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| Product | Description | |
|---|---|---|
| Native Vaccinia virus Topoisomerase I | Topoisomerase I relaxes supercoiled DNA molecules. The enzyme initiates transient breakages and rejoins of phosphodiester bonds in superhelical turns of closed-circular DNA. Enzyme activity is independent of right-and left-handed superhelices. Applications: Enzyme activity is increased in the presence of 2.5 mm mg2+. topoisomerase i from vaccinia virus can be used for studying pivotal biological pr ocess such as-replication, transcription, recombination as well as dna structure and topology which includes chromatin reconstitution in vitro and the degree of supercoiling of dna. additionally, the product helps in relaxing the dna coils and exposes the restriction sites which.me; swivelase; ω-protein; deoxyribonucleate topoisomerase; topoisomerase; type I DNA topoisomerase; DNA topoisomerase; TOPO I. Enzyme Commission Number: EC 5.99.1.2. CAS No. 80449-01-0. TOPO I. Mole weight: mol wt 32 kDa. Storage: -20°C. Form: buffered aqueous solution; Solution in 50 mM Tris HCl, pH 7.5, containing 100 mM NaCl, 1 mM EDTA, 1 mM DTT, 0.1% Triton X-100, and 50% glycerol. Source: Vaccinia virus. Topoisomerase I; EC 5.99.1.2; type I DNA topoisomerase; untwisting enzyme; relaxing enzyme; nicking-closing enzyme; swivelase; ω-protein; deoxyribonucleate topoisomerase; topoisomerase; type I DNA topoisomerase; DNA topoisomerase; TOPO I. Cat No: NATE-0708. |  |
| Native Versatile Peroxidase from Bjerkandera adusta | Versatile peroxidase (EC 1.11.1.16, VP, hybrid peroxidase, polyvalent peroxidase) is an enzyme with systematic name reactive-black-5:hydrogen-peroxide oxidoreductase. This enzyme catalyses the following chemical reaction: (1) Reactive Black 5 + H2O2 ? oxidized Reactive Black 5 + 2 H2O (2) donor + H2O2 ? oxidized donor + 2 H2O Versatile peroxidase is a hemoprotein. Group: Enzymes. Synonyms: EC 1.11.1.16; VP; hybrid peroxidase; polyvalent peroxidase. Enzyme Commission Number: EC 1.11.1.16. CAS No. 114995-15-2;42613-30-9. Versatile Peroxidase. Stability: 12 months. Storage: store at -20 °C. Form: Freeze-dried brown-coloured amorphous powder, no stabilizing agent added. Source: Bjerkandera adusta. EC 1.11.1.16; VP; hybrid peroxidase; polyvalent peroxidase. Cat No: NATE-1580. | |
| Native Vibrio cholerae Neuraminidase | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. At least four mammalian sialidase homologs have been described in the.say of neuraminidase. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Enzyme Commission Number: EC 3.2.1.18. CAS No. 9001-67-6. Neuraminidase. Activity: Type I, 1-5 units/mg protein (Lowry, using NAN-lactose); Type II, 8-24 units/mg protein (Lowry, using NAN-lactose); Type III, > 1.5 units/mg protein. Storage: 2-8°C. Form: Type I, buffered aqueous solution; Aqueous solution, pH 5.5, containing 0.15 M NaCl and 4 mM CaCl2; Type II, buffered aqueous solution, Solution in 50 mM sodium acetate, pH 5.5, containing 0.15 M sodium chloride and 4 mM calcium chloride; Type III, sterile filte. | |
| Native Vibrio fischeri (Photobacterium f) Luciferase | In enzymology, an alkanal monooxygenase (FMN-linked) (EC 1.14.14.3) is an enzyme that catalyzes the chemical reaction:RCHO + reduced FMN + O2<-> RCOOH + FMN + H2O + hnu. The 3 substrates of this enzyme are RCHO, reduced FMN, and O2, whereas its 4 products are RCOOH, FMN, H2O, and hn. This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor. Applications: Luciferase from vibrio fischeri has been used in a s.; aldehyde monooxygenase; luciferase; Vibrio fischeri luciferase; alkanal,reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing); alkanal,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing); EC 1.14.14.3; 9014-00-0. Enzyme Commission Number: EC 1.13.12.7. CAS No. 9014-00-0. Luciferase. Form: lyophilized powder. Source: Vibrio fischeri (Photobacterium f). alkanal monooxygenase (FMN); bacterial luciferase; aldehyde monooxygenase; luciferase; Vibrio fischeri luciferase; alkanal,reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing); alkanal,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing); EC 1.14.14.3; 9014-00-0. Cat No: NATE-0423. | |
| Native Vibrio sp. Lysophospholipase | In enzymology, a lysophospholipase (EC 3.1.1.5) is an enzyme that catalyzes the chemical reaction: 2-lysophosphatidylcholine + H2O <-> glycerophosphocholine + a carboxylate. Thus, the two substrates of this enzyme are 2-lysophosphatidylcholine and H2O, whereas its two products are glycerophosphocholine and carboxylate. Native lysophospholipase (ec 3.1.1.5) was purified from vibrio sp. Applications: Useful for the enzymatic determination of lysolecithin. Group: Enzymes. Synonyms: lysophospholipase; EC 3.1.1.5; 2-lysophosphatidylcholine acylhydrolase; lecithinase B; lysolecithinase; phospholipase B. Enzyme Commission Number: EC 3.1.1.5. CAS No. 9001-85-8. Lysophospholipase. Activity: > 20.0 U/mg. Appearance: White to brownish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Vibrio sp. lysophospholipase; EC 3.1.1.5; 2-lysophosphatidylcholine acylhydrolase; lecithinase B; lysolecithinase; phospholipase B. Cat No: DIA-157. | |
