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| Product | Description | |
|---|---|---|
| Iron(II) sulfate heptahydrate | In manufacture of Fe, Fe Compounds, other sulfates; in Fe electroplating baths; in fertilizer; as food and feed supplement; in radiation dosimeters; as reducing agent in chemical processes; as wood preservative; as weed-killer; in prevention of chlorosis in plants; in other pesticides; in writing ink; in process engraving and lithography; as dye for leather; in etching aluminum; in water treatment; in qualitative analysis ("brown ring" test for nitrates); as polymerization catalyst. As analytical reagent; as raw material for ferrite; raw material to produce magnetic iron oxide, iron(III) oxide and iron blue inorganic pigment, iron catalyst and poly iron sulfate; as chromatographic reagent. In agriculture, it is used as pesticide in agriculture to control wheat smut, scab of apple and bear, fruit tree decay; as fertilizer to remove moss and lichen of food trunk. Medically it is used as local astringent, blood tonic and anti-anemia. Ferrous sulfate heptahydrate (feed grade) can be used as the iron fortifier for feed additive. Ferrous sulfate heptahydrate (food grade) is used as nutrition supplements, such as iron fortifier, coloring agent for fruit and vegetable. According to Chinese regulation, it can be used in following foods and with allowed amounts: Sweets with filling and salt: 3000~6000 mg/kg; Cereals with high iron content and corresponding products (maximum daily consumption 50g): 860~960 mg/kg; Dairy |  |
| Anti-Cancer Library Plus | Quantity: well-chosen 1468 anti-tumor compounds with unique structures; - High antitumor activity: 99% of compounds with IC50 below 3 μM; - Covers 42 tumor related targets with each compound having clear target; - Detailed information: each compound has information about activity testing method, providing reference for your experimental design; - HNMR/LCMS validated to ensure high purity and quality; - A supplemental tool for anticancer drug development and target identification. Uses: Scientific use. Product Category: L2180. Categories: Anti-Cancer Libraries Plus. |  |
| Casein | Casein. Synonyms: Casein, vitamin tested;Casein, Hammarsten bovine;ANTI-CSN2 (N-TERM) antibody produced in rabbit;CASB;CSN2;Bile Salte No.3;RHODIUM STAND;Casein, Bovine Milk, Carbohydrate and Fatty Acid Free. CAS No. 9000-71-9. Pack Sizes: 1 kg. Product ID: CDF4-0152. Molecular formula: C81H125N22O39P. Category: Stabilizers and Thickeners. Product Keywords: Food Ingredients; Stabilizers and Thickeners; Casein; CDF4-0152; 9000-71-9; C81H125N22O39P; 232-555-1; 9000-71-9. Purity: 0.99. Color: Yellow to tan. EC Number: 232-555-1. Physical State: purified Powder. Solubility: H2O: insoluble, forms a cloudy suspension. Quality Level: 200. Melting Point: 280 °C (dec.)(lit.). Product Description: Casein from bovine milk is a phosphoprotein and forms three-dimensional colloidal supramolecular micelles. There are four main types of casein which make up approximately 80% of the total protein in bovine milk: α-s1 casein, α-s2 casein, β-casein, and κ-casein. Casein is proposed to be the main protective constituent in milk. Casein is an amphiphilic protein. |  |
| Catalase from bovine liver | Catalase from bovine liver. Synonyms: H2O2:H2O2 oxidoreductase. CAS No. 9001-5-2. Product ID: CDC10-0039. Category: Antioxidant Cosmetic Chemicals. Product Keywords: Cosmetic Ingredients; Antioxidant Cosmetic Chemicals; Catalase from bovine liver; CDC10-0039; 9001-05-2; H2O2:H2O2 oxidoreductase; MFCD00081483; 9001-05-2. Physical State: aqueous suspension. Quality Level: 200. Storage: 2-8°C. Application: Catalase from bovine liver has been used for measuring the hydrogen peroxide conetent in cancer tissue homogenates. It has also been used to test the effect of organophosphate insecticide chlorpyrifos-ethyl (CE) [0,0-diethyl 0 (3,5,6-trichloro-2-pyridyl) phosphorothioate] on its enzyme activity. Density: 1.06 g/mL at 20 °C. Product Description: Catalase from bovine liver contains 506 residues. It is a tetramer and each monomer corresponds to a molecular weight of 61 kDa. The active site in each momomer comprises nicotinamide adenine dinucleotide phosphate (NADPH) and iron binding region. | |
