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| Product | Description | |
|---|---|---|
| Escherichia coli Asparaginase-polyethylene glycol | Asparaginase is an enzyme that catalyzes the hydrolysis of asparagine to aspartic acid. Asparaginases are enzymes expressed and produced by microorganisms. Asparaginase coupled to methoxy-polyethylene glycol, m.w. 5 kda, through secondary amine linkage. Group: Enzymes. Synonyms: PEG-Asparaginase; Asparaginase-polyethylene glycol. Asparaginase. Activity: ~70 units/mg protein. Storage: -20°C. Form: lyophilized powder. Contains PEG plus 5% Citrate buffer salts. Source: Escherichia coli. PEG-Asparaginase; Asparaginase-polyethylene glycol. Cat No: NATE-0538. |  |
| α-Amylase from Escherichia coli, Recombinant | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9000-90-2. Purity: > 95 % as judged by SDS-PAGE. α-Amylase. Mole weight: 60459.5 Da. Activity: 23.61 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. W3110. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-1174. | |
| α-Galactosidase, positionally specific from Escherichia coli, 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). Activity using maltose as substrate at ph 6.0 at 25 deg c is ~2x > that obtained using p-nitrophenyl-α-d-glucoside as substrate at ph 6.8 at 37 oc. protein determined by biuret. Applications: Α-glucosidase is potential enzyme for the biosynthesis of complex carbohydrates. 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. GLA. Activity: > 50 units/mg protein. Storage: 2-8°C. Form: Lyophilized powder containing potassium phosphate buffer salt. Source: E. coli. Species: Escherichia coli. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Cat No: NATE-0293. | |
| α-Glucosidase from Escherichia coli, Recombinant | Glycoside hydrolases (also called glycosidases or glycosyl hydrolases) assist in the hydrolysis of glycosidic bonds in complex sugars. They are extremely common enzymes with roles in nature including degradation of biomass such as cellulose and hemicellulose, in anti-bacterial defense strategies (e.g., lysozyme), in pathogenesis mechanisms (e.g., viral neuraminidases) and in normal cellular function (e.g., trimming mannosidases involved in N-linked glycoprotein biosynthesis). Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds. Group: Enzymes. Synonyms: Alpha-glucosidase; EC 3.2.1.20; maltase; glucoinvertase; glucosidosucra. Enzyme Commission Number: EC 3.2.1.20. CAS No. 9001-42-7. Purity: > 95 % as judged by SDS-PAGE. α-Glucosidase. Mole weight: 72992.3 Da. Activity: 34.1 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. W3110. Alpha-glucosidase; EC 3.2.1.20; maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; alpha-glucopyranosidase; glucosidoinvertase; alpha-D-glucosidase; alpha-glucoside hydrolase; alpha-1,4-glucosidase; alpha-D-glucoside glucohydrolase; glycosidases; glycosyl hydrolases; α-Glucosidase. Cat No: NATE-1177. | |
| Amylase 13A from Escherichia coli, Recombinant | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9000-90-2. Purity: >90% by SDS-PAGE. α-Amylase. Mole weight: 58.6 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: Escherichia coli. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A; Amylase 13A. Cat No: NATE-1304. | |
| Apotryptophanase from Escherichia coli | soluble powder, 75-150 units/mg solid. Group: Fluorescence/luminescence spectroscopy. |  |
| Asparaginase?polyethylene glycol from Escherichia coli | lyophilized powder, ~70 units/mg protein. Group: Fluorescence/luminescence spectroscopy. | |
| Beta-glucuronidase (Escherichia coli) | Beta-glucuronidase is an important lysosomal enzyme involved in the degradation of glucuronate-containing glycosaminoglycan [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9001-45-0. Pack Sizes: 25 KU; 50 KU; 100 KU. Product ID: HY-P2803. |  |
| Cellulase 8A from Escherichia coli, Recombinant | Cellulase is any of several enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis, the decomposition of cellulose and of some related polysaccharides; specifically, the hydrolysis of the 1,4-beta-D-glycosidic linkages in cellulose, hemicellulose, lichenin, and cereal beta-D-glucans. Cellulases break down the cellulose molecule into monosaccharides ("simple sugars") such as beta-glucose, or shorter polysaccharides and oligosaccharides. The name is also used for any naturally occurring mixture or complex of various such enzymes, that act serially or synergistically to decompose cellulosic material. Group: Enzymes. Synonyms: Cellulase, th....1.4. CAS No. 9012-54-8. Purity: >90% by SDS-PAGE. Cellulase. Mole weight: 41.5 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: E. coli. Cellulase, thermostable; 1,4-(1,3:1,4)-β-D-Glucan 4-glucano-hydrolase; EC 3.2.1.4; Cellulase; endo-1,4-β-D-glucanase; β-1,4-glucanase; β-1,4-endoglucan hydrolase; celluase A; cellulosin AP; endoglucanase D; alkali cellulase; cellulase A 3; celludextrinase; 9.5 cellulase; avicelase; pancellase SS; Cellulase 8A. Cat No: NATE-1365. | |
| Chaperonin 10 from Escherichia coli | ?95.0% (SDS-PAGE), recombinant, expressed in E. coli overproducing strain, lyophilized powder. Group: Fluorescence/luminescence spectroscopy. | |
| Chaperonin 60 from Escherichia coli | >95% (SDS-PAGE), recombinant, expressed in E. coli overproducing strain, lyophilized powder. Group: Fluorescence/luminescence spectroscopy. | |
| Endonuclease III from Escherichia coli | ?90% (SDS-PAGE), recombinant, expressed in E. coli overproducing strain, buffered aqueous glycerol solution, ?10,000 units/mg protein. Group: Fluorescence/luminescence spectroscopy. | |