| Native Wheat Carboxypeptidase W | Carboxypeptidase D can refer to one of several enzymes. A family of serine carboxypeptidases (i.e. enzymes that use an active site serine residue) includes (EC 3.4.16.6, cereal serine carboxypeptidase II, Saccharomyces cerevisiae KEX1 gene product, carboxypeptidase Kex1, gene KEX1 serine carboxypeptidase, KEX1 carboxypeptidase, KEX1 proteinase, KEX1DELTAp, CPDW-II, serine carboxypeptidase, Phaseolus proteinase) is an enzyme. This enzyme has an optimal pH of 4.5-6.0, is inhibited by diisopropyl fluorophosphate. Applications: Carboxypeptidase w from wheat has been used in a study to assess the proteolytic activities in dormant rye (secale cereale l.) grain. carboxypeptidase w from wheat has also been used in a study to investigate the structure determination of the human protective protein. Group: Enzymes. Synonyms: Carboxypeptidase W; 9046-67-7; EC 3.4.16.6; carboxypeptidase D; cereal. Enzyme Commission Number: EC 3.4.16.6. CAS No. 9046-67-7. CPDW-II. Activity: > 50 units/mg protein. Storage: -20°C. Source: Wheat. Carboxypeptidase W; 9046-67-7; EC 3.4.16.6; carboxypeptidase D; cereal serine carboxypeptidase II; Saccharomyces cerevisiae KEX1 gene product; carboxypeptidase Kex1; gene KEX1 serine carboxypeptidase; KEX1 carboxypeptidase; KEX1 proteinase; KEX1DELTAp; CPDW-II; serine carboxypeptidase (misleading); Phaseolus proteinase. Cat No: NATE-0154. | |
| Native Wheat germ Acid Phosphatase | Acid phosphatases (APase) are a family of enzymes that non-specifically catalyze the hydrolysis of monoesters and anhydrides of phosphoric acid to produce inorganic phosphate at an optimum pH of 4 to 7. Acid phosphatase from potatoes is a 111 kDa diner consisting of two subunits at 41 and 35 kDa. This phosphatase has also been shown to cleave DNA. Applications: Acid phosphatase (apase) non-specifically catalyzes the hydrolysis of monoesters and anhydrides of phosphoric acid to produce inorganic phosphate. it is used to study the production, transport, and recycling of phosphate and the metabolic and energy transduction pr ocesses of the cell. this product is from wheat germ and has been used to determine the effect of phosphatase treatment on 3f3/2 staining. Group: Enzymes. Synonyms: acid phosphatase; 9001-77-8; acid phosphomonoesterase; phosphomon. Enzyme Commission Number: EC 3.1.3.2. CAS No. 9001-77-8. Mole weight: 58 kDa (gel filtration). Activity: > 1 unit/mg. Storage: -20°C. Form: lyophilized powder. Source: Wheat germ. acid phosphatase; 9001-77-8; acid phosphomonoesterase; phosphomonoesterase; glycerophosphatase; acid monophosphatase; acid phosphohydrolase; acid phosphomonoester hydrolase; uteroferrin; acid nucleoside diphosphate phosphatase; orthophosphoric-monoester phosphohydrolase (acid optimum); EC 3.1.3.2; APase. Cat No: NATE-0084. | |
| Native Wheat germ 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 proteases, Citrate synthase, EF hands, hemoglobins, lipecalins, and α/β hydrolases. GR is stimulated by melatonin and is reportedly irreversibly inhibited by a number of oxygen radical generating systems. Group: Enzymes. Synonyms: EC 1.6.4.2; 9. Enzyme Commission Number: EC 1.6.4.2. CAS No. 9001-48-3. GR. Mole weight: mol wt 118 kDa. Activity: > 0.08 units/mg protein. Storage: -20°C. Source: Wheat germ. 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-0319. | |
| Native wheat germ Lipase | Triacylglycerol lipase is an enzyme with system name triacylglycerol acylhydrolase. This enzyme catalyses the following chemical reaction:triacylglycerol + H2O<-> diacylglycerol + a carboxylate. Group: Enzymes. Synonyms: Triacylglycerol acylhydrolase; Triacylglycerol lipase. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Activity: Lipase: 5-15 units/mg proteinAcid Phosphatase < 1.0 units/mg protein. Storage: 2-8°C. Form: Lyophilized powder. Contains acid phosphatase. Source: Wheat germ. EC 3.1.1.3; lipase; triglyceride lipase; tributyrase; butyrinase; glycerol ester hydrolase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969-4-9; Meito MY 30; Tweenesterase; GA 56; capalase L; triglyceride hydrolase; triolein hydrolase; tween-hydrolyzing esterase; amano CE; cacordase; triglyceridase; triacylglycerol ester hydrolase; amano P; amano AP; PPL; glycerol-ester hydrolase; GEH; meito Sangyo OF lipase; hepatic lipase; lipazin; post-heparin plasma protamine-resistant lipase; salt-resistant post-heparin lipase; heparin releasable hepatic lipase; amano CES; amano B; tributyrase; triglyceride lipase; liver lipase; hepatic monoacylglycerol acyltransferase; 9001-62-1. Cat No: NATE-1615. | |