| Chemically modified Cholesterol Oxidase from Brevibacterium species | Oxidoreductase that catalyzes the interconversion of cholesterol to cholest-4-en-3-one. Rely on the proven diagnostic quality of this product. Applications: Use cholesterol oxidase in diagnostic tests for the determination of cholesterol in combination with cholesterol esterase. Group: Enzymes. Synonyms: Cholesterol-O2 oxidoreductase; 3 beta-Hydroxy steroid oxidoreductase; 3β-hydroxysteroid: oxygen oxidoreductase; cholesterol: oxygen oxidoreductase; cholesterol oxidase. CHOD. Mole weight: 60 kD (native and SDS). Activity: 10-20 U/mg lyophilizate. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Protect from light. Appearance: Yellow lyophilizate. Storage: No decrease in activity over 6 weeks at +35°C. Source: Brevibacterium species. Cholesterol-O2 oxidoreductase; 3 beta-Hydroxy steroid oxidoreductase; 3β-hydroxysteroid: oxygen oxidoreductase; cholesterol: oxygen oxidoreductase; cholesterol oxidase; EC 1.1.3.6. Cat No: DIA-284. |  |
| Chemically modified Cucurbita species Ascorbate Oxidase | Oxidoreductase that oxidizes ascorbic acid to dehydroascorbate. Take advantage of the improved stability in liquid reagents. Rely on the proven diagnostic quality of this product. Applications: Use ascorbate oxidase, chemically modified, in a variety of diagnostic tests to eliminate the interference of ascorbic acid, since ascorbic acid interferes with the trinder reaction that is widely used for the colorimetric determination of analytes. it is useful in liquid as well as dry chemistry test, e.g., for the determination of uric acid, lactate or creatinine. Group: Enzymes. Synonyms: ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; L-ascorbate: O2 oxidoreductase; AA oxidase; L-ascorbate oxidase. AAO. Mole weight: Approximately 140 kD. Activity: >180 U/mg lyophilizate (+37°C, L-ascorbate); Specific activity (+37°C): >1,800 U/mg protein. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Keep tightly sealed. Appearance: Turquoise lyophilizate. Source: Cucurbita species. ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; L-ascorbate: O2 oxidoreductase; AA oxidase; EC 1.10.3.3; 9029-44-1; L-ascorbate oxidase. Cat No: DIA-283. | |
| Chemically modified Glycerol-3-phosphate Oxidase from E. coli | Recombinant oxidoreductase that catalyzes the interconversion of glycerol 3-phosphate to dihydroxyacetone phosphate. Take advantage of the enhanced liquid stability of this enzyme. Rely on the proven diagnostic quality of this product. Applications: Use glycerol-3-phosphate oxidase in diagnostic tests for the determination of triglycerides together with glycerol kinase and lipoprotein lipase. Group: Enzymes. Synonyms: glycerol-3-phosphate oxidase; sn-glycerol-3-phosphate: oxygen 2-oxidoreductase; glycerol phosphate oxidase; glycerol-1-phosphate oxidase; glycerol phosphate oxidase; L-alpha-glycerophosphate oxidase; alpha-glycerophosphate oxidase; L-alpha-glycerol-3-phos. Glycerol-3-phosphate oxidase. Mole weight: 75 kD (SDS-PAGE); 74 kD (gel filtration, Sephadex G 150). Activity: >10 U/mg lyophilizate (+37°C, L-α-glycerol phosphate); Specific activity (+25°C): >40 U/mg protein. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: Green yellow amorphous lyophilizate. Source: E. coli. glycerol-3-phosphate oxidase; EC 1.1.3.21; sn-glycerol-3-phosphate: oxygen 2-oxidoreductase; glycerol phosphate oxidase; glycerol-1-phosphate oxidase; glycerol phosphate oxidase; L-alpha-glycerophosphate oxidase; alpha-glycerophosphate oxidase; L-alpha-glycerol-3-phosphate oxidase. Cat No: DIA-287. | |
| Chemically modified Porcine L-Lactate Dehydrogenase | Dehydrogenase that catalyzes the interconversion of L(+)-lactate to pyruvate. Take advantage of the enhanced liquid stability of this enzyme. Rely on the proven diagnostic quality of this product. Applications: Use l-lactate dehydrogenase (l-ldh), chemically modified, in a variety of diagnostic tests for the removal of pyruvate in determinations working with nadh (i.e., triglycerides, lipase, aldolase, aminotransferases, glutamate dehydrogenase). Group: Enzymes. Synonyms: lactic acid dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; L-lactate dehydrogenase; L-LDH; LAD; LD; Lactate. LDH. Activity: >25 U/mg lyophilizate; >150 U/mg protein. Stability: At +2 to +8°C within specification range for 12 months. Appearance: White lyophilizate. Source: Porcine heart. Species: Porcine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: DIA-279. | |
