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| Product | Description | |
|---|---|---|
| Maltodextrin | Maltodextrin. CAS: 9050-36-6. Packing: Bag. |  New Jersey NJ |
| Maltodextrin | Maltodextrin is a carbohydrate derived from starch. Uses: 1. food industry: maltodextrin is commonly used as a food additive in the production of candy, beverages, infant formula, dry mixes, and other processed foods. 2. sports nutrition: maltodextrin is used as a source of carbohydrates in sports drinks and nutrition bars for athletes and fitness enthusiasts. 3. medical and pharmaceuticals: maltodextrin is used as a binder and filler in the production of tablets and capsules for pharmaceuticals and dietary supplements. 4. cosmetic industry: maltodextrin can be used in cosmetic products such as lotions and creams as a thickening agent to improve texture and viscosity. 5. industrial applications: maltodextrin can be used as a source of fermentation for the production of ethanol, organic acids, and other chemicals. Group: Natural polymers and biopolymers. Alternative Names: Dextrin maize starch. CAS No. 9050-36-6. Molecular formula: 342.3. Mole weight: C12H22O11. 98%. |  |
| Maltodextrin | Maltodextrin is a polysaccharide that is used primarily in foods and beverages as a thickener, sweetener, and/or stabilizer. It is produced from vegetable starch by partial hydrolysis and is usually found as a white hygroscopic spray-dried powder. Maltodextrin is easily digestible, being absorbed as rapidly as glucose and may be either moderately sweet or almost flavorless. It can be found as an ingredient in a variety of processed foods. Uses: Chocolates & confectionery Baby food & pharmaceuticals Energy drinks & bars Milk & bakery products. Group: Natural Product. Alternative Names: Corn Syrup Solids Modified Corn Starch Modified Rice Starch Modified Tapioca Starch Modified Wheat Starch. Grades: Industrial Grade, Food Grade, Pharmaceutical Grade. CAS No. 9050-36-6. Pack Sizes: 25kg Paper / HDPE bags. |  |
| Maltodextrin | Maltodextrin occurs as a nonsweet, odorless, white powder or granules. The solubility, hygroscopicity, sweetness, and compressibility of maltodextrin increase as the DE increases. Synonyms: Cargill Dry. CAS No. 9050-36-6. Product ID: PE-0189. Molecular formula: (C6H10O5)n·H2O. Mole weight: 900-9000. Category: Coating Agents; Tablet and Capsule Diluent; Tablet Binder; Viscosity increasing Agents; Filler; Stabilizer; Thickening Agents; Surface polish, etc. Product Keywords: Thickener Excipients; Stabilizers; Thickener Excipients; ; PE-0189; Maltodextrin; Coating Agents; Tablet and Capsule Diluent; Tablet Binder; Viscosity increasing Agents; Filler; Stabilizer; Thickening Agents; Surface polish, etc; (C6H10O5)n·H2O; 9050-36-6. UNII: 7CVR7L4A2D. Chemical Name: Maltodextrin. Grade: Pharmceutical Excipients. Administration route: Oral. Dosage Form: Oral tablets and granules. Stability and Storage Conditions: Maltodextrin is stable for at least 1 year when stored at a cool temperature (<30°C) and less than 50% relative humidity.Maltodextrin solutions may require the addition of an antimicrobial preservative. Maltodextrin should be stored in a well-closed container in a cool, dry place. Source and Preparation: Maltodextrin is prepared by heating and treating starch with acid and/or enzymes in the presence of water. This process partially hydrolyzes the starch, to produce a solution of glucose polymers of varying chain length. |  |
| Maltodextrin | Maltodextrin. Uses: For analytical and research use. Group: Impurity standards. CAS No. 9050-36-6. Molecular Formula: C12H22O11. Mole Weight: 342.3. Catalog: APB9050366. |  |
| Maltodextrin | Maltodextrin. We stock inventory in warehouses throughout the United States, allowing us to serve customers in all regions in a timely and cost effective manner. |  California |
| Maltodextrin BP/USP | Maltodextrin BP/USP. CAS No. 9050-36-6. |  |
