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| Product | Description | |
|---|---|---|
| Homopiperazine-N,N-bis-[2-(ethanesulfonic acid)] | Used in the immunoassay studies. Pretreatment reagents and methods, and application to assays for immunosuppressant drugs. Buffered, phosphate-containing media suitable for aluminum toxicity studies. Group: Biochemicals. Alternative Names: Tetrahydro-1H-1,4-diazepine-1,4(5H)-diethanesulfonic Acid Disodium Salt; Homo-PIPES. CAS No. 202185-84-0. Pack Sizes: 25g. Molecular Formula: C?H??N?Na?O?S?, Molecular Weight: 316.39. US Biological Life Sciences. |  Worldwide |
| 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. |  |
| Native Bacillus cereus Sphingomyelinase | Sphingomyelin phosphodiesterase is a hydrolase enzyme that is involved in sphingolipid metabolism reactions. SMase is a member of the DNase I superfamily of enzymes and is responsible for breaking sphingomyelin (SM) down into phosphocholine and ceramide. The activation of SMase has been suggested as a major route for the production of ceramide in response to cellular stresses. Applications: Sphingomyelinase has been used in a study to assess the interaction of actin with the hiv-1 accessory protein nef. sphingomyelinase has also been used in a study to investigate x-ray scattering as a quality-control tool for liposomal drug-delivery systems. Group: Enzymes. Synonyms: Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; SMase. Enzyme Commission Number: EC 3.1.4.12. CAS No. 9031-54-3. SMase. Activity: > 100 units/mg protein. Storage: 2-8°C. Form: Type I, buffered aqueous glycerol solution, Solution in 50% glycerol containing 50 mM Tris-HCl, pH 7.5; Type II, Lyophilized powder containing potassium phosphate buffer salts and stabilizer. Source: Bacillus cereus. Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; SMase. Cat No: NATE-0672. | |
| Native Clostridium perfringens (C. welchII) Phospholipase C | Phospholipase C is induced by thrombin and platelet-activating factor, forming 1,2-diacylglycerol and phosphatidic acid. PLC hydrolyzes the phosphate bond on phosphatidylcholine and other glycerophospholipids yielding diacylglycerol; this enzyme will also hydrolyze the phosphate bonds of sphingomyelin, cardiolipin, choline plasmalogen and ceramide phospholipids. Group: Enzymes. Synonyms: Phospholipase C; PLC; 9001-86-9; lipophosphodiesterase I; lecithinase C; Clostridium welchii α-toxin; Clostridium oede. Enzyme Commission Number: EC 3.1.4.3. CAS No. 9001-86-9. Phospholipase C. Activity: Type I, > 150 units/mg protein; Type II, 10-50 units/mg protein; Type III, Type IV, > 1,000 units/mg protein (Lowry). Storage: -20°C. Form: Type I, Lyophilized powder in buffered salts; Type II, lyophilized powder; Type III, buffered aqueous glycerol solution; Solution in 60% (v/v) glycerol containing 10 mM Tris-HCl, pH 8.0 and 10 mM EDTA; Type IV, lyophilized powder, Contains phosphate buffer salts, EDTA and stabilizer. Source: Clostridium perfringens (C. welchII). Phospholipase C; PLC; 9001-86-9; lipophosphodiesterase I; lecithinase C; Clostridium welchii α-toxin; Clostridium oedematiens β-and γ-toxins; lipophosphodiesterase C; phosphatidase C; heat-labile hemolysin; α-toxin; EC 3.1.4.3. Cat No: NATE-0593. | |
| Native Porcine Isocitric Dehydrogenase (NADP) | Isocitrate dehydrogenase (IDH) is an enzyme that catalyzes the oxidative decarboxylation of Isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2. This is a two-step process, which involves oxidation of Isocitrate (a secondary alcohol) to oxalosuccinate (a ketone), followed by the decarboxylation of the carboxyl group beta to the ketone, forming alpha-ketoglutarate. In humans, IDH exists in three isoforms:IDH3 catalyzes the third step of the citric acid cycle while converting NAD+ to NADH in the mitochondria. The isoforms IDH1 and IDH2 catalyze the same reaction outside the context of the citric acid cycle and use NADP+ as a cofactor instead of NAD+. They localize to the cytosol as well as the mitochondrion and peroxisome. Group: Enzymes. Synonyms: oxalosuccinate decarboxylase; Isocitrate dehyd. Enzyme Commission Number: EC 1.1.1.42. CAS No. 9028-48-2. IDH. Activity: Type I, 0.5-3.0 unit/mg solid; Type II, 3-20 units/mg protein. Storage: -20°C. Form: Type II, buffered aqueous glycerol solution, Solution in 50% glycerol in EDTA buffer salts, pH 6.0. Source: Porcine heart. Species: Porcine. oxalosuccinate decarboxylase; Isocitrate dehydrogenase (NADP); oxalsuccinic decarboxylase; Isocitrate (NADP) dehydrogenase; Isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; NADP-specific Isocitrate dehydrog | |
| Acetylcholinesterase Human, Recombinant | Acetylcholinesterase, also known as AChE or acetylhydrolase, is a hydrolase that hydrolyzes the neurotransmitter acetylcholine. AChE is found at mainly neuromuscular junctions and cholinergic brain synapses, where its activity serves to terminate synaptic transmission. It belongs to carboxylesterase family of enzymes. It is the primary target of inhibition by organophosphorus compounds such as nerve agents and pesticides. Group: Enzymes. Synonyms: true cholinesterase; choline esterase I; cholinesterase; acetylthiocholinesterase; acetylcholine hydrolase; acetyl; β-methylcholinesterase; AcCholE; EC 3.1.1.7; 9000-81-1; Acetylcholinesterase; AChE; acetylhydrolase. Enzyme Commission Number: EC 3.1.1.7. CAS No. 9000-81-1. Acetylcholinesterase. Activity: > 1,000 units/mg protein (Lowry). Storage: -20°C. Form: Lyophilized powder containing phosphate buffer salt. Source: HEK 293 cells. Species: Human. Cat No: NATE-0020. | |
| 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. | |
| Amidase from Pseudomonas aeruginosa, Recombinant | The amidase from Pseudomonas aeruginosa catalyzes the hydrolysis of a small range of short aliphatic amides. Each amidase monomer is formed by a globular four-layer αββα sandwich domain with an additional 81-residue long C-terminal segment. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. Applications: The importance of these hydrolases in biotechnology is growing rapidly, because their potential applications span through chemical and pharmaceutical industries as well as in bioremediation. immobilized amidase can be used efficiently for production of ac...onyms: acylamidase; acylase (misleading); amidohydrolase (ambiguous); deaminase (ambiguous); fatty acylamidase; N-acetylaminohydrolase (ambiguous); amidase; EC 3.5.1.4; acylamide amidohydrolase. Enzyme Commission Number: EC 3.5.1.4. CAS No. 9012-56-0. Amidase. Activity: >200 units/mg protein (biuret). Storage: Store at -20°C. Form: Solution in 50% glycerol containing 7 mM 2-mercaptoethanol and phosphate buffer salt. Source: E. coli. Species: Pseudomonas aeruginosa. acylamidase; acylase (misleading); amidohydrolase (ambiguous); deaminase (ambiguous); fatty acylamidase; N-acetylaminohydrolase (ambiguous); amidase; EC 3.5.1.4; acylamide amidohydrolase. Cat No: NATE-0809. | |
| b-Glycerophosphate Disodium Salt Hydrate 99+% | Used as an organic phosphate donor and to buffer cell culture media. Group: Biochemicals. Alternative Names: Glycerol 2-phosphate disodium salt hydrate. Grades: Reagent Grade. CAS No. 154804-51-0. Pack Sizes: 5g, 25g, 100g, 250g. Molecular Formula: C3H7Na2O6P; xH2O, Molecular Weight: 234. US Biological Life Sciences. | Worldwide |
| Dipotassium hydrogenphosphate | Dipotassium phosphate (K2HPO4) (also dipotassium hydrogen orthophosphatepotassium phosphate dibasic) is a highly water-soluble salt which is often used as a fertilizer, food additive and buffering agent. It is a common source of phosphorus and potassium.A dipotassium phosphate solution is formed by the stoichiometric reaction of phosphoric acid with two equivalents of potassium hydroxide:H3PO4 + 2 KOH → K2HPO4 + 2 H2O. Group: Electrolytes. Alternative Names: Isolyte; DIPOTASSIUM PHOSPHATE; Mediject P; SEC-POTASSIUM PHOSPHATE; DKP. CAS No. 7758-11-4. Product ID: dipotassium; hydrogen phosphate. Molecular formula: 174.176g/mol. Mole weight: HK2O4P. OP(=O)([O-])[O-].[K+].[K+]. InChI=1S/2K.H3O4P/c;;1-5(2, 3)4/h;;(H3, 1, 2, 3, 4)/q2*+1;/p-2. ZPWVASYFFYYZEW-UHFFFAOYSA-L. |  |
