase; enzymatic branching factor; branching glycosyltransferase; enzyme Q; gluc |  |
| 1,2-α-glucosylglycerol phosphorylase | The enzyme has been isolated from the bacterium Bacillus selenitireducens. In the absence of glycerol the enzyme produces α-D-glucopyranose and phosphate from β-D-glucopyranose 1-phosphate. In this reaction the glucosyl residue is transferred to a water molecule with an inversion of the anomeric conformation. Group: Enzymes. Synonyms: 2-O-α-D-glucopyranosylglycerol phosphorylase. Enzyme Commission Number: EC 2.4.1.332. 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-2570; 1,2-α-glucosylglycerol phosphorylase; EC 2.4.1.332; 2-O-α-D-glucopyranosylglycerol phosphorylase. Cat No: EXWM-2570. | |
| 2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent) | Involved in the biosynthetic pathway of the aminoglycoside antibiotics of the butirosin family. The enzyme from Bacillus circulans was shown to be a radical S-adenosyl-L-methionine (SAM) enzyme. cf. EC 1.1.1.329, 2-deoxy-scyllo-inosamine dehydrogenase. Group: Enzymes. Synonyms: btrN (gene name); 2-deoxy-scyllo-inosamine dehydrogenase (SAM-dependent). Enzyme Commission Number: EC 1.1.99.38. 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-0466; 2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent); EC 1.1.99.38; btrN (gene name); 2-deoxy-scyllo-inosamine dehydrogenase (SAM-dependent). Cat No: EXWM-0466. | |
| 2-deoxy-scyllo-inosose synthase | Requires Co2+. Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Requires an NAD+ cofactor, which is transiently reduced during the reaction. The enzyme from the bacterium Bacillus circulans forms a complex with the glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase (EC 4.3.3.6), which appears to stabilize the complex. Group: Enzymes. Synonyms: btrC (gene name); neoC (gene name); kanC (gene name). Enzyme Commission Number: EC 4.2.3.124. 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-5137; 2-deoxy-scyllo-inosose synthase; EC 4.2.3.124; btrC (gene name); neoC (gene name); kanC (gene name). Cat No: EXWM-5137. | |
| 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase | Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Unlike the enzyme from the bacterium Streptomyces kanamyceticus, which can also accept UDP-D-glucose (cf. EC 2.4.1.284, 2-deoxystreptamine glucosyltransferase), the enzyme from Bacillus circulans can only accept UDP-N-acetyl-α-D-glucosamine. Group: Enzymes. Synonyms: btrM (gene name); neoD (gene name); kanF (gene name). Enzyme Commission Number: EC 2.4.1.283. 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-2516; 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase; EC 2.4.1.283; btrM (gene name); neoD (gene name); kanF (gene name). Cat No: EXWM-2516. | |
| 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate isomerase | The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. The enzyme can interconvert the (E) isomer formed in the reaction into the (Z) isomer, although this isomerization is not part of the pathway leading to bacilysin. Group: Enzymes. Synonyms: BacB. Enzyme Commission Number: EC 5.3.3.19. 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-5497; 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate isomerase; EC 5.3.3.19; BacB. Cat No: EXWM-5497. | |
| 6-carboxytetrahydropterin synthase | Binds Zn2+. Isolated from the bacteria Bacillus subtilis and Escherichia coli. The reaction is part of the biosynthesis pathway of queuosine.The enzyme from Escherichia coli can also convert 6-pyruvoyl-5,6,7,8-tetrahydropterin and sepiapterin to 6-carboxy-5,6,7,8-tetrahydropterin. Group: Enzymes. Synonyms: CPH4 synthase; queD (gene name); ToyB; ykvK (gene name). Enzyme Commission Number: EC 4.1.2.50. 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-4887; 6-carboxytetrahydropterin synthase; EC 4.1.2.50; CPH4 synthase; queD (gene name); ToyB; ykvK (gene name). Cat No: EXWM-4887. | |
| Alanine Dehydrogenase from Bacillus cereus, Recombinant | L-Alanine dehydrogenase is an A-stereospecific dehydrogenase that catalyzes the reversible deamination of L-alanine to pyruvate and ammonium. It is important for the geneRation of pyruvate during sporulation. L-Alanine dehydrogenase from Bacillus subtilis has a predominately ordered kinetic mechanism in which NAD binds before L-alanine. Subsequently, ammonia, pyruvate, and NADH are released in that specific order. Optimal pH for the amination reaction is 8.8-9.0, whereas it is 10-10.5 for the deamination reaction. The enzyme is inactivated by divalent metal ions and p-chloromercuribenzoate, mercuric ion being most effective. The inactivation may be reversed by L-or D-cysteine. Group: Enzymes. Synonyms: L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alan. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. Activity: > 350 units/ml. Storage: -20°C. Source: E. coli. Species: Bacillus cereus. L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Cat No: NATE-0044. | |
| α-Galactosidase 4A from Bacillus halodurans, 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: 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: Bacillus halodurans. 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-1404. | |
| α-Glucosidase | α-Glucosidase. Synonyms: alpha-Glucosidase (from Yeast) 100kU pack;a-Glucosidase (EC 3.2.1.20);β-D-Glucoside glycohydrolase (EC 3.2.1.21);MALTASE;MALTASE TYPE I;MALTASE TYPE V;A-glucosidase from bacillus*stearothermophilus ly;A-glucosidase type I from bakers yeast. CAS No. 9001-42-7. Pack Sizes: 1 kg. Product ID: CDF4-0060. Molecular formula: NULL. Category: Enzyme Preparations. Product Keywords: Food Ingredients; Enzyme Preparations; α-Glucosidase; CDF4-0060; 9001-42-7; NULL; 232-604-7; 9001-42-7. Purity: 0.99. Color: off-White. EC Number: 232-604-7. Physical State: Powder. Storage: 2-8°C. Application: For the determination of α-amylase and the synthesis of various 1'-O-sucrose and 1-O-fructose esters. Melting Point: 154.3-155.3 °C. Product Description: This product has been enhanced for energy efficiency and waste prevention when used in starch hydrolysis research. |  |