| Chemically modified Pseudomonas species Cholesterol Esterase | Hydrolase that splits fatty acids from sterols. Take advantage of the enhanced stability of this enzyme in liquid reagents. Rely on the proven diagnostic quality of this product. Applications: Use cholesterol esterase, chemically modified in diagnostic tests for the determination of cholesterol in combination with cholesterol oxidase. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; sterol esterase; CE. Cholesterol Esterase. Mole weight: ~129 kD. Activity: >10 U/mg lyophilizate; >100 U/mg protein. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: Brownish lyophilizate. Source: Pseudomonas species. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; 9026-00-0; sterol esterase; CE. Cat No: DIA-281. | |
| Chemically modified Pseudomonas species Lipoprotein Lipase | Enzyme that hydrolyzes triglycerides into three free fatty acids and glycerol. Take advantage of the enhanced liquid stability of this enzyme. Rely on the proven diagnostic quality of this product. Applications: Use lipoprotein lipase in diagnostic tests for the determination of triglycerides together with glycerol kinase and glycerol-3-phosphate dehydrogenase. Group: Enzymes. Synonyms: Lipoprotein lipase; LPL; Clearing factor lipase; Diacylglycerol lipase; Diglyceride lipase. LPL. Mole weight: 47 kD. Activity: >10 U/mg lyophilizate. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: Brownish lyophilizate. Source: Pseudomonas species. Lipoprotein lipase; LPL; EC 3.1.1.34; Clearing factor lipase; Diacylglycerol lipase; Diglyceride lipase. Cat No: DIA-282. | |
| DNA Damage and Repair Compound Library Plus | Quantity: well-chosen 667 compounds with unique structures targeting DNA damage & repair; - High bioactivity: All compounds with IC50 below 3 μM; - Targets included 19 DNA damage & repair related proteins; - Detailed information: each compound has information about activity testing method, providing reference for your experimental design; - HNMR/LCMS validated to ensure high purity and quality; - A powerful tool for DNA damage/repair targeting drug development and target identification. Uses: Scientific use. Product Category: L3980. Categories: DNA Damage and Repair Compounds Libraries Plus. | |
| Glycerol-3-phosphate Oxidase from E. coli, Recombinant | Recombinant oxidoreductase that catalyzes the interconversion of glycerol 3-phosphate to dihydroxyacetone phosphate. Rely on the proven diagnostic quality of this product. Applications: Use glycerol-3-phosphate oxidase in diagnostic tests for the determination of triglycerides together with glycerol kinase and lipoprotein lipase. Group: Enzymes. Synonyms: glycerol-3-phosphate oxidase; sn-glycerol-3-phosphate: oxygen 2-oxidoreductase; glycerol phosphate oxidase; glycerol-1-phosphate oxidase; glycerol phosphate oxidase; L-alpha-glycerophosphate oxidase; alpha-glycerophosphate oxidase; L-alpha-glycerol-3-phosphate oxidase; GPO. CAS No. 9046-28-0. Glycerol-3-phosphate oxidase. Mole weight: 75 kD (SDS-PAGE); 74 kD (gel filtration, Sephadex G 150). Activity: >90 U/mg lyophilizate (+37°C). Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: Greenish yellow lyophilizate. Source: E. coli. glycerol-3-phosphate oxidase; EC 1.1.3.21; sn-glycerol-3-phosphate: oxygen 2-oxidoreductase; glycerol phosphate oxidase; glycerol-1-phosphate oxidase; glycerol phosphate oxidase; L-alpha-glycerophosphate oxidase; alpha-glycerophosphate oxidase; L-alpha-glycerol-3-phosphate oxidase. Cat No: DIA-286. | |
| Hexokinase from Yeast, chemically modified | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Recombinant enzyme that converts hexose to hexose-6-phosphate. take advantage of the improved stability in liquid reagents. rely on the proven diagnostic quality of this product. Applications: Use hexokinase in diagnostic tests for blood glucose using the hexokinase method and for the determination of creatine kinase. Group: Enzymes. Synonyms: hexokinase type . Hexokinase. Mole weight: 57 kD (SDS-PAGE). Activity: > 40 U/mg lyophilizate. Stability: At +2 to +8°C within specification range for 18 months. Store dry. Appearance: White lyophilizate. Source: Yeast. hexokinase type IV glucokinase; hexokinase D; hexokinase type IV; hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase. Cat No: NATE-0989. | |
