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| Product | Description | |
|---|---|---|
| Biuret | 100g Pack Size. Group: Organics. Formula: C2H5N3O2. CAS No. 108-19-0. Prepack ID 12779060-100g. Molecular Weight 103.08. See USA prepack pricing. |  |
| Biuret | Biuret. Group: Biochemicals. Alternative Names: Allophanic acid amide; Carbamoylurea. Grades: Highly Purified. CAS No. 108-19-0. Pack Sizes: 50g, 100g, 250g, 500g, 1kg. Molecular Formula: NH2CONHCONH2. US Biological Life Sciences. |  Worldwide |
| Biuret | Biuret. Uses: For analytical and research use. Group: Impurity standards. CAS No. 108-19-0. Molecular Formula: C2H5N3O2. Mole Weight: 103.08. Catalog: APB108190. |  |
| Biuret-15N3 | Biuret-15N3 is the 15N3 labelled analogue of Biuret (B591500) which is used as a source of non-protein nitrogen in feed for ruminant. It is an impurity of urea based fertilisers as it has a poisonous effect on plants if present in high concentrations. Like peptide bonds, biuret forms violet-colored complexes with copper(II) ion in alkaline solution. This color change response is used to identify and quantify protein concentration (due to peptides present) and is known as biuret test. Group: Biochemicals. Grades: Highly Purified. CAS No. 287484-46-2. Pack Sizes: 1mg, 5mg. Molecular Formula: C2H515N3O2, Molecular Weight: 106.06. US Biological Life Sciences. | Worldwide |
| Biuret 98+% | Biuret 98+%. Group: Biochemicals. Grades: Reagent Grade. Pack Sizes: 25g, 100g, 250g, 1Kg. US Biological Life Sciences. | Worldwide |
| biuret amidohydrolase | Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.54 (allophanate hydrolase), this enzyme forms part of thecyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria.Urea-1-carboxylate rather than urea (as was thought previously) is the 2-nitrogen intermediate in cyanuric-acid metabolism in bacteria. The product, urea-1-carboxylate,can spontaneously decarboxylate under acidic conditions to form urea but, under physiological conditions, it can be converted into CO2 and ammonia by the action of EC 3.5.1.54. Group: Enzymes. Enzyme Commission Number: EC 3.5.1.84. CAS No. 95567-88-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4475; biuret amidohydrolase; EC 3.5.1.84; 95567-88-7. Cat No: EXWM-4475. |  |
| Biuret Powder, Laboratory Grade, 50 g | Biuret Powder, Laboratory Grade, 50 g. Notes: This powder is not used to make biuret. It is a positive control to let you know your biuret solution is working properly. Storage Code: Green; general chemical storage. Grades: chem-grade laboratory. Product ID: 848202. -- SOLD FOR EDUCATIONAL USE ONLY -- |  |
| Biuret Reagent, Laboratory Grade, 100 mL | Characteristic: Blue. Notes: Solution changes from blue to violet in the presence of protein. Storage Code: White; corrosive. DOT Class: Corrosive. Grades: chem-grade laboratory. Product ID: 848211. -- SOLD FOR EDUCATIONAL USE ONLY -- | |
| Biuret Reagent, Laboratory Grade, 1 L | Characteristic: Blue. Notes: Solution changes from blue to violet in the presence of protein. Storage Code: White; corrosive. DOT Class: Corrosive. Grades: chem-grade laboratory. Product ID: 848214. -- SOLD FOR EDUCATIONAL USE ONLY -- | |
| Biuret Reagent, Laboratory Grade, 30 mL | Characteristic: Blue. Notes: Solution changes from blue to violet in the presence of protein. Storage Code: White; corrosive. DOT Class: Corrosive. Grades: chem-grade laboratory. Product ID: 848209. -- SOLD FOR EDUCATIONAL USE ONLY -- | |
| Biuret Reagent, Laboratory Grade, 4 L | Characteristic: Blue. Notes: Solution changes from blue to violet in the presence of protein. Storage Code: White; corrosive. DOT Class: Corrosive. Grades: chem-grade laboratory. Product ID: 848215. -- SOLD FOR EDUCATIONAL USE ONLY -- | |
| Biuret Reagent, Laboratory Grade, 500 mL | Characteristic: Blue. Notes: Solution changes color from blue to violet in the presence of protein. Storage Code: White; corrosive. DOT Class: Corrosive. Grades: chem-grade laboratory. Product ID: 848213. -- SOLD FOR EDUCATIONAL USE ONLY -- | |
| Biuret Solution | Biuret Solution. Pack Sizes: Milliliter Quantities: 6 x 500 ml, 6 x 1 L. Order Number: 62425. |  www.prochemonline.com |
| 1-tert-Butyl-3-isopropyl-5-phenyl-2-biuret | Heterocyclic Organic Compound. Alternative Names: 1-tert-Butyl-3-isopropyl-5-phenyl-2-biuret;N-(1,1-Dimethylethyl)-2-(1-methylethyl)-N'-phenyl-imidodicarbonic diamide. CAS No. 107484-83-3. Molecular formula: C15H23N3O2. Mole weight: 277.36. Catalog: ACM107484833. |  |
| Adenosine deaminase Bovine, Recombinant | Adenosine deaminase is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system. Protein determined by biuret. Applications: Adenosine deaminase is useful in various molecular biology assays, such as glycerol release assays. adenosine deaminase is a potential target for treatments of combined immunodeficiency disease. Group: Enzymes. Synonyms: ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Enzyme Commission Number: EC 3.5.4.4. CAS No. 9026-93-1. ADA. Mole weight: 32.5-33 kDa. Activity: 60-130 units/mg protein; > 130 units/mg protein; 150-200 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.2 M (NH4)2SO4, 0.01 M potassium phosphate, pH 6.0. Source: E. coli. Species: Bovine. ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Cat No: NATE-0032. | |
| allophanate hydrolase | Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of thecyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 6.3.4.6, urea carboxylase, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate. The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate. Group: Enzymes. Synonyms: allophanate lyase; AtzF; TrzF. Enzyme Commission Number: EC 3.5.1.54. CAS No. 9076-72-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4443; allophanate hydrolase; EC 3.5.1.54; 9076-72-6; allophanate lyase; AtzF; TrzF. Cat No: EXWM-4443. | |
| 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. | |
| cyanuric acid amidohydrolase | Along with EC 3.5.1.54 (allophanate hydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of the cyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. This is a key enzyme in the pathway, catalysing the ring cleavage of cyanuric acid. The enzyme is specific for cyanuric acid as substrate as neither the structurally related compounds ammeline (2,4-diamino-6-hydroxy-s-triazine) and ammelide (2-amino-4,6-dihydroxy-s-triazine) nor a number of pyrimidine compounds, such as uracil and cytosine, can act as substrates. Group: Enzymes. Synonyms: AtzD. Enzyme Commission Number: EC 3.5.2.15. CAS No. 132965-78-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4498; cyanuric acid amidohydrolase; EC 3.5.2.15; 132965-78-7; AtzD. Cat No: EXWM-4498. | |