| Di Potassium Hydrogen Phosphate | White crystalline solid. Uses: buffer solution, fertilizer. Group: phosphate salt. Alternative Names: Dipotassium Phosphate (DKP). CAS No. 7758-11-4. |  |
| di-Potassium hydrogen phosphate anhydrous | 1kg Pack Size. Group: Buffers, Salts. Formula: K2HPO4. CAS No. 7758-11-4. Prepack ID 33750632-1kg. Molecular Weight 174.18. See USA prepack pricing. |  |
| di-Potassium hydrogen phosphate anhydrous | 5kg Pack Size. Group: Buffers, Salts. Formula: K2HPO4. CAS No. 7758-11-4. Prepack ID 33750632-5kg. Molecular Weight 174.18. See USA prepack pricing. | |
| di-Potassium hydrogen phosphate trihydrate | 1kg Pack Size. Group: Buffers, Inorganic Chemicals, Salts. Formula: HK2O4P · 3H2O. CAS No. 16788-57-1. Prepack ID 46074591-1kg. Molecular Weight 228.22. See USA prepack pricing. | |
| Dipotassium phosphate | Dipotassium hydrogen phosphate is a potassium salt that is the dipotassium salt of phosphoric acid. It has a role as a buffer. It is a potassium salt and an inorganic phosphate. CAS No. 7758-11-4. Product ID: PE-0665. Molecular formula: K2HPO4. Category: Buffer agent. Product Keywords: Excipients for Sustained & Controlled Release Materials; Dipotassium phosphate; PE-0665; Buffer agent; K2HPO4; 7758-11-4. Standard: CP. Color: White. EC Number: 231-834-5. Physical State: Solid. Solubility: H2O: 1 M at 20 °C, clear, colorless. Storage: Store at +5°C to +30°C. Applications: Dipotassium phosphate as a food additive, dipotassium phosphate is used in imitation dairy creamers, dry powder beverages, mineral supplements, and starter cultures. It functions as an emulsifier, stabilizer and texturizer; it also is a buffering agent, and chelating agent especially for the calcium in milk products. Boiling Point: 340 °C. Density: 2,44 g/cm3. Product Description: Dipotassium phosphate as a food additive, dipotassium phosphate is used in imitation dairy creamers, dry powder beverages, mineral supplements, and starter cultures. It functions as an emulsifier, stabilizer and texturizer; it also is a buffering agent, and chelating agent especially for the calcium in milk products. |  |
| Disodium hydrogenphosphate | Disodium hydrogenphosphate. Synonyms: Disodium hydrogenorthophosphate;disodium, hydrogen phosphate. CAS No. 7558-79-4. Product ID: CDC10-0241. Molecular formula: HNa2O4P. Category: Buffering Agents. Product Keywords: Cosmetic Ingredients; Buffering Agents; Disodium hydrogenphosphate; CDC10-0241; 7558-79-4; HNa2O4P; Disodium hydrogenorthophosphate; disodium,hydrogen phosphate; 231-448-7; MFCD00003496; 7558-79-4. Purity: 231-448-7. Color: White granular. EC Number: 231-448-7. Physical State: Powder. Quality Level: 200. Storage: Store at RT. Boiling Point: 158ºC at 760 mmHg. Melting Point: 243-245ºC. Density: 1.064 g/mL at 20ºC. Product Description: Disodium phosphate (DSP), or sodium hydrogen phosphate, is the inorganic compound with the formula Na2HPO4. It is one of several sodium phosphates. The salt is known in anhydrous form as well as forms with 2, 7, 8, and 12 hydrates. All are water-soluble White powders; the anhydrous salt being hygroscopic. | |
| Di Sodium Hydrogen Phosphate Anhydrous | White powder. Uses: food additive, buffer agent. Group: phosphate salt. Alternative Names: Disodium Phosphate. CAS No. 7558-79-4. | |
| di-Sodium hydrogen phosphate dihydrate | 1kg Pack Size. Group: Buffers, Salts. Formula: HNa2O4P · 2H2O. CAS No. 10028-24-7. Prepack ID 10104750-1kg. Molecular Weight 177.99. See USA prepack pricing. | |
| Di Sodium Hydrogen Phosphate Heptahydrate | White crystalline solid. Uses: ph buffer, emulsifier. Group: phosphate salt. CAS No. 7782-85-6. | |
| Disodium pytophosphate | Disodium pyrophosphate or sodium acid pyrophosphate is an inorganic compound consisting of sodium cations and pyrophosphate anion. It is a white, water-soluble solid that serves as a buffering and chelating agent, with many applications in the food industry. When crystallised from water, it forms a hexahydrate, but it dehydrates above room temperature. Pyrophosphate is a polyvalent anion with a high affinity for polyvalent cations, e.g. Ca2+.Disodium pyrophosphate is produced by heating sodium dihydrogen phosphate:2 NaH2PO4 → Na2H2P2O7 + H2O. Group: Electrolytes. Alternative Names: DISODIUM PYROPHOSPHATE; disodium pytophosphate; DI-SODIUM DIHYDROGEN PYROPHOSPHATE; Diphosphoric acid disodium salt; DSPP; SODIUM ACID PYROPHOSPHATE; SODIUM DIHYDROGEN PYROPHOSPHATE; SAPP. CAS No. 7758-16-9. Product ID: disodium [hydroxy(oxido)phosphoryl] hydrogen phosphate. Molecular formula: 221.94. Mole weight: H2Na2O7P2. OP(=O)([O-])OP(=O)(O)[O-]. [Na+]. [Na+]. GYQBBRRVRKFJRG-UHFFFAOYSA-L. | |
| Disodium pytophosphate | Disodium pyrophosphate or sodium acid pyrophosphate is an inorganic compound consisting of sodium cations and pyrophosphate anion. It is a white, water-soluble solid that serves as a buffering and chelating agent, with many applications in the food industry. When crystallised from water, it forms a hexahydrate, but it dehydrates above room temperature. Pyrophosphate is a polyvalent anion with a high affinity for polyvalent cations, e.g. Ca2+.Disodium pyrophosphate is produced by heating sodium dihydrogen phosphate:2 NaH2PO4 → Na2H2P2O7 + H2O. Group: Metal & ceramic materials. Alternative Names: DISODIUM PYROPHOSPHATE;disodium pytophosphate;DI-SODIUM DIHYDROGEN PYROPHOSPHATE;Diphosphoric acid disodium salt;DSPP;SODIUM ACID PYROPHOSPHATE;SODIUM DIHYDROGEN PYROPHOSPHATE;SAPP. CAS No. 7758-16-9. Molecular formula: H2Na2O7P2. Mole weight: 221.94. Appearance: White powder. Purity: N/A. IUPACName: disodium [hydroxy(oxido)phosphoryl] hydrogen phosphate. Canonical SMILES: OP(=O)([O-])OP(=O)(O)[O-]. [Na+]. [Na+]. Density: 2.311 g/cm³ (25ºC). ECNumber: 231-835-0. Catalog: ACM7758169. |  |
| Glycerokinase from Cellulomonas sp. | 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. Phosphoryl moiety of atp to one of the primary hydroxyl group of glycerol, forming sn-glycerol-3-p. the enzyme has the highest specificity for glycerol, and also phosphorylates dihydroxyacetone and glyceraldehyde (table 1,2). mg++ is essentially required for the reaction. Applications: This enzyme is useful for enzymatic deter...se, g3o-301, g3o-311, g3o-321) or pyruvate kinase (pyk-301) and lactate dehydrogenase (lcd-209, lcd-211), lipoprotein lipase (lpl-311, lpl-314) in clinical analysis. 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. Activity: 20 U/mg-solid or more. Storage: -20°C. Form: Lyophilized powder containing phosphate buffer salts and sodium gluconate. Source: Cellulomonas sp. EC 2.7.1.30; glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase; 9030-66-4. Cat No: NATE-0287. | |
| Leuconostoc mesenteroides Glucose-6-phosphate Dehydrogenase, Recombinant | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Glucose 6-phosphate dehydrogenase (g-6-p-dh) is a key regulatory enzyme in the first step of the pentose phosphate pathway. g-6-p-dh is a glycoprotein with a molecular mass of 128 kda (gel filtration). Applications: Glucose-6-phosphate...its/mg protein (biuret). Storage: 2-8°C. Form: Type I, Lyophilized powder containing Ficoll and Tris buffer salts; Type II, ammonium sulfate suspension, Supplied in 3.2M ammonium sulfate containing 50mM Tris and 1mM magnesium chloride, pH 7.5. Source: E. coli. Species: Leuconostoc mesenteroides. EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase; 9001-40-5. Cat No: DIA-323. | |