| arabinogalactan endo-β-1,4-galactanase | This enzyme, isolated from the bacterium Bacillus subtilis, hydrolyses the β(1?4) bonds found in type I plant arabinogalactans, which are a component of the primary cell walls of dicots. The predominant product is a tetrasaccharide. cf. EC 3.2.1.181, galactan endo-β-1,3-galactanase. Group: Enzymes. Synonyms: endo-1,4-β-galactanase; galactanase (ambiguous); arabinogalactanase; ganB (gene name). Enzyme Commission Number: EC 3.2.1.89. CAS No. 58182-40-4. endo-1,4-β-Galactanase. 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-3953; arabinogalactan endo-β-1,4-galactanase; EC 3.2.1.89; 58182-40-4; endo-1,4-β-galactanase; galactanase (ambiguous); arabinogalactanase; ganB (gene name). Cat No: EXWM-3953. | |
| BamH I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 50-fold overdigestion with enzyme approximately 90% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 4000U; 20000U; 4000U; 20000U. G↑GATCC CCTAG↓G. Activity: 20000; 50000u.a./ml. Appearance: 10 X SE-buffer G, BSA. Storage: -20°C. Form: Liquid. Source: An E.coli strain, that carries the cloned gene BamHI from Bacillus amyloliquefaciens H. Pack: 10 mM Tris-HCl (pH 7.6); 50 mM NaCl; 0,1 mM EDTA; 100 μg/ml BSA; 1 mM DTT; 50% glycerol. Cat No: ET-1030RE. | |
| BCL I | BCL I. Uses: Designed for use in research and industrial production. Additional or Alternative Names: RESTRICTION ENDONUCLEASES BCL I;FBA I;BCL I;BCL I RESTRICTION ENZYME;restriction endonuclease bcl I from*bacillus cald;RESTRICTION ENDONUCLEASE BCL I FROM*BACI LLUS CALDOL;BCL I 5'.T/GATCA.3' FROM THE THERMOPHILE BACILLUS CALDOLYTICUS SOLUTION IN 50%. Product Category: Heterocyclic Organic Compound. CAS No. 81295-11-6. Purity: 0.96. Product ID: ACM81295116. Alfa Chemistry ISO 9001:2015 Certified. Categories: BC Lions. |  |
| benzil reductase [(S)-benzoin forming] | The enzyme also reduces 1-phenylpropane-1,2-dione. The enzyme from Bacillus cereus in addition reduces 1,4-naphthoquinone and 1-(4-methylphenyl)-2-phenylethane-1,2-dione with high efficiency. Group: Enzymes. Synonyms: YueD. Enzyme Commission Number: EC 1.1.1.320. 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-0233; benzil reductase [(S)-benzoin forming]; EC 1.1.1.320; YueD. Cat No: EXWM-0233. | |
| β-Xylosidase from Bacillus subtilis, Recombinant | Releases reducing sugars from birchwood xylan (X0502), also catalyzes the hydrolysis of 4-methylumbelliferyl-β-D-cellobioside and 4-methylumbelliferyl-β-D-glucopyranoside. This enzyme does not possess endo-xylanase, arabinoxylanase or β-glucanase activities. β-Xylosidase undergoes post-translation glycosylation which has been shown to be critical for its proper activity and stability. Deglycosylation altered the the optimum temperature and pH for activity and decreased its thermostability. Group: Enzymes. Synonyms: β-Xylosidase; β-Xylosidase, thermostable; 9025-53-0. Enzyme Commission Number: EC 3.2.1.37. CAS No. 9025-53-0. Purity: > 95 % as judged by SDS-PAGE. β-Xylosidase. Mole weight: 64909.6 Da. Activity: 20.67 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Bacillus subtilis subsp. subtilis str. 168. β-Xylosidase; β-Xylosidase, thermostable; 9025-53-0. Cat No: NATE-1190. | |
| Bgl II | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 10-fold overdigestion with enzyme more than 90% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 1000U; 5000U. A↑GATCT TCTAG↓A. Activity: 10000u.a./ml. Appearance: 10 X SE-buffer O. Storage: -20°C. Form: Liquid. Source: An E.coli strain that carries the cloned Bgl II gene from Bacillus globigii. Pack: 10 mM Tris-HCl (pH 7.5); 50 mM NaCl; 0,1 mM EDTA; 7 mM 2-mercaptoethanol; 200 μg/ml BSA; 50% glycerol. Cat No: ET-1034RE. | |
| Bmt I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA (Hind III-digest) in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 20-fold overdigestion with enzyme about 95% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 1000U; 5000U. GCTAG↑C C↓GATCG. Activity: 20000u.a./ml. Appearance: 10 X SE-buffer W. Storage: -20°C. Form: Liquid. Source: An E.coli strain that carries the cloned Bmt I gene from Bacillus megaterium S2. Pack: 10 mM Tris-HCl (pH 7.5); 200 mM NaCl; 0.1 mM EDTA; 1 mM DTT; 200 μg/ml BSA; 50% glycerol. Cat No: ET-1036RE. | |
| Chitinase 18A from Bacillus cereus, 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: 38.3 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: Bacillus cereus. Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase; Chitosanase 18A. Cat No: NATE-1377. | |
| Chitinase 18A from Bacillus licheniformis, 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: 49.2 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: Bacillus licheniformis. Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase; Chitosanase 18A. Cat No: NATE-1378. | |
| Chitosanase 46A from Bacillus subtilis, 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 3.2.1.132. CAS No. 51570-20-8. Purity: >90% by SDS-PAGE. Chitosanase. Mole weight: 29.5 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: Bacillus subtilis. Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase; Chitosanase 46A. Cat No: NATE-1376. | |
| Chitosanase 8B from Bacillus cereus, 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 3.2.1.132. CAS No. 51570-20-8. Purity: >90% by SDS-PAGE. Chitosanase. Mole weight: 47.8 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: Bacillus cereus. Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase; Chitosanase 8B. Cat No: NATE-1375. | |
| Chitosanase from Bacillus sp. (food grade) | Chitosanase is a powdered chitosanase preparation made by submerged fermentation of a selected strain of the bacterium Bacillus sp. The enzyme catalyzes the breakdown of chitosan, a partially or completely de-acetylated derivative of chitin (β-1,4 homopolymer of N-acetyl glucosamine). Applications: Chitosanase can be used for hydrolyzing chitosan (degree of de-acetylatin: 40~100%). especially, it can be used for the production of chitosan oligosaccharides from chitosan, which have a variety of biological activities such as immuno-stimulating activity, anti-tumor activity, anti-microbial activity, etc. Group: Enzymes. Synonyms: Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase. Chitosanase. Mole weight: 45,000Da estimated by SDS-PAGE. Activity: 35,000U/g. Storage: The product should be stored in a cool, dry environment with temperatures below 4°C. Form: White or light yellow colored, freeze-dried powder. Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase. Cat No: CHIC-001. | |