| 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. | |
| Low endotoxin gelatin from porcine skin | Gelatin is a protein product obtained from the degradation of collagen. It is almost odorless and tasteless. It absorbs water and swells in cold water, and can swell to 5 to 12 times its original weight. Soluble in hot water, glycerol and acetic acid, insoluble in ethanol, ether, chloroform and other organic solvents. It can be stored for a long time in dry conditions, and it is easily deteriorated by bacteria when exposed to moisture in humid air. Gelatin is a kind of macromolecular hydrophilic colloid, which is partially degraded by collagen in connective tissues such as animal skin, bone, sarcolemma, and muscle to become white or light yellow, translucent, slightly glossy flakes or powders. Gelatin is widely used in food, pharmaceutical and chemical industries. Uses: ·vaccines and injectables ·cross-linking group functionalization ·inkjet printing and two-photon polymerization. Group: Natural polymers and biopolymers. CAS No. 9000-70-8. Molecular formula: ≤ 6500. ≥70 % protein basis (biuret). |  |
| Native Achromobacter lyticus Achromopeptidase | Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase) is an enzyme. This enzyme catalyses the following chemical reaction:Preferential cleavage:Lys-, including-Lys-Pro-. This enzyme is isolated from Achromobacter lyticus. Group: Enzymes. Synonyms: Achromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; EC 3.4.21.50; 123175-82-6; Lysyl endopeptidase. Enzyme Commission Number: EC 3.4.21.50. CAS No. 123175-82-6. Achromopeptidase. Storage: -20°C. Form: lyophilized powder, Protein ~5 % by biuret, 300-600 units/mg solid. Source: Achromobacter lyticus. Achromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; EC 3.4.21.50; 123175-82-6; Lysyl endopeptidase. Cat No: NATE-0021. | |
| Native Aerobacter aerogenes Sulfatase | Sulfatases EC 3.1.6.1 are enzymes of the esterase class that catalyze the hydrolysis of sulfate esters. These may be found on a range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. In the latter case the resultant N-sulfates can also be termed sulfamates. Sulfatases play important roles in the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodelling sulfated glycosaminoglycans in the extracellular space. Together with sulfotransferases, sulfatases form the major catalytic machinery for the synthesis and breakage o...17-5; sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; arylsulfatase. Enzyme Commission Number: EC 3.1.6.1. CAS No. 9016-17-5. Sulfatases. Activity: 2-5 units/mg protein (biuret), 10-20 units/mL. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 0.01 M Tris, pH 7.5. Source: Aerobacter aerogenes. EC 3.1.6.1; 9016-17-5; sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; arylsulfatase. Cat No: NATE-0686. | |
| Native Almonds Mandelonitrile Lyase | In enzymology, a mandelonitrile lyase is an enzyme that catalyzes the chemical reaction:mandelonitrile<-> hydrogen cyanide + benzaldehyde. Hence, this enzyme has one substrate, mandelonitrile, and two products, hydrogen cyanide and benzaldehyde. This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. This enzyme participates in cyanoamino acid metabolism. It has 2 cofactors:flavin, and flavoprotein. Mandelonitrile lyase is a cyanogenic enzyme. Applications: Mandelonitrile lyase from almonds has been used in a study to assess the apoplastic antioxidant system in prunus. it has also been used in a study to investigate screening for new hydroxynitrilases from plants. Group: Enzymes. Synonyms: mandelonitrile lyase; EC 4.1.2.10; (R)-oxynit. Enzyme Commission Number: EC 4.1.2.10. CAS No. 9024-43-5. PhaMDL. Activity: 80-240 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 50 mM imidazole, 2.8 M (NH4)2SO4, pH 6.0. Source: Almonds. mandelonitrile lyase; EC 4.1.2.10; (R)-oxynitrilase; oxynitrilase; D-oxynitrilase; D-α-hydroxynitrile lyase; mandelonitrile benzaldehyde-lyase; PaHNL; AtHNL; PhaMDL; (R)-HNL; (R)-PeHNL; (R)-hydroxynitrile lyase; R-selective hydroxynitrile lyase; R-selective HNL; (R)-(+)-mandelonitrile lyase; 9024-43-5. Cat No: NATE-0557. | |
| Native Arthrobacter globiformis Uricase | The enzyme urate oxidase (UO) catalyzes the oxidation of uric acid to 5-hydroxyisourate:Uric acid + O2 + H2O ? 5-hydroxyisourate + H2O2 ? allantoin + CO2. Group: Enzymes. Synonyms: uric acid oxidase; uricase; uricase II; urate oxidase; factor-independent urate hydroxylase; EC 1.7.3.3; 9002-12-4; UO. Enzyme Commission Number: EC 1.7.3.3. CAS No. 9002-12-4. UO. Mole weight: 4 × ~32 KDa (tetramer). Activity: 15-30 units/mg protein (biuret). Storage: -20°C. Form: lyophilized powder. Source: Arthrobacter globiformis. uric acid oxidase; uricase; uricase II; urate oxidase; factor-independent urate hydroxylase; EC 1.7.3.3; 9002-12-4; UO. Cat No: NATE-0729. | |
| Native Arthrobacter luteus Lyticase | Lyticase hydrolyzes poly-β (1?3)-glucose such as yeast cell wall glucan. Applications: Yeast cells are difficult to disrupt because the cell walls may form capsules or resistant spores. dna can be extracted from yeast by using lysing enzymes such as lyticase, chitinase, zymolase, and gluculase to induce partial spheroplast formation; spheroplasts are subsequently lysed to release dna. lyticase is preferred to digest cell walls of yeast and generate spheroplasts from fungi for transformation. reported to be useful for lysis of ashbya, candida, debaryomyces, eremothecium, endomyces, hansenula, hanseniaspora, kloeckera, kluyveromyces, lipomyces, metschikowia, pichia, pullularia, torulopsis, saccharomyces, saccharomycopsis, saccharomycodes, and schwanniomyces species. Group: Enzymes. Synonyms: Lyticase; 37340-57-1. CAS No. 37340-57-1. Lyticase. Activity: > 200 units/mg solid; > 1,500 units/mg protein; > 2,000 units/mg protein, Protein > 20 % by biuret. Storage: 2-8°C. Form: lyophilized powder. Source: Arthrobacter luteus. Lyticase; 37340-57-1. Cat No: NATE-0431. | |
| Native Aspergillus oryzae α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. amylases from aspergillus oryzae are commonly used as baking additives to prevent staling in the baking industry, clarify haze from fruit juices and alcoholic beverages, and to produce glucose and maltose syrup products. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Mole weight: Mr ~51 kDa. Activity: > 150 units/mg protein (biuret); ~1.5 units/mg; ~30 units/mg. Storage: -20°C. Form: powder containing dextrin. Source: Aspergillus oryzae. 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-0740. | |