| MES Monohydrate | MES is one of the "Good" buffers developed for biological applications. MES is not recommended at pH 7.4; other buffers should be considered. All qualities are tested for trace ions and all can be used for biological and biochemistry applications. MES Monohydrate has been used: In the preparation of a solution used for the suspension and dilution of protoplasts to measure the density and number of protoplasts using a haemocytometer As a component of Murashige and Skoog basal salt media In the preparation of total ionic strength adjustment buffer (TISAB). Group: Biochemicals. Alternative Names: 2- (N-Morpholino) ethanesulfonic acid monohydrate; ?2- (4-Morpholino) ethanesulfonic acid monohydrate. Grades: Reagent Grade. CAS No. 145224-94-8. Pack Sizes: 25g, 100g, 250g, 1Kg. Molecular Formula: C6H13NO4S·H2O, Molecular Weight: 213.25. US Biological Life Sciences. |  Worldwide |
| Native Candida cylindracea 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. Hydrolase that splits fatty acids from sterols. rely on the proven diagnostic quality of this product. Applications: Use cholesterol esterase in diagnostic tests for the determination of cholesterol in combination with cholesterol oxidase. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester s. Cholesterol Esterase. Activity: >10.5 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: Almost white lyophilizate. Source: Candida cylindracea. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; 9026-00-0; sterol esterase; CE. Cat No: NATE-0984. | |
| Native Corynebacterium lilium Creatinine Deiminase | Hydrolase for creatinine determination that catalyzes the conversion of creatinine to N-methylhydantoin and ammonia. Rely on the proven diagnostic quality of this product. Applications: Use creatinine deaminase in diagnostic tests for the determination of creatinine in combination with n-carbamoylsarcosine amidase, n-methylhydantoinase (atp-hydrolysing) and sarcosine oxidase. Group: Enzymes. Synonyms: Creatinine hydrolase; creatinine desiminase. Creatinine Deiminase. Activity: 45.0-90.0 U/mg lyophilizate. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Protect from light. Appearance: Beige lyophilizate. Source: Corynebacterium lilium. Creatinine hydrolase; Creatinine deaminase; EC 3.5.4.21; creatinine desiminase. Cat No: DIA-291. | |
| Native E.coli Galactose 1-Dehydrogenase | In enzymology, a galactose 1-dehydrogenase (EC 1.1.1.48) is an enzyme that catalyzes the chemical reaction: D-galactose + NAD+ rightleftharpoons D-galactono-1,4-lactone + NADH + H+. Thus, the two substrates of this enzyme are D-galactose and NAD+, whereas its 3 products are D-galactono-1,4-lactone, 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 galactose metabolism. Dehydrogenase that catalyzes the oxidation of galactose to d-galactono-1,4-lactone. rely on the proven diagnostic quality of this recombinant enzyme. Applications: Use galactose 1-dehydrogenase in diagnostic tests for the determination of total galactose. Group: Enzymes. Synonyms: D-galactose:NAD+ 1-oxidoreductase; D-galactose dehydrogenase; beta-galactose dehydrogenase; NAD+-dependent D-galactose dehydrogenase; galactose 1-dehy. CAS No. 9028-54-0. Galactose dehydrogenase. Activity: >50 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Appearance: White lyophilizate. Source: E.coli. D-galactose:NAD+ 1-oxidoreductase; D-galactose dehydrogenase; beta-galactose dehydrogenase; NAD+-dependent D-galactose dehydrogenase; galactose 1-dehydrogenase; EC 1.1.1.48; Galactose dehydrogenase; Galactose 1-Dehydrogenase. Cat No: NATE-0979. | |
| Native E.coli Sarcosine Oxidase | Oxidoreductase that catalyzes the demethylation of sarcosine to glycine. Use Sarcosine Oxidase in your preferred creatinine reagent mix and rely on the proven diagnostic quality of this product. Applications: Use sarcosine oxidase in diagnostic tests for the determination of creatinine. this can be done using one of two methods: (1) in combination with creatinase and creatininase. (2) in combination with creatinine deaminase, n-carbamoylsarcosine amidase and n-methylhydantoinase (atp-hydrolyzing). Group: Enzymes. Synonyms: Sarcosine Oxidase; SAO. CAS No. 9029-22-5. SAO. Mole weight: 40 kD. Activity: 22-40 U/mg lyophilizate; >45 U/mg protein. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Protect from light. Appearance: Yellow lyophilizate. Source: E. coli. Sarcosine Oxidase; EC 1.5.3.1; SAO. Cat No: DIA-290. | |