| Lysostaphin from Staphylococcus simulans, Recombinant | Lysostaphin is a Staphylococcus simulans metalloendopeptidase. It can function as an antimicrobial against Staphylococcus aureus. Lysostaphin is a 27 KDa glycylglycine endopeptidase, an antibacterial enzyme which is capable of cleaving the crosslinking pentaglycin bridges in the cell wall of Staphylococci. Applications: Lysostaphin from staphyl oc occus simulans has been used in a study to assess molecular cloning, sequencing, and expression of lytm, a unique autolytic gene of staphyl oc occus aureus. it has also been used in a study to investigate the sequence analysis of a staphyl oc occus aureus gene encoding a peptidoglycan hydrolase activity. Group: Enzymes. Synonyms: Lysostaphin; EC 3.4.24.75; glycyl-glycine endopeptidase; 9011-93-2. Enzyme Commission Number: EC 3.4.24.75. CAS No. 9011-93-2. Lysostaphin. Activity: Type I, > 2,000 units/mg protein; Type II, > 500 units/mg protein. Storage: -20°C. Form: Type I, lyophilized powder, Contains potassium phosphate buffer salts and sodium chloride; Type II, lyophilized powder. Source: E. coli. Species: Staphylococcus simulans. Lysostaphin; EC 3.4.24.75; glycyl-glycine endopeptidase; 9011-93-2. Cat No: NATE-0430. | |
| Mono Sodium Phosphate (Hydrous) | White crystalline solid. Uses: ph buffer, emulsifier. Group: phosphate salt. CAS No. 10049-21-5. | |
| Native α-Glucosidase from Bacillus stearothermophilus | Alpha-glucosidase is a glucosidase located in the brush border of the small intestine that acts upon 1,4-alpha bonds. This is in contrast to beta-glucosidase. Alpha-glucosidase breaks down starch and disaccharides to glucose. Maltase, a similar enzyme that cleaves maltose, is nearly functionally equivalent. Α-glucosidase hydrolyzes carbohydrates by acting on 1,4-α linkages. inhibition of α-glucosidase is a prominent target in the management of non-insulin-dependent diabetes mellitus. Applications: Α-glucosidase is potential enzyme for the biosynthesis of complex carbohydrates. Group: Enzymes. Synonyms: 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; al. Enzyme Commission Number: EC 3.2.1.20. CAS No. 9001-42-7. α-Glucosidase. Activity: >50 units/mg. Storage: 2-8°C. Form: Lyophilized powder containing potassium phosphate buffer salt. Source: Bacillus stearothermophilus. 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. Cat No: NATE-1163. | |
| Native Arachis hypogaea (peanut) Phospholipase D | Phospholipase D is a phospholipid hydrolyzing enzyme and an important component of receptor-mediated signal transduction responses and regulated secretion. Hydrolyzes the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid. Phospholipase D is involved in conferring drought susceptibility in peanuts, which increases the risk of aflatoxin contamination. Phospholipase d is a phospholipid hydrolyzing enzyme and an important component of receptor-mediated signal transduction responses and regulated secretion. Applications: Research has shown adp-ribosylation factor regulation of phospholipase d is important in the release of nascent secretory vesicles from the trans-golgi network. it has also been used in a study to investigate stimulation of na+-ca2+ exchange activity in canine cardiac sarcolemmal vesicals. Group: Enzymes. Synonyms: Phospholipase D; EC 3.1.4.4; lipophosphodiesterase II; lecithinase D; choline phosphatase; PLD; 9001-87-0. Enzyme Commission Number: EC 3.1.4.4. CAS No. 9001-87-0. PLD. Activity: > 60 units/mg protein. Storage: -20°C. Form: Partially purified, lyophilized powder containing buffer salts. Source: Arachis hypogaea (peanut). Phospholipase D; EC 3.1.4.4; lipophosphodiesterase II; lecithinase D; choline phosphatase; PLD; 9001-87-0. Cat No: NATE-0594. | |
| Native Bacillus stearothermophilus Fructose-6-phosphate Kinase | Fructose-1,6-bisphosphatase (FBP) is an important enzyme in glucose metabolism. It catalyzes the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate. Fructose-6-phosphate kinase converts fructose-6-phosphate into fructose 1,6-bisphophate in the rate limiting step of the glycolysis cycle. Bacillus stearothermophilus phosphofructokinase (bspfk) is a homotetramer that is allosterically inhibited by phosphoenolpyruvate (pep), which binds along one dimer-dimer interface. Applications: Fructose-6-phosphate kinase from bacillus stearothermophilus was shown to interact with neuronal nitric oxide synthase (nnos) causing a defect in glycolytic metabolism and increased fatigability in dystrophic muscle. Group: Enzymes. Sy. Enzyme Commission Number: EC 2.7.1.11. CAS No. 9001-80-3. FBP. Activity: > 50 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing phosphate buffer salt. Source: Bacillus stearothermophilus. EC 2.7.1.11; phosphohexokinase; phosphofructokinase I; phosphofructokinase (phosphorylating); 6-phosphofructose 1-kinase; ATP-dependent phosphofructokinase; D-fructose-6-phosphate 1-phosphotransferase; fructose 6-phosphate kinase; fructose 6-phosphokinase; nucleotide triphosphate-dependent phosphofructokinase; phospho-1,6-fructokinase; PFK; 9001-80-3. Cat No: NATE-0252. | |
| Native Bacillus stearothermophilus Glucokinase | 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. GCK. Activity: > 300 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Bacillus stearothermophilus. EC 2.7.1.2; glucokinase; glucokinase (phosphorylating); 9001-36-9; GCK; FGQTL3; GK; GLK; HHF3; HK4; HKIV; HXKP; LGLK; MODY2. Cat No: NATE-0282. | |
| Native Baker's yeast (S. cerevisiae) D-Ribulose-5-phosphate 3-Epimerase | RPE is a metalloenzyme and has been shown to use the divalent Zn2+ ion predominantly for catalysis. Human D-ribulose-5-phosphate 3-epimerase (hRPE) has been shown to use Fe2+ for catalysis. Applications: D-ribulose-5-phosphate 3-epimerase is an enzyme that converts the reversible conversion of d-ribulose 5-phosphate into d-xylulose 5-phosphate, which is important for the cellular response against oxidative stress. d-ribulose-5-phosphate 3-epimerase is involved in the pentose phosphate pathway, pentose and glucuronate interconversions and carbon fixation. this product is from bakers yeast and is provided as a lyophilized powder. it is useful in enzyme syste...EC 5.1.3.1. CAS No. 9024-20-8. RPE. Activity: 50-100 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: lyophilized powder. Lyophilized and essentially sulfate-free; contains approx. 35% Citrate buffer salts. Source: Baker's yeast (S. cerevisiae). EC 5.1.3.1; RPE; phosphoribulose epimerase; erythrose-4-phosphate isomerase; phosphoketopentose 3-epimerase; xylulose phosphate 3-epimerase; phosphoketopentose epimerase; ribulose 5-phosphate 3-epimerase; D-ribulose phosphate-3-epimerase; D-ribulose 5-phosphate epimerase; D-ribulose-5-P 3-epimerase; D-xylulose-5-phosphate 3-epimerase; pentose-5-phosphate 3-epimerase; 9024-20-8. Cat No: NATE-0659. | |
| Native Baker's yeast (S. cerevisiae) Inorganic Pyrophosphatase | 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. This ubiquitous enzyme serves to drive metabolic reactions that produce pyrophosphate, since these reactions typically have...phohydrolase; 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. Inorganic pyrophosphatase. Mole weight: 71 kDa (homodimer consisting of two equal subunits of molecular weight 32-35 kDa). Activity: Type I, > 1,000 units/mg protein (BCA); Type II, > 500 units/mg protein (E1%/280). Storage: -20°C. Form: Type I, lyophilized powder containing 90% buffer salts; Type II, Lyophilized powder containing 85% buffer salts. Source: Baker's yeast (S. cerevisiae). Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-0354. | |
| Native Baker's yeast (S. cerevisiae) Transaldolase | Transaldolase is an enzyme (EC 2.2.1.2) of the non-oxidative phase of the pentose phosphate pathway. In humans, transaldolase is encoded by the TALDO1 gene. The following chemical reaction is catalyzed by transaldolase:sedoheptulose 7-phosphate + glyceraldehyde 3-phosphate<-> erythrose 4-phosphate + fructose 6-phosphate. Applications: Useful in systems requiring low sulfate concentrations. Group: Enzymes. Synonyms: Transaldolase; EC 2.2.1.2; 9014-46-4; dihydroxyacetonetransferase; dihydroxyacetone synthase; formaldehyde transketolase; D-Sedoheptulose-7-phosphate:D-Glyceraldehyde-3-phosphate dihydroxyacetonetransferase. Enzyme Commission Number: EC 2.2.1.2. CAS No. 9014-46-4. Transaldolase. Activity: 10-30 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized, essentially sulfate-free; contains approx. 5% Citrate buffer salts. Source: Baker's yeast (S. cerevisiae). Transaldolase; EC 2.2.1.2; 9014-46-4; dihydroxyacetonetransferase; dihydroxyacetone synthase; formaldehyde transketolase; D-Sedoheptulose-7-phosphate:D-Glyceraldehyde-3-phosphate dihydroxyacetonetransferase. Cat No: NATE-0714. | |