| CoA-disulfide reductase | A flavoprotein. Not identical with EC 1.8.1.6 (cystine reductase), EC 1.8.1.7 (glutathione-disulfide reductase) or EC 1.8.1.13 (bis-γ-glutamylcystine reductase). The enzyme from the bacterium Staphylococcus aureus has a strong preference for NADPH, while the bacterium Bacillus megaterium contains both NADH and NADPH-dependent enzymes. Group: Enzymes. Synonyms: CoA-disulfide reductase (NADH2); NADH2:CoA-disulfide oxidoreductase; CoA:NAD+ oxidoreductase (misleading); CoADR; coenzyme A disulfide reductase. Enzyme Commission Number: EC 1.8.1.14. CAS No. 206770-55-0. 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-1640; CoA-disulfide reductase; EC 1.8.1.14; 206770-55-0; CoA-disulfide reductase (NADH2); NADH2:CoA-disulfide oxidoreductase; CoA:NAD+ oxidoreductase (misleading); CoADR; coenzyme A disulfide reductase. Cat No: EXWM-1640. | |
| cobalt-factor III methyltransferase | Isolated from Bacillus megaterium. The enzyme catalyses both methylation at C-17 and ring contraction. Contains a [4Fe-4S] cluster. It can also convert cobalt-precorrin-3 to cobalt-precorrin-4. The reductant may be thioredoxin. Group: Enzymes. Synonyms: CbiH60 (gene name). Enzyme Commission Number: EC 2.1.1.272. 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-1878; cobalt-factor III methyltransferase; EC 2.1.1.272; CbiH60 (gene name). Cat No: EXWM-1878. | |
| cobalt-precorrin-6A reductase | The enzyme catalyses a step in the anaerobic (early cobalt insertion) pathway of adenosylcobalamin biosynthesis. The enzyme from the bacterium Bacillus megaterium has no activity with NADPH. The equivalent enzyme in the aerobic pathway is EC 1.3.1.54, precorrin-6A reductase. Group: Enzymes. Synonyms: cbiJ (gene name). Enzyme Commission Number: EC 1.3.1.106. 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-1278; cobalt-precorrin-6A reductase; EC 1.3.1.106; cbiJ (gene name). Cat No: EXWM-1278. | |
| Cyclodextrin Glucanotransferase (Crude Enzyme) | In enzymology, a cyclomaltodextrin glucanotransferase is an enzyme that catalyzes the chemical reaction of cyclizing part of a 1,4-alpha-D-glucan molecule through the formation of a 1,4-alpha-D-glucosidic bond. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Industry; synthesis; nutrition; pharmacology. Group: Enzymes. Synonyms: Bacillus macerans amylase; cyclodextrin glucanotransfera. Enzyme Commission Number: EC 2.4.1.19. CAS No. 9030-9-5. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. Bacillus macerans amylase; cyclodextrin glucanotransferase; α-cyclodextrin glucanotransferase; α-cyclodextrin glycosyltransferase; β-cyclodextrin glucanotransferase; β-cyclodextrin glycosyltransferase; γ-cyclodextrin glycosyltransferase; cyclodextrin glycosyltransferase; cyclomaltodextrin glucotransferase; cyclomaltodextrin glycosyltransferase; konchizaimu; α-1,4-glucan 4-glycosyltransferase, cyclizing; BMA; CGTase; neutral-cyclodextrin glycosyltransferase; 1,4-α-D-glucan 4-α-D-(1,4-α-D-glucano)-transferase (cyclizing). Pack: 100ml. Cat No: NATE-1812. | |
| cycloisomaltooligosaccharide glucanotransferase | Specific for (1?6)-α-D-glucans (dextrans) and, unlike cyclomaltodextrin glucanotransferase (EC 2.4.1.19), without activity towards (1?4)-α-D-glucans, such as amylose. It also has no activity on oligosaccharides, such as amylopectin and pullulan,containing (1?6)-α-D-glucosidic linkages at branch points. The enzyme from Bacillus circulans T-3040 has been shown to form cycloisomalto-oligosaccharides of three sizes (7, 8 and 9 glucose units). It will also catalyse the disproportionation of two isomalto-oligosaccharides molecules to yield a series of isomalto-oligosachharides and the addition of D-glucose to cycloisomalto-oligosaccharides with ring opening to form isomalto-oligosaccharides. Group: Enzymes. Enzyme Commission Number: EC 2.4.1.248. 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-2477; cycloisomaltooligosaccharide glucanotransferase; EC 2.4.1.248. Cat No: EXWM-2477. | |
| cyclo(L-leucyl-L-leucyl) synthase | The reaction proceeds following a ping-pong mechanism forming a covalent intermediate between an active site serine and the first L-leucine residue. The proteins from bacteria of the genus Bacillus also form small amounts of cyclo(L-phenylalanyl-L-leucyl) and cyclo(L-leucyl-L-methionyl). Group: Enzymes. Synonyms: YvmC; cLL synthase; cyclodileucine synthase. Enzyme Commission Number: EC 2.3.2.22. 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-2296; cyclo(L-leucyl-L-leucyl) synthase; EC 2.3.2.22; YvmC; cLL synthase; cyclodileucine synthase. Cat No: EXWM-2296. | |
| cyclomaltodextrin glucanotransferase | Cyclomaltodextrins (Schardinger dextrins) of various sizes (6,7,8, etc. glucose units) are formed reversibly from starch and similar substrates. Will also disproportionate linear maltodextrins without cyclizing (cf. EC 2.4.1.25, 4-α-glucanotransferase). Group: Enzymes. Synonyms: Bacillus macerans amylase; cyclodextrin glucanotransferase; α-cyclodextrin glucanotransferase; α-cyclodextrin glycosyltransferase; β-cyclodextrin glucanotransferase; β-cyclodextrin glycosyltransferas. Enzyme Commission Number: EC 2.4.1.19. CAS No. 9030-9-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2416; cyclomaltodextrin glucanotransferase; EC 2.4.1.19; 9030-09-5; Bacillus macerans amylase; cyclodextrin glucanotransferase; α-cyclodextrin glucanotransferase; α-cyclodextrin glycosyltransferase; β-cyclodextrin glucanotransferase; β-cyclodextrin glycosyltransferase; γ-cyclodextrin glycosyltransferase; cyclodextrin glycosyltransferase; cyclomaltodextrin glucotransferase; cyclomaltodextrin glycosyltransferase; konchizaimu; α-1,4-glucan 4-glycosyltransferase, cyclizing; BMA; CGTase; neutral-cyclodextrin glycosyltransferase; 1,4-α-D-glucan 4-α-D-(1,4-α-D-glucano)-transferase (cyclizing). Cat No: EXWM-2416. | |
| cystathionine β-synthase (O-acetyl-L-serine) | A pyridoxal 5'-phosphate protein. The enzyme, purified from the bacterium Bacillus subtilis, also has a low activity with L-serine (cf. EC 4.2.1.22, cystathionine β-synthase). Group: Enzymes. Synonyms: MccB; O-acetylserine dependent cystathionine β-synthase. Enzyme Commission Number: EC 2.5.1.134. 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-2750; cystathionine β-synthase (O-acetyl-L-serine); EC 2.5.1.134; MccB; O-acetylserine dependent cystathionine β-synthase. Cat No: EXWM-2750. | |