| Native Bacillus licheniformis α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. this product is from bacillus licheniformis and is type xii-a. α-amylase, from creative enzymes, has been used in various plant studies, such as metabolism studies in arabidopsis. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Activity: Type XII-A, saline solution, > 500 units/mg protein (biuret); Type B, liquid. Source: Bacillus licheniformis. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0742. | |
| Native Bacillus stearothermophilus 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. 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: > 75 units/mg protein (biuret). Storage: 2-8°C. Form: buffered aqueous solution; Stabilized solution in Tris buffer, pH 7.3. Source: Bacillus stearothermophilus. EC 2.7.1.30; glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase; 9030-66-4. Cat No: NATE-0286. | |
| Native Bacillus stearothermophilus 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. 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. Inorganic pyrophosphatase. Activity: 15-25 units/mg protein (biuret). Storage: 2-8°C. Form: lyophilized powder. Source: Bacillus stearothermophilus. Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-0353. | |
| Native Bacillus stearothermophilus Phosphotransacetylase | Phosphotransacetylase converts CoA to acetyl CoA. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. This enzyme participates in 3 metabolic pathways:taurine and hypotaurine metabolism, pyruvate metabolism, and propanoate metabolism. Applications: Phosphotransacetylase, from bacillus stearothermophilus, is used to convert coa to acetyl coa. phosphotransacetylase (pta) is used to study transport systems for acetate. it is used to study metabolic pathways in various bacterium. Group: Enzymes. Synonyms: phosphate acetyltransferase; phosphotransacetylase; phosphoacylase; PTA; EC 2.3.1.8; 9029-91-8. Enzyme Commission Number: EC 2.3.1.8. CAS No. 9029-91-8. PTA. Activity: > 3,000 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized powder containing potassium phosphate. Source: Bacillus stearothermophilus. phosphate acetyltransferase; phosphotransacetylase; phosphoacylase; PTA; EC 2.3.1.8; 9029-91-8. Cat No: NATE-0641. | |
| Native Baker's yeast (S. cerevisiae) Glutathione Reductase | Glutathione reductase (GR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the precess is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl ...reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Enzyme Commission Number: EC 1.6.4.2. CAS No. 9001-48-3. GR. Mole weight: mol wt 118 kDa. Activity: 100-300 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4, pH 7.0, containing 0.1 mM dithiothreitol. Source: Baker's yeast (S. cerevisiae). EC 1.6.4.2; 9001-48-3; Glutathione Reductase; GR; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Cat No: NATE-0317. | |
| Native Baker's yeast (S. cerevisiae) Pyruvate Decarboxylase | Pyruvate decarboxylase (PDC) is a homotetrameric enzyme that catalyses the decarboxylation of pyruvic acid to acetaldehyde and carbon dioxide in the cytoplasm. Pyruvate decarboxylase depends on cofactors thiamine pyrophosphate (TPP) and magnesium. PDC contains a β-α-β structure, yielding parallel β-sheets. Applications: Pyruvate decarboxylase (pdc) is used to study residues involved in thiamine pyrophosphate (tpp) binding. it is used to study the regulation of fermentation pathways in plant species. Group: Enzymes. Synonyms: Pyruvate decarboxylase; EC 4.1.1.1; α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase; 9001-04-1; 2-Oxo-acid carboxy-lyase; PDC. Enzyme Commission Number: EC 4.1.1.1. CAS No. 9001-4-1. PDC. Activity: 5.0-20.0 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.2 M (NH4)2SO4 pH 6.5, stabilized with 5% glycerol, 5 mM potassium phosphate, 1 mM magnesium acetate, 0.5 mM EDTA, and 25 μM c ocarboxylase. Source: Baker's yeast (S. cerevisiae). Pyruvate decarboxylase; EC 4.1.1.1; α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase; 9001-04-1; 2-Oxo-acid carboxy-lyase; PDC. Cat No: NATE-0510. | |
| 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 Barley β-Amylase | β-Amylase hydrolyzes the α-(1,4) glucan linkages in polysaccharides of three or more α-(1,4) linked D-glucose units. Natural substrates such as starch and glycogen are broken down into glucose and maltose. Pure, crystalline β-amylase preparation consists of four isoenzymes with different isoelectric points. The enzyme polymerizes very rapidly through the sulfhydryl groups in the absence of reducing agents. p-Chloromercuribenzoate inhibits the polymerization and the enzymatic activity. The reducing agents mercaptoethanol or dithiothreitol can completely restore the activity. Applications: Β-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. β-amylase, has been used in various plant studies, such as carbon starvation studies in populus tremuloides. β-amylase, from barley, has been used to study how pressure and temperature affect catalytic activity. Group: Enzymes. Synonyms: saccharogen amylase; glycogenase; β amylase, β-amylase; 1,4-α-D-glucan maltohydrola. Enzyme Commission Number: EC 3.2.1.2. CAS No. 9000-91-3. β-Amylase. Activity: 20-80 units/mg protein (biuret). Storage: 2-8°C. Source: Barley. saccharogen amylase; glycogenase; β amylase, β-amylase; 1,4-α-D-glucan maltohydrolase; EC 3.2.1.2; 9000-91-3. Cat No: NATE-0761. | |
| Native β-hemolytic Streptococcus Streptokinase | Streptokinase (SK) is an enzyme secreted by several species of streptococci that can bind and activate human plasminogen. SK is used as an effective and inexpensive thrombolysis medication in some cases of myocardial infarction (heart attack) and pulmonary embolism. Streptokinase belongs to a group of medications known as fibrinolytics, and complexes of streptokinase with human plasminogen can hydrolytically activate other unbound plasminogen by activating through bond cleavage to produce plasmin. There are three domains to Streptokinase, denoted α (residues 1-150), β (residues 151-287), and γ (residues 288-414). Each domain binds plasminogen, altho...bral hemorrhage. streptokinase is also used in the treatment of complicated parapneumonic effusions and empyema where adverse reactions, allergic type, are rare. streptokinase has been used in a study to compare primary coronary intervention and thrombolytic therapy in my ocardial infarction patients. Group: Enzymes. Synonyms: Streptokinase; SK; EC 3.4.99.0; 9002-01-1. Enzyme Commission Number: EC 3.4.99.0. CAS No. 9002-1-1. SK. Activity: > 3,500 units/mg solid. Storage: -20°C. Form: Lyophilized powder containing ~50% total protein by biuret and sodium glutamate. Total protein composed of enzyme protein and human serum albumin. Source: β-hemolytic Streptococcus | |