| FMN Reductase from Escherichia coli (Fre), Recombinant | E.coli. Applications: Bacterial (e. coli) nad(p)h-dependent fmn-oxidoreductase is a recombinant protein of ca. 26kda overexpressed in e.coli. the sequence of cloned fre (swissprot accession number p0aen1) was confirmed by dna sequencing (100% identity). Group: Enzymes. Synonyms: NAD(P)H:flavin oxidoreduct. Enzyme Commission Number: EC 1.5.1.29. Mole weight: 26kDa. Activity: >2U/mg. Appearance: Coupling of bacterial luciferase to FMN-NAD(P)H oxidoreductase has been used to provide ultrasensitive analytical tools for thequantification of NADH and the substrates of NADH-, NADPH- dependent enzymes (e.g. glucose, lactate, malate, ethanol, sorbitol,oxaloacetate). Although FMN-reductase often present in luciferase enzyme preparations may be sufficient for producing light in the presence of NAD(P)H, highly purified and characterized Fre enzyme can offer some advantages such as an increased sensitivity,better control of the signal intensity and duration, and saving of the luciferase enzyme. Species: FMN Reductase. NAD(P)H:flavin oxidoreductase; NAD(P)H:flavin mono-nucleotide oxidoreductase; NAD(P)H(2):FMN oxidoreductase; NAD(P)H-FMN reductase; NAD(P)H-dependent FMN reductase; NAD(P)H:FMN oxidoreductase; riboflavin mononucleotide reductase; flavin mononucleotide reductase; EC 1.5.1.29. Pack: stable lyophilized form. Cat No: NATE-1744. | |
| Fpg Protein from Escherichia coli | ?90% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous glycerol solution, >20,000 units/mg protein. Group: Fluorescence/luminescence spectroscopy. | |
| Fpg Protein from Escherichia coli, Recombinant | Fpg protein, a key enzyme in the DNA base excision repair pathway (BER), catalyses the excision of a broad spectrum of modified purines such as formamidopyrimidine (Fapy) and 8-oxoguanine (8-oxo-G). Fpg possess both DNA glycosylase activity that removes the mutated base and AP-lyase activity that releases ribose, leaving both 5'-and 3'-phosphorylated ends in the DNA. Several analytical methods based on Fpg protein activity in vitro were developed for detection and quantitation of oxidative damage to DNA mainly for FapyA, FapyG and 8-oxo-G. The fpg gene was cloned by Boiteux, et al. Fpg protein possess a zinc finger motif at its C-terminus (one zinc atom per molecule). ... Protein. Mole weight: mol wt 30.2 kDa (269 amino acids, predicted from the nucleotide sequence). Activity: >20 ,000 units/mg protein. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 50 mM potassium HEPES, pH 7.5, 1 mM DTT, 1 mM EDTA, and 200 mM NaCl. Source: E. coli. Species: Escherichia coli. Fapy-DNA glycosylase; deoxyribonucleate glycosidase; 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase; 2,6-diamino-4-hydroxy-5 (N-methyl)formamidopyrimidine-DNA glycosylase; formamidopyrimidine-DNA glycosylase; DNA-formamidopyrimidine glycosidase; Fpg protein; DNA-formamidopyrimidine glycosylase; EC 3.2.2.23; 78783-53-6; | |
| ?-Galactosidase-biotin labeled from Escherichia coli | lyophilized powder, 350-1200 units/mg protein. Group: Fluorescence/luminescence spectroscopy. | |
| Glucokinase from Escherichia coli, Recombinant | Glucokinase (EC 2.7.1.2) is an enzyme that facilitates phosphorylation of glucose to glucose-6-phosphate. Glucokinase occurs in cells in the liver, pancreas, gut, and brain of humans and most other vertebrates. In each of these organs it plays an important role in the regulation of carbohydrate metabolism by acting as a glucose sensor, triggering shifts in metabolism or cell function in response to rising or falling levels of glucose, such as occur after a meal or when fasting. Mutations of the gene for this enzyme can cause unusual forms of diabetes or hypoglycemia. Group: Enzymes. Synonyms: EC 2.7.1.2; glucokinase; glucokinase (phosphorylating); 9001-36-9; GCK; FGQTL3; GK; GLK; HHF3; HK4; HKIV; HXKP; LGLK; MODY2. Enzyme Commission Number: EC 2.7.1.2. CAS No. 9001-36-9. Purity: >95% as judged by SDS-PAGE. GCK. Mole weight: 35 kDa. Activity: 5.8 U/mg protein, 98.6 U/ml. Storage: Glucokinase should be stored at 4 °C, remaining stable up to 3 years under these storage conditions. Form: 3.2 M ammonium sulphate. Source: E. coli. Species: Escherichia coli. EC 2.7.1.2; glucokinase; glucokinase (phosphorylating); 9001-36-9; GCK; FGQTL3; GK; GLK; HHF3; HK4; HKIV; HXKP; LGLK; MODY2. Cat No: NATE-1571. | |
| Glycogen branching enzyme from Escherichia coli, Recombinant | Glycogen branching enzyme is an enzyme that adds branches to the growing glycogen molecule during the synthesis of glycogen, a storage form of glucose. More specifically, during glycogen synthesis, a glucose 1-phosphate molecule reacts with uridine triphosphate (UTP) to become UDP-glucose, an activated form of glucose. The activated glucosyl unit of UDP-glucose is then transferred to the hydroxyl group at the C-4 of a terminal residue of glycogen to form an α-1,4-glycosidic linkage, a reaction catalyzed by glycogen synthase. Importantly, glycogen synthase can only catalyze the synthesis of α-1,4-glycosidic linkages. Since glycogen is a readily mobili...;-1,4-glucan-6-glycosyltransferase; starch branching enzyme; 1,4-α-D-glucan:1,4-α-D-glucan 6-α-D-(1,4-α-D-glucano)-transferase. Enzyme Commission Number: EC 2.4.1.18. CAS No. 9001-97-2. Purity: > 95 % as judged by SDS-PAGE. Glycogen branching enzyme. Mole weight: 88157.0 Da. Activity: 15.44 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. W3110. Branching enzyme, amylo-(1,4?1,6)-transglycosylase; Q-enzyme; α-glucan-branching glycosyltransferase; amylose isomerase; enzymatic branching factor; branching glycosyltransferase; enzyme Q; glucos | |
| Inactivated Escherichia coli | Suitable for DNA extraction, PCR, sequencing, next generation sequencing, >10^8 bacteria/ml. Group: Fluorescence/luminescence spectroscopy. | |