| Maltodextrin - dextrose equivalent 10-15 | Maltodextrin can be used as a binding additive for 3D printing manufacturing. It can be used as a forming agent in the preparation of soya bean sprout extract. Synonyms: Cargill Dry; Glucidex; Glucodry; Lycatab DSH; Maldex; Maldex G; Maltodextrinum; Maltosweet; Maltrin; Maltrin QD; Paselli MD10 PH; Star-Dri; Tapi; Lycatab. CAS No. 9050-36-6. Molecular formula: (C6H10O5)n.H2O. Mole weight: 180.156. |  |
| Maltodextrin - dextrose equivalent 13.0-17.0 | Maltodextrin - dextrose equivalent 13.0-17.0 is a carbohydrate mixture widely used in the biomedical industry. With its dextrose equivalent ranging from 13.0 to 17.0, it serves as a readily available source of energy for cells. | |
| Maltodextrin - dextrose equivalent 16.5-19.5 | Maltodextrin - dextrose equivalent 16.5-19.5 is a compound product commonly used as a carbohydrate source in various pharmaceutical and biotechnology applications. It is extensively utilized as an excipient in drug formulations is acting as a bulking compound or carrier. | |
| Maltodextrin - dextrose equivalent 4.0-7.0 | Maltodextrin - dextrose equivalent 4.0-7.0 is comprised of a versatile and multifaceted composition at a dextrose equivalent range of 4.0-7.0. Remarkably sought after as a prominent carbohydrate reservoir for the impeccably delicate cell culture media and the meticulous pharmaceutical formulations, this product stands unparalleled in terms of its exquisitely balanced solubility and unmatched digestibility. | |
| Maltodextrin oligosaccharides - DP10 to DP40 | | |
| Maltodextrin oligosaccharides - DP2 to DP15 | | |
| Bifidobacterium Lactis (25 Billion Cfu/gm) in a maltodextrin carrier | Bifidobacterium Lactis (25 Billion Cfu/gm) in a maltodextrin carrier. |  CA, FL & NJ |
| cyclomaltodextrinase | Also hydrolyses linear maltodextrin. Group: Enzymes. Synonyms: cycloheptaglucanase; cyclohexaglucanase; cyclodextrinase; cyclomaltodextrin dextrin-hydrolase (decyclizing). Enzyme Commission Number: EC 3.2.1.54. CAS No. 37288-41-8. 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-3917; cyclomaltodextrinase; EC 3.2.1.54; 37288-41-8; cycloheptaglucanase; cyclohexaglucanase; cyclodextrinase; cyclomaltodextrin dextrin-hydrolase (decyclizing). Cat No: EXWM-3917. |  |
| cyclomaltodextrin glucanotransferase | Cyclomaltodextrins (Schardinger dextrins) of various sizes (6,7,8, etc. glucose units) are formed reversibly from starch and similar substrates. Will also disproportionate linear maltodextrins without cyclizing (cf. EC 2.4.1.25, 4-α-glucanotransferase). Group: Enzymes. Synonyms: Bacillus macerans amylase; cyclodextrin glucanotransferase; α-cyclodextrin glucanotransferase; α-cyclodextrin glycosyltransferase; β-cyclodextrin glucanotransferase; β-cyclodextrin glycosyltransferas. Enzyme Commission Number: EC 2.4.1.19. CAS No. 9030-9-5. 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-2416; cyclomaltodextrin glucanotransferase; EC 2.4.1.19; 9030-09-5; Bacillus macerans amylase; cyclodextrin glucanotransferase; α-cyclodextrin glucanotransferase; α-cyclodextrin glycosyltransferase; β-cyclodextrin glucanotransferase; β-cyclodextrin glycosyltransferase; γ-cyclodextrin glycosyltransferase; cyclodextrin glycosyltransferase; cyclomaltodextrin glucotransferase; cyclomaltodextrin glycosyltransferase; konchizaimu; α-1,4-glucan 4-glycosyltransferase, cyclizing; BMA; CGTase; neutral-cyclodextrin glycosyltransferase; 1,4-α-D-glucan 4-α-D-(1,4-α-D-glucano)-transferase (cyclizing). Cat No: EXWM-2416. | |
| HairFix XH Maltodextrin | Naturally-derived, sugar-based hair fixative polymer designed especially for use in clear, hard holding hair gels, mousses, and other styling aids. Non-ionic polymer supplied as a 25% aqueous solution. Uses: Hair gels, mousse, creams & lotions, waxes & pomades. Group: Natural nonionics alkylpolyglucosides. CAS No. 1323833-53-2/7732-18-5. Appearance: Yellowish, viscous liquid, faint odor. Catalog: CI-HC-0028. |  |