| D-amino-acid transaminase | A pyridoxal-phosphate protein. The enzyme from thermophilic Bacillus species acts on many D-amino acids with D-alanine and D-2-aminobutyrate as the best amino donors. It can similarly use any of several 2-oxo acids as amino acceptor, with 2-oxoglutarate and 2-oxobutyrate among the best. The enzyme from some other sources has a broader specificity. Group: Enzymes. Synonyms: D-aspartate transaminase; D-alanine aminotransferase; D-aspartic aminotransferase;D-alanine-D-glutamate transaminase; D-alanine transaminase; D-amino acid aminotransferase. Enzyme Commission Number: EC 2.6.1.21. CAS No. 37277-85-3. ALT. 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-2861; D-amino-acid transaminase; EC 2.6.1.21; 37277-85-3; D-aspartate transaminase; D-alanine aminotransferase; D-aspartic aminotransferase;D-alanine-D-glutamate transaminase; D-alanine transaminase; D-amino acid aminotransferase. Cat No: EXWM-2861. | |
| Diacetylchitobiose deacetylase from Bacillus cereus, Recombinant | Diacetylchitobiose deacetylase is an enzyme from Bacillus cereus that exhibits deacetylase activity to the N-acetyl moiety of the N-acetylglucosamine and the diacetylchitobiose and triacetylchitotriose. Group: Enzymes. Synonyms: N,N'-diacetylchitobiose deacetylase (nonreducing end); EC 3.5.1.-. Enzyme Commission Number: EC 3.5.1.-. Purity: >90% as judged by SDS-PAGE. Diacetylchitobiose deacetylase. Mole weight: 28.3 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: Bacillus cereus. N,N'-diacetylchitobiose deacetylase (nonreducing end); EC 3.5.1.-. Cat No: NATE-1542. | |
| diglucosyl diacylglycerol synthase (1,6-linking) | The enzyme is found in several bacterial species. The enzyme from Bacillus subtilis is specific for glucose. The enzyme from Mycoplasma genitalium can incoporate galactose with similar efficiency, but forms mainly 1,2-diacyl-diglucopyranosyl-sn-glycerol in vivo. The enzyme from Staphylococcus aureus can also form glucosyl-glycero-3-phospho-(1'-sn-glycerol). Group: Enzymes. Synonyms: monoglucosyl diacylglycerol (1?6) glucosyltransferase; MGlcDAG (1?6) glucosyltransferase; DGlcDAG synthase (ambiguous); UGT106B1; ypfP (gene name). Enzyme Commission Number: EC 2.4.1.315. 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-2551; diglucosyl diacylglycerol synthase (1,6-linking); EC 2.4.1.315; monoglucosyl diacylglycerol (1?6) glucosyltransferase; MGlcDAG (1?6) glucosyltransferase; DGlcDAG synthase (ambiguous); UGT106B1; ypfP (gene name). Cat No: EXWM-2551. | |
| dihydroanticapsin dehydrogenase | The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Group: Enzymes. Synonyms: BacC; ywfD (gene name). Enzyme Commission Number: EC 1.1.1.385. 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-0304; dihydroanticapsin dehydrogenase; EC 1.1.1.385; BacC; ywfD (gene name). Cat No: EXWM-0304. | |
| EC 3.2.1.6 | EC 3.2.1.6. Synonyms: beta-glucanasefromaspergillusniger;beta-D-Glucanase;1,3-(1,3:1,4)-BETA-D-GLUCAN 3(4)-GLUCANOHYDROLASE;1,3-BETA-D-GLUCAN 3(4)-GLUCANOHYDROLASE; LAMINARINASE; BETA-GLUCANASE; EC 3.2.1.6;beta-Glucanase from Bacillus subtilis. CAS No. 9074-98-0. Pack Sizes: 1 kg. Product ID: CDF4-0036. Category: Enzyme Preparations. Product Keywords: Food Ingredients; Enzyme Preparations; EC 3.2.1.6; CDF4-0036; 9074-98-0; 232-979-7; 9074-98-0. Purity: 0.99. Color: Light yellow-Brown. EC Number: 232-979-7. Physical State: Powder. Storage: 2-8°C. Melting Point: 177-178 °C(Solv: ethanol (64-17-5); water (7732-18-5)). Density: 1.388[at 20°C]. Product Description: This product has been enhanced for energy eficiency and waste prevention when used in cellulosic ethanol research. | |
| Endoproteinase GluC from Staphylococcus aureus, Recombinant | Protease S. aureus V8 (Endoproteinase-Glu-C) specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acids. In the presence of ammonium, the enzyme specificity is limited to glutamic sites. It has a molecular weight of 27 kDa daltons and optimum pH's of 4.0 and 7.8 with hemoglobin as the substrate. Protease S. aureus V8 is inhibited by diisopropylfluorophosphate and monovalent anions such as F-, Cl-, CH3COO-and NO3. Enzyme activity is determined by the casein digestion assay described by Drapeau. Endoproteinase gluc (staphylococcus aureus protease v8) is a serine proteinase which selectively cleaves peptide bonds c-terminal to...tide identification. Group: Enzymes. Synonyms: EC 3.4.21.19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase. CAS No. 66676-43-5. V8 Protease. Mole weight: 29849 daltons. Activity: 38.3 μmol/min/mg. Storage: at -20°C. Form: Supplied freeze-dried from a Tris-HCl and sodium chloride buffer. Source: Bacillus subtilis. Species: Staphylococcus aureus. EC 3.4.21.19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase. Cat No: NATE-1270. | |
| Esterase from Bacillus stearothermophilus, Recombinant | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Esterase, from bacillus stearothermophilus, may be used for the characterization of novel esterases. this product is recombinant and expressed in e. coli. Group: Enzymes. Synonyms: EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylestera. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 8.0 units/mg. Storage: -20°C. Source: E. coli. Species: Bacillus stearothermophilus. EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase; 9016-18-6. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0241. | |
| Esterase from Bacillus subtilis, Recombinant | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Esterase, from bacillus subtilis, may be used in protein engineering research as well as to study the kinetic resolution of acetates of arylaliphatic tertiary alcohols. this product is recombinant and expressed in e. coli (> 10 units/mg). Group: Enzymes. Synonyms: EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacet. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: Type I, > 10 units/mg; Type II, > 0.8 units/mg. Storage: -20°C. Source: E. coli. Species: Bacillus subtilis. EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase; 9016-18-6. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0242. | |
| factor-independent urate hydroxylase | This enzyme was previously thought to be a copper protein, but it is now known that the enzymes from soy bean (Glycine max), the mould Aspergillus flavus and Bacillus subtilis contains no copper nor any other transition-metal ion. The 5-hydroxyisourate formed decomposes spontaneously to form allantoin and CO2, although there is an enzyme-catalysed pathway in which EC 3.5.2.17, hydroxyisourate hydrolase, catalyses the first step. The enzyme is different from EC 1.14.13.113 (FAD-dependent urate hydroxylase). Group: Enzymes. Synonyms: uric acid oxidase; uricase; uricase II; urate oxidase. Enzyme Commission Number: EC 1.7.3.3. CAS No. 9002-12-4. UO. 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-1626; factor-independent urate hydroxylase; EC 1.7.3.3; 9002-12-4; uric acid oxidase; uricase; uricase II; urate oxidase. Cat No: EXWM-1626. | |