| Inorganic Pyrophosphatase from Escherichia coli, Recombinant | Pyrophosphatase (or inorganic pyrophosphatase) is an enzyme (EC 3.6.1.1) that catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. This is a highly exergonic reaction, and therefore can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The functionality of this enzyme plays a critical role in lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, and DNA synthesis,as well as other biochemical transformations. Applications: Inorganic pyrophosphatase (ppase) is a ubiquitous enzyme catalyzing the reaction ppi + h2o ? 2pi. it plays an important role in protein, rna, and dna synthesis. Group: Enzymes. Synonyms: Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Enzyme Commission Number: EC 3.6.1.1. CAS No. 9024-82-2. Purity: > 90%. Inorganic pyrophosphatase. Activity: > 800 units/mg protein. Storage: -20°C. Form: Lyophilized powder in Tris-buffered salts containing protease inhibitors. Source: E. coli. Species: Escherichia coli. Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-0355. | |
| Isoamylase from Escherichia coli, Recombinant | Isoamylase is an enzyme with system name glycogen 6-alpha-D-glucanohydrolase. This enzyme catalyses the following chemical reaction:Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins. This enzyme also readily hydrolyses amylopectin. Group: Enzymes. Synonyms: EC 3.2.1.68; debranching enzyme; glycogen alpha-1,6-glucanohydrolase; isoamylase. Enzyme Commission Number: EC 3.2.1.68. CAS No. 9067-73-6. Purity: > 95 % as judged by SDS-PAGE. Isoamylase. Mole weight: 77396.8 Da. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. W3110. EC 3.2.1.68; debranching enzyme; glycogen alpha-1,6-glucanohydrolase; isoamylase. Cat No: NATE-1212. | |
| Laccase from Escherichia coli, Recombinant | Laccase is a blue copper oxidase that reduces molecular oxygen to water. Laccase oxidizes polyphenols, methoxy-substituted phenols and diamines, but not tyrosine. Oxidation by laccase is an one-electron reaction that generates a free radical. Group: Enzymes. Synonyms: Laccases; EC 1.10.3.2; 80498-15-3; urishiol oxidase; urushiol oxidase; p-diphenol oxidase; benzenediol:oxygen oxidoreductase. Enzyme Commission Number: EC 1.10.3.-. Purity: >90% as judged by SDS-PAGE. Laccase. Mole weight: 55.4 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: Escherichia coli. Laccases; EC 1.10.3.2; 80498-15-3; urishiol oxidase; urushiol oxidase; p-diphenol oxidase; benzenediol:oxygen oxidoreductase. Cat No: NATE-1569. | |
| Lactaldehyde dehydrogenase from Escherichia coli, Recombinant | In enzymology, a lactaldehyde dehydrogenase (EC 1.2.1.22) is an enzyme that catalyzes the chemical reaction: (S)-lactaldehyde + NAD+ + H2O <-> (S)-lactate + NADH + 2 H+. The 3 substrates of this enzyme are (S)-lactaldehyde, NAD+, and H2O, whereas its 3 products are (S)-lactate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. Group: Enzymes. Synonyms: E.C. 1.2.1.22; lactaldehyde dehydrogenase; L-lactaldehyde:NAD oxidoreductase; nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase; (S)-lactaldehyde:NAD+ oxidoreductase. Enzyme Commission Number: EC 1.2.1.22. CAS No. 37250-90-1. Lactaldehyde dehydrogenase. Mole weight: 53337.9 Da. Source: Escherichia coli. E.C. 1.2.1.22; lactaldehyde dehydrogenase; L-lactaldehyde:NAD oxidoreductase; nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase; (S)-lactaldehyde:NAD+ oxidoreductase. Cat No: NATE-1213. | |
| Lipid A, monophosphoryl from Escherichia coli F583 (Rd mutant) | lyophilized powder. Group: Fluorescence/luminescence spectroscopy. | |
| Lipopolysaccharides from Escherichia coli | Lipopolysaccharides produced by Escherichia coli are endotoxins. Synonyms: Lipopolysaccharide E. Coli; Escherichia coli lipopolysaccharides; Lipopolysaccharides, Escherichiacoli; Citopyros; Escherichia coli lipopolysaccharide; Lipopolysaccharide, Escherichia coli; Lipopolysaccharides, Escherichia coli. CAS No. 93572-42-0. |  |
| Lipopolysaccharides from Escherichia coli K-235 | Lipopolysaccharides from Escherichia coli K-235. Group: Polysaccharide. |  |
| Lipopolysaccharides from Escherichia coli O111:B4 | Lipopolysaccharides from Escherichia coli O111:B4. Group: Polysaccharide. | |
| Lipopolysaccharides from Escherichia coli O111:B4 | Ready Made solution, 1 mg/mL, 0.2 ?m filtered. Group: Fluorescence/luminescence spectroscopy. | |
| Lipopolysaccharides from Escherichia coli O127:B8 | Lipopolysaccharides from Escherichia coli O127:B8. Group: Polysaccharide. | |
| Lipopolysaccharides from Escherichia coli O127:B8 | Ready Made solution, 1 mg/mL, 0.2 ?m filtered. Group: Polysaccharide. | |
| Lipopolysaccharides from Escherichia coli O128:B12 | Lipopolysaccharides from Escherichia coli O128:B12. Group: Polysaccharide. | |
| Lipopolysaccharides from Escherichia coli O26:B6 | Lipopolysaccharides from Escherichia coli O26:B6. Group: Polysaccharide. | |
| Lipopolysaccharides from Escherichia coli O26:B6 | Ready Made solution, 1 mg/mL, 0.2 ?m filtered. Group: Polysaccharide. | |
| Lipopolysaccharides from Escherichia coli O55:B5 | Lipopolysaccharides from Escherichia coli O55:B5. Group: Polysaccharide. | |
| Lipopolysaccharides from Escherichia coli O55:B5 | Ready Made solution, 1 mg/mL, 0.2 ?m filtered. Group: Polysaccharide. | |
| Lipopolysaccharides (rough strains) from Escherichia coli EH100 (Ra mutant) | Lipopolysaccharides (rough strains) from Escherichia coli EH100 (Ra mutant). Group: Polysaccharide. | |
| Lipopolysaccharides (rough strains) from Escherichia coli F583 (Rd mutant) | Lipopolysaccharides (rough strains) from Escherichia coli F583 (Rd mutant). Group: Polysaccharide. | |