| Native Baker's yeast Uridine-5'-diphosphoglucose pyrophosphorylase | UTP-glucose-1-phosphate uridylyltransferase is an enzyme associated with glycogenesis. It synthesizes UDP-glucose from glucose-1-phosphate and UTP; i.e., glucose-1-phosphate + UTP<-> UDP-glucose + pyrophosphate. Applications: Uridine-5?-diphosphoglucose pyrophosphorylase has been used in assays to determine the concentration of pyrophosphate in human urine samples. Group: Enzymes. Synonyms: UDP glucose pyrophosphorylase; glucose-1-phosphate uridylyltransferase; UDPG phosphorylase; UDPG pyrophosphorylase; uridine 5'-diphosphoglucose pyrophosphorylase; uridine diphosphoglucose pyrophosphorylase; uridine diphosphate-D-glucose pyrophosphorylase; uridine-diphosphate glucose pyrophosphorylase; EC 2.7.7.9; 9026-22-6. Enzyme Commission Number: EC 2.7.7.9. CAS No. 9026-22-6. UDPG pyrophosphorylase. Activity: > 50 units/mg protein. Storage: -20°C. Form: Lyophilized, sulfate-free powder containing Citrate buffer salt. Source: Baker's yeast. UDP glucose pyrophosphorylase; glucose-1-phosphate uridylyltransferase; UDPG phosphorylase; UDPG pyrophosphorylase; uridine 5'-diphosphoglucose pyrophosphorylase; uridine diphosphoglucose pyrophosphorylase; uridine diphosphate-D-glucose pyrophosphorylase; uridine-diphosphate glucose pyrophosphorylase; EC 2.7.7.9; 9026-22-6. Cat No: NATE-0728. | |
| Native Bovine Glutathione Peroxidase | Glutathione peroxidase is an enzyme which reduced lipid hydroperoxides into their corresponding alcohols. It also reduces free hydrogen peroxide in to water. In vivo it is responsible for protecting hemoglobin from oxidative breakdown. Applications: Glutathione peroxidase from bovine erythr ocytes was used as a positive control in cloning and characterization of full-length cdnas encoding two glutathione peroxidases (gpxs) from globodera rost ochiensis. it was used for the determination of glutathione peroxidase activity in human milk. Group: Enzymes. Synonyms: EC 1.11.1.9; GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase; 9013-66-5; GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase; Glutathione Peroxidase. Enzyme Commission Number: EC 1.11.1.9. CAS No. 9013-66-5. Mole weight: mol wt 84.5 kDa. Activity: > 300 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing 25% sucrose and 2.5% dithiothreitol with sodium phosphate buffer salts. Source: Bovine erythr ocytes. Species: Bovine. EC 1.11.1.9; GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase; 9013-66-5; GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase; Glutathione Peroxidase. Cat No: NATE-0322. | |
| Native Bovine Guanylate Kinase | In enzymology, a guanylate kinase (EC 2.7.4.8) is an enzyme that catalyzes the chemical reaction:ATP + GMP<-> ADP + GDP. Thus, the two substrates of this enzyme are ATP and GMP, whereas its two products are ADP and GDP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. This enzyme participates in purine metabolism. Group: Enzymes. Synonyms: guanylate kinase; deoxyguanylate kinase; 5'-GMP kinase; GMP kinase; guanosine monophosphate kinase; ATP:GMP phosphotransferase; EC 2.7.4.8; 9026-59-9. Enzyme Commission Number: EC 2.7.4.8. CAS No. 9026-59-9. GMP kinase. Activity: 10-40 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Bovine brain. Species: Bovine. guanylate kinase; deoxyguanylate kinase; 5'-GMP kinase; GMP kinase; guanosine monophosphate kinase; ATP:GMP phosphotransferase; EC 2.7.4.8; 9026-59-9. Cat No: NATE-0309. | |
| Native Bovine Phosphodiesterase, 3',5'-cyclic-nucleotide-specific | Hydrolyzes the 3',5'-phosphodiester bond in cyclic nucleotide monophosphates, such as cAMP and cGMP, to the corresponding nucleotide 5'-monophosphate. Applications: May be used to assay the protein activator, calmodulin. Group: Enzymes. Synonyms: cyclic 3',5'-mononucleotide phosphodiesterase; PDE. Enzyme Commission Number: EC 3.1.4.17. CAS No. 9040-59-9. PDE. Mole weight: mol wt ~60 kDa. Activity: 15-30 units/mg protein (in the presence of 0.03 mM Ca2+ and a saturating level (10 units per ml) of calmodulin (P2277)). Storage: -20°C. Form: Lyophilized powder containing Tris-HCl buffer salts and lactose. Source: Bovine brain. Species: Bovine. cyclic 3',5'-mononucleotide phosphodiesterase; PDE; cyclic 3',5'-nucleotide phosphodiesterase; cyclic 3',5'-phosphodiesterase; 3',5'-nucleotide phosphodiesterase; 3':5'-cyclic nucleotide 5'-nucleotidohydrolase; 3',5'-cyclonucleotide phosphodiesterase; cyclic nucleotide phosphodiesterase; 3', 5'-cyclic nucleoside monophosphate phosphodiesterase; 3':5'-monophosphate phosphodiesterase (cyclic CMP); cytidine 3':5'-monophosphate phosphodiesterase (cyclic CMP); cyclic 3',5-nucleotide monophosphate phosphodiesterase; nucleoside 3',5'-cyclic phosphate diesterase; nucleoside-3',5-monophosphate phosphodiesterase; EC 3.1.4.17. Pack: Package size based on activated units. Cat No: NATE-0515. | |
| Native Bovine Phospholipase A2 | Phospholipase A2 (PLA2) hydrolyzes the β-ester bond of zwitterionic glycerophospholipids. Preferred substrates are phosphatidylcholine, phosphatidylethanolamine, and their plasmalogen analogues. Phosphatidylinositol and phosphatidylserine are also hydrolyzed. It aggressively attacks phospholipids in membranes of intact cells. PLA2 specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Group: Enzymes. Synonyms: Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Enzyme Commission Number: EC 3.1.1.4. CAS No. 9001-84-7. PLA2. Activity: > 20 units/mg protein. Storage: -20°C. Form: lyophilized powder; Contains Tris buffer salts. Source: Bovine pancreas. Species: Bovine. Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Cat No: NATE-0583. | |
| Native Bovine Protein Disulfide Isomerase | Protein Disulfide Isomerase (PDI) has the C-terminal ER retention sequence Lys-Asp-Glu-Leu. It has active, intracellular traffic to different cell compartments. PDI supports internalization of Chlamydia, cholera and diphtheria toxins in some hosts. PDI is required for Sindbis virus infection and aids in reducing HIV gp120 protein thiols. PDI facilitates formation of the correct disulfide bonds by promoting rapid reshuffling of disulfide pairings. Protein disulfide isomerase (pdi) from bovine liver is a homodimer with a molecular weight of 107 kda (gel filtration) and the molecular weight of the monomer has been reported at 57 kda (sds-page). the enzyme is a glycoprotein ... is mainly l ocated in the er, where it assists in protein-folding and thiol-disulfide exchanges. it is used to study functional role of pdi in parasite infection and the interaction between macrophage pdi and l. chagasi. Group: Enzymes. Synonyms: Protein disulfide isomerase; PDI; EC 5.3.4.1; 37318-49-3; S-S rearrangase. Enzyme Commission Number: EC 5.3.4.1. CAS No. 37318-49-3. Purity: >95% (SDS-PAGE). PDI. Activity: 100-400 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts and stabilizer. Source: Bovine liver. Species: Bovine. Protein disulfide isomerase; PDI; EC 5.3.4.1; 37318-49-3; S-S rearrangase. Cat No: NATE-0533. | |