| Native Wheat germ Topoisomerase I | Topoisomerase I relaxes supercoiled DNA molecules. The enzyme initiates transient breakages and rejoins of phosphodiester bonds in superhelical turns of closed-circular DNA. Enzyme activity is independent of right-and left-handed superhelices. Topoisomerase i relaxes supercoiled dna molecules. the enzyme initiates transient breakages and rejoins of phosphodiester bonds in superhelical turns of closedcircular dsdna. Applications: Suitable for: o analsis of degree of dna supercoiling o forming knots and circles in single stranded dna o converting complementary single stranded dna to double stranded, circular forms o rejoining nicks in double-stranded dna. Group: Enzymes. Synonyms: Topoisomerase I; EC 5.99.1.2; type I DNA topoisomerase; untwisting enzyme; relaxing enzyme; nicking-closing enzyme; swivelase; ω-protein; deoxyribonucleate topoisomerase; topoisomerase; type I DNA topoisomerase; DNA topoisomerase; TOPO. Enzyme Commission Number: EC 5.99.1.2. CAS No. 80449-01-0. TOPO I. Mole weight: mol wt 97 kDa. Storage: -70°C. Form: buffered aqueous glycerol solution. Source: Wheat germ. Topoisomerase I; EC 5.99.1.2; type I DNA topoisomerase; untwisting enzyme; relaxing enzyme; nicking-closing enzyme; swivelase; ω-protein; deoxyribonucleate topoisomerase; topoisomerase; type I DNA topoisomerase; DNA topoisomerase; TOPO I. Cat No: NATE-0709. | |
| Native Wheat Phytase | Phytase catalyzes the hydrolysis of phytic acid to inositol and free orthophosphate. Wheat phytase can degrade inositol phosphate-6 and 5 at a pH of 4 and 5. Phytase catalyzes the hydrolysis of phytic acid to inositol and free orthophosphate. Applications: Phytase has been used in a study to quantify the number of feedstuffs showing significant phytase activity. it has also been used in a study to investigate the effect of adjusting the ph to 5.0 (optimum for wheat phytase) during whole wheat bread making on phytase activity. Group: Enzymes. Synonyms: myo-inositol-hexakisphosphate 4-phosphohydrolase; 9001-89-2; 6-phytase; phytase; phytate 6-phosphatase; myo-inositol-hexakisphosphate 6-phosphohydrolase; 4-phytase; EC 3.1.3.26. Enzyme Commission Number: EC 3.1.3.26. CAS No. 9001-89-2. Phytase. Activity: 0.01-0.04 unit/mg solid. Storage: -20°C. Source: Wheat. myo-inositol-hexakisphosphate 4-phosphohydrolase; 9001-89-2; 6-phytase; phytase; phytate 6-phosphatase; myo-inositol-hexakisphosphate 6-phosphohydrolase; 4-phytase; EC 3.1.3.26. Cat No: NATE-0566. | |
| Native White-rot fungus (Phaner ochaete chrysosporium) Manganese peroxidase | Manganese peroxidase (MnP) is a hemecontaining glycoprotein that is produced by ligninolytic basidiomycetes. It requires hydrogen peroxide as an oxidant. MnP oxidizes Mn2+ to Mn3+. Mn3+ oxidizes phenolic rings to phenoxy radicals which results in the decomposition of various compounds. Applications: Manganese peroxidase from white-rot fungus (phaner ochaete chrysosporium) is from the peroxidase family and is used to oxidize manganese. it may be used to study wound healing. Group: Enzymes. Synonyms: manganese peroxidase; peroxidase-M2; Mn-dependent (NADH-oxidizing) peroxidase; EC 1.11.1.13; 114995-15-2; MnP. Enzyme Commission Number: EC 1.11.1.13. CAS No. 114995-15-2. MnP. Activity: > 20 U/g. Storage: -20°C. Form: powder; only partially soluble in water or buffer; light brown. Source: White-rot fungus (Phaner ochaete chrysosporium). manganese peroxidase; peroxidase-M2; Mn-dependent (NADH-oxidizing) peroxidase; EC 1.11.1.13; 114995-15-2; MnP. Cat No: NATE-0454. | |
| Native Xanthine Dehydrogenase from Bovine milk | Xanthine oxidoreductase (XOR) catalyzes the formation of uric acid from hypoxanthine and xanthine, last two steps of purine catabolism. The mammalian enzyme is synthesized as a xanthine dehydrogenase form (XDH, EC 1.17.1.4), which uses NAD as the electron acceptor, but is converted into an xanthine oxidase form (XO, EC 1.1.3.22) by reversible (through sulfhydryl group oxidation) or irreversible (proteolysis) manner. Since most industrial protocols of XOR purification includes proteolysis step, commercial XOR enzyme is available only as oxidase form unable to use NAD as a an electron acceptor. Group: Enzymes. Synonyms: xanthine dehydrogenase; NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase; XDH; EC 1.17.1.4. Enzyme Commission Number: EC 1.17.1.4. CAS No. 9054-84-6. XDH. Form: Lyophilized. Source: Bovine milk. Species: Bovine. xanthine dehydrogenase; NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase; XDH; EC 1.17.1.4. Cat No: NATE-1065. | |
| Native Xanthine dehydrogenase from Microorganism | Xanthine dehydrogenase belongs to the group of molybdenum-containing hydroxylases involved in the oxidative metabolism of purines. The enzyme is a homodimer. Xanthine dehydrogenase can be converted to xanthine oxidase by reversible sulfhydryl oxidation or by irreversible proteolytic modification. Applications: Useful for the enzymatic determiantion of inorganic phosphate. Group: Enzymes. Synonyms: xanthine dehydrogenase; NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase; XDH; EC 1.17.1.4. Enzyme Commission Number: EC 1.17.1.4. CAS No. 9054-84-6. XDH. Mole weight: 240 kDa. Activity: > 100 U/mL. Appearance: Brownish solution. Storage: Storage at ?20°C in the presence of a desiccant is recommended. Form: Liquid. Source: Microorganism. xanthine dehydrogenase; NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase; XDH; EC 1.17.1.4. Cat No: NATE-1064. | |