| Native Bovine α-L-Fucosidase | In enzymology, an alpha-L-fucosidase (EC 3.2.1.51) is an enzyme that catalyzes the chemical reaction:an alpha-L-fucoside + H2O<-> L-fucose + an alcohol. Thus, the two substrates of this enzyme are alpha-L-fucoside and H2O, whereas its two products are L-fucose and alcohol. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O-and S-glycosyl compounds. This enzyme participates in n-glycan degradation and glycan structures-degradation. Group: Enzymes. Synonyms: α-L-Fucosidase; EC 3.2.1.51; α-fucosidase. Enzyme Commission Number: EC 3.2.1.51. CAS No. 9037-65-4. FUCA. Activity: > 2.0 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.2 M (NH4)2SO4, 10 mM NaH2PO4 10 mM Citrate, pH 6.0. Source: Bovine kidney. Species: Bovine. α-L-Fucosidase; EC 3.2.1.51; α-fucosidase. Cat No: NATE-0266. | |
| Native Bovine Cholesterol Esterase | Cholesterol esterase (CE) is a reversible enzyme that can hydrolyze or synthesize fatty acid esters of cholesterol and other sterols. Hydrolysis of water insoluble long chain fatty acid esters requires bile salt activation. Hydrolysis of water soluble esters of short chain fatty acids and lysophospholipids does not require activation by bile salts. It also hydrolyzes tri-, di-, and mono-acylglycerols, phospholipids, lysophospholipids, and ceramide. This monomeric glycoprotein may have multiple functions in lipid and lipoprotein metabolism, as well as in atherosclerosis. Protein determined by biuret. Applications: Cholesterol esterase bound to membrane-associated heparin on b...terase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; 9026-00-0; sterol esterase; CE. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Cholesterol Esterase. Activity: > 200 units/g protein. Storage: -20°C. Form: Lyophilized powder. This product is partially purified from bovine pancreas and is supplied as an off-white to tan lyophilized powder containing 30-65% protein (biuret), potassium phosphate. Source: Bovine pancreas. Species: Bovine. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrol | |
| Native Bovine Creatine Phosphokinase | Creatine kinase plays a key role in the energy metabolism of cells with intermittently high and fluctuating energy requirements. Examples of such cells include cardiac or skeletal muscle cells and neural tissues of brain and retina. The enzyme catalyzes the reversible transfer of the phosphoryl group from phosphorylcreatine to ADP, in order to generate ATP.1 The molecular mass of the protein is found to be approximately 80 kDa Da. It is made up of 2 subunits, each having a molecular weight of 40 kDa ± 2000. The lighter subunit is present in larger amounts. Protein determined by biuret. Applications: Creatine phosphokinase from bovine heart has been used to investigate wheth...osphotransferase; CK; CPK; MM-CK; MB-CK; BB-CK; creatine phosphokinase; creatine phosphotransferase; phosphocreatine kinase; adenosine triphosphate-creatine transphosphorylase; Mi-CK; CK-BB; CK-MM; CK-MB; CKMiMi; MiMi-CK; 9001-15-4. Enzyme Commission Number: EC 2.7.3.2. CAS No. 9001-15-4. Activity: > 100 U/mg. Storage: -20°C. Form: salt-free, lyophilized powder. Source: Bovine heart. Species: Bovine. EC 2.7.3.2; ATP:creatine phosphotransferase; CK; CPK; MM-CK; MB-CK; BB-CK; creatine phosphokinase; creatine phosphotransferase; phosphocreatine kinase; adenosine triphosphate-creatine transphosphorylase; Mi-CK; CK-BB; CK-MM; CK-MB; CKMiMi; MiMi-CK; 9001-15-4. Cat No: NATE-0136. | |
| Native Bovine Deoxyribonuclease I | Deoxyribonuclease I (usually called DNase I), is an endonuclease coded by the human gene DNASE1. DNase I is a nuclease that cleaves DNA preferentially at phosphodiester linkages adjacent to a pyrimidine nucleotide, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3', on average producing tetranucleotides. It acts on single-stranded DNA, double-stranded DNA, and chromatin. In addition to its role as a waste-management endonuclease, it has been suggested to be one of the deoxyribonucleases responsible for DNA fragmentation during apoptosis. Protein determined by biuret. Applications: Used for the removal of dna from protein samples. dnase...rom bovine pancreas has also been used in a study to investigate the effects of minor and major groove-binding drugs and intercalators on the dna association of minor groove-binding proteins reca and deoxyribonuclease i. Group: Enzymes. Synonyms: DNASE1; deoxyribonuclease I; deoxyribonuclease-1; DNase I; 9003-98-9; EC 3.1.21.1; pancreatic DNase; DNase; thymonuclease, dornase; dornava; dornavac; pancreatic deoxyribonuclease; pancreatic dornase; deoxyribonuclease (pancreatic); pancreatic DNase; DNAase; deoxyribonucleic phosphatase; alkaline deoxyribonuclease; alkaline DNase; endodeoxyribonuclease I; DNA depolymerase; Escherichia coli endonuclease I; deoxyribonuclease A; DNA end | |
| Native Bovine L-Arginase | Arginase (EC 3.5.3.1, arginine amidinase, canavanase, L-arginase, arginine transamidinase) is a manganese-containing enzyme. The reaction catalyzed by this enzyme is:arginine + H2O ? ornithine + urea. It is the final enzyme of the urea cycle. It is ubiquitous to all domains of life. Group: Enzymes. Synonyms: Arginase; arginine amidinase; canavanase; L-arginase; arginine transamidinase; EC 3.5.3.1. Enzyme Commission Number: EC 3.5.3.1. CAS No. 9000-96-8. Purity: Protein > 70 % by biuret. Arginase. Storage: -20°C. Form: powder. Source: Bovine liver. Species: Bovine. Arginase; arginine amidinase; canavanase; L-arginase; arginine transamidinase; EC 3.5.3.1. Cat No: NATE-0379. | |