| Native Porcine L-Lactate Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Dehydrogenase that catalyzes the interconversion of specific for l(+)-lactate to pyruvate. apply this ready-to-use enzyme directly in your diagnostic test. rely on the proven diagnostic quality of this product. Applications: Use l-lactate dehydrogenase in a variety of diagnostic tests for the removal of pyruvate in determinations working with nadh (i.e., triglycerides, lipase,...ehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. CAS No. 9001-60-9. LDH. Activity: >550 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Appearance: White suspension in ammonium sulfate, 3.2 mol/l; Tris, 10 mmol/l, pH approximately 6.5. Source: Porcine muscle. Species: Porcine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0982. | |
| Native Porcine Malate Dehydrogenase, IFCC Quality | Dehydrogenase that catalyzes the interconversion of malate to oxaloacetate. Rely on the proven diagnostic quality of this product. Tested according to the recommendations of the International Federation of Clinical Chemistry (IFCC). Applications: Use malate dehydrogenase in diagnostic tests for the determination of aspartate aminotransferase or in applications for citric and acetic acid testing. Group: Enzymes. Synonyms: Malate Dehydrogenase, IFCC Quality; malic dehydrogenase; L-malate dehydrogenase; malic acid dehydrogenase; MDH. MDH. Mole weight: 70 kDa. Activity: >70 U/mg lyophilizate. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White lyophilizate. Source: Porcine heart. Species: Porcine. Malate Dehydrogenase, IFCC Quality; malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; S-malate: NAD+ oxidoreductase; EC 1.1.1.37; Malate Dehydrogenase. Cat No: DIA-278. | |
| Native Yeast Formate Dehydrogenase | Formate dehydrogenase is involved in the stress response of plants and catalyzes the reduction of NAD+ to NADH. Dehydrogenase that catalyzes the interconversion of formate to carbon dioxide. rely on the proven diagnostic quality of this product. Applications: Use formate dehydrogenase in diagnostic tests for the determination of oxalate in combination with oxalate decarboxylase or for the determination of formic acid. also used in cofactor recycling systems for nadh. Group: Enzymes. Synonyms: formate-NAD oxidoreductase; FDH; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. FDH. Activity: >0.4 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White lyophilizate. Source: Yeast. EC 1.2.1.2; 9028-85-7; formate-NAD oxidoreductase; FDH; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Cat No: NATE-0978. | |
| Pyruvate Oxidase from E.coli, Recombinant | Recombinant oxidoreductase that catalyzes the interconversion of pyruvate to acetyl phosphate. Rely in the proven diagnostic quality of this product. Applications: Use pyruvate oxidase in a variety of diagnostic tests, such as for the determination of pyruvate, lactate or aminotransferases. Group: Enzymes. Synonyms: pyruvic oxidase; phosphate-dependent pyruvate oxidase; Pyruvate:oxygen oxidoreductase (phosphorylating); PoxB. CAS No. 9001-96-1. Pyruvate oxidase. Activity: >1.5 U/mg lyophilizate; >3 U/mg protein. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Appearance: Yellow lyophilizate. Source: E. coli. pyruvate oxidase; EC 1.2.3.3; pyruvic oxidase; phosphate-dependent pyruvate oxidase; 9001-96-1; Pyruvate:oxygen oxidoreductase (phosphorylating); PoxB. Cat No: DIA-289. | |
| Tissue, Array, Canine, Male, Adult, Normal, Multi-Tissue I (Frozen) HisTek | Tissues are snap frozen in liquid nitrogen immediately after excision, and embedded in OCT. All US Biologicals frozen tissue products, including frozen tissue arrays, frozen tissue sections, and frozen tissue panels, can be used for both immunohistochemistry and in situ hybridization. These products are ideal for rapid cellular localization of RNA and protein expression, especially for antibodies that don't recognize paraffin embedded tissue. At least one of the tissue slides from each lot was stained with H & E to ensure quality. Group: Biologicals. Alternative Names: Adrenal, Bone Marrow, Brain-Cerebellum, Brain-Cerebrum, Colon, Esophagus, Heart, Kidney, Liver, Lung, Mesothileal (Pericardium), Nerve, Pancreas, Prostate, Rectum, Skeletal Muscle, Skin, Small Intestine, Spleen, Stomach, Testis, Thymus, Thyroid, Tonsil. Grades: Molecular Biology Grade. Pack Sizes: 1 Slide, 5 Slides. US Biological Life Sciences. | Worldwide |