| Isomalto oligo saccharide Maltitol Maltodextrin Mannitol Monk Fruit. | Isomalto oligo saccharide Maltitol Maltodextrin Mannitol Monk Fruit. Group: Sweeteners. |  |
| (1?4)-α-D-glucan 1-α-D-glucosylmutase | The enzyme from Arthrobacter sp., Sulfolobus acidocaldarius acts on (1?4)-α-D-glucans containing three or more (1?4)-α-linked D-glucose units. Not active towards maltose. Group: Enzymes. Synonyms: malto-oligosyltrehalose synthase; maltodextrin α-D-glucosyltransferase. Enzyme Commission Number: EC 5.4.99.15. CAS No. 170780-49-1. 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-5554; (1?4)-α-D-glucan 1-α-D-glucosylmutase; EC 5.4.99.15; 170780-49-1; malto-oligosyltrehalose synthase; maltodextrin α-D-glucosyltransferase. Cat No: EXWM-5554. | |
| 4-α-glucanotransferase | This entry covers the former separate entry for EC 2.4.1.3 (amylomaltase). The plant enzyme has been termed D-enzyme. An enzymic activity of this nature forms part of the mammalian and yeast glycogen debranching system (see EC 3.2.1.33 amylo-α-1,6-glucosidase). Group: Enzymes. Synonyms: disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; amylomaltase; dextrin transglycosylase; 1,4-α-D-glucan:1,4-α-D-glucan 4-α-D-glycosyltransferase. Enzyme Commission Number: EC 2.4.1.25. CAS No. 9032-9-1. Amylomaltase. 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-2479; 4-α-glucanotransferase; EC 2.4.1.25; 9032-09-1; disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; amylomaltase; dextrin transglycosylase; 1,4-α-D-glucan:1,4-α-D-glucan 4-α-D-glycosyltransferase. Cat No: EXWM-2479. | |
| Amylomaltase 13A from Thermotoga maritima, Recombinant | Amylomaltase (4-α-glucanotransferase; EC 2.4.1.25) catalyzes glucan transfer from one α-1,4-glucan to another α-1,4-glucan or to glucose. Group: Enzymes. Synonyms: EC 2.4.1.25; Amylomaltase; 4-alpha-glucanotransferase; disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; dextrin transglycosylase; 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase. Enzyme Commission Number: EC 2.4.1.25. CAS No. 9032-9-1. Purity: >90% by SDS-PAGE. Amylomaltase. Mole weight: 53.9 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Thermotoga maritima. EC 2.4.1.25; Amylomaltase 13A; Amylomaltase; 4-alpha-glucanotransferase; disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; dextrin transglycosylase; 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase. Cat No: NATE-1305. | |
| Amylomaltase 13A from Thermotoga neapolitana, Recombinant | Amylomaltase (4-α-glucanotransferase; EC 2.4.1.25) catalyzes glucan transfer from one α-1,4-glucan to another α-1,4-glucan or to glucose. Group: Enzymes. Synonyms: EC 2.4.1.25; Amylomaltase; 4-alpha-glucanotransferase; disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; dextrin transglycosylase; 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase. Enzyme Commission Number: EC 2.4.1.25. CAS No. 9032-9-1. Purity: >90% by SDS-PAGE. Amylomaltase. Mole weight: 54.0 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Thermotoga neapolitana. EC 2.4.1.25; Amylomaltase 13A; Amylomaltase; 4-alpha-glucanotransferase; disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; dextrin transglycosylase; 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase. Cat No: NATE-1299. | |
| Amylomaltase 13B from Thermotoga maritima, Recombinant | Amylomaltase (4-α-glucanotransferase; EC 2.4.1.25) catalyzes glucan transfer from one α-1,4-glucan to another α-1,4-glucan or to glucose. Group: Enzymes. Synonyms: EC 2.4.1.25; Amylomaltase; 4-alpha-glucanotransferase; disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; dextrin transglycosylase; 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase. Enzyme Commission Number: EC 2.4.1.25. CAS No. 9032-9-1. Purity: >90% by SDS-PAGE. Amylomaltase. Mole weight: 68.2 kD. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Thermotoga maritima. EC 2.4.1.25; Amylomaltase 13B; Amylomaltase; 4-alpha-glucanotransferase; disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; dextrin transglycosylase; 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase. Cat No: NATE-1306. | |