| γ-D-glutamyl-L-lysine dipeptidyl-peptidase | The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the recycling of the murein peptide. Group: Enzymes. Synonyms: YkfC. Enzyme Commission Number: EC 3.4.14.13. 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-4047; γ-D-glutamyl-L-lysine dipeptidyl-peptidase; EC 3.4.14.13; YkfC. Cat No: EXWM-4047. | |
| γ-D-glutamyl-meso-diaminopimelate peptidase | A 45-kDa metallopeptidase from Bacillus sphaericus, the substrates being components of the bacterial spore wall. A member of peptidase family M14 (carboxypeptidase A family). Endopeptidase II has similar activity, but differs in cellular location, molecular mass and catalytic mechanism. Group: Enzymes. Synonyms: endopeptidase I; γ-D-glutamyldiaminopimelate endopeptidase; γ-D-glutamyl-L-meso-diaminopimelate peptidoglycan hydrolase; γ-glutamyl-L-meso-diaminopimelyl endopeptidase; γ-D-glutamyl-meso-diaminopimelate endopeptidase; γ-D-glutamyl-meso-diaminopimelic peptidoglycan hydrolase; γ-D-glutamyl-m. Enzyme Commission Number: EC 3.4.19.11. CAS No. 62572-28-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4083; γ-D-glutamyl-meso-diaminopimelate peptidase; EC 3.4.19.11; 62572-28-5; endopeptidase I; γ-D-glutamyldiaminopimelate endopeptidase; γ-D-glutamyl-L-meso-diaminopimelate peptidoglycan hydrolase; γ-glutamyl-L-meso-diaminopimelyl endopeptidase; γ-D-glutamyl-meso-diaminopimelate endopeptidase; γ-D-glutamyl-meso-diaminopimelic peptidoglycan hydrolase; γ-D-glutamyl-meso-diaminopimelic endopeptidase; γ-D-glutamyl-meso-D-aminopimelic endopeptidase. Cat No: EXWM-4083. | |
| Glucan 1,4-α-maltohexaosidase 13A from Bacillus halodurans, Recombinant | Glucan 1,4-alpha-maltohexaosidase (EC 3.2.1.98, exo-maltohexaohydrolase, 1,4-alpha-D-glucan maltohexaohydrolase) is an enzyme with systematic name 4-alpha-D-glucan maltohexaohydrolase. This enzyme catalyses the following chemical reaction: Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non-reducing chain ends. The products have the alpha-configuration. Group: Enzymes. Synonyms: Glucan 1,4-alpha-maltohexaosidase; EC 3.2.1.98; exo-maltohexaohydrolase; 1,4-alpha-D-glucan maltohexaohydrolase; 4-α-D-glucan maltohexaohydrolase4-α-D-glucan maltohexaohydrolase. Enzyme Commission Number: EC 3.2.1.98. CAS No. 72561-12-7. Purity: >90% by SDS-PAGE. Glucan 1,4-α-maltohexaosidase. Mole weight: 64.9 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: Bacillus halodurans. Glucan 1,4-alpha-maltohexaosidase; EC 3.2.1.98; exo-maltohexaohydrolase; 1,4-alpha-D-glucan maltohexaohydrolase; 4-α-D-glucan maltohexaohydrolase4-α-D-glucan maltohexaohydrolase. Cat No: NATE-1296. | |
| glucosamine-1-phosphate N-acetyltransferase | The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Hemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Group: Enzymes. Enzyme Commission Number: EC 2.3.1.157. CAS No. 9031-91-8. GlcNAc1-phosphate uridyltransferase. 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-2096; glucosamine-1-phosphate N-acetyltransferase; EC 2.3.1.157; 9031-91-8. Cat No: EXWM-2096. | |
| glutamate-tRNAGln ligase | When this enzyme acts on tRNAGlu, it catalyses the same reaction as EC 6.1.1.17, glutamate-tRNA ligase. It has, however, diminished discrimination, so that it can also form glutamyl-tRNAGln. This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon. This accounts for the ability of this enzyme in, for example, Bacillus subtilis, to recognize both tRNA1Gln (UUG anticodon) and tRNAGlu (UUC anticodon) but not tRNA2Gln (CUG anticodon). The ability of this enzyme to recognize both tRNAGlu and one of the tRNAGln isoacceptors derives from their sharing a major identity element, a hypermodified derivative of U34 (5-methylaminomethyl-2-thiouridine). The glutamyl-tRNAGln is not used in protein synthesis until it is converted by EC 6.3.5.7, glutaminyl-tRNA synthase (glutamine-hydrolysing), into glutaminyl-tRNAGln. Group: Enzymes. Synonyms: nondiscriminating glutamyl-tRNA synthetase. Enzyme Commission Number: EC 6.1.1.24. CAS No. 9068-76-2. 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-5656; glutamate-tRNAGln ligase; EC 6.1.1.24; 9068-76-2; nondiscriminating glutamyl-tRNA synthetase. Cat No: EXWM-5656. | |
| glycine oxidase | A flavoenzyme containing non-covalently bound FAD. The enzyme from Bacillus subtilis is active with glycine, sarcosine, N-ethylglycine, D-alanine, D-α-aminobutyrate, D-proline, D-pipecolate and N-methyl-D-alanine. It differs from EC 1.4.3.3, D-amino-acid oxidase, due to its activity on sarcosine and D-pipecolate. The intermediate 2-iminoacetate is used directly by EC 2.8.1.10, thiazole synthase. Group: Enzymes. Enzyme Commission Number: EC 1.4.3.19. CAS No. 39307-16-9. 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-1473; glycine oxidase; EC 1.4.3.19; 39307-16-9. Cat No: EXWM-1473. | |
| Glycine Oxidase H244K from Bacillus subtilis, recombinant | Glycine oxidase (GO) from Bacillus subtilis (EC 1.4.3.19) is a homotetrameric flavin-dependent oxidoreductase. Each GO monomer is non-covalently bound to flavin adenine dinucleotide. GO catalyzes oxidative deamination of various primary and secondary amines (e.g. glycine, sarcosine, N-ethylglycine) and some D-amino acids (e.g. D -alanine, D -proline, D -valine) to the corresponding α-keto acids and hydrogen peroxide. Primarily, glycine oxidase catalyzes the oxidation of glycine in the biosynthesis of thiamine. The variant H244K shows a higher substrate specificity ratio for glycine versus sarcosine and a 5-fold improved specific activity in comparison to the wild-type. Group: Enzymes. Synonyms: Glycine oxidase; glycine oxygen oxidoreductase (deaminating); GO; EC 1.4.3.19; 39307-16-9. Enzyme Commission Number: EC 1.4.3.19. CAS No. 39307-16-9. Purity: > 90% by SDS-PAGE. Mole weight: 43.1 kDa (1-369 aa, NT His Tag). Activity: 1200 mU/mg. Storage: Store at -20°C. Stable for at least 1 year as supplied. Avoid repeated freeze and thaw cycles. Form: Liquid. Source: E. coli. Species: Bacillus subtilis. Glycine oxidase; glycine oxygen oxidoreductase (deaminating); GO; EC 1.4.3.19; 39307-16-9. Cat No: NATE-1674. | |