| Native Xanthomonas sp. α-1? (2,3,4) Fucosidase solution | Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the FUCA1 gene. Alpha-Fucosidase is an enzyme that breaks down fucose. Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fucosidase with accumulation of fucose in the tissues. Different phenotypes include clinical features such as neurologic deterioration, growth retardation, visceromegaly, and seizures in a severe early form; coarse facial features, angiokeratoma corporis diffusum, spasticity and delayed psychomotor development in a longer surviving form; and an unusual spondylometaphyseoepiphyseal dysplasia in yet another form. Group: Enzymes. Synonyms: α-1? (2,3,4) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA; EC 3.2.1.51; 9037-65-4. Enzyme Commission Number: EC 3.2.1.51. CAS No. 9037-65-4. FUCA. Activity: > 0.5 units/mg protein. Storage: 2-8°C. Form: buffered aqueous solution, Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl. Source: Xanthomonas sp. α-1? (2,3,4) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA; EC 3.2.1.51; 9037-65-4. Pack: vial of 0.004 unit. Cat No: NATE-0262. | |
| Native Xanthomonas sp. α-1? (2,3,4) Fucosidase solution | Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the FUCA1 gene. Alpha-Fucosidase is an enzyme that breaks down fucose. Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fucosidase with accumulation of fucose in the tissues. Different phenotypes include clinical features such as neurologic deterioration, growth retardation, visceromegaly, and seizures in a severe early form; coarse facial features, angiokeratoma corporis diffusum, spasticity and delayed psychomotor development in a longer surviving form; and an unusual spondylometaphyseoepiphyseal dysplasia in yet another form. | |
| Native Xanthomonas sp. α-1? (3,4) Fucosidase solution | Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the FUCA1 gene. Alpha-Fucosidase is an enzyme that breaks down fucose. Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fucosidase with accumulation of fucose in the tissues. Different phenotypes include clinical features such as neurologic deterioration, growth retardation, visceromegaly, and seizures in a severe early form; coarse facial features, angiokeratoma corporis diffusum, spasticity and delayed psychomotor development in a longer surviving form; and an unusual spondylometaphyseoepiphyseal dysplasia in yet another form. | |
| Native Xanthomonas sp. α-1? (3,4) Fucosidase solution | Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the FUCA1 gene. Alpha-Fucosidase is an enzyme that breaks down fucose. Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fucosidase with accumulation of fucose in the tissues. Different phenotypes include clinical features such as neurologic deterioration, growth retardation, visceromegaly, and seizures in a severe early form; coarse facial features, angiokeratoma corporis diffusum, spasticity and delayed psychomotor development in a longer surviving form; and an unusual spondylometaphyseoepiphyseal dysplasia in yet another form. Group: Enzymes. Synonyms: α-1? (3,4) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA; EC 3.2.1.51; 9037-65-4. Enzyme Commission Number: EC 3.2.1.51. CAS No. 9037-65-4. FUCA. Activity: > 2 units/mg protein. Storage: 2-8°C. Form: buffered aqueous solution, Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl. Source: Xanthomonas sp. α-1? (3,4) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA; EC 3.2.1.51; 9037-65-4. Pack: vial of 0.02 unit. Cat No: NATE-0263. | |
| Native Yeast 6-Phosphogluconic Dehydrogenase | In enzymology, a phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) is an enzyme that catalyzes the chemical reaction:6-phospho-D-gluconate + NADP+<-> D-ribulose 5-phosphate + CO2 + NADPH. Thus, the two substRates of this enzyme are 6-phospho-D-gluconate and NADP+, whereas its 3 products are D-ribulose 5-phosphate, CO2, and NADPH. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. Applications: 6-phosphoglyconic dehydrogenase (6pgd) is a key enzyme in the oxidative portion of the hexose monophosphate shunt. it is specific for oxidized nicotinamide adenine dinucleotide ph.luconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase; EC 1.1.1.44; phosphogluconate dehydrogenase; decarboxylating; 9073-95-4. Enzyme Commission Number: EC 1.1.1.44. CAS No. 9073-95-4. 6-Phosphogluconic Dehydrogenase. Activity: 3.0-6.0 units/mg solid. Storage: 2-8°C. Form: lyophilized powder. Source: Yeast. 6-Phosphogluconic Dehydrogenase; phosphogluconic acid dehydrogenase; 6-phosphogluconic dehydrogenase; 6-phosphogluconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase; EC 1.1.1.44; phosphogluconate dehydrogenase; decarboxylating; 9073-95-4. Cat No: NATE-0009. | |