| Native Brewer's bottom yeast Orotidine-5'-monophosphate pyrophosphorylase | Orotate phosphoribosyltransferase (OPRTase) or Orotic acid phosphoribosyltransferase is an enzyme involved in pyrimidine biosynthesis. It catalyzes the formation of orotidine 5'-monophosphate (OMP) from orotate and phosphoribosyl pyrophosphate. In yeast and bacteria, orotate phosphoribosyltransferase is an independent enzyme with a unique gene coding for the protein, whereas in mammals and other multicellular organisms, the catalytic function is carried out by a domain of the bifunctional enzyme UMP synthase. Applications: This is the preferred enzyme for assaying orotidine 5?-monophosphate and for the production of omp analogs from the corresponding orot...ty: ~25 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: Lyophilized powder containing approx. 50% buffer salts. Source: Brewer's bottom yeast. orotidylic acid phosphorylase; orotidine-5'-phosphate pyrophosphorylase; OPRTase; orotate phosphoribosyl pyrophosphate transferase; orotic acid phosphoribosyltransferase; orotidine 5'-monophosphate pyrophosphorylase; orotidine monophosphate pyrophosphorylase; orotidine phosphoribosyltransferase; orotidylate phosphoribosyltransferase; orotidylate pyrophosphorylase; orotidylic acid pyrophosphorylase; orotidylic phosphorylase; orotidylic pyrophosphorylase; EC 2.4.2.10; 9030-25-5. Cat No: NATE-0498. | |
| Native Candida utilis L-Glutamic Dehydrogenase (NADP) | L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate. Group: Enzymes. Synonyms: L-Glutamic Dehydrogenase; EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD (P)-glutamate dehydrogenase; NAD (P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP). Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. Activity: 50-200 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salt. Source: Candida utilis. L-Glutamic Dehydrogenase; EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD (P)-glutamate dehydrogenase; NAD (P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP). Cat No: NATE-0394. | |
| Native Cellulomonas sp. 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. Phosphoryl moiety of atp to one of the primary hydroxyl group of glycerol, forming sn-glycerol-3-p. the enzyme has the highest specificity for glycerol, and also phosphorylates dihydroxyacetone and glyceraldehyde (table 1,2). mg++ is essentially required for the reaction. Applications: This enzyme is useful for enzymatic dete...1) and lactate dehydrogenase (lcd-209, lcd-211), lipoprotein lipase (lpl-311, lpl-314) in clinical analysis. 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. Mole weight: mol wt ~128 kDa ((by gel filtration). Activity: 25-75 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing phosphate buffer salts and sodium gluconate. Source: Cellulomonas sp. EC 2.7.1.30; glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase; 9030-66-4. Cat No: NATE-0287. | |
| Native Chicken Glyceraldehyde-3-phosphate Dehydrogenase | Glyceraldehyde-3-phosphate dehydrogenase catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as part of glycolysis. It has also been shown to have roles in initiation of apoptosis, transcription activation and the shuttling of ER to Golgi vesicles. Group: Enzymes. Synonyms: EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phos. Enzyme Commission Number: EC 1.2.1.12. CAS No. 9001-50-7. Glyceraldehyde-3-phosphate Dehydrogenase. Activity: > 40 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Citrate buffer salts. Source: Chicken muscle. Species: Chicken. EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phosphate dehydrogenase (NAD+); glyceraldehyde-3-phosphate dehydrogenase (NAD+); NADH-glyceraldehyde phosphate dehydrogenase; glyceraldehyde-3-P-dehydrogenase; 9001-50-7. Cat No: NATE-0279. | |
| Native Corallina officinalis Bromoperoxidase | Bromoperoxidase from Corallina officinalis is a phenoxazine dye. The brilliant cresyl blue (BCB) test determines the activity of glucose-6-phosphate dehydrogenase (G6PDH). The activity of this enzyme is greatest in growing oocytes and declines as oocytes mature. It stains reticulocytes and trichomonads. Bromoperoxidase contains a significant amount of nonheme iron. It is activated by vanadate ions. Maximal activity is achieved with stoichiometric vanadium incorporation. Applications: Bromoperoxidase from corallina officinalis may be used for staining brain tissue, nuclei, plant chromosomes, reticulocytes, platelets and reticulated red cells. it may be used for the detection of biochemical molecules and the bcb enzyme assay. the bcb assay is also used industrially in optical data storage. Group: Enzymes. Synonyms: BCB; Bromide Peroxidase; Bromoperoxidase; 69279-19-2. CAS No. 69279-19-2. BCB. Activity: > 100 units/mg protein (Lowry). Storage: -20°C. Form: Partially purified, lyophilized powder containing MES buffer salts. Source: Corallina officinalis. BCB; Bromide Peroxidase; Bromoperoxidase; 69279-19-2. Cat No: NATE-0091. | |
| Native Crotalus durissus terrificus venom Phospholipase A2 | Phospholipase A2 (PLA2) hydrolyzes the β-ester bond of zwitterionic glycerophospholipids. Preferred substrates are phosphatidylcholine, phosphatidylethanolamine, and their plasmalogen analogues. Phosphatidylinositol and phosphatidylserine are also hydrolyzed. It aggressively attacks phospholipids in membranes of intact cells. PLA2 specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Group: Enzymes. Synonyms: Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Enzyme Commission Number: EC 3.1.1.4. CAS No. 9001-84-7. PLA2. Activity: ~200 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Crotalus durissus terrificus venom. Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Cat No: NATE-0584. | |
| Native Enterobacter aerogenes Glycerol Dehydrogenase | Glycerol dehydrogenase is an enzyme in the oxidoreductase family that utilizes the NAD+ to catalyze the oxidation of glycerol to form glycerone (dihydroxyacetone). Applications: Glycerol dehydrogenase was used in the kinetic enzymatic determination of glycerol in wine and beer. Group: Enzymes. Synonyms: EC 1.1.1.6; NAD+-linked glycerol dehydrogenase; glycerol:NAD+ 2-oxidoreductase; GDH; GlDH; GlyDH; 9028-14-2; glycerin dehydrogenase. Enzyme Commission Number: EC 1.1.1.6. CAS No. 9028-14-2. GDH. Activity: 20-80 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Enterobacter aerogenes. EC 1.1.1.6; NAD+-linked glycerol dehydrogenase; glycerol:NAD+ 2-oxidoreductase; GDH; GlDH; GlyDH; 9028-14-2; glycerin dehydrogenase. Cat No: NATE-0284. | |
| Native Enterobacter aerogenes myo-Inositol Dehydrogenase | In enzymology, an inositol 2-dehydrogenase (EC 1.1.1.18) is an enzyme that catalyzes the chemical reaction:myo-inositol + NAD+<-> 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+. Thus, the two substrates of this enzyme are myo-inositol and NAD+, whereas its 3 products are 2,4,6/3,5 pentahydroxycyclohexanone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in inositol metabolism and inositol phosphate metabolism. Group: Enzymes. Synonyms: myo-inositol 2-dehydrogenase; myo-inositol:NAD+ oxidoreductase; inositol dehydrogenase; myo-inositol dehydrogenase; EC 1.1.1.18; 9028-25-5. Enzyme Commission Number: EC 1.1.1.18. CAS No. 9028-25-5. myo-Inositol Dehydrogenase. Activity: > 10 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing buffer salts and stabilizers. Source: Enterobacter aerogenes. myo-inositol 2-dehydrogenase; myo-inositol:NAD+ oxidoreductase; inositol dehydrogenase; myo-inositol dehydrogenase; EC 1.1.1.18; 9028-25-5. Cat No: NATE-0467. | |
| Native Enterobacter cloacae β-Lactamase | β--lactamase inactivates β-lactam antibiotics by breaking open the β-lactam ring. Protein determined by biuret. Applications: Β-lactamase is used to inactivate β-lactam antibiotics by breaking open the β-lactam ring. β-lactamase is used to study antibiotic resistance and resistance suppression1. this product is produced from enterobacter cloacae. Group: Enzymes. Synonyms: β-lactamase; 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; EC . Enzyme Commission Number: EC 3.5.2.6. CAS No. 9073-60-3. β-Lactamase. Activity: 6-18 units/mg protein (using benzylpenicillin); 0.2-0.6 units/mg protein (using benzylpenicillin). Storage: 2-8°C. Form: Lyophilized powder containing sodium phosphate and sodium Citrate buffer salts. Source: Enterobacter cloacae. β-lactamase; 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; EC 3.5.2.6; 9073-60-3. Cat No: NATE-0774. | |