| Native Bovine Nucleoside 5'-Diphosphate Kinase | Nucleoside-diphosphate kinases are enzymes that catalyze the exchange of phosphate groups between different nucleoside diphosphates. NDK activities maintain an equilibrium between the concentrations of different nucleoside triphosphates such as, for example, when GTP produced in the citric acid (Krebs) cycle is converted to ATP. Nucleoside Diphosphate Kinase exists in two isoforms in eukaryotic cells, NDK-A and NDK-B. These enzymes are found expressed both in the mitochondria and the cytoplasm. Nucleoside diphosphate kinase exists in two isoforms in eukaryotic cells, ndk-a and ndk-b. these enzymes are found expressed both in the mit ochondria and the cytoplasm. Applica...cleotide phosphate kinase; UDP kinase; uridine diphosphate kinase; ATP:nucleoside diphosphate phosphotransferase; NDPK; NDKs; NDP Kinase; EC 2.7.4.6; 9026-51-1. Enzyme Commission Number: EC 2.7.4.6. CAS No. 9026-51-1. NDPK. Activity: > 1,000 units/mg protein (biuret). Storage: 2-8°C. Form: buffered aqueous glycerol solution. Source: Bovine liver. Species: Bovine. nucleoside-diphosphate kinase; nucleoside 5'-diphosphate kinase; nucleoside diphosphate (UDP) kinase; nucleoside diphosphokinase; nucleotide phosphate kinase; UDP kinase; uridine diphosphate kinase; ATP:nucleoside diphosphate phosphotransferase; NDPK; NDKs; NDP Kinase; EC 2.7.4.6; 9026-51-1. Cat No: NATE-0477. | |
| Native Bovine Protein Kinase A | Protein Kinase A (PKA) catalyzes the transfer of the terminal phosphate of ATP to threonine or serine residues in a variety of protein substrates. The enzyme is composed of two subunit types: a catalytic subunit and a regulatory subunit. In the absence of cAMP, the two subunits are bound to each other and no catalysis can take place. In the presence of cAMP, the regulatory subunit binds cAMP, thus releasing the catalytic subunit. Group: Enzymes. Synonyms: Protein kinase A; PKA; Protein Kinase; 3',5'-cyclic-AMP-dependent Protein Kinase. Enzyme Commission Number: EC 2.7.11.11. CAS No. 9026-43-1. PKAC. Activity: >0.4 units/μg protein. Storage: Store the product at -20 °C. The dry solid is shipped at ambient temperature with minimal loss in activity. When stored at -20 °C with desiccant, the protein will lose <10% activity per year. Form: Lyophilized from a solution containing: 5-10% potassium phosphate buffer, pH 7.5, 5-10% EDTA, and 80-90% protein (biuret assay). Source: Bovine heart. Species: Bovine. Protein kinase A; PKA; Protein Kinase; 3',5'-cyclic-AMP-dependent Protein Kinase. Cat No: NATE-1944. | |
| Native Bovine Thrombin | Thrombin is a serine protease that in humans is encoded by the F2 gene. Prothrombin (coagulation factor II) is proteolytically cleaved to form thrombin in the coagulation cascade, which ultimately results in the reduction of blood loss. Thrombin in turn acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzing many other coagulation-related reactions. Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects. Applications: Thrombin is used for site specific cleavage of recombinant fusion proteins containing an accessible thrombin recognition site for removal of ...Ia; E thrombin; β-thrombin; γ-thrombin. Enzyme Commission Number: EC 3.4.21.5. CAS No. 9002-4-4. Thrombin. Activity: 600-2,000 NIH units/mg protein (biuret) or > 2,000 NIH units/mg protein (E1%/280 = 19.5); > 125 NIH units/mg protein (biuret). Form: Type I, Lyophilized from saline sodium Citrate buffer, pH 6.5; Type II, buffered aqueous solution, In 0.05 M phosphate buffer, pH 7.0. Source: Bovine plasma. Species: Bovine. thrombin; 9002-04-4; EC 3.4.21.5; fibrinogenase; thrombase; thrombofort; topical; thrombin-C; tropostasin; activated blood-coagulation factor II; blood-coagulation factor IIa; factor IIa; E thrombin; β-thrombin; γ-thrombin. Cat No: NATE-0698. | |
| Native Bovine Trypsin Acetylated | Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized. The trypsin molecule has two domains: one is related to the enzyme active site and the trypt...e bacterial multidrug atp-binding cassette transporter. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin; Acetyltrypsin. Enzyme Commission Number: EC 3.4.21.4. Trypsin. Activity: > 8,500 BAEE units/mg protein (biuret). Storage: -20°C. Source: Bovine pancreas. Species: Bovine. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin; Acetyltrypsin. Cat No: NATE-0720. | |
| Native Canavalia ensiformis (Jack bean) α-Mannosidase | α-Mannosidase is an acid hydrolase which is located in plant vacuoles and is thought to be involved with the turnover of N-linked glycoproteins. α-Mannosidase has been shown to inhibit the proliferation of B-lymphocytes. α-Mannosidase from Canavalia ensiformis is a tretamer composed of two subunits that each contain two components at 44 and 66 kDa. Applications: Liberates mannose from a variety of synthetic and natural α-mannosides. α-mannosidase can be used to liberate mannose from a variety of synthetic and natural α-mannosides. it has also been used in a study to investigate the causes of neurodegeneration in mucolipidosis ii ?knock-in? mice. Group: Enzymes. Synonyms: α-mannosidase; α-D-mannosidase; p-nitrophenyl-α-mannosidase; α-D-mannopyranosidase; 1,2-&a. Enzyme Commission Number: EC 3.2.1.24. CAS No. 9025-42-7. Mannosidase. Activity: > 15 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.0 M (NH4)2SO4 and 0.1 mM zinc acetate, pH 7.5. Source: Canavalia ensiformis (Jack bean). α-mannosidase; α-D-mannosidase; p-nitrophenyl-α-mannosidase; α-D-mannopyranosidase; 1,2-α-mannosidase; 1,2-α-D-mannosidase; exo-α-mannosidase; EC 3.2.1.24; 9025-42-7; Mannosidase. Cat No: NATE-0754. | |
| Native Chicken Myokinase | Adenylate kinase (EC 2.7.4.3) (also known as ADK or myokinase) is a phosphotransferase enzyme that catalyzes the interconversion of adenine nucleotides, and plays an important role in cellular energy homeostasis. Mutational analysis of the amino acid proline 17 of myokinase from chicken muscle is critical for structural stability, substrate binding and enzyme activity. Applications: Myokinase from chicken muscle has been used in a study to assess the release of enzymes via acute myositis and neurogenic atrophy in muscles. it has also been used in a study to investigate the development of sarcoplasmic reticulum membranes in chicken pectoralis muscle cells. Group: Enzymes. Synonyms: Adenylate kinase; EC 2.7.4.3; ADK; myokinase; 9013-02-9; Adenylic kinase; Adenylokinase. Enzyme Commission Number: EC 2.7.4.3. CAS No. 9013-2-9. Myokinase. Activity: 1,500-3 ,000 units/mg protein (biuret). Storage: -20°C. Form: essentially salt-free, lyophilized powder. Source: Chicken muscle. Species: Chicken. Adenylate kinase; EC 2.7.4.3; ADK; myokinase; 9013-02-9; Adenylic kinase; Adenylokinase. Cat No: NATE-0037. | |