| Native Yeast Alcohol dehydrogenase | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Dehydrogenase that catalyzes the interconversion of alcoho.rimary alcohol dehydrogenase; yeast alcohol dehydrogenase. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Activity: >300 U/mg. Appearance: White lyophilizate (50 mg lyophilizate contain approximately 30 mg enzyme protein,15 mg sucrose, 5 mg phosphate). Storage: -20°C. Form: Solids containing <2% Citrate buffer salts. Source: Yeast. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Cat No: NATE-0975. | |
| Native Yeast Aldehyde Dehydrogenase | In enzymology, an aldehyde dehydrogenase [NAD(P)+] (EC 1.2.1.5) is an enzyme that catalyzes the chemical reaction: an aldehyde + NAD(P)+ + H2O <-> an acid + NAD(P)H + H+. The 4 substrates of this enzyme are aldehyde, NAD+, NADP+, and H2O, whereas its 4 products are acid, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in 5 metabolic pathways: glycolysis / gluconeogenesis, histidine metabolism, tyrosine metabolism, phenylalanine metabolism, and metabolism of xenobiotics by cytochrome p450. Applications: Component of nadh and nadph recycling systems. Group: Enzymes. Synonyms: aldehyde:NAD(P)+ oxidoreductase; aldehyde dehydrogenase [NAD(P)+]; ALDH; Aldehyde Dehydrogenase; EC 1.2.1.5. Enzyme Commission Number: EC 1.2.1.5. CAS No. 9028-88-0. ALDH. Activity: ~20 units/mg protein (At 25 °C with acetaldehyde as the substrate.). Form: Lyophilized. Source: Yeast. aldehyde:NAD(P)+ oxidoreductase; aldehyde dehydrogenase [NAD(P)+]; ALDH; Aldehyde Dehydrogenase; EC 1.2.1.5. Cat No: NATE-0902. | |
| Native Yeast Coenzyme A, Trilithium Salt | Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle. All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester, such as acetyl-CoA) as a substrate. In humans, CoA biosynthesis requires cysteine, pantothenate, and adenosine triphosphate (ATP). Group: Coenzymes. Synonyms: Coenzyme A, Trilithium Salt; CoA-Li; 18439-24-2. CAS No. 18439-24-2. Purity: Determined by enzyme analysis with PTA* (> 75%) *PTA = Phosphotrasacetylase (LM) (EC 2.3.1.8.). CoA. Mole weight: 685.41. Storage: Keep tightly stoppered in the dark below 5°C. For Prolonged storage, keep below-20°C. Source: Yeast. Coenzyme A, Trilithium Salt; CoA-Li; 18439-24-2. Cat No: NATE-0146. | |
| 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. | |
| Native Yeast Malate Dehydrogenase | Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner mitochondr.te: NAD+ oxidoreductase; EC 1.1.1.37; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Activity: > 1,000 units/mg protein (at 25°C and pH 7.5). Storage: 1 -10°C. Form: Ammonium sulfate suspension. Source: Yeast. 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: NATE-1030. | |
| Native Yeast Phytase | Phytase catalyzes the hydrolysis of phytic acid to inositol and free orthophosphate. Wheat phytase can degrade inositol phosphate-6 and 5 at a pH of 4 and 5. Group: Enzymes. Synonyms: myo-inositol-hexakisphosphate 4-phosphohydrolase; 9001-89-2; 6-phytase; phytase; phytate 6-phosphatase; myo-inositol-hexakisphosphate 6-phosphohydrolase; 4-phytase; EC 3.1.3.26. Enzyme Commission Number: EC 3.1.3.26. CAS No. 9001-89-2. Phytase. Activity: 5000 u/g. Storage: Store at -20°C. Form: Powder. Source: Yeast. myo-inositol-hexakisphosphate 4-phosphohydrolase; 9001-89-2; 6-phytase; phytase; phytate 6-phosphatase; myo-inositol-hexakisphosphate 6-phosphohydrolase; 4-phytase; EC 3.1.3.26. Cat No: NATE-0565. | |
| Native Zucchini Ascorbate Oxidase | In enzymology, a L-ascorbate oxidase (EC 1.10.3.3) is an enzyme that catalyzes the chemical reaction:2 L-ascorbate + O2? 2 dehydroascorbate + 2 H2O. Thus, the two substRates of this enzyme are L-ascorbate and O2, whereas its two products are dehydroascorbate and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor with oxygen as acceptor. This enzyme participates in ascorbate metabolism. It employs one cofactor, copper. Applications: Aao can be used in clinical tests for determining levels of ascorbic acid in blood or for the removal of interference effects caused by ascorbic acid in clinical analysis. Group: Enzymes. Synonyms: 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; L-ascorbate ox. Enzyme Commission Number: EC 1.10.3.3. CAS No. 9029-44-1. Mole weight: 70kD. Activity: > 100 units/mg protein. Appearance: Light tanish, brownish, greyish to blue green free flowing powder. Form: Freeze dried powder. Source: Zucchini. 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; L-ascorbate oxidase. Cat No: NATE-1137. | |
| Native Zymomonas mobilis Alcohol Dehydrogenase | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Applications: The enzyme is useful for determination of alcohols or aldehydes. Group: Enzymes. Synonyms: aldehyde reductase; ADH. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. Mole weight: ca. 148,000; Subunit molecular weight : ca. 37,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least six months. Source: Zymomonas mobilis. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1; 9031-72-5. Cat No: NATE-1900. | |