| Native Equine Glutathione S-Transferase | Glutathione S-transferases are a family of proteins that catalyze the conjugation of reduced glutathione with a variety of hydrophobic chemicals containing electrophilic centers. Group: Enzymes. Synonyms: EC 2.5.1.18; glutathione S-transferase; glutathione S-alkyltransferase; glutathione S-aryltransferase; S-(hydroxyalkyl)glutathione lyase; glutathione S-aralkyltransferase; glutathione S-alkyl transferase; GST; 50812-37-8. Enzyme Commission Number: EC 2.5.1.18. CAS No. 50812-37-8. Glutathione S-Transferase. Mole weight: mol wt 45-50 kDa. Activity: > 25 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris and phosphate buffer salts, reduced glutathione and EDTA. Source: Equine liver. Species: Equine. EC 2.5.1.18; glutathione S-transferase; glutathione S-alkyltransferase; glutathione S-aryltransferase; S-(hydroxyalkyl)glutathione lyase; glutathione S-aralkyltransferase; glutathione S-alkyl transferase; GST; 50812-37-8. Cat No: NATE-0325. | |
| 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 Galactose-adapted yeast Galactose-1-phosphate Uridyltransferase | Galactose-1-phosphate uridyltransferase (GALT) facilitates the simultaneous conversion of uridine diphosphoglucose (UDP-glucose) and galactose-1-phosphate (gal-1P) to uridine diphosphogalactose (UDP-galactose) and glucose-1-phosphate. Classic Galactosemia (CG) is an inherited metabolic condition caused by deficiency of GALT activity. Group: Enzymes. Synonyms: EC 2.7.7.12; UDP-glucose-hexose-1-phosphate uridylyltransferase; uridyl transferase; hexose-1-phosphate uridylyltransferase; uridyltransferase; hexose 1-phosphate uridyltransferase; UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase; 9016-11-9. Enzyme Commission Number: EC 2.7.7.12. CAS No. 9026-21-5. GALT. Activity: 20-60 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: lyophilized powder; Contains buffer salts as Citrate and reduced glutathione. Source: Galactose-adapted yeast. EC 2.7.7.12; UDP-glucose-hexose-1-phosphate uridylyltransferase; uridyl transferase; hexose-1-phosphate uridylyltransferase; uridyltransferase; hexose 1-phosphate uridyltransferase; UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase; 9016-11-9. Cat No: NATE-0277. | |
| Native Horseradish Superoxide Dismutase | Superoxide dismutases (SOD) are enzymes that alternately catalyze the dismutation (or partitioning) of the superoxide (O2-) radical into either ordinary molecular oxygen (O2) or hydrogen peroxide (H2O2). Superoxide is produced as a by-product of oxygen metabolism and, if not regulated, causes many types of cell damage. Hydrogen peroxide is also damaging, but less so, and is degraded by other enzymes such as catalase. Thus, SOD is an important antioxidant defense in nearly all living cells exposed to oxygen. One exception is Lactobacillus plantarum and related lactobacilli, which use a different mechanism to prevent damage from reactive (O2-). Applications: Superoxide dism...mutase and glutathione reductase, and environmental and xenobiotic stress tolerance in maize inbreds. superoxide dismutase from horseradish has also been used in a study to investigate chemiluminometric enzyme sensors for flow-injection analysis. Group: Enzymes. Synonyms: EC 1.15.1.1; 9054-89-1; SOD; Superoxide:superoxide oxidoreductase; Superoxide Dismutase. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Activity: 1,000-4,000 units/mg protein. Stability: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Horseradish. EC 1.15.1.1; 9054-89-1; SOD; Superoxide:superoxide oxidoreductase; Superoxide Dismutase. Cat No: NATE-0679. | |
| Native Human Glutathione Peroxidase | Glutathione peroxidase is an enzyme which reduced lipid hydroperoxides into their corresponding alcohols. It also reduces free hydrogen peroxide in to water. In vivo it is responsible for protecting hemoglobin from oxidative breakdown. At the reported ph optimum of 8.8, we have found the activity to be approx. 10 times that at ph 7.0. however, to remain consistent with literature and avoid complications arising from non-enzymatic oxidation of gsh, our unit is defined at ph 7.0. Group: Enzymes. Synonyms: EC 1.11.1.9; GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase; 9013-66-5; GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase; Glutathione Peroxidase. Enzyme Commission Number: EC 1.11.1.9. CAS No. 9013-66-5. GSH-Px. Activity: > 30 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing 25% sucrose, 3% dithiothreitol, and sodium phosphate buffer salts. Source: Human erythr ocytes. Species: Human. EC 1.11.1.9; GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase; 9013-66-5; GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase; Glutathione Peroxidase. Cat No: NATE-0323. | |
| Native Human Glyceraldehyde-3-phosphate Dehydrogenase | Glyceraldehyde-3-phosphate dehydrogenase catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as part of glycolysis. It has also been shown to have roles in initiation of apoptosis, transcription activation and the shuttling of ER to Golgi vesicles. Group: Enzymes. Synonyms: EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceralde. Enzyme Commission Number: EC 1.2.1.12. CAS No. 9001-50-7. Glyceraldehyde-3-phosphate Dehydrogenase. Activity: 50-150 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing sodium Citrate buffer salts. Source: Human erythrocytes. Species: Human. EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phosphate dehydrogenase (NAD+); glyceraldehyde-3-phosphate dehydrogenase (NAD+); NADH-glyceraldehyde phosphate dehydrogenase; glyceraldehyde-3-P-dehydrogenase; 9001-50-7. Cat No: NATE-0280. | |
| Native Human 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. Applications: Superoxide dismutase from human erythr ocytes has been used in a study to identify in vitro glycated sites of hu...-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. Activity: > 2,500 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Human erythrocytes. Species: Human. Superoxide dismutases; EC 1.15.1.1; 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. Cat No: NATE-0680. | |
| Native Klebsiella pneumoniae Pullulanase | Pullulanase is a lipoprotein generated as a precursor containing a 19-amino acid signal peptide followed by a palmitate-modified cysteine residue. The signal peptide gets cleaved prior to secretion into the extracellular matrix. Pullulanase is a lipoprotein generated as a precursor containing a 19-amino acid signal peptide followed by a palmitate-modified cysteine residue. the signal peptide gets cleaved prior to secretion into the extracellular matrix. Applications: Pullulanase has been used in a study to assess its l ocation in escherichia coli k12 carrying the cloned structural gene from klebsiella pneumoniae. it has also been used in a study to investigate the role of...lpha;-1,6-glucanohydrolase; 9075-68-7. Enzyme Commission Number: EC 3.2.1.41. CAS No. 9075-68-7. Pullulanase. Activity: Type I, 10-30 units/mg protein; Type II, > 5 units/mg protein (biuret). Storage: -20°C. Form: Type I, Lyophilized powder containing potassium phosphate buffer salts and stabilizer; Type II, ammonium sulfate suspension, Suspension in 3.2 M (NH4)2SO4 solution, pH 6.2. Source: Klebsiella pneumoniae. Pullulanase; EC 3.2.1.41; limit dextrinase (erroneous); amylopectin 6-glucanohydrolase; bacterial debranching enzyme; debranching enzyme; α-dextrin endo-1,6-α-glucosidase; R-enzyme; pullulan α-1,6-glucanohydrolase; 9075-68-7. Cat No: NATE-0643. | |