| Native Clostridium kluyveri Diaphorase | Native Clostridium kluyveri Diaphorase. Applications: Diaphorase from clostridium kluyveri, or lipoyl dehydrogenase, has been used in a study to assess the protein-protein interactions in assembly of lipoic acid on the 2-oxoacid dehydrogenases of aerobic metabolism. lipoyl dehydrogenase has also been used in a study to investigate the redox regulation of tyrosine nitration and 3-nitrotyrosine reduction by antioxidants. Group: Enzymes. Synonyms: dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxidoreductase (NADH); lipoamide reductase; lipo. Enzyme Commission Number: EC 1.8.1.4. CAS No. 9001-18-7. Diaphorase. Activity: 3.0-20.0 units/mg protein (biuret). Storage: Store at -20°C. Form: Lyophilized powder. Source: Clostridium kluyveri. dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxidoreductase (NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate dehydrogenase; lipoic acid dehydrogenase; lipoyl dehydrogenase; dihydrolipoyl dehydrogenase; EC 1.8.1.4; 9001-18-7; Lipoamide Dehydrogenase. Cat No: NATE-0875. | |
| Native Crotalus adamanteus L-Amino Acid Oxidase | In enzymology, an L-amino acid oxidase (LAAO) (EC 1.4.3.2) is an enzyme that catalyzes the chemical reaction:an L-amino acid + H2O + O2<-> a 2-oxo acid + NH3 + H2O2. The enzyme was first described in 1944 by A. Zeller and A. Maritz. Not only are LAAOs quite variable in terms of molecular mass, they also vary widely regarding stability. In a similar vein, this enzyme performs in a myriad of biological activities including apoptosis-induction, edema-induction, hemorrhaging, and inhibition or induction of platelet aggregation. Applications: L-amino acid oxidase (laao) is used to convert l-amino acids to their corresponding α-keto acids. one unit will oxidatively de...w-injection pr ocedure with chemiluminescence detection for on-site determination of l-alanine. Group: Enzymes. Synonyms: L-amino acid oxidase; LAAO; L-AAO; EC 1.4.3.2; 9000-89-9; ophio-amino-acid oxidase; L-amino-acid:oxygen oxidoreductase (deaminating). Enzyme Commission Number: EC 1.4.3.2. CAS No. 9000-89-9. LAAO. Activity: Type I, > 0.3 unit/mg solid; Type II, > 3.0 units/mg protein (biuret). Storage: Type I, -20°C; Type II, 2-8°C. Form: Type I, dried venom; Type II, aqueous suspension. Source: Crotalus adamanteus. L-amino acid oxidase; LAAO; L-AAO; EC 1.4.3.2; 9000-89-9; ophio-amino-acid oxidase; L-amino-acid:oxygen oxidoreductase (deaminating). Cat No: NATE-0366. | |
| 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 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 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 Human Catalase | Catalase activates the decomposition of hydrogen peroxide, a reactive oxygen species, into water and oxygen. It functions as a natural antioxidant, protecting cells against oxidative damage to proteins, lipids and nucleic acids. Catalase has also been used to study the role reactive oxygen species play in gene expression and apoptosis. Protein determined by biuret. Group: Enzymes. Synonyms: EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase; 9001-05-2. Enzyme Commission Number: EC 1.11.1.6. CAS No. 9001-5-2. Purity: > 90% (SDS-PAGE). CAT. Mole weight: tetramer mol wt ~250 kDa. Activity: > 30,000 units/mg protein. Storage: -20°C. Form: buffered aqueous solution. Solution in 50 mM Tris, pH 8.0. Source: Human erythrocytes. Species: Human. EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase; 9001-05-2. Cat No: NATE-0108. | |
| Native Human Oxyhemoglobin | Hemoglobin is found in the erythrocytes of all vertebrates. It is a conjugated protein with the prosthetic group heme which contains iron. The heme group is involved with the transport of oxygen from the lungs to tissues, while the globin portion of hemoglobin plays a major role in transporting carbon dioxide from the tissues to the lungs. The iron in heme is in the ferrous state. In oxyhemoglobin, it is apparently still in the ferrous state, but the oxygen is loosely bound to it. Group: Others. Synonyms: Oxyhemoglobin; hemoglobin; Human Oxyhemoglobin. Purity: 90% (biuret). Activity: At least 50 U/mg protein. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Human Erythrocytes. Species: Human. Oxyhemoglobin; hemoglobin; Human Oxyhemoglobin. Cat No: NATE-1881. | |
| Native Human Thrombin | Thrombin is a serine protease that in humans is encoded by the F2 gene. Prothrombin (coagulation factor II) is proteolytically cleaved to form thrombin in the coagulation cascade, which ultimately results in the reduction of blood loss. Thrombin in turn acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzing many other coagulation-related reactions. Lyophilized powder containing sucrose, sodium chloride and tris. thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects. Group: Enzymes. Synonyms: thrombin; 9002-04-4; EC 3.4.21.5; fibrinogenase; thrombase; thrombofort; topical; thrombin-C; tropostasin; activated blood-coagulation factor II; blood-coagulation factor IIa; factor IIa; E thrombin; β-thrombin; γ-thromb. Enzyme Commission Number: EC 3.4.21.5. CAS No. 9002-4-4. Thrombin. Activity: 600-2,000 NIH units/mg protein (biuret) or > 2,000 NIH units/mg protein (E1%/280 = 19.5); > 125 NIH units/mg protein (biuret). Form: lyophilized powder. Source: Human plasma. Species: Human. thrombin; 9002-04-4; EC 3.4.21.5; fibrinogenase; thrombase; thrombofort; topical; thrombin-C; tropostasin; activated blood-coagulation factor II; blood-coagulation factor IIa; factor IIa; E thrombin; β-thrombin; γ-thrombin. Cat No: NATE-0699. | |
| 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 Lactobacillus leichmanii D-Lactic Dehydrogenase | D-lactic dehydrogenase catalyzes the conversion of D-lactate into D-pyruvate while reducing NAD+ to NADH and H+. Applications: In the food industry, the primary catalysis is coupled to conversion of nadh and h+ to nad+ with diaphorase coupled with converting the non-fluorescent resazurin to the highly fluorescent substance resorufin to measure the content of d-lactate in food products. Group: Enzymes. Synonyms: EC 1.1.1.28, D-Lactic Dehydrogenase; 9028-36-8; lactic acid dehydrogenase; D-specific lactic dehydrogenase; D-(-)-lactate dehydrogenase (NAD); D-lactic acid dehydrogenase; D-lactic dehydrogenase; (R)-Lactate:NAD+ oxidoreductase; D-LDH. Enzyme Commission Number: EC 1.1.1.28. CAS No. 9028-36-8. D-LDH. Activity: > 30 units/mg protein; ~1000 U/mL; 250-500 units/mg protein (biuret); 150-300 units/mg protein; 1,000-3,000 units/mg protein (biuret). Storage: 2-8°C. Form: Suspension in 3.2 M (NH4)2SO4, 0.1 M potassium phosphate, pH 7.0. Source: Lactobacillus leichmanii. EC 1.1.1.28, D-Lactic Dehydrogenase; 9028-36-8; lactic acid dehydrogenase; D-specific lactic dehydrogenase; D-(-)-lactate dehydrogenase (NAD); D-lactic acid dehydrogenase; D-lactic dehydrogenase; (R)-Lactate:NAD+ oxidoreductase; D-LDH. Cat No: NATE-0195. | |