| Native Zymomonas mobilis Glucokinase | Glucokinase (EC 2.7.1.2) is an enzyme that facilitates phosphorylation of glucose to glucose-6-phosphate. Glucokinase occurs in cells in the liver, pancreas, gut, and brain of humans and most other vertebrates. In each of these organs it plays an important role in the regulation of carbohydrate metabolism by acting as a glucose sensor, triggering shifts in metabolism or cell function in response to rising or falling levels of glucose, such as occur after a meal or when fasting. Mutations of the gene for this enzyme can cause unusual forms of diabetes or hypoglycemia. Applications: The enzyme is useful for diagnostic reagent, for example, glucose determination or ck determination, and for the specificdetermination of glucose. tris-hci buffer is not suitable for the practical use of zm-gck. Group: Enzymes. Synonyms: EC 2.7.1.2; glucokinase; glucokinase (phosphorylating); 9001-36-9; GCK; FGQTL3; GK; GLK; HHF3; HK4; HKIV; HXKP; LGLK; MODY2. Enzyme Commission Number: EC 2.7.1.2. CAS No. 9001-36-9. GCK. Mole weight: ca. 66,000; Subunit molecular weight : ca. 33,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Zymomonas mobilis. EC 2.7.1.2; glucokinase; glucokinase (phosphorylating); 9001-36-9; GCK; FGQTL3; GK; GLK; HHF3; HK4; HKIV; HXKP; LGLK; MODY2. Cat No: NATE-1903. | |
| Native Zymomonas mobilis Glucose-6-Phosphate Dehydrogenase | 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). Applications: The enzyme is useful for diagnostic reagent, for example, glucose determination or ck determination, and for the specificdetermination of glucose. Group: Enzymes. Synonyms: Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; GPD. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Mole weight: ca. 208000; Subunit molecular weight: ca. 52,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Zymomonas mobilis. Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; GPD. Cat No: NATE-1898. | |
| Na-Tosyl-D-a,ß-diaminopropionic Acid | Na-Tosyl-D-a,ß-diaminopropionic Acid. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 1g. US Biological Life Sciences. |  Worldwide |
| Na-Tosyl-L-arginine 98+% | Na-Tosyl-L-arginine 98+%. Group: Biochemicals. Grades: Reagent Grade. Pack Sizes: 1g, 5g, 25g, 100g. US Biological Life Sciences. | Worldwide |
| Na-Tosyl-L-arginine amide hydrochloride 98+% | Na-Tosyl-L-arginine amide hydrochloride 98+%. Group: Biochemicals. Grades: Reagent Grade. CAS No. 14279-64-2. Pack Sizes: 5g, 25g. US Biological Life Sciences. | Worldwide |
| Na-Tosyl-L-arginine methyl ester hydrochloride 98+% (HPLC) | Na-Tosyl-L-arginine methyl ester hydrochloride 98+% (HPLC). Group: Biochemicals. Grades: Reagent Grade. Pack Sizes: 5g, 25g, 100g, 250g. US Biological Life Sciences. | Worldwide |
| Na-Tosyl-L-lysine chloromethylketone hydrochloride 98+% (HPLC) | Na-Tosyl-L-lysine chloromethylketone hydrochloride 98+% (HPLC). Group: Biochemicals. Grades: Reagent Grade. CAS No. 4272-74-6. Pack Sizes: 100mg, 250mg, 1g. US Biological Life Sciences. | Worldwide |
| Na-Tosyl-L-lysine methyl ester hydrochloride 99+% (TLC) | Na-Tosyl-L-lysine methyl ester hydrochloride 99+% (TLC). Group: Biochemicals. Grades: Reagent Grade. CAS No. 5266-48-8. Pack Sizes: 1g, 2.5g. US Biological Life Sciences. | Worldwide |
| Na-Tosyl-Ne-Boc-L-lysine | Na-Tosyl-Ne-Boc-L-lysine. Group: Biochemicals. Alternative Names: Tos-L-Lys(Boc)-OH. Grades: Highly Purified. CAS No. 16948-09-7. Pack Sizes: 500mg, 1g, 2g, 5g, 10g. US Biological Life Sciences. | Worldwide |
| Na-Tosyl-Ne-Boc-L-lysine 98+% (HPLC) | Na-Tosyl-Ne-Boc-L-lysine 98+% (HPLC). Group: Biochemicals. Grades: Reagent Grade. Pack Sizes: 1g, 5g, 25g. US Biological Life Sciences. | Worldwide |
| Na+-transporting two-sector ATPase | A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. An enzyme found in alkaliphilic bacteria that is similar to EC 3.6.3.14 (H+-transporting two-sector ATPase) where Na+ replaces H+. Group: Enzymes. Enzyme Commission Number: EC 7.2.2.1 (Formerly EC 3.6.3.15). 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-4651; Na+-transporting two-sector ATPase; EC 3.6.3.15. Cat No: EXWM-4651. | |
| Na-Trityl-D-asparagine 99+% (HPLC) | Na-Trityl-D-asparagine 99+% (HPLC). Group: Biochemicals. Grades: Reagent Grade. Pack Sizes: 1g, 5g. US Biological Life Sciences. | Worldwide |
| Na-Trityl-L-asparagine | Na-Trityl-L-asparagine. Group: Biochemicals. Grades: Reagent Grade. CAS No. 132388-58-0. Pack Sizes: 1g, 5g. US Biological Life Sciences. | Worldwide |
| Na-Trityl-Nb-Fmoc-D-2,3-diaminopropionic acid 99+% (HPLC) | Na-Trityl-Nb-Fmoc-D-2,3-diaminopropionic acid 99+% (HPLC). Group: Biochemicals. Grades: Reagent Grade. Pack Sizes: 100mg, 250mg, 1g, 5g. US Biological Life Sciences. | Worldwide |
| Na-Trityl-Nb-Fmoc-L-2,3-diaminopropionic acid 99+% (HPLC) | Na-Trityl-Nb-Fmoc-L-2,3-diaminopropionic acid 99+% (HPLC). Group: Biochemicals. Grades: Reagent Grade. Pack Sizes: 100mg, 250mg, 1g, 5g. US Biological Life Sciences. | Worldwide |