| Amylomaltase 57A from Pyrococcus furiosus, Recombinant | Amylomaltase (4-α-glucanotransferase; EC 2.4.1.25) catalyzes glucan transfer from one α-1,4-glucan to another α-1,4-glucan or to glucose. Group: Enzymes. Synonyms: EC 2.4.1.25; Amylomaltase 57A; Amylomaltase; 4-alpha-glucanotransferase; disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; dextrin transglycosylase; 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase. Enzyme Commission Number: EC 2.4.1.25. CAS No. 9032-9-1. Purity: >90% by SDS-PAGE. Amylomaltase. Mole weight: 33.5 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Pyrococcus furiosus. EC 2.4.1.25; Amylomaltase 57A; Amylomaltase; 4-alpha-glucanotransferase; disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; dextrin transglycosylase; 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase. Cat No: NATE-1295. | |
| glycogen phosphorylase | This entry covers several enzymes from different sources that act in vivo on different forms of (1?4)-α-D-glucans. Some of these enzymes catalyse the first step in the degradation of large branched glycan polymers - the phosphorolytic cleavage of α-1,4-glucosidic bonds from the non-reducing ends of linear poly(1?4)-α-D-glucosyl chains within the polymers. The enzyme stops when it reaches the fourth residue away from an α-1,6 branching point, leaving a highly branched core known as a limit dextrin. The accepted name of the enzyme should be modified for each specific instance by substituting "glycogen" with the name of the natural substrate, e.g. maltodextrin...ission Number: EC 2.4.1.1. CAS No. 9035-74-9. GPBB. 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-2326; glycogen phosphorylase; EC 2.4.1.1; 9035-74-9; muscle phosphorylase a and b; amylophosphorylase; polyphosphorylase; amylopectin phosphorylase; glucan phosphorylase; α-glucan phosphorylase; 1,4-α-glucan phosphorylase; glucosan phosphorylase; granulose phosphorylase; maltodextrin phosphorylase; muscle phosphorylase; myophosphorylase; potato phosphorylase; starch phosphorylase; 1,4-α-D-glucan:phosphate α-D-glucosyltransferase; phosphorylase (ambiguous). Cat No: EXWM-2326. | |
| Glycogen Phosphorylase from Human, Recombinant | Glycogen phosphorylase is one of the phosphorylaseenzymes (EC 2.4.1.1). It breaks up glycogeninto glucosesubunits. Glycogenis left with one less glucosemolecule, and the free glucosemolecule is in the form of glucose-1-phosphate. In order to be used for metabolism, it must be converted to glucose-6-phosphateby the enzyme phosphoglucomutase. Glycogen phosphorylase can only act on linearchainsof glycogen (a 1-4 glycosidic linkage). Its work will immediately come to a halt four residues away from a 1-6 branch (which are exceedingly common in glycogen). In these situations, a debranching enzymeis necessary, which will straighten out the chain in that area. Additionally, an...e; amylopectin phosphorylase; glucan phosphorylase; α-glucan phosphorylase; 1,4-α-glucan phosphorylase; glucosan phosphorylase; granulose phosphorylase; maltodextrin phosphorylase; muscle phosphorylase; myophosphorylase; potato phosphorylase; starch phosphorylase; 1,4-α-D-glucan:phosphate α-D-glucosyltransferase; phosphorylase; EC 2.4.1.1; GPBB. CAS No. 9035-74-9. Purity: Greater than 85.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. GPBB. Stability: GPBB although stable at 10°C for 7 days, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered colourless liquid formualtio | |
| Maltotetraose | Maltotetraose can serve as a substrate for enzyme-linked assays to measure amylase activity in biological fluids. Maltotetraose has oral active, and reduces TNF-α -induced inflammatory responses by inhibiting NF-κB activity and decreasing ICAM-1 expression. Maltotetraose also inhibits PDGF -induced vascular smooth muscle cell migration and neovascularization. Additionally, Maltotetraose derivatives can function as probes for detecting bacterial infections by targeting the maltodextrin transporter. With good long-term safety, Maltotetraose holds promise for research in atherosclerosis-related diseases [1] [2] [3] [4]. Uses: Scientific research. Group: Natural products. Alternative Names: Amylotetraose; Fujioligo 450; α-1,4-Tetraglucose. CAS No. 34612-38-9. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg. Product ID: HY-N2464. |  |