| Lipopolysaccharides (rough strains) - from Escherichia coli J5 (Rc mutant) | | |
| Lipopolysaccharides (rough strains) from Escherichia coli J5 (Rc mutant) | Lipopolysaccharides (rough strains) from Escherichia coli J5 (Rc mutant). Group: Polysaccharide. | |
| Microbial DNA standard from Escherichia coli | Suitable for PCR, sequencing and NGS, 10 ng/?L. Group: Fluorescence/luminescence spectroscopy. | |
| N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli, Recombinant | In enzymology, a N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) is an enzyme that catalyzes the chemical reaction: N-acetyl-D-glucosamine 6-phosphate + H2O ? D-glucosamine 6-phosphate + acetate. Thus, the two substrates of this enzyme are N-acetyl-D-glucosamine 6-phosphate and H2O, whereas its two products are D-glucosamine 6-phosphate and acetate. Group: Enzymes. Synonyms: N-acetyl-D-glucosamine-6-phosphate amidohydrolase; acetylglucosamine phosphate deacetylase; acetylaminodeoxyglucosephosphate acetylhydrolase; 2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase; EC 3.5.1.25. Enzyme Commission Number: EC 3.5.1.25. CAS No. 9027-50-3. Purity: >90% as judged by SDS-PAGE. N-acetylglucosamine 6-phosphate deacetylase. Mole weight: 43.0 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: Escherichia coli. N-acetyl-D-glucosamine-6-phosphate amidohydrolase; acetylglucosamine phosphate deacetylase; acetylaminodeoxyglucosephosphate acetylhydrolase; 2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase; EC 3.5.1.25. Cat No: NATE-1540. | |
| Native Escherichia coli Acetate Kinase | In molecular biology, acetate kinase (EC 2.7.2.1), which is predominantly found in micro-organisms, facilitates the production of acetyl-CoA by phosphorylating acetate in the presence of ATP and a divalent cation. Short-chain fatty acids (SCFAs) play a major role in carbon cycle and can be utilized as a source of carbon and energy by bacteria. The enzyme is important in the process of glycolysis, enzyme levels being increased in the presence of excess glucose. The growth of a bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme is involved in excretion of excess carbohydRate. A related enzyme, butyRate kinase, facili...rom escherichia coli has been used as part of an atp-regenerating system to study the kinetics of agonist-stimulated transphosphatidylatio. Group: Enzymes. Synonyms: Acetate kinase (phosphorylating); Acetic kinase; Acetokinase; AK; EC 2.7.2.1; 9027-42-3; Acetate kinase. Enzyme Commission Number: EC 2.7.2.1. CAS No. 9027-42-3. Acetate kinase. Activity: > 150 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized powder containing trehalose with small amounts of potassium phosphate, magnesium chloride, and dithiothreitol. Source: Escherichia coli. Acetate kinase (phosphorylating); Acetic kinase; Acetokinase; AK; EC 2.7.2.1; 9027-42-3; Acetate kinase. Cat No: NATE-0017. | |
| Native Escherichia coli Alkaline Phosphatase | Alkaline phosphatase (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Applications: Alkaline phosphatase is used for conjugation to antibodies and other proteins for elisa, western blotting, and hist ochemical detection. it may be used for protein labeling when high sensitivity is required. Group: Enzymes. Synonyms: Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Enzyme Commission Number: EC 3.1.3.1. CAS No. 9001-78-9. ALP. Activity: Type I, >30 units per mg protein; Type II, >20 units per mg protein; Type III, >10 units per mg protein. Storage: 2-8°C. Form: A suspension in 2.6M ammonium sulfate, pH 8.0. Source: Escherichia coli. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Cat No: NATE-0056. | |
| Native Escherichia coli Apotryptophanase | Apotryptophanase hydrolizes tryptophan and is capable of catalyzing α,β-elimination reactions with a number of substituted amino acids, including S-methyl-, S-ethyl-and S-benzyl-L-cysteine. DTNB inactivates tryptophanase. Applications: Apotryptophanase is used for the quantitative determination of pyridoxal-phosphate. apotryptophanase, from creative enzymes, has been used to study pregnancy-associated plp deficiency and vitamin b-6 deficiency. Group: Enzymes. Synonyms: L-tryptophanase; L-tryptophan indole-lyase (deaminating); TNase; EC 4.1.99.1; 9024-00-4. Enzyme Commission Number: EC 4.1.99.1. CAS No. 9024-00-4. TNase. Activity: 75-150 units/mg solid. Storage: -20°C. Form: soluble powder. Source: Escherichia coli. L-tryptophanase; L-tryptophan indole-lyase (deaminating); TNase; EC 4.1.99.1; 9024-00-4. Cat No: NATE-0706. | |
| Native Escherichia coli Asparaginase | Asparaginase (EC 3.5.1.1, USAN) or Colaspase (BAN) is an enzyme that catalyzes the hydrolysis of asparagine to aspartic acid. Asparaginases are enzymes expressed and produced by microorganisms. Applications: Asparaginase is used in enzymatic assays and to convert asparagine to aspartic acid. asparaginase is used to reduce the formation of acrylamide in starchy food products. it is also used as a chemotherapy agent for acute lymphoblastic leukemia. product is from escherichia coli and is provided as a lyophilized powder containing sodium chloride. Group: Enzymes. Synonyms: EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Enzyme Commission Number: EC 3.5.1.1. CAS No. 9015-68-3. Asparaginase. Storage: 2-8°C. Form: lyophilized powder. Source: Escherichia coli. EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Cat No: PHAM-226. | |