| Na-Trityl-Ne-Fmoc-L-lysine 99+% (HPLC) | Na-Trityl-Ne-Fmoc-L-lysine 99+% (HPLC). Group: Biochemicals. Grades: Reagent Grade. Pack Sizes: 1g, 5g. US Biological Life Sciences. | Worldwide |
| Natriuretic Peptide, C-Type | ?95% (HPLC). Group: Fluorescence/luminescence spectroscopy. |  |
| Natriuretic Peptide, C-Type, Human and Porcine - CAS 127869-51-6 | Member of the natriuretic peptide family that shares structural homology with ANP and plays a role in the regulation of body fluid homeostasis, vascular tone, and vascular growth. Group: Fluorescence/luminescence spectroscopy. | |
| Nattokinase | Nattokinase. Alternative Names: Nattoesse Haruno-Ogawa;4-(carboxymethyl)-2-[(1R)-1-[[2-[(2,5-dichlorobenzoyl)amino]acetyl]amino]-3-methylbutyl]-6-oxo-1,3,2-dioxaborinane-4-carboxylic;Liposomal NATTOKINASE, NATTOKINASE NanoEmulsion, NanoActive NATTOKINASE, Oil-Soluble NATTOKINASE;4-(carboxymethyl)-2-[(1R)-1-[[2-[(2,5-dichlorobenzoyl)amino]acetyl]amino]-3-methylbutyl]-6-oxo-1,3,2-dioxaborinane-4-carboxylic acid;4-(Carboxymethyl)-2-[(1R)-1-{[N-(2,5-dichlorobenzoyl)glycyl]amino}-3-methylbutyl]-6-oxo-1,3,2-dioxaborinane-4-carboxylic acid;Nattokinase (peptidolytic);NattoLife. CAS No. 133876-92-3. Product ID: PIPE-0322. Molecular formula: C20H23BCl2N2O9. Mole weight: 517.12162. EINECS: 229-880-6. Category: Natural Extract. |  |
| Nattokinase | Nattokinase is an enzyme extracted and purified from a Japanese food called Natto. Natto is a food made from fermented soybeans that has been eaten in Japan for many years. Natto is produced by fermentation by adding the bacterium Bacillus natto, a beneficial bacteria, to boiled soybeans. The resulting nattokinase enzyme is produced when the bacterium acts on the soybeans. While other soy foods contain enzymes, it is only the natto preparation that contains the specific nattokinase enzyme. Applications: Functional health productspharmaceutical stufffood additive. Group: Others. Purity: 20000fu/g. Appearance: Light yellow to white powder. Nattokinase. Cat No: EXTC-134. | |
| Nattokinase 20,000 Fu/gm | Nattokinase 20,000 Fu/gm. |  CA, FL & NJ |
| Nattokinase, Natto fermentation | Nattokinase, Natto fermentation is a potent fibrinolytic enzyme. Nattokinase can break down blood clots by directly hydrolyzing fibrin and plasmin substrate. Nattokinase can be used for the research of cardiovascular diseases [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 133876-92-3. Pack Sizes: 5 mg; 10 mg; 50 mg; 100 mg. Product ID: HY-P2373. |  |
| Natto powder | Natto powder. Applications: Natto powder can be used in functional food, drinks, health care products and pharmaceuticals. Group: Others. Appearance: Light yellow powder. Source: NATTO is a fermented food with probiotic properties made according to a traditional Japanese recipe. This Natto is produced through the fermentation of organic soy with Bacillus subtilis natto, a very special bacterium imported from Japan. Natto powder. Cat No: EXTC-208. | |
| Natural Alpha Pinene | Natural Alpha Pinene. | CA, FL & NJ |
| Natural Caprylyl Glycol | Natural Caprylyl Glycol. Uses: Designed for use in research and industrial production. CAS No. 1117-86-8. Product ID: APB1117868. Alfa Chemistry ISO 9001:2015 Certified. |  |
| Natural Compound Library in Chinese Pharmacopoeia | A unique collection of 2070 natural products included in Chinese Pharmacopoeia (CP), a powerful tool for drug development and pharmacological study; - Diversified structures: including flavonoids, polyphenols, Alkaloids, etc. ; - Detailed compound information with structure, solubility, targeted signal pathways, action sites, and biological activity description; - Clear source: known active natural products selected from animals, plants, or microorganisms with clear species information; - NMR and HPLC/LCMS validated to ensure high purity and quality. Uses: Scientific use. Product Category: L6800. Categories: Natural Compound Libraries in Chinese Pharmacopoeia. |  |
| Natural Cotton Mask | Natural Cotton Mask. Product ID: CDC10-0636. Category: Classic Mask. Product Keywords: Cosmetic Ingredients; Cosmetic packaging material; Natural Cotton Mask; CDC10-0636; Classic Mask; Cotton fibers. |  |
| Natural Cotton Mask | Natural Cotton Mask. Product ID: CDC10-0697. Category: Cosmetic Packaging Material. Product Keywords: Cosmetic Ingredients; Mask; CDC10-0697; Natural Cotton Mask; Cosmetic Packaging Material;. | |
| Natural gum rubber | Natural gum rubber. Group: Polymers. |  |
| Natural Lycopene 10% HPLC Powder (Lycopersicon Esculentum Mill.) (Tomato Peels) | Natural Lycopene 10% HPLC Powder (Lycopersicon Esculentum Mill.) (Tomato Peels). Categories: orotic acid; 65-86-1. | CA, FL & NJ |
| Naturally occurring substances | Naturally occurring substances. Uses: Designed for use in research and industrial production. Additional or Alternative Names: Naturally occurring substances;Einecs 310-127-6. Product Category: Heterocyclic Organic Compound. CAS No. 999999-99-4. Product ID: ACM999999994. Alfa Chemistry ISO 9001:2015 Certified. | |