| Maltotriose | Maltotriose is a trisaccharide (three-part sugar) consisting of three glucose molecules linked with α-1,4 glycosidic bonds.It is most commonly produced by the digestive enzyme alpha-amylase (a common enzyme in human saliva) on amylose in starch. The creation of both maltotriose and maltose during this process is due to the random manner in which alpha amylase hydrolyses α-1,4 glycosidic bonds.It is the shortest chain oligosaccharide that can be classified as maltodextrin. Group: Heterocyclic organic compound. Alternative Names: 4-O-[4-O-(α-D-Glucopyranosyl)-α-D-glucopyranosyl]-D-glucose. CAS No. 1109-28-0. Molecular formula: C18H32O16. Mole weight: 504.44. Appearance: White to off-white powder. Purity: 0.98. IUPACName: (2R,3R,4S,5S,6R)-2-[(2R,3S,4R,5R,6R)-4,5-Dihydroxy-2-(hydroxymethyl)-6-[(2R,3S,4R,5R)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol. Canonical SMILES: C (C1C (C (C (C (O1)OC2C (OC (C (C2O)O)OC3C (OC (C (C3O)O)O)CO)CO)O)O)O)O. Density: 1.4403 g/cm³. ECNumber: 214-174-2;232-945-1. Catalog: ACM1109280. | |
| Maltotriose | Maltotriose is a trisaccharide (three-part sugar) consisting of three glucose molecules linked with α-1,4 glycosidic bonds.It is most commonly produced by the digestive enzyme alpha-amylase (a common enzyme in human saliva) on amylose in starch. The creation of both maltotriose and maltose during this process is due to the random manner in which alpha amylase hydrolyses α-1,4 glycosidic bonds.It is the shortest chain oligosaccharide that can be classified as maltodextrin. Group: Polysaccharide. Alternative Names: 4-O-[4-O-(α-D-Glucopyranosyl)-α-D-glucopyranosyl]-D-glucose. CAS No. 1109-28-0. Product ID: (2R,3R,4S,5S,6R)-2-[(2R,3S,4R,5R,6R)-4,5-Dihydroxy-2-(hydroxymethyl)-6-[(2R,3S,4R,5R)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol. Molecular formula: 504.44. Mole weight: C18H32O16. C (C1C (C (C (C (O1)OC2C (OC (C (C2O)O)OC3C (OC (C (C3O)O)O)CO)CO)O)O)O)O. InChI=1S/C18H32O16/c19-1-4-7 (22)8 (23)12 (27)17 (31-4)34-15-6 (3-21)32-18 (13 (28)10 (15)25)33-14-5 (2-20)30-16 (29)11 (26)9 (14)24/h4-29H, 1-3H2/t4-, 5-, 6-, 7-, 8+, 9-, 10-, 11-, 12-, 13-, 14-, 15-, 16?, 17-, 18-/m1/s1. FYGDTMLNYKFZSV-DZOUCCHMSA-N. 98%. | |
| Native Rabbit Phosphorylase a | Phosphorylase A is the active form of glycogen phosphorylase which converts glycogen and orthophosphate (Pi) to glucose 1-phoshate (G-1-P). Phosphorylase A can be inhibited by these compounds:Polychlorinated biphenyls, polychlorinated biphenylols and polybrominated biphenyls. Dimeric phosphorylase b is converted to the more active tetramer, phosphorylase a, by the action of phosphorylase kinase. Phosphorylase a is the active form of glycogen phosphorylase which converts glycogen and orthophosphate (pi) to glucose 1-phoshate (g-1-p). Applications: Phosphorylase from rabbit muscle has been used in a study to assess the molecular mechanisms of oleanolic acid. it has also been use...mission Number: EC 2.4.1.1. CAS No. 9035-74-9. Purity: 2× crystallization. GPBB. Activity: 20-30 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing β-glycerophosphate and EDTA. Source: Rabbit muscle. Species: Rabbit. Phosphorylase a; EC 2.4.1.1; 9032-10-4; muscle phosphorylase a and b; amylophosphorylase; polyphosphorylase; amylopectin phosphorylase; glucan phosphorylase; α-glucan phosphorylase; 1,4-α-glucan phosphorylase; glucosan phosphorylase; granulose phosphorylase; maltodextrin phosphorylase; muscle phosphorylase; myophosphorylase; potato phosphorylase; starch phosphorylase; 1,4-α-D-glucan:phosphate α-D-glucosyltransferase; | |