| Heat Stable α Amylase (High Temperature) (Food Grade) | Heat Stable Alpha Amylase (High Temperature) is made from the best strain of Bacillus licheniformis through deep fermentation and extraction technique. FDA regards the strain as safety.This food-grade product possesses better heat resistance and keeps adaptable under condition of lower pH. It is applied broadly for liquidizing in the industry of starch sugar. 1.it is an endo-enzyme. 2.it hydrolyzes the α-1,4-glucosidic linkages of gelatinized strach randomly to soluble dextrins,reducing the high viscosity of the starch slurry. Applications: Enzyme for starch sugar. Group: Enzymes. Synonyms: Heat Stable Alpha Amylase (High Temperature); Heat Stable Alpha Amylase; Alpha Amylase; High Temperature Alpha Amylase; Starch Sugar. CAS No. 9000-90-2. α-Amylase. Activity: 150,000u/ml. Storage: Should be stored in a cool place avoiding high temperature. Liquid: 3 months at 25°C, activity remain >90%; 6 months, activity remains >80%. Increase dosage after shelf life. Form: Liquid. Source: Bacillus licheniformis. Heat Stable Alpha Amylase (High Temperature); Heat Stable Alpha Amylase; Alpha Amylase; High Temperature Alpha Amylase; Starch Sugar. Pack: 25kgs/drum, 1.125kgs/drum. Cat No: SUG-001. | |
| Keratanase II from Bacillus circulans, Recombinant | Keratansae II hydrolyzes 1, 3-beta-glucosaminidic linkages to galactose in keratan sulfate. On cleavage, the enzyme requires the sulfate at 6-0 position of the participating glucosamine, but acts independently of the sulfate at 6-0 position of the galactose linked to the glucosamine. Applications: Used in the screening and diagnosis of morquio a syndrome (mps iva). validation of an lc-ms/ms assay for detecting relevant disaccharides from keratan sulfate as a biomarker for morquio a syndrome. Group: Enzymes. Purity: >90%. Endo-β-galactosidase. Storage: Reconstituted protein can be stored at 4°C or in small aliquots at -20°C or below. Avoid repeated freeze-thaw cycles. Form: Powder. Source: E. coli. Species: Bacillus circulans. Endo-β-galactosidase; endo-β-galactosidase; keratan sulfate endogalactosidase; keratanase; keratan-sulfate 1,4-β-D-galactanohydrolase; Keratanase II. Cat No: NATE-1618. | |
| Keratan sulfate Endo-N-acetylglucosaminidase 111A from Bacillus circulans | BcKsh111A (GH111), E.C. number 3.2.1.-, is an endo-β -N-acetylglucosaminidase from Bacillus circulans. Recombinant BcKsh111A (GH111), purified from Escherichia coli, is a single domain family 111 Glycoside Hydrolase (GH111). Group: Enzymes. Synonyms: endo-β -N-acetylglucosaminidase; single domain family 111 Glycoside Hydrolase; Keratan sulfate Endo-N-acetylglucosaminidase 111A; Keratan sulfate Endo-N-acetylglucosaminidase; GH111. Enzyme Commission Number: EC 3.2.1.-. Purity: >90% as judged by SDS-PAGE. α-L-Arabinofuranosidase. Mole weight: 69,07 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: Bacillus circulans. endo-β -N-acetylglucosaminidase; single domain family 111 Glycoside Hydrolase; Keratan sulfate Endo-N-acetylglucosaminidase 111A; Keratan sulfate Endo-N-acetylglucosaminidase; GH111. Cat No: NATE-1940. | |
| Keratinase, Recombinant | Keratinase is a particular class of extracellular proteolytic inducible enzyme with the capability of degrading insoluble keratin substrates. It is important for hydrolyzing hair, feather, and collagen in sewage system during waste water treatment. It is also useful in food industry, animal feed preparation etc. Insoluble feather keratin from poultry industry may be converted by enzymatic hydrolysis to glues, feedstuffs, fertilizers, films or used for the production of rare amino acids serine, cysteine and proline. Applications: Keratinase was used for enzymatic treatment of elementary body (eb), gag molecules, and cells in the study of the role glycosaminoglycans (gags) in the invasion of host cells by chlamydia pneumoniae strains. Group: Enzymes. Synonyms: Keratinase; KerA; Keratinase from Bacillus licheniformis; Keratinolytic protease; EC 3.4.21. Enzyme Commission Number: EC 3.4.21. Keratinase. Mole weight: ~39 kDa. Activity: 300 - 1000 units/mg. Storage: Store at -20°C. Form: Lyophilized powder. Source: E. coli BL21. Keratinase; KerA; Keratinase from Bacillus licheniformis; Keratinolytic protease; EC 3.4.21. Cat No: NATE-0853. | |
| Lactamase (Crude Enzyme) | Penicillinase from Bacillus cereushas been shown to contain three distinct species when purified and examined for homogeneity by sedimentation analysis, amino-terminal analysis, and vertical acrylamide gel electrophoresis. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; medicine; biotechnology; pharmacology. Group: Enzymes. Synonyms: penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase. Enzyme Commission Number: EC 3.5.2.6. CAS No. 9073-60-3. β-Lactamase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase. Pack: 100ml. Cat No: NATE-1839. | |
| L-Ala-D/L-Glu epimerase | The enzyme, characterized from the bacteria Escherichia coli and Bacillus subtilis, is involved in the recycling of the murein peptide, of which L-Ala-D-Glu is a component. In vitro the enzyme from Escherichia coli epimerizes several L-Ala-L-X dipeptides with broader specificity than the enzyme from Bacillus subtilis. Group: Enzymes. Synonyms: YkfB; YcjG; AEE; AE epimerase. Enzyme Commission Number: EC 5.1.1.20. 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-5379; L-Ala-D/L-Glu epimerase; EC 5.1.1.20; YkfB; YcjG; AEE; AE epimerase. Cat No: EXWM-5379. | |
| L-alanine-L-anticapsin ligase | The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. The enzyme requires Mg2+ or Mn2+ for activity, and has a broad substrate specificity in vitro. Group: Enzymes. Synonyms: BacD; alanine-anticapsin ligase; L-Ala-L-anticapsin ligase; ywfE (gene name). Enzyme Commission Number: EC 6.3.2.49. 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-5767; L-alanine-L-anticapsin ligase; EC 6.3.2.49; BacD; alanine-anticapsin ligase; L-Ala-L-anticapsin ligase; ywfE (gene name). Cat No: EXWM-5767. | |
| L-arginine-specific L-amino acid ligase | The enzyme, characterized from the bacterium Bacillus subtilis, requires Mn2+ for activity. It shows strict substrate specificity toward L-arginine as the first (N-terminal) amino acid of the product. The second amino acid could be any standard protein-building amino acid except for L-proline. Group: Enzymes. Synonyms: RizA; L-amino acid ligase RizA. Enzyme Commission Number: EC 6.3.2.48. 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-5766; L-arginine-specific L-amino acid ligase; EC 6.3.2.48; RizA; L-amino acid ligase RizA. Cat No: EXWM-5766. | |