| Native Escherichia coli β-Galactosidase | β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Applications: This enzyme is useful for structural investigation of carbohydrates, the determination of lactose (foodstuff analysis) and as an enzyme label for enzyme immunoassay. Group: Enzymes. Synonyms: β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.23. CAS No. 9031-11-2. β-gal. Mole weight: 540 kDa. Activity: Grade? 500U/mg-solid or more. Stability: Stable at-20°C for at least 6 months. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Escherichia coli. β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. Cat No: DIA-189. | |
| Native Escherichia coli β-Galactosidase-biotin labeled | β-galactosidase is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Applications: Β-galactosidase was used as a control antigen in the selection of human antibody fragments by phage display. Group: Enzymes. Synonyms: β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. β-gal. Activity: 350-1200 units/mg protein. Form: Lyophilized powder containing Tris-acetate, DTT, MgCl2, and isopropyl β-D-thiogalactopyranoside. Source: E. coli. β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase; β-Galactosidase-biotin labeled; biotin β-gal. Cat No: NATE-1585. | |
| Native Escherichia coli β-Glucuronidase | β-glucuronidase catalyzes the breakdown of complex carbohydrates. In humans it converts conjugated bilirubin into the unconjugated form, making bilirubin suitable for reabsorption. Type ix-a, 1,000-5,000 units/mg protein; type vii-a, lyophilized powder, 5,000-20,000 units/mg protein. Applications: Β-glucuronidase is used as a reporter gene in gus assays to monitor gene expression. Group: Enzymes. Synonyms: β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase; EC 3.2.1.31; 9001-45-0; β-D-glucuronoside glucuronosohydrolase; GUSB. Enzyme Commission Number: EC 3.2.1.31. CAS No. 9001-45-0. GUSB. Form: lyophilized powder. Source: Escherichia coli. β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase; EC 3.2.1.31; 9001-45-0; β-D-glucuronoside glucuronosohydrolase; GUSB. Cat No: NATE-0330. | |
| Native Escherichia coli Chloramphenicol Acetyltransferase | Chloramphenicol acetyltransferase (or CAT) is a bacterial enzyme (EC 2.3.1.28) that detoxifies the antibiotic chloramphenicol and is responsible for chloramphenicol resistance in bacteria. This enzyme covalently attaches an acetyl group from acetyl-CoA to chloramphenicol, which prevents chloramphenicol from binding to ribosomes. A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism. Applications: Chloramphenicol acetyltransferase from escherichia coli has been used in a study to assess the construction of a novel expression system in klebsiella pneumoniae and its application for 1,3-propanediol produ...etyl-CoA:chloramphenicol 3-O-acetyltransferase; CAT; 9040-07-7; chloramphenicol acetyltransferase; chloramphenicol acetylase; chloramphenicol transacetylase; CAT I; CAT II; CAT III. CAS No. 9040-7-7. Chloramphenicol Acetyltransferase. Mole weight: mol wt 75 kDa (three identical subunits). Activity: 50,000-150,000 units/mg protein (Lowry). Storage: -20°C. Form: Type I, lyophilized powder. Partially purified; contains Tris buffer salts; Type II, buffered aqueous glycerol solution. Clear, colorless solution in 50% glycerol containing 5 mM Tris-HCl, pH 7.8, and 0.5 mM 2-mercaptoethanol. Source: Escherichia coli. Acetyl-CoA:chloramphenicol 3-O-acetyltransferase; CAT; 9 | |
| Native Escherichia coli Diacylglycerol Kinase | Diacylglycerol kinase (DGK or DAGK) is a family of enzymes that catalyzes the conversion of diacylglycerol (DAG) to phosphatidic acid (PA) utilizing ATP as a source of the phosphate. In non-stimulated cells, DGK activity is low allowing DAG to be used for glycerophospholipid biosynthesis but on receptor activation of the phosphoinositide pathway, DGK activity increases driving the conversion of DAG to PA. As both lipids are thought to function as bioactive lipid signaling molecules with distinct cellular targets, DGK therefore occupies an important position, effectively serving as a switch by terminating the signalling of one lipid while simultaneously activating signa...n of dgka and plsb genes of phospholipid synthesis by multiple stress responses in escherichia coli. diacylglycerol kinase from escherichia coli has also been used in a study to identify an alcohol binding site in the first cysteine-rich domain of protein kinase cdelta. Group: Enzymes. Synonyms: Diacylglycerol Kinase; DGK; DAGK; EC 2.7.1.107; Diacylglycerol kinase (ATP); sn-1,2-Diacylglycerol kinase. Enzyme Commission Number: EC 2.7.1.107. CAS No. 60382-71-0. DAGK. Mole weight: mol wt 13.7 kDa. Stability: -70°C. Form: suspension. Source: E. coli. Diacylglycerol Kinase; DGK; DAGK; EC 2.7.1.107; Diacylglycerol kinase (ATP); sn-1,2-Diacylglycerol kinase. Cat No: NATE-0181. | |
| Native Escherichia coli Glutaminase | Glutaminase catalyzes the conversion of glutamine to glutamate. Glutaminase is an amidohydrolase enzyme that generates glutamate from glutamine. Glutaminase has tissue-specific isoenzymes. Glutaminase has an important role in glial cells. Glutaminase catalyzes the following reaction:Glutamine + H2O ? Glutamate + NH3. Group: Enzymes. Synonyms: EC 3.5.1.2; glutaminase I; L-glutaminase; glutamine aminohydrolase; Glutaminase; 9001-47-2. Enzyme Commission Number: EC 3.5.1.2. CAS No. 9001-47-2. Glutaminase. Activity: Type I, 500-1,500 units/mg protein; Type II, 50-200 units/mg protein. Storage: -20°C. Form: Type I, Lyophilized powder containing stabilizer and potassium succinate; Type II, Lyophilized powder containing potassium succinate and EDTA. Source: Escherichia coli. EC 3.5.1.2; glutaminase I; L-glutaminase; glutamine aminohydrolase; Glutaminase; 9001-47-2. Cat No: NATE-0307. | |