| Native Rabbit Phosphorylase b | Phosphorylase b is a non-active form and is present in resting muscle. Phosphorylase b kinase activity increases significantly when the Mg2+:ATP ratio exceeds. The breakdown of ATP during muscle contraction is thought to trigger in vivo conversion of phosphorylase b into a. Phosphorylase b is activated by inosine monophosphate. Applications: Phosphorylase b is used to study the conversion mechanism of inactive phosphorylase b to active phosphorylase in muscle. phosphorylase b is used to study which factors influence the conversion of phosphorylase b to phosphorylase a such as temperature, amp, fluoride and detergents. it is used to study phosphorylase b deficiency mutations. t...α-glucan phosphorylase; 1,4-α-glucan phosphorylase; glucosan phosphorylase; granulose phosphorylase; maltodextrin phosphorylase; muscle phosphorylase; myophosphorylase; potato phosphorylase; starch phosphorylase; 1,4-α-D-glucan:phosphate α-D-glucosyltransferase; phosphorylase (ambiguous). Enzyme Commission Number: EC 2.4.1.1. CAS No. 9012-69-5. Purity: 2× crystallization. GPBB. Mole weight: mol wt 97.2 kDa by calculation. Activity: Type I, > 20 units/mg protein; Type II, > 7 units/mg. Storage: -20°C. Form: Type I, Lyophilized powder containing lactose, 5?-AMP, and Mg (OAc)2 (10 μmole per 100 mg protein); Type II, lyophilized powder, light yellow. Sour | |
| Native Trichoderma longibrachiatum β-Glucanase | β-glucanases degrade β-1,4-glucans of cellulose, xyloglucan and β-1,4-xylan. β-Glucanase represents a group of carbohydrate enzymes which break down glycosidic bonds within beta-glucan. It forms the main constituent of fungal cell walls and could be a potential structural and storage polysaccharide of marine macro-algae. It has the ability to degrade fungal cell walls and may be involved in defense mechanism of plants against pathogenic fungi. Applications: Β-glucanase was used as a cellulase enzyme in the combined biological and chemical pretreatment method for lignocellulosic ethanol production from energy cane. it was also used in the enz...-(1,3; 1,4)-β-D-glucan 3 (4)-glucanohydrolase; EC 3.2.1.6. Enzyme Commission Number: EC 3.2.1.6. CAS No. 62213-14-3. β-glucanase. Form: powder. contains maltodextrin, silica and sodium benzoate. Source: Trichoderma longibrachiatum. endo-1,3-β-D-glucanase; laminarinase; laminaranase; β-1,3-glucanase; β-1,3-1,4-glucanase; endo-1,3-β-glucanase; endo-β-1,3 (4)-glucanase; endo-β-1,3-1,4-glucanase; endo-β-(1?3)-D-glucanase; endo-1,3-1,4-β-D-glucanase; endo-β-(1-3)-D-glucanase; endo-β-1,3-glucanase IV; endo-1,3-β-D-glucanase; 1,3-(1,3; 1,4)-β-D-glucan 3 (4)-glucanohydrolase; EC 3.2.1.6. Cat No: NATE-0768. | |
| Sugar , Compressible | Sugar , Compressible. Product ID: PE-0487. Category: Sweetening agent. Product Keywords: Pharmaceutical Excipients; Excipients for Solid Dosage Form; Sugar , Compressible; Sweeteners Excipients; Sweetening agent. UNII: NA. Grade: Pharmceutical Excipients. Administration route: Oral. Dosage Form: Capsules; Tablets. Stability and Storage Conditions: Compressible sucrose is stable at room temperature and low humidity. Store in an airtight container in a cool, dry place. Source and Preparation: This product is prepared by co-crystallization of sucrose and other excipients such as maltodextrin. Compressible sucrose can also be prepared by dry granulation process. Applications: Compressible sucrose is mainly used for direct compression of chewable tablets. Small changes in water content affect the properties of tablet forming. | |