| Native Leuconostoc mesenteroides D-Lactic Dehydrogenase | In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c<-> pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. Group: Enzymes. Synonyms: EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Enzyme Commission Number: EC 1.1.1.28. CAS No. 9028-36-8. D-LDH. Activity: 1,000-3,000 units/mg protein (biuret). Stability: 2-8°C. Form: ammonium sulfate suspension. Source: Leuconostoc mesenteroides. EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Cat No: NATE-0196. | |
| Native microorganisms Creatininase | Creatininase from Pseudomonas sp. is a homohexameric enzyme with a molecular mass of 28.4 kDa per subunit. It is a cyclic amidohydrolase catalysing the reversible conversion of creatinine to creatine. Each monomer contains a binuclear zinc centre near the C termini of the β-strands and the N termini of the main α-helices. These zinc ions indicate the location of the active site. Protein determined by biuret. Applications: This enzyme is useful for enzymatic determination of creatinine when coupled with creatine amidinohydrolase, sarcosine dehydrogenase or sarcosine oxidase and formaldehyde dehydrogenase in clinical analysis. Group: Enzymes. Synonyms: EC 3.5.2.10, creatinine hydrolase; Creatininase; 9025-13-2. Enzyme Commission Number: EC 3.5.2.10. CAS No. 9025-13-2. Creatininase. Mole weight: mol wt ~175 kDa. Activity: 100-300 units/mg protein. Storage: 2-8°C. Form: Lyophilized powder containing sucrose and BSA as stabilizers. Source: microorganisms. EC 3.5.2.10, creatinine hydrolase; Creatininase; 9025-13-2. Cat No: NATE-0163. | |
| Native Microorganisms Pyruvate Oxidase | Pyruvate Oxidase consists of four subunits with identical molecular weights. PoxB reacts with certain aldehydes and phosphate can be replaced by arsenate. Oxygen as well as several artificial compounds can function as electron acceptors. Pyruvate Oxidase is activated by phospholipids as well as monomeric and micellar amphiphiles. Applications: Pyruvate oxidase (poxb) converts pyruvate directly to acetate and co2. it is used to study pyruvate metabolism. it is used to study aerobic metabolism of bacterium, such as lactobacillus plantarumand strept oc occus pneumoniae. pyruvate oxidase is used for enzymatic determination of pyruvate, got, and gpt in clinical analysis. Group: Enzymes. Synonyms: pyruvate oxidase; EC 1.2.3.3; pyruvic oxidase; phosphate-dependent pyruvate oxidase; 9001-96-1; Pyruvate:oxygen oxidoreductase (phosphorylating); PoxB. Enzyme Commission Number: EC 1.2.3.3. CAS No. 9001-96-1. Pyruvate oxidase. Mole weight: mol wt ~260 kDa. Activity: > 1.5 units/mg; > 35 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized powder containing FAD and sugar as stabilizer. Source: Microorganisms. pyruvate oxidase; EC 1.2.3.3; pyruvic oxidase; phosphate-dependent pyruvate oxidase; 9001-96-1; Pyruvate:oxygen oxidoreductase (phosphorylating); PoxB. Cat No: NATE-0613. | |
| Native Pichia pastoris Alcohol Oxidase | In enzymology, an alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the chemical reaction:a primary alcohol + O2? an aldehyde + H2O2. Thus, the two substRates of this enzyme are primary alcohol and O2, whereas its two products are aldehyde and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. It employs one cofactor, FAD. Applications: Alcohol oxidase may be used to study protein translocation into peroxisomes. this product is from pichia pastoris. it has been used for the bacterial expression and immunological verification of hv-p68 cdna clones. Group: Enzymes. Synonyms: EC 1.1.3.13; 9073-63-6; alcohol oxidase; ethanol oxidase; Alcohol:oxygen oxidoreductase. Enzyme Commission Number: EC 1.1.3.13. CAS No. 9073-63-6. Activity: 10-40 units/mg protein (biuret). Storage: -20°C. Form: Buffered aqueous solution. Solution in 30% sucrose with 0.1 M phosphate buffer at pH 8.0. Source: Pichia pastoris. EC 1.1.3.13; 9073-63-6; alcohol oxidase; ethanol oxidase; Alcohol:oxygen oxidoreductase. Cat No: NATE-0047. | |
| Native Pigeon Carnitine Acetyltransferase | Carnitine acetyltransferase maintains the cellular and mitochondrial levels of acetyl-CoA, a key cofactor required for oxidative metabolism, by catalyzing an equilibrium between acetyl-CoA and acetyl-L-carnitine, a storage form of activated acetate. Carnitine acetyltransferase also maintains the pool of acetyl-CoA required for neuronal and nonneuronal acetylcholine production. Protein determined by biuret. Group: Enzymes. Synonyms: acetyl-CoA-carnitine O-acetyltransferase; acetylcarnitine transferase; carnitine acetyl coenzyme A transferase; carnitine acetylase; carnitine acetyltransferase; carnitine-acetyl-CoA transferase; CATC; 9029-90-7; carnitine O-acetyltransferase; EC 2.3.1.7; CRAT; CAT. Enzyme Commission Number: EC 2.3.1.7. CAS No. 9029-90-7. CRAT. Activity: > 70 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Crystalline suspension in 3.2 M (NH4)2SO4 solution, 50 mM potassium phosphate, 1 mM dithiothreitol, pH 7.0. Source: Pigeon breast muscle. Species: Pigeon. acetyl-CoA-carnitine O-acetyltransferase; acetylcarnitine transferase; carnitine acetyl coenzyme A transferase; carnitine acetylase; carnitine acetyltransferase; carnitine-acetyl-CoA transferase; CATC; 9029-90-7; carnitine O-acetyltransferase; EC 2.3.1.7; CRAT; CAT. Cat No: NATE-0159. | |
| Native Porcine Acylase I | In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Protein determined by biuret. Applications: Acylase i from porcine kidney has been used to study the acylase i-catalyzed deacetylation of various s-alkyl-n-acetyl-l-cysteines and their carb...ort acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. ACY1. Activity: > 2,000 units/mg protein; 500-1,500 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Porcine kidney. Species: Porcine. aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-0031. | |
| Native Porcine Carboxypeptidase B | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Protein determined by biuret. Applications: Carboxypeptidase b has been used in a study to develop a non-invasive...ith carboxypeptidase b, which is a c-terminal lysine-specific endopeptidase, is measured using flow cytometry analysis. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. CAS No. 9025-24-5. CPB1. Storage: -20°C. Form: lyophilized powder. Contains HEPES buffer salts and carbohydrate. Source: Porcine pancreas. Species: Porcine. carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Cat No: NATE-0152. | |