| Native Escherichia coli Glycerokinase | Glycerol kinase is a phosphotransferase enzyme involved in triglycerides and glycerophospholipids synthesis. Glycerol kinase catalyzes tge MgATP-dependent phosphorylation of glycerol to produce sn-glycerol-3-phosphate and is the rate limiting enzyme in the utilization of glycerol. It is also subject to feedback regulation by fructose-1,6-bisphosphate. Applications: Glycerol kinase (glpk) was used to study the effects of pain controlling neuropeptides on human fat cell lipolysis. Group: Enzymes. Synonyms: EC 2.7.1.30; glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase; 9030-66-4. Enzyme Commission Number: EC 2.7.1.30. CAS No. 9030-66-4. GK. Activity: Type I, 50-100 units/mg protein; Type II, 300-600 units/mL. Storage: -20°C. Form: Type I, lyophilized powder, Partially purified lyophilized powder, balance is primarily salts and EDTA; Type II, ammonium sulfate suspension, Suspension in 3.1 M (NH4)2SO4 pH 7.3, with 1% BSA and 2% trehalose. Source: Escherichia coli. EC 2.7.1.30; glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase; 9030-66-4. Cat No: NATE-0288. | |
| Native Escherichia coli L-Arginine Decarboxylase | In enzymology, an arginine decarboxylase (EC 4.1.1.19) is an enzyme that catalyzes the chemical reaction:L-arginine<-> agmatine + CO2. Hence, this enzyme has one substRate, L-arginine, and two products, agmatine and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. It employs one cofactor, pyridoxal phosphate. Group: Enzymes. Synonyms: arginine decarboxylase; EC 4.1.1.19; 9024-77-5; SpeA; L-arginine carboxylyase; L-Arginine Decarboxylase; ADC. Enzyme Commission Number: EC 4.1.1.19. CAS No. 9024-77-5. ADC. Activity: 5-15 units/mg protein. Storage: -20°C. Source: Escherichia coli. arginine decarboxylase; EC 4.1.1.19; 9024-77-5; SpeA; L-arginine carboxylyase; L-Arginine Decarboxylase; ADC. Cat No: NATE-0033. | |
| Native Escherichia coli L-Glutamine Synthetase | Glutamine synthetase (GS) (EC 6.3.1.2) is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine:Glutamate + ATP + NH3 ? Glutamine + ADP + phosphate. Glutamine Synthetase uses ammonia produced by Nitrate reduction, amino acid degradation, and photorespiration. The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites. Applications: L-glutamine synthetase may be used for the purification of proteases from escherichia coli. Group: Enzymes. Synonyms: glutamine synthetase; glutamylhydroxamic synthetase; L-glutamine synthetase; glutamate-ammonia ligase; L-Glutamate:ammonia ligase (ADP-forming); EC 6.3.1.2; GS; 9023-70-5. Enzyme Commission Number: EC 6.3.1.2. CAS No. 9023-70-5. Purity: affinity chromatography. GS. Activity: 400-2,000 units/mg protein. Storage: -20°C. Form: lyophilized powder; Contains potassium phosphate, sodium Citrate and magnesium acetate buffer salts. Source: Escherichia coli. glutamine synthetase; glutamylhydroxamic synthetase; L-glutamine synthetase; glutamate-ammonia ligase; L-Glutamate:ammonia ligase (ADP-forming); EC 6.3.1.2; GS; 9023-70-5. Cat No: NATE-0321. | |
| Native Escherichia coli N-Acetylneuraminic Acid Aldolase | In enzymology, a N-acetylneuraminate lyase (EC 4.1.3.3) is an enzyme that catalyzes the chemical reaction:N-acetylneuraminate<-> N-acetyl-D-mannosamine + pyruvate. Hence, this enzyme has one substrate, N-acetylneuraminate, and two products, N-acetyl-D-mannosamine and pyruvate. This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. This enzyme participates in aminosugars metabolism. Applications: This enzyme is useful for enzymatic determination of n-acetylneuraminic acid and sialic acid when coupled with the related enzymes in clinical analysis. for industrial use, this enzyme is useful for enzymatic synthe...o. 9027-60-5. NALase. Mole weight: mol wt ~98 kDa. Activity: > 20 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salt. Source: Escherichia coli. N-acetylneuraminic acid aldolase; acetylneuraminate lyase; sialic aldolase; sialic acid aldolase; sialate lyase; N-acetylneuraminic aldolase; neuraminic aldolase; N-acetylneuraminate aldolase; neuraminic acid aldolase; N-acetylneuraminic acid aldolase; neuraminate aldolase; N-acetylneuraminic lyase; N-acetylneuraminic acid lyase; NPL; NALase; NANA lyase; acetylneuraminate pyruvate-lyase; N-acetylneuraminate pyruvate-lyase; 9027-60-5; EC 4.1.3.3. Cat No: NATE-0490. | |
| Native Escherichia coli Nitrate Reductase (cytochrome) | Nitrate reductase (cytochrome) is an enzyme with system name ferrocytochrome:nitrate oxidoreductase. This enzyme catalises the following chemical reaction:2 ferrocytochrome + 2 H+ + nitrate<-> 2 ferricytochrome + nitrite. Group: Enzymes. Synonyms: Nitrate reductase (cytochrome); respiratory Nitrate reductase; benzyl viologen-Nitrate reductase; EC 1.9.6.1; 9029-42-9. Enzyme Commission Number: EC 1.9.6.1. CAS No. 9029-42-9. Nitrate reductase. Activity: > 5 units/g solid. Storage: -20°C. Form: lyophilized powder. Source: Escherichia coli. Nitrate reductase (cytochrome); respiratory Nitrate reductase; benzyl viologen-Nitrate reductase; EC 1.9.6.1; 9029-42-9. Cat No: NATE-0485. | |
| Native Escherichia coli Penicillin Amidase | The biosynthesis of Penicillin amidase in E. coli by hydrophobic protein chromatography is an inducible reaction which is regulated by metabolized carbon source (e.g. polyols, carboxylic acid etc.). It is also influenced by catabolite repression. It catalyzes the formation of amide bonds through an acyl-enzyme intermediate. Penicillin amidase is a periplasmic 80k heterodimer with a and b chains (209 and 566 amino acids, respectively). it is widely distributed among microorganisms, including bacteria, yeast and filamentous fungi. among all the sources, the enzyme produced by e. coli is most well-characterized and common for industrial application. Applications: Penicillin...; benzylpenicillin acylase; novozym 217; semacylase; α-acylamino-β-lactam acylhydrolase; ampicillin acylase; EC 3.5.1.11; 9014-06-6. Enzyme Commission Number: EC 3.5.1.11. CAS No. 9014-6-6. Penicillin Amidase. Mole weight: Mr ~70 kDa. Activity: Type I, 5-10 units/mg protein; Type II, > 10 units/mg protein (E1%/280). Storage: 2-8°C. Form: Type II, ammonium sulfate suspension, Suspension in 0.1 M phosphate, pH 7.5 and 3 M ammonium sulfate. Source: Escherichia coli. penicillin amidase; penicillin acylase; benzylpenicillin acylase; novozym 217; semacylase; α-acylamino-β-lactam acylhydrolase; ampicillin acylase; EC 3.5.1.11; 9014-06-6. Cat No: NATE-0541. | |