| L-isoleucine 4-hydroxylase | The enzyme, characterized from the bacterium Bacillus thuringiensis, can also catalyse the hydroxylation of L-leucine, L-norvaline, L-norleucine, and L-allo-isoleucine, as well as the sulfoxidation of L-methionine, L-ethionine, S-methyl-L-cysteine, S-ethyl-L-cysteine, and S-allyl-L-cysteine. Group: Enzymes. Synonyms: ido (gene name). Enzyme Commission Number: EC 1.14.11.45. 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-0664; L-isoleucine 4-hydroxylase; EC 1.14.11.45; ido (gene name). Cat No: EXWM-0664. | |
| L-Lactic Dehydrogenase from Bacillus stearothermophilus, Recombinant | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Recombinant, expressed in e. coli, lyophilized powder, > 200 units/mg protein (lowry). Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: > 200 units/mg protein (Lowry). Stability: 2-8°C. Form: lyophilized powder. Source: E. coli. Species: Bacillus stearothermophilus. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0382. | |
| lysine-8-amino-7-oxononanoate transaminase | A pyridoxal 5'-phosphate enzyme. Participates in the pathway for biotin biosynthesis. The enzyme from the bacterium Bacillus subtilis cannot use S-adenosyl-L-methionine as amino donor and catalyses an alternative reaction for the conversion of 8-amino-7-oxononanoate to 7,8-diaminononanoate (cf. EC 2.6.1.62, adenosylmethionine-8-amino-7-oxononanoate transaminase). Group: Enzymes. Synonyms: DAPA aminotransferase (ambiguous); bioA (gene name) (ambiguous); bioK (gene name). Enzyme Commission Number: EC 2.6.1.105. 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-2845; lysine-8-amino-7-oxononanoate transaminase; EC 2.6.1.105; DAPA aminotransferase (ambiguous); bioA (gene name) (ambiguous); bioK (gene name). Cat No: EXWM-2845. | |
| menaquinol oxidase (H+-transporting) | Cytochrome aa3-600, one of the principal respiratory oxidases from Bacillus subtilis, is a member of the heme-copper superfamily of oxygen reductases, and is a close homologue of the cytochrome bo3 ubiquinol oxidase from Escherichia coli, but uses menaquinol instead of ubiquinol as a substrate.The enzyme also pumps protons across the membrane bilayer, generating a proton motive force. Group: Enzymes. Synonyms: cytochrome aa3-600 oxidase; cytochrome bd oxidase; menaquinol:O2 oxidoreductase (H+-transporting). Enzyme Commission Number: EC 7.1.1.5 (Formerly EC 1.10.3.12). 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-0478; menaquinol oxidase (H+-transporting); EC 1.10.3.12; cytochrome aa3-600 oxidase; cytochrome bd oxidase; menaquinol:O2 oxidoreductase (H+-transporting). Cat No: EXWM-0478. | |
| 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 | |
| Mid-temperature Refining α-Amylase for beer | Mid-temperature a-amylase is extracted from Bacillus subtilis submerged fermentation. Be suitable for biological pharmacy, starch sugar, alcohol, beer, monosodium glutamate, fermentation industry, fruit juice, textile, paper-making and so on. Applications: Alcohol, beer. Group: Enzymes. Synonyms: Mid-temperature Refining Alpha-Amylase; for beer; beer; Alpha-Amylase; Mid-temperature Alpha-Amylase; Beer Industry Enzyme; Alpha-Amylase; Mid-temperature Refining Alpha-Amylase for beer; BER-1513. CAS No. 9000-90-2. α-Amylase. Appearance: liqud. Source: Bacillus subtilis. High-temperature Alpha-amylase; beer;High-temperature a-amylase ;a-amylase; EC 3.2.1.1; FOOD HTAA 3211; Alpha-amylase?Glycogenase; bacillus licheniformis; Beer enzyme; liquefaction; incision enzyme; paste starch; High-temperature Alpha-amylase for beer; BER-1511. Pack: 25kg/barrel or subject to client requirement. Cat No: BER-1513. | |
| Native Bacillus amyloliquefaciens α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. this product is from bacillus amyloliquefaciens and is supplied as a liquid. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. α-amylase from bacillus amy...ng sugars, which are then used for ethanol fermentation by saccharomyces cerevisiae fncc 3012. the enzyme catalyzes amylolysis of gelatinised waxy maize starch to produce reducing sugars. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Mole weight: 55 kDa. Activity: > 250 units/g. Form: liquid. Source: Bacillus amyloliquefaciens. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0741. | |
| Native Bacillus amyloliquefaciens Protease | Bacterial protease produced by submerged fermentation of a selected strain of Bacillus amyloliquefaciens. Secretion of protease by Bacillus amyloliquefaciens can be inhibited by treatment with the fatty acid synthetase inhibitor cerulenin. Bacterial protease produced by submerged fermentation of a selected strain of bacillus amyloliquefaciens. secretion of protease by bacillus amyloliquefaciens can be inhibited by treatment with the fatty acid synthetase inhibitor cerulenin. Applications: Protease from bacillus amyloliquefaciens has been used for the unhairing of hides and skins. it has also been used in a study to investigate peptide bond formation using the carbamoylmethyl ester as the acyl donor. Group: Enzymes. Synonyms: Protease; Neutrase. CAS No. 9001-92-7. Protease. Form: liquid, > 0.8 U/g. Source: Bacillus amyloliquefaciens. Protease; Neutrase. Cat No: NATE-0632. | |
| Native Bacillus cereus Phospholipase C | Phospholipase C is an enzyme with system name phosphatidylcholine cholinephosphohydrolase. This enzyme catalyses the following chemical reaction: a phosphatidylcholine + H2O<-> 1, 2-diacyl-sn-glycerol + phosphocholine. The bacterial enzyme is a zinc protein. It also acts on sphingomyelin and phosphatidylinositol. Native phospholipase c (ec 3.1.4.3) was purified from bacillus cereus. Applications: Useful for enzymatic determination of lecithin. Group: Enzymes. Synonyms: Phospholipase C; EC 3.1.4.3; lipophosphodiesterase I; Clostridium welchii alpha-toxin; Clostridium oedematiens beta-and gamma-toxins; lipophosphodiesterase C; phosphatidase C; heat-labile hemolysin; alpha-toxin. Enzyme Commission Number: EC 3.1.4.3. CAS No. 9001-86-9. Phospholipase C. Activity: > 30 U/mg. Appearance: White to brownish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus cereus. Phospholipase C; EC 3.1.4.3; lipophosphodiesterase I; Clostridium welchii alpha-toxin; Clostridium oedematiens beta-and gamma-toxins; lipophosphodiesterase C; phosphatidase C; heat-labile hemolysin; alpha-toxin. Cat No: DIA-163. | |