| Native Leuconostoc mesenteroides Mannitol Dehydrogenase | In enzymology, a mannitol 2-dehydrogenase (EC 1.1.1.67) is an enzyme that catalyzes the chemical reaction:D-mannitol + NAD+<-> D-fructose + NADH + H+. Thus, the two substrates of this enzyme are D-mannitol and NAD+, whereas its 3 products are D-fructose, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in fructose and mannose metabolism. Applications: This preparation is useful in the determination of mannitol in urine. can be used for the production of d-mannitol. it has been used in a study to assess glucosylglycerol and glucosylglycerate as enzyme stabilizers. Group: Enzymes. Synonyms: mannitol dehydrogenase; D-mannitol dehydrogenase; mannitol dehydrogenase; mannitol 2-dehydrogenase; EC 1.1.1.67; 9001-65-4. Enzyme Commission Number: EC 1.1.1.67. CAS No. 9001-65-4. Mannitol Dehydrogenase. Mole weight: 136 kDa. Activity: > 60 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing buffer salts, potassium phosphate, and dithiothreitol. Source: Leuconostoc mesenteroides. mannitol dehydrogenase; D-mannitol dehydrogenase; mannitol dehydrogenase; mannitol 2-dehydrogenase; EC 1.1.1.67; 9001-65-4. Cat No: NATE-0435. | |
| Native Mold sn-Glycerol-3-phosphocholine Phosphodiesterase | In enzymology, a glycerophosphocholine phosphodiesterase (EC 3.1.4.2) is an enzyme that catalyzes the chemical reaction:sn-glycero-3-phosphocholine + H2O<-> choline + sn-glycerol 3-phosphate. Thus, the two substrates of this enzyme are sn-glycero-3-phosphocholine and H2O, whereas its two products are choline and sn-glycerol 3-phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. Group: Enzymes. Synonyms: glycerophosphinicocholine diesterase; glycerylphosphorylcholinediesterase; sn-glycero-3-phosphorylcholine diesterase; glycerolphosphorylcholine phosphodiesterase; glycerophosphohydrolase; EC 3.1.4.2; 9025-85-8. Enzyme Commission Number: EC 3.1.4.2. CAS No. 9025-85-8. Glycerophosphocholine phosphodiesterase. Activity: > 5 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salt. Source: Mold. glycerophosphinicocholine diesterase; glycerylphosphorylcholinediesterase; sn-glycero-3-phosphorylcholine diesterase; glycerolphosphorylcholine phosphodiesterase; glycerophosphohydrolase; EC 3.1.4.2; 9025-85-8. Cat No: NATE-0674. | |
| Native Pineapple Bromelain | Bromelain is a cysteine endopeptidase with broad specificity for cleavage of proteins. Bromelain may be from a stem or piece of fruit. Stem bromelain (SBM) (EC 3.4.22.32), a proteolytic enzyme, is a widely accepted phytotherapeutical drug member of the bromelain family of proteolytic enzymes obtained from Ananas comosus. Some of the therapeutic benefits of SBM are reversible inhibition of platelet aggregation, angina pectoris, bronchitis, sinusitis, surgical traumas, thrombophlebitis, pyelonephritis and enhanced absorption of drugs, particularly of antibiotics. Its anti-metastasis and anti-inflammatory activities are apparently independent of its proteolytic activity. Applications: Bromelain may be used to inhibit the biosysnthesis of proinflammatory prostaglandins. it may be used to reduce clotting efficiency. bromelain, from pineapple stem, has been used to make enzymatic hydrolysates of honeybee-collected pollen. Group: Enzymes. Synonyms: stem bromelain; EC 3.4.22.32; 37189-34-7; bromelain; pineappl. Enzyme Commission Number: EC 3.4.22.32. CAS No. 37189-34-7. Bromelain. Activity: > 3 units/mg protein; 5-15 units/mg protein. Form: Lyophilized powder containing mannitol and potassium phosphate buffer salts. Source: Pineapple stem. Species: Pineapple. stem bromelain; EC 3.4.22.32; 37189-34-7; bromelain; pineapple stem bromelain; SBM. Cat No: NATE-0665. | |
| Native Pseudomonas atlantica Agarase | Agarase is an enzyme with system name agarose 4-glycanohydrolase. It found in agarolytic bacteria and is the first enzyme in the agar catabolic pathway. It is responsible for allowing them to use agar as their primary source of Carbon and enables their ability to thrive in the ocean. Agarases are classified as either α-agarases or β-agarases based upon whether they degrade αor β linkages in agarose, breaking them into oligosaccharides. When secreted, α-agarases yield oligosaccharides with 3.6 anhydro-L-galactose at the reducing end whereas β-agarases result in D-galactose residues. Group: Enzymes. Synonyms: agarase; AgaA; AgaB; endo-β-agarase; agarose 3-glycanohydrolase; EC 3.2.1.81; 37288-57-6. Enzyme Commission Number: EC 3.2.1.81. CAS No. 37288-57-6. Agarase. Activity: > 5,000 units/mg protein (Lowry). Storage: 2-8°C. Form: lyophilized powder. Contains phosphate buffer salts. May contain bovine serum albumin to standardize protein content. Source: Pseudomonas atlantica. agarase; AgaA; AgaB; endo-β-agarase; agarose 3-glycanohydrolase; EC 3.2.1.81; 37288-57-6. Cat No: NATE-0040. | |
| Native Pseudomonas lemoignei β-Hydroxybutyrate Dehydrogenase | In mammalian systems, β-hydroxybutyrate dehydrogenase is localized on the inner mitochondrial membrane and requires phosphatidyl choline for activity. In contrast, the enzyme from Pseudomonas is a soluble cytosolic enzyme that does not require a phospholipid allosteric activator. The enzyme is required for the utilization of ketone bodies as a source of metabolic energy. It catalyzes the oxidation of 3-hydroxybutyrate to acetoacetate, the first step in the conversion of ketone bodies to citric acid, which is then further metabolized via the tricarboxylic acid cycle (Krebs cycle). Applications: Suitable for the determination of acetoacetate and d (-)-3-hy...1.1.30; 9028-38-0. Enzyme Commission Number: EC 1.1.1.30. CAS No. 9028-38-0. 3-HBDH. Activity: > 200 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing sucrose, β-NAD and Tris buffer salts. Source: Pseudomonas lemoignei. 3-hydroxybutyrate dehydrogenase; 3-HBDH; NAD-β-hydroxybutyRate dehydrogenase; hydroxybutyRate oxidoreductase; β-hydroxybutyRate dehydrogenase; D-β-hydroxybutyRate dehydrogenase; D-3-hydroxybutyRate dehydrogenase; D-(-)-3-hydroxybutyRate dehydrogenase; β-hydroxybutyric acid dehydrogenase; 3-D-hydroxybutyRate dehydrogenase; β-hydroxybutyric dehydrogenase; EC 1.1.1.30; 9028-38-0. Cat No: NATE-0003. | |
| Native Pseudomonas sp. Sarcosine Dehydrogenase | In enzymology, sarcosine dehydrogenase (EC 1.5.99.1) is a mitochondrial enzyme that catalyzes the chemical reaction N-demethylation of sarcosine to give glycine. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with other acceptors. Sarcosine dehydrogenase is closely related to dimethylglycine dehydrogenase, which catalyzes the demethylation reaction of dimethylglycine to sarcosine. Both sarcosine dehydrogenase and dimethylglycine dehydrogenase use FAD as a cofactor. Sarcosine dehydrogenase is linked by electron-transferring flavoprotein (ETF) to the respiratory redox chain. Group: Enzymes. Synonyms: sarcosine dehydrogenase; EC 1.5.99.1; sarcosine N-demethylase; monomethylglycine dehydrogenase; sarcosine: (acceptor) oxidoreductase (demethylating); 37228-65-2; EC 1.5.8.3. Enzyme Commission Number: EC 1.5.99.1. CAS No. 37228-65-2. Sarcosine dehydrogenase. Activity: 0.5-1.5 units/mg protein. Storage: 2-8°C. Form: Lyophilized powder containing approx. 60% sucrose, 10% potassium phosphate buffer salts and trace EDTA. Source: Pseudomonas sp. sarcosine dehydrogenase; EC 1.5.99.1; sarcosine N-demethylase; monomethylglycine dehydrogenase; sarcosine: (acceptor) oxidoreductase (demethylating); 37228-65-2; EC 1.5.8.3. Cat No: NATE-0663. | |
| Native Pseudomonas testosteroni 3α-Hydroxysteroid Dehydrogenase | In enzymology, a 3alpha-hydroxysteroid dehydrogenase (B-specific) (EC 1.1.1.50) is an enzyme that catalyzes the chemical reaction:androsterone + NAD (P)+<-> 5alpha-androstane-3,17-dione + NAD (P)H + H+. The 3 substRates of this enzyme are androsterone, NAD+, and NADP+, whereas its 4 products are 5alpha-androstane-3,17-dione, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor, more specifically it is part of the group of hydroxysteroid dehydrogenases. Group: Enzymes. Synonyms: hydroxyprostaglandin dehydrogenase; 3α-hydroxysteroid oxidoreductase; sterognost 3α; 3α-hydroxysteroid dehydrogenase (B-specific); 3α-hydroxysteroid 3-dehydrog. Enzyme Commission Number: EC 1.1.1.50. CAS No. 9028-56-2. 3α-Hydroxysteroid Dehydrogenase. Activity: > 15 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salt and EDTA. Source: Pseudomonas testosteroni. hydroxyprostaglandin dehydrogenase; 3α-hydroxysteroid oxidoreductase; sterognost 3α; 3α-hydroxysteroid dehydrogenase (B-specific); 3α-hydroxysteroid 3-dehydrogenase (B-specific); 3α-hydroxysteroid:NAD (P)+ 3-oxidoreductase (B-specific); EC 1.1.1.50. Cat No: NATE-0007. | |