| Native Escherichia coli Superoxide Dismutase | Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice by preventing the conversion of NO to peroxynitrate, an inducer of apoptosis. Superoxide dismutases are a group of low molecular weight metalloproteins present in all aerobic cells of plants, animals...5.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuperoxide dismutase; superoxide dismutase I; superoxide dismutase II; SOD; Cu,Zn-SOD; Mn-SOD; Fe-SOD; SODF; SODS; SOD-1; SOD-2; SOD-3; SOD-4; hemocuprein; erythrocuprein; cytocuprein; cuprein ; hepatocuprein; 9054-89-1. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Mole weight: mol wt 32.5 kDa. Activity: > 1 ,000 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Escherichia coli. Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuper | |
| Native Escherichia coli Thioredoxin Reductase | Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide. Applications: Thioredoxin reductase from escherichia coli can be used in peroxidase-coupled thioredoxin system assay for assessing the peroxidase activitiy of cys-based thiol peroxidases. the product was used for determining the enzymatic activity of his6-ahp1p. Group: Enzymes. Synonyms: NADP-thioredoxi. Enzyme Commission Number: EC 1.8.1.9. CAS No. 9074-14-0. TrxR. Activity: >25 units/mg protein (Bradford). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4 containing 30 mM potassium phosphate buffer, pH 7.5, and 2 mM EDTA. Source: Escherichia coli. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR. Cat No: NATE-0718. | |
| Native Streptolysin O from Escherichia coli | Streptolysin O possesses a single polypeptide chain with a molecular weight of f62 kDa. Streptolysin O binds to membrane cholesterol and oligomerizes to create a ring structure that consists of 45 to 50 units. The ring structure inserts into the membrane to make a large pore (25 to 30 nm), which DNA, RNA, peptides and proteins may pass. It is thiol-activated. It is inhibited by allicin, an active component of garlic. Streptolysin-o is one of several toxic immunogenic exoenzymes produced by most strains of group a and many strains of groups c and g, β-hemolytic streptococci. the o in the name stands for oxygenlabile; the other related toxin being oxygen-stable streptolysin-s. the main function of streptolysin o is to cause hemolysis (the breaking open of red blood cells) in particular, beta-hemolysis. Applications: Used in the formulation of anti-streptolysin o (aso) assays which are used in the diagnosis of group a streptococcal based illnesses. Group: Enzymes. Synonyms: Streptolysin O; 98072-47-0; SLO. Enzyme Commission Number: EC.3.2.2.5. CAS No. 9032-65-9. Purity: > 90%. SLO. Appearance: Clear to slightly cloudy solution. Source: Escherichia coli. Streptolysin O; 98072-47-0; SLO. Cat No: NATE-1161. | |
| Native T4-infected Escherichia coli Polynucleotide Kinase | Polynucleotide kinase catalyses a "forward reaction" transfer of the γ-phosphate of ATP to the 5' hydroxyl terminus of single-and double-stranded nucleic acids (DNA and RNA) and 3'-nucleoside monophosphates. In exchange reactions containing ADP, the enzyme will catalyze the exchange of 5'-terminal phosphate groups and ATP. The 3'-phosphatase activity enables the enzyme to remove 3'-phosphoryl groups from phosphorylpolynucleotides. Applications: Suitable for: o sequencing or nucleic acid tagging (dna and rna) by 5?-end labeling o 5? phosphorylation of oligonucleotides o removal of 3?-phosphate groups from phosphorylpolynucleotides. Group: Enzymes. Synonyms: polynucleotide 5'-hydroxyl-kinase; EC 2.7.1.78; 37211-65-7; ATP:5'-dephosphopolynu. Enzyme Commission Number: EC 2.7.1.78. CAS No. 37211-65-7. PNK. Mole weight: mol wt 33 kDa. Activity: 10 units/μL. Storage: -20°C. Form: buffered aqueous glycerol solution. Source: T4-infected Escherichia coli. polynucleotide 5'-hydroxyl-kinase; EC 2.7.1.78; 37211-65-7; ATP:5'-dephosphopolynucleotide 5'-phosphatase; PNK; polynucleotide 5'-hydroxyl kinase (phosphorylating); 5'-hydroxyl polynucleotide kinase; 5'-hydroxyl polyribonucleotide kinase; 5'-hydroxyl RNA kinase; DNA 5'-hydroxyl kinase; DNA kinase; polynucleotide kinase; polynucleotide 5'-hydroxy-kinase. Cat No: NATE-0605. | |
| Nitroreductase from Escherichia coli | ?90% (SDS-PAGE), recombinant, expressed in E. coli. Group: Fluorescence/luminescence spectroscopy. | |
| Nitroreductase from Escherichia coli, Recombinant | Nitroreductase increases the sensitivity of organisms to nitro-containing drugs such as metronidazole by converting the nitro group to a cytotoxic nitro radical. Shows ability to reduce quinines. Enzyme for activating prodrugs in antibody directed enzyme prodrug therapy. Applications: Nitroreductase has been used in a study that used a set of pcr primers to clone a gene encoding a hypothetical nitroreductases (named as ssap-ntrb) from uropathogenic staphyl oc occus. it has also been used to improve prodrug activation. nitroreductase from escherichia coli has been used in a study to assess anaerobic bacteria as a gene delivery system for cancer treatment. it has also been used in a study to investigate its applications in antibody-directed enzyme prodrug therapy. Group: Enzymes. Synonyms: Nitroreductase. Purity: > 90% (SDS-PAGE). Nitroreductase. Mole weight: monomer mol wt 24 kDa. Storage: -20°C. Source: E. coli. Species: Escherichia coli. Nitroreductase. Cat No: NATE-0488. | |