| Tissue, Array, Rabbit, Male, Adult, Normal, Multi-Tissue I (Frozen) HisTek | Tissues are snap frozen in liquid nitrogen immediately after excision, and embedded in OCT. All US Biologicals frozen tissue products, including frozen tissue arrays, frozen tissue sections, and frozen tissue panels, can be used for both immunohistochemistry and in situ hybridization. These products are ideal for rapid cellular localization of RNA and protein expression, especially for antibodies that don't recognize paraffin embedded tissue. At least one of the tissue slides from each lot was stained with H & E to ensure quality. Group: Biologicals. Alternative Names: Adrenal, Bone Marrow, Brain-Cerebellum, Brain-Cerebrum, Colon, Esophagus, Heart, Kidney, Liver, Lung, Lymphoid Tissue, Mesothileal (Pericardium), Nerve, Pancreas, Prostate, Rectum, Salivary Gland, Skeletal Muscle, Skin, Small Intestine, Spleen, Stomach, Testis, Thymus, Tonsil. Grades: Molecular Biology Grade. Pack Sizes: 1 Slide, 5 Slides. US Biological Life Sciences. | Worldwide |
| Tissue, Array, Rat Adult Normal, Multi, tissue II, Adipose, Stomach, Small intestine, Colon, Uterus, Placenta, ovary, testis HisTek | Tissue was fixed in formalin immediately after excision, and embedded in paraffin. The paraffin embedded tissue array can be used for both immunohistochemistry and in situ hybridization. It is ideal for rapid cellular localization of RNA and protein expression. At least one of the tissue slides from each lot was stained with H & E to ensure the quality. Group: Biologicals. Grades: Molecular Biology Grade. Pack Sizes: 5Arrays. US Biological Life Sciences. | Worldwide |
| Tissue, Genomic DNA, Human Tumor Cell Line, K 562 (Human Chronic Myelogenous Leukemia; Bone Marrow), BioGenomics | Tissue genomic DNAs are isolated from a wide variety of tissues. The genomic DNAs are isolated from tissues by proprietary modified guanidine thiocyanate techniques. The quality and purity of genomic DNA are tested by spectrophotometer and electrophoresis. A260/280 is between 1.8 and 2.0 (detected in 10mM Tris Cl, pH 7.5). Contamination by RNA, polysaccharides and proteoglycans has been effectively eliminated. Group: Biologicals. Grades: Molecular Biology Grade. Pack Sizes: 100ug. US Biological Life Sciences. | Worldwide |
| Tissue, Section, Human Adult Normal, Testis (Frozen) HisTek | Frozen tissue slides suitable for use in identifying cellular localization of RNA or protein using in situ hybridization or immunohistochemistry. Tissue of 5-10um thickness is mounted on a positively-charged glass slide. The slide is fixed and and fixed by cold acetone. One of the tissue section slides from each lot was stained with H & E to ensure the quality. It is an ideal product for rapid cellular localization of RNA and protein expression. Group: Biologicals. Grades: Molecular Biology Grade. Pack Sizes: 5 Sections. US Biological Life Sciences. | Worldwide |
| Tissue, Section, Human Tumor, Testis (Frozen) HisTek | Frozen tissue slides suitable for use in identifying cellular localization of RNA or protein using in situ hybridization or immunohistochemistry. Tissue of 5-10um thickness is mounted on a positively-charged glass slide. The slide is fixed and and fixed by cold acetone. One of the tissue section slides from each lot was stained with H & E to ensure the quality. It is an ideal product for rapid cellular localization of RNA and protein expression. Group: Biologicals. Grades: Molecular Biology Grade. Pack Sizes: 5 Sections. US Biological Life Sciences. | Worldwide |
| Tissue, Western Blot, Human Adult Normal, Blot IV, heart, brain, kidney, liver, lung, pancreas, spleen, skeletal muscle, stomach, small intestine, colon, rectum, uterus, prostate, testis, placenta HisTek | Protein Western Blots are manufactured by using high-quality protein isolated from documented tissues. The tissue is excised, immediately frozen, and then pathologically identified. Protein is isolated by proprietary techniques. Each lane of the blot contains 50ug of protein. Group: Biologicals. Grades: Molecular Biology Grade. Pack Sizes: 1 Blot. US Biological Life Sciences. | Worldwide |
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