| Transglutaminase 2 from Cynomolgus, Recombinant | Transglutaminases are a family of enzymes that catalyze the posttranslational modification of proteins by inserting an isopeptide bond within or between polypeptide chains. These enzymes catalyze the acyl transfer reaction between the γ-carboxyamide groups of peptide-bound glutamine residues and a variety of primary amines, particularly the ε-amino group of lysine. The resulting crosslink is of great significance, since it is highly stable and also resistant to mechanical and proteolytic degradation. Applications: Labeling, immobilisation, conjugation and modification of proteins. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; trans...l., Anal. Biochem. 44 (221-231). Appearance: White lyophilized solid. Storage: Store at -20°C in working aliquots. Repeated freezing and thawing is not recommended.Delivery is possible at ambient temperature. Form: The purified transglutaminase is lyophilized from 10 mM Tris-HCl pH 7.4, 300 mM NaCl, 1 mM DTT, 1 mM EDTA, contains maltodextrin. Source: HEK-293F. Species: Cynomolgus. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine & | |
| Transglutaminase 2 from Dog, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: The transglutaminase 2 catalyzes acyl transfer reactions from glutamine residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. the transglutaminase 2 may also be used for immunoprecipitation. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor X...1). Appearance: White lyophilized solid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing.Delivery is possible at ambient temperature. Form: The transglutaminase is lyophilized from 10 mM Tris-HCl pH 8.1, 150 mM NaCl, 1 mM EDTA, 5 mM DTT. Sample contains maltodextrin. Source: Insect cells. Species: Dog. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 250 μ | |
| Transglutaminase 2 from Human tissue, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: Transglutaminase 2 catalyzes acyl transfer reactions from glutamin residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. transglutaminase 2 may also be used for immunoprecipitation. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa...e: White lyophilized solid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing.Delivery is possible at ambient temperature. Form: The transglutaminase is lyophilized from 10 mM Tris-HCl pH 8.1, 150 mM NaCl, 1 mM EDTA, 5 mM DTT. Sample contains maltodextrin. Source: Insect cells. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 250 μg; 1mg. | |
| Transglutaminase 2 from Mouse, Recombinant | Transglutaminase 2 is based on clone IRAKp961C066Q. It is N-terminally fused to a hexahistidine-tag resulting in the encoded N-terminal amino acid sequence MHHHHHHAEELLL. Transglutaminase 2 is produced in E. coli and purified by ion metal chelating chromatography to more than 95 % purity. Applications: The transglutaminase 2 catalyzes acyl transfer reactions from glutamine residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. the transglutaminase 2 may also be used... monodansylcadaverine-incorporation into N,N-dimethylated casein according to Lorand et al., Anal. Biochem. 44 (221-231). Appearance: White lyophilized solid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing.Delivery is possible at ambient temperature. Form: The transglutaminase is lyophilized from 50 mM NaH2PO4, 150 mM NaCl, pH 8. Sample contains maltodextrin. Source: E. coli. Species: Mouse. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine &ga | |
| Transglutaminase 2 from Rabbit, Recombinant | This enzyme is based on the NCBI database sequence XM_008256006. It is N-terminally fused to a hexahistidine-tag resulting in the encoded N-terminal amino acid sequence MHHHHHHAEDLIL . This enzyme is produced in E. coli and purified by ion metal chelating chromatography to more than 95 % purity. Applications: The transglutaminase 2 catalyzes acyl transfer reactions from glutamin residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue.the transglutaminase 2 may also b...lyzed monodansylcadaverine-incorporation into N,N-dimethylated casein according to Lorand et al., Anal. Biochem. 44 (221-231)]. Appearance: White lyophilized solid. Storage: Store at -20 °C in working aliquots. Repeated freezing and thawing is not recommended.Delivery is possible at ambient temperature. Form: The enzyme is lyophilized from 50 mM NaH2PO4