| Penicillin Amidase from Escherichia coli | 5-10 units/mg protein. Group: Fluorescence/luminescence spectroscopy. | |
| Phosphatase from Escherichia coli, Recombinant | A phosphatase is an enzyme that removes a phosphate group from its substrate by hydrolysing phosphoric acid monoesters into a phosphate ion and a molecule with a free hydroxyl group (see dephosphorylation). This action is directly opposite to that of phosphorylases and kinases, which attach phosphate groups to their substrates by using energetic molecules like ATP. A common phosphatase in many organisms is alkaline phosphatase. Another large group of proteins present in archaea, bacteria, and eukaryote exhibits deoxyribonucleotide and ribonucleotide phosphatase or pyrophosphatase activities that catalyse the decomposition of dNTP/NTP into dNDP/NDP and a free phosphate ... phosphatase is collectively called as protein phosphatase, which removes a phosphate group from the phosphorylated amino acid residue of the substrate protein. Protein phosphorylation is a common posttranslational modification of protein catalyzed by protein kinases, and protein phosphatases reverse the effect. Group: Enzymes. Synonyms: HAD2. Enzyme Commission Number: EC 3.1.3.-. Purity: >95 % as judged by SDS-PAGE. Phosphatase. Mole weight: 26827.7 Da. Activity: 1.905 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. MG1655. Phosphatase; HAD2; EC 3.1.3.-. Cat No: NATE-1226. | |
| Phospho-β-Glucosidase 1A from Escherichia coli, Recombinant | In enzymology, a 6-phospho-beta-glucosidase (EC 3.2.1.86) is an enzyme that catalyzes the chemical reaction: 6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H2O ? D-glucose + D-glucose 6-phosphate. Thus, the two substrates of this enzyme are 6-phospho-beta-D-glucosyl-(1,4)-D-glucose and H2O, whereas its two products are D-glucose and D-glucose 6-phosphate. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. Group: Enzymes. Synonyms: 6-phospho-beta-D-glucosyl-(1,4)-D-glucose glucohydrolase; phospho-beta-glucosidase A; phospho-beta-glucosidase; phosphocellobiase; 6-phospho-beta-glucosidase; EC 3.2.1.86; Phospho-β-Gluco. Enzyme Commission Number: EC 3.2.1.86. CAS No. 37205-51-9. Purity: >90% by SDS-PAGE. Phospho-β-Glucosidase. Mole weight: 57.1 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: Escherichia coli. 6-phospho-beta-D-glucosyl-(1,4)-D-glucose glucohydrolase; phospho-beta-glucosidase A; phospho-beta-glucosidase; phosphocellobiase; 6-phospho-beta-glucosidase; EC 3.2.1.86; Phospho-β-Glucosidase; Phospho-β-Glucosidase 1A. Cat No: NATE-1444. | |
| Phosphomannose Isomerase from Escherichia coli | recombinant, expressed in E. coli, ammonium sulfate suspension, ?50 units/mg protein. Group: Fluorescence/luminescence spectroscopy. | |
| Phosphomannose Isomerase from Escherichia coli, Recombinant | Phosphomannose Isomerase (PMI) catalyses the interconversion of mannose 6-phosphate (Man-6-P) and fructose 6-phosphate (Fru-6-P), which provides a link between glucose metabolism and mannosylation. Applications: Pmi is used to study cell wall synthesis and energy production. pmi has been used to study how edta and metal ions, such as zn++, co++, fe++, mn++ and cu++., can affect recovery and thermal stability. it may be used to study pmi?s effect on various alginate biosynthetic enzymes such as phosphomannomutase (pmm), gdp-mannose pyrophosphorylase (gmp), and gdp-mannose dehydrogenase (gmd). Group: Enzymes. Synonyms: phosphomannose isomerase; phosphohexomutase; phosphohexoisomerase; mannose phosphate isomerase; phosphomannoisomerase; D-mannose-6-phosphate ketol-isomerase; EC 5.3.1.8; mannos. Enzyme Commission Number: EC 5.3.1.8. CAS No. 9023-88-5. PMI. Activity: > 50 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension; Supplied as a suspension in 3.2 M ammonium sulfate. Source: E. coli. Species: Escherichia coli. phosphomannose isomerase; phosphohexomutase; phosphohexoisomerase; mannose phosphate isomerase; phosphomannoisomerase; D-mannose-6-phosphate ketol-isomerase; EC 5.3.1.8; mannose-6-phosphate isomerase; PMI. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0599. | |
| Polynucleotide Phosphorylase from Escherichia coli, Recombinant | Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity. It is also involved in mRNA processing and degradation in bacteria, plants, and humans. Applications: Polynucleotide phosphorylase (pnp) has been used in a study to show that spontaneous mutations resulting from replication errors are reduced in a pnp-deficient strain. it has also been used in a study to show that the absence of pnpase makes e. coli cells sensitive to uv, which suggests pnp has a role in survival of uv damage. Group: Enzymes. Synonyms: PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Enzyme Commission Number: EC 2.7.7.8. CAS No. 9014-12-4. Polynucleotide phosphorylase. Storage: -70°C. Form: Supplied as a solution in 20 mM Hepes buffer pH 7.9, 0.1 mM EDTA, 2 mM DTT, 12.5 mM MgCl2, 200 mM KCl, 21.4% (w/v) Glycerol. Source: E. coli. Species: Escherichia coli. PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Cat No: NATE-0608. | |
| Pyrophosphatase, Inorganic from Escherichia coli | recombinant, expressed in E. coli, lyophilized powder, ?90%, ?800 units/mg protein. Group: Fluorescence/luminescence spectroscopy. | |
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