| Native Bacillus circulans β-Galactosidase | β-Galactosidase (EC 3.2.1.23) preparation derived from Bacillus circulans. The enzyme catalyzes the hydrolysis of lactose and the galactosyl transfer reaction. In the galactosyl transfer reaction, it is advantageous to react at high temperature because of the low solubility of lactose. Group: Enzymes. Synonyms: β-Galactosidase; beta-gal; β-gal; GLB; 9031-11-2; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Enzyme Commission Number: EC 3.2.1.23. CAS No. 9031-110-2. β-gal. Activity: > 4,000 unit/g. Appearance: Yellow-light brown, powder. Storage: store under cool and dry condition. Source: Bacillus circulans. β-Galactosidase; beta-gal; β-gal; GLB; 9031-11-2; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Pack: 5 kg, powder. Cat No: NATE-1745. | |
| Native Bacillus licheniformis Alkaline Protease | Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Subtilisin a is a member of the serine s8 endoproteinase family. it has broad specificity with a preference for a large uncharged residue in the p1 position. it hydrolyzes native and denatured proteins, and is active under alkaline conditions. Applications: The enzyme has been used to optimize release of all mitochondrial populations from homogenized ventricular tissue of rat heart.1 it has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax...ex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; triCorn proteinase; triCorn protease; EC 3.4.25.1. Enzyme Commission Number: EC 3.4.25.1. CAS No. 140879-24-9. Alkaline Protease. Mole weight: 27 Kda. Activity: 7.0-14.0 units/mg. Form: lyophilized powder. Source: Bacillus licheniformis. ingensin; macropain; multicatalytic endopeptidase complex; prosome; multicatalytic proteinase (complex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; triCorn proteinase; triCorn protease; EC 3.4.25.1. Cat No: NATE-0444. | |
| Native Bacillus licheniformis α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. this product is from bacillus licheniformis and is type xii-a. α-amylase, from creative enzymes, has been used in various plant studies, such as metabolism studies in arabidopsis. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Activity: Type XII-A, saline solution, > 500 units/mg protein (biuret); Type B, liquid. Source: Bacillus licheniformis. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0742. | |
| Native Bacillus licheniformis Keratinase (feed grade) | Keratinase is a particular class of extracellular proteolytic inducible enzyme with the capability of degrading insoluble keratin substrates. It is important for hydrolyzing hair, feather, and collagen in sewage system during waste water treatment. It is also useful in food industry, animal feed preparation etc. Insoluble feather keratin from poultry industry may be converted by enzymatic hydrolysis to glues, feedstuffs, fertilizers, films or used for the production of rare amino acids serine, cysteine and proline. Group: Enzymes. Synonyms: KerA; Keratinolytic protease; EC 3.4.21. Enzyme Commission Number: EC 3.4.21. Keratinase. Form: Powder. Source: Bacillus licheniformis. Keratinase; KerA; Keratinase from Bacillus licheniformis; Keratinolytic protease; EC 3.4.21. Cat No: FEED-0001. | |
| Native Bacillus licheniformis NADH Oxidase | NADH Oxidase from Bacillus licheniformis was shown to display hydrogen peroxide-forming activity. Nadh oxidase is a surface enzyme with increased oxidative activity in polymorphonuclear leukocytes during phagocytosis. Applications: Nadh oxidase from bacillus licheniformis has been used in a study to assess nitrogen assimilation by bacillus licheniformis growing in chemostat cultures. it has also been used in a study to investigate the role of glutamate dehydrogenase in ammonia assimilation in bacillus macerans. Group: Enzymes. Synonyms: NADH Oxidase; 9032-21-7. CAS No. 9032-21-7. NADH Oxidase. Activity: > 35 units/mg protein. Form: lyophilized powder. Source: Bacillus licheniformis. NADH Oxidase; 9032-21-7. Pack: vial of > 15 units. Cat No: NATE-0473. | |
| Native Bacillus licheniformis Proteinase | Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 kda. Applications: The enzyme from creative enzymes has been used to optimize release of all mit ochondrial populations from homogenized ventricular tissue of rat heart. it has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax-embedded liver specimens for detecting human and viral dna. this is a proteolytic enzyme isolated from th...ls to study the silencing of cardiac mit ochondrial nhe1. Group: Enzymes. Synonyms: protease; peptidase; proteinase; EC 3.4.21.62; 9014-01-1; Alkaline Protease; Protease from Bacillus licheniformis; Proteinase from Bacillus licheniformis; Subtilo peptidase A. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9001-92-7. Purity: crystallization. Proteinase. Mole weight: 27 KDa. Activity: 7.0-14.0 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Bacillus licheniformis. protease; peptidase; proteinase; EC 3.4.21.62; 9014-01-1; Alkaline Protease; Protease from Bacillus licheniformis; Proteinase from Bacillus licheniformis; Subtilo peptidase A. Cat No: NATE-0639. | |
| Native Bacillus megaterium Diaphorase (NADH) | In enzymology, a NADPH dehydrogenase is an enzyme that catalyzes In enzymology, a NAD (P)H dehydrogenase (quinone) (EC 1.6.5.2) is an enzyme that catalyzes the chemical reaction NAD (P)H + H+ + a quinone<-> NAD (P)+ + a hydroquinone. The 4 substrates of this enzyme are NADH, NADPH, H+, and quinone, whereas its 3 products are NAD+, NADP+, and hydroquinone. Native diaphorase (ec 1.6.5.2) was purified from bacillus megaterium. Applications: Useful for enzymatic determination of reduced nad. Group: Enzymes. Synonyms: EC 1.6.99.3; cytochrome c reductase; type 1 dehydrogenase; beta-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydr. Enzyme Commission Number: EC 1.6.99.3. CAS No. 9079-67-8. Diaphorase. Activity: 30-60 U/mg. Appearance: Yellow dried powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus megaterium. EC 1.6.99.3; cytochrome c reductase; type 1 dehydrogenase; beta-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine dinucleotide dehydrogenase; diphosphopyridine diaphorase; DPNH diaphorase; NADH diaphorase; NADH hydrogenase; NADH oxidoreductase; NADH-menadione oxidoreductase; reduced diphosphopyridine nucleotide diaphorase; Beta-NADH dehydrogenase dinucleotide. Cat No: DIA-142. | |
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