| Native Rabbit Aldolase | Fructose-bisphosphate aldolase (EC 4.1.2.13), often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate. Gluconeogenesis and the Calvin cycle, which are anabolic pathways, use the reverse reaction. Glycolysis, a catabolic pathway, uses the forward reaction. Aldolase is divided into two classes by mechanism. Applications: Aldolase is used to convert fructose 1,6-diphosphate to dihydroxyacetone p...aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Enzyme Commission Number: EC 4.1.2.13. CAS No. 9024-52-6. Aldolase. Activity: Type I, lyophilized powder, > 8.0 units/mg protein; Type II, ammonium sulfate suspension, 10-20 units/mg protein. Storage: -20°C. Form: lyophilized powder. Essentially sulfate-free containing Citrate buffer salts. Source: Rabbit muscle. Species: Rabbit. aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Cat No: NATE-0048. | |
| Native Rabbit Glyceraldehyde-3-phosphate Dehydrogenase | Glyceraldehyde-3-phosphate dehydrogenase catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as part of glycolysis. It has also been shown to have roles in initiation of apoptosis, transcription activation and the shuttling of ER to Golgi vesicles. Group: Enzymes. Synonyms: EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phospha. Enzyme Commission Number: EC 1.2.1.12. CAS No. 9001-50-7. Glyceraldehyde-3-phosphate Dehydrogenase. Activity: > 75 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Citrate buffer salts. Source: Rabbit muscle. Species: Rabbit. EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phosphate dehydrogenase (NAD+); glyceraldehyde-3-phosphate dehydrogenase (NAD+); NADH-glyceraldehyde phosphate dehydrogenase; glyceraldehyde-3-P-dehydrogenase; 9001-50-7. Cat No: NATE-0281. | |
| Native Rabbit Phosphoglucose Isomerase | Phosphoglucose Isomerase (PGI) is an enzyme crucial for the interconversion of D-glucose 6-phosphate and D-fructose 6-phosphate. PGI is responsible for the second step of glycolysis and is involved in glucogenesis. It is highly conserved in bacteria and eukaryotes. Applications: Phosphoglucose isomerase (pgi) is an enzyme crucial for the interconversion of d-glucose 6-phosphate and d-fructose 6-phosphate. pgi is responsible for the second step of glycolysis and is involved in glucogenesis. it is highly conserved in bacteria and eukaryotes. it is used in sugar assays to convert fructose to glucose. this product is type xi and is from rabbit muscle. it is useful in enzyme systems requiring low sulfate. Group: Enzymes. Synonyms: Glucose-6-phosphate isomerase. Enzyme Commission Number: EC 5.3.1.9. CAS No. 9001-41-6. PGI. Activity: > 200 units/mg protein. Storage: -20°C. Form: lyophilized powder; Essentially sulfate-free powder containing Citrate buffer salts. Source: Rabbit muscle. Species: Rabbit. Glucose-6-phosphate isomerase; EC 5.3.1.9; phosphohexose isomerase; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; phosphoglucose isomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase; 9001-41-6; PGI. Cat No: NATE-0555. | |
| Native Rabbit Triosephosphate Isomerase | Triose-phosphate isomerase (TPI or TIM) is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. Applications: Triosephosphate isomerase has been used in a study to assess molecular characterizations of cryptosporidium, giardia, and enter ...e phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3. Enzyme Commission Number: EC 5.3.1.1. CAS No. 9023-78-3. TPI. Activity: Type I, > 4,000 units/mg protein; Type II, > 3,500 units/mg protein. Storage: -20°C. Form: Type I, ammonium sulfate suspension; Crystalline suspension in 3.2 M (NH4)2SO4 solution, pH 6.0; Type II, lyophilized powder, Sulfate-free, contains EDTA and borate buffer salts. Source: Rabbit muscle. Species: Rabbit. Triose-phosphate isomerase; phosphotriose isomerase; triose phosphoisomerase; triose phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3. Cat No: NATE-0712. | |
| Native Rhodopseudomonas sphaeroides β-Hydroxybutyrate Dehydrogenase | In mammalian systems, β-hydroxybutyrate dehydrogenase is localized on the inner mitochondrial membrane and requires phosphatidyl choline for activity. In contrast, the enzyme from Pseudomonas is a soluble cytosolic enzyme that does not require a phospholipid allosteric activator. The enzyme is required for the utilization of ketone bodies as a source of metabolic energy. It catalyzes the oxidation of 3-hydroxybutyrate to acetoacetate, the first step in the conversion of ketone bodies to citric acid, which is then further metabolized via the tricarboxylic acid cycle (Krebs cycle). Applications: Suitable for the determination of acetoacetate and d (-)-3...nase; EC 1.1.1.30; 9028-38-0. Enzyme Commission Number: EC 1.1.1.30. CAS No. 9028-38-0. 3-HBDH. Activity: 250-750 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Rhodopseudomonas sphaeroides. 3-hydroxybutyrate dehydrogenase; 3-HBDH; NAD-β-hydroxybutyRate dehydrogenase; hydroxybutyRate oxidoreductase; β-hydroxybutyRate dehydrogenase; D-β-hydroxybutyRate dehydrogenase; D-3-hydroxybutyRate dehydrogenase; D-(-)-3-hydroxybutyRate dehydrogenase; β-hydroxybutyric acid dehydrogenase; 3-D-hydroxybutyRate dehydrogenase; β-hydroxybutyric dehydrogenase; EC 1.1.1.30; 9028-38-0. Cat No: NATE-0004. | |
| Native Streptococcus faecalis Ornithine Transcarbamylase | Ornithine transcarbamylase (OTC) is an enzyme that catalyzes the reaction between carbamoyl phosphate (CP) and ornithine (Orn) to form citrulline (Cit) and phosphate (Pi). In plants and microbes, OTC is involved in arginine (Arg) biosynthesis, whereas in mammals it is located in the mitochondria and is part of the urea cycle. Group: Enzymes. Synonyms: Ornithine transcarbamylase; EC 2.1.3.3; citrulline phosphorylase; ornithine transcarbamylase; OTC; OTCase; carbamylphosphate-ornithine transcarbamylase; L-ornithine carbamoyltransferase; L-ornithine carbamyltransferase; L-ornithine transcarbamylase; ornithine carbamyltransferase; 9001-69-8. Enzyme Commission Number: EC 2.1.3.3. CAS No. 9001-69-8. OTC. Activity: > 600 units/mg protein. Storage: -20°C. Form: Lyophilized powder contains Tris buffer salts. Source: Streptococcus faecalis. Ornithine transcarbamylase; EC 2.1.3.3; citrulline phosphorylase; ornithine transcarbamylase; OTC; OTCase; carbamylphosphate-ornithine transcarbamylase; L-ornithine carbamoyltransferase; L-ornithine carbamyltransferase; L-ornithine transcarbamylase; ornithine carbamyltransferase; 9001-69-8. Cat No: NATE-0499. | |
| Native Streptomyces griseus Chitosanase | 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. Applications: Chitosanase from streptomyces griseus has been used in a study to assess the effect of chitin sources on production of chitinase and chitosanase. chitosanase from streptomyces griseus has also been used in a study to investigate the effective production of chitinase an...cete aphanomyces euteiches, a major parasite of legume plants. it has also been used for the enzymatic hydrolysis of the fully de-n-acetylated chitosan to get chitosan oligomer mixtures during the preparation of biocompatible chitosan-alginate gel. 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. Chitosanase. Activity: >50 units/mg protein (Bradford). Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Streptomyces griseus. Chitosanase; EC 3.2.1.132; 51570-20-8; Chitosan N-acetylglucosaminohydrolase. Cat No: NATE-0125. | |
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