| Native Porcine Deoxyribonuclease II | Deoxyribonuclease II, also called as acid DNAse, hydrolyzes deoxyribonucleotide linkages in native and denatured DNA yielding products with 3'-phosphates. In vitro, its optimum pH range is 4.5-5.0. It also acts upon p-nitrophenyl-phosphodiesters at pH 5.6-5.9. The molecular weight is approximately 38 kDa Da. Applications: Dnase ii from creative enzymes has been used to treat transformed cells during the purification of β-lactamase. it has also been used for the preparation of adenoma tissue in a study that investigated the effect of somatoprim on growth hormone secretion in human adenoma cell cultures (hsa). deoxyribonuclease ii from porcine spleen has been used in an immunohistological study of the immune system cells in paraffin-embedded tissues. deoxyribonuclease ii from porcine spleen has also been used in a study to investigate its reassociation with the lysosomal membrane. Group: Enzymes. Synony. Enzyme Commission Number: EC 3.1.22.1. CAS No. 9025-64-3. DNASE2. Activity: 2,000-6,000 Kunitz units/mg protein (biuret). Storage: -20°C. Form: lyophilized powder. Contains sodium chloride. Source: Porcine spleen. Species: Porcine. DNASE2; deoxyribonuclease II; EC 3.1.22.1; 9025-64-3; DNase II; pancreatic DNase II; deoxyribonucleate 3'-nucleotidohydrolase; DNase II; pancreatic DNase II; acid deoxyribonuclease; acid Dnase. Cat No: NATE-0202. | |
| Native Porcine Elastase | Pancreatic elastase is a form of elastase that is produced in the acinar cells of the pancreas, initially produced as an inactive zymogen and later activated in the duodenum by trypsin. Elastases form a subfamily of serine proteases, characterized by a distinctive structure consisting of two beta barrel domains converging at the active site that hydrolyze amides and esters amongst many proteins in addition to elastin, a type of connective tissue that holds organs together. Pancreatic elastase 1 is a serine endopeptidase, a specific type of protease that has the amino acid serine at its active site. Group: Enzymes. Synonyms: EC 3.4.21.36, pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase; elastase-1; pancreatopeptidase; ELA1. Enzyme Commission Number: EC 3.4.21.36. CAS No. 39445-21-1. ELA1. Activity: Type I, > 15 units/mg; Type II, > 4.0 units/mg protein; Type III, > 1 units/mg protein (biuret). Storage: -20°C. Form: Type I, white powder; Type II, Type III, lyophilized powder, Contains sodium carbonate. Source: Porcine pancreas. Species: Porcine. EC 3.4.21.36, pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase; elastase-1; pancreatopeptidase; ELA1. Pack: Package size based on protein content. Cat No: NATE-0211. | |
| Native Porcine Esterase | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Porcine liver esterase is used to catalyze the hydrolysis of pentaacetyl catechin and epicatechin for use in pharmaceutical and industrial applications. pig liver esterase is commonly used for kinetic resolutions and assymetric synthesis in organic chemistry. esterase from porcine liver has been used in a study to assess the effect of 5-aminolaevulinic acid peptide prodrugs on photosensitization for photodynamic therapy. esterase from porcine liver has also been used in a study to investigate how site-specific atherogenic gene expression correlates with subsequent variable lesion development in c...ms: EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase; 9016-18-6. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: Type I, > 15 units/mg solid; Type II, > 50 units/mg; Type III, > 150 units/mg protein (biuret). Storage: -20°C. For | |
| Native Porcine Fumarase | Fumarase catalyzes the reversible hydration of fumarate to malate. In its mitochondrial form, fumarate is involved in the Krebs Cycle, while the cytosolic form is involved in amino acid metabolism. Fumarase (fh in human) is a well-known tricarboxylic-acid-cycle enzyme found in both the cytoplasm and mit ochondria of all eukaryotes. Applications: Fumarase is used as a protein calibration standard in the purification of intact dna polymerase a/primase from mouse cells. Group: Enzymes. Synonyms: EC 4.2.1.2; fumarase; L-malate hydro-lyase; (S)-malate hydro-lyase; 9032-88-6. Enzyme Commission Number: EC 4.2.1.2. CAS No. 9032-88-6. Fumarase. Activity: 300-500 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.2 M (NH4)2SO4, 0.05 M KH2PO4, pH 7.5, 0.014 M 2-mercaptoethanol. Source: Porcine heart. Species: Porcine. EC 4.2.1.2; fumarase; L-malate hydro-lyase; (S)-malate hydro-lyase; 9032-88-6. Cat No: NATE-0267. | |
| Native Porcine Leucine Aminopeptidase | Leucine aminopeptidase (LAP) is a proteolytic enzyme which hydrolyzes the peptide bond adjacent to a free amino group. It is called leucine aminopeptidase because it rapidly catalyzes the hydrolysis of leucine containing peptides. However, it also catalyzes the hydrolytic release of other amino acids located at the N-terminal end of various peptides and proteins. The enzyme from porcine kidney has been extensively studied. It has a molecular weight of 255,000 and it consists of four subunits each having one atom of zinc. Group: Enzymes. Synonyms: Leucine Aminopeptidase; 9054-63-1; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidas. Enzyme Commission Number: EC 3.4.11.1. Purity: 90% (biuret). LAP. Activity: >100 U/mg protein. Storage: Stable when stored at 4°C. Do not freeze. Form: Ammonium Sulfate. Source: Porcine Kidney. Species: Porcine. Leucine Aminopeptidase; 9054-63-1; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I; EC 3.4.11.1; leucyl aminopeptidase; LAP. Cat No: NATE-1879. | |
| Native Porcine Leucine Aminopeptidase, microsomal | Leucyl aminopeptidases are enzymes that preferentially catalyze the hydrolysis of leucine residues at the N-terminus of peptides and proteins. Other N-terminal residues can also be cleaved, however. LAPs have been found across superkingdoms. Identified LAPs include human LAP, bovine lens LAP, porcine LAP, Escherichia coli (E. coli) LAP (also known as PepA or XerB), and the solanaceous-specific acidic LAP (LAP-A) in tomato (Solanum lycopersicum). Group: Enzymes. Synonyms: Leucine Aminopeptidase, microsomal; 9054-63-1; leucine aminopeptidase; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL prot. Enzyme Commission Number: EC 3.4.11.1. CAS No. 9054-63-1. LAP. Activity: Type VI-S, > 12 units/mg protein (biuret); Type IV-S, 10-40 units/mg protein (Bradford). Form: Type VI-S, lyophilized powder; Type IV-S, ammonium sulfate suspension. Source: Porcine kidney. Species: Porcine. Leucine Aminopeptidase, microsomal; 9054-63-1; leucine aminopeptidase; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I; EC 3.4.11.1; leucyl aminopeptidase; LAP. Cat No: NATE-0378. | |
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