| Natural Methyl Cinnamate | Methyl cinnamate is the methyl ester of cinnamic acid and is a white or transparent solid with a strong, aromatic odor. It is found naturally in a variety of plants, including in fruits, like strawberry, and some culinary spices, such as Sichuan pepper and some varieties of basil. Uses: Flavour and Perfume. Group: Plant Extracts. INCI Names: Methyl Cinnamate. Grades: FOOD GRADE. CAS No. 103-26-4. Pack Sizes: 25 kgs Jerrycan, 200 kg Drums. Product ID: AM-002. Olfactive Profile: Fruity, balsamic, similar to strawberry. EC No: 203-093-8. FEMA No: 2698. Origin: Indonesia. |  New Jersey |
| Natural milk powder (PCB's ) | certified Reference Material. Group: Certified reference materials (crms). | |
| Natural milk powder (pesticides) | certified Reference Material. Group: Certified reference materials (crms). | |
| Natural Phytol 95% GC | Natural Phytol 95% GC. CAS No. 150-86-7. | CA, FL & NJ |
| Natural Product Derivatives Library | The library consists of more than 4, 000 members belonging 22 scaffolds (average 180 compounds per scaffold). - The library includes the following sub-libraries:- Cytisine-based sub-library- Matrine-based sub-library- Podophyllotoxin-based sub-library- Sub-library based on naturally occurring privileged BBS such ashydroxy-prolines, triptamine, nor-tropolone etc. - TargetMol "Beyond RO5" filters have been applied for the library population (See Phys-chem parameters for the library members). - NO Med-Chem restrictions (widely accepted and proprietary TargetMol substructure filters on reactive functionalities, toxicophoric, instability suspicions etc. ). - More than 90% purity for each library member confirmed by LC-MS or NMR analysis. Uses: Scientific use. Product Category: NY1000. Categories: Natural Product Derivatives Libraries. | |
| Natural Product Derivatives Library for CADD | Large quantity: contains 135, 000 natural product derivatives and the number is continuously updating. Uses: Scientific use. Product Category: L6030. Categories: Natural Product Derivatives Libraries for CADD. | |
| Natural Product Library | A unique collection of 3720 natural products that can be used for high-throughput screening and high-content screening. - Provides biological information and pharmacological information of the products, which serve as theoretical references and research basis for screening. - Clear source: a selection of known active natural products from animals, plants and microorganisms; plant species are labeled with accurate English and Latin names to facilitate your later research corroboration. - Good structural diversity: a wide range of compound structures including flavonoids and alkaloids, with detailed classification information. - NMR, HPLC/LCMS and other detection techniques to ensure the correct structure and high purity of the product and reduce false positives. Uses: Scientific use. Product Category: L6010. Categories: Natural Product Libraries. | |
| Natural Product Library for HTS | A unique collection of 4160 pure natural products and their derivatives with known biological activity for drug discovery, pharmacological study, stem cell differentiation, fingerprint study and quality research, and can be used for high throughput screening (HTS) and high content screening (HCS); - Documentation with clear source: isolated natural products from plant, animal, microorganism, etc. - Structurally diverse: 4160 natural products, including diverse types of structures, such as alkaloids, limonoids, sequiterpenes, diterpenes, pentacyclic triterpenes, sterols, and many other representatives which provide the structural diversity inherent in this group; - Detailed compound information with structure, solubility, target, activity, IC50 value, and biological activity description; - Cost-effective and competitive price to save your fundings. Uses: Scientific use. Product Category: L6000. Categories: Natural Product Libraries for HTS. | |
| Natural protease-enzyme blend for hair care | An all-natural protease-enzyme blend that enhances natural hair color and restores shine by removing excess protein-build up. Applications: Hair conditioners. Group: Enzymes. Synonyms: Natural protease; Natural protease enzyme blend; hair care; hair conditioners; protease enzyme blend; enhances natural hair color; enzyme for hair; natural hair color; Natural protease-enzyme blend for hair care. Cosmetic enzymes. Appearance: powder or liquid. Lipase; Cosmetic; lipase-based enzyme blend; breaks down human sebum; breaks down residual oil; human sebum; breaks down human sebum and residual oil; residual oil; human sebum; Lipase-based enzyme blend for cosmetic. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: BODY-2816. | |
| Natural Raspberry Ketone | Natural Raspberry Ketone. CAS No: 5471-51-2 |  Sarchem Laboratories New Jersey NJ |
| Natural Tiramisu Flavor Powder (Non GMO) | Natural Tiramisu Flavor Powder (Non GMO). | CA, FL & NJ |
| Natural Vanillin | Natural Vanillin. Group: Food ingredients. Pack Sizes: 25Kgs Drums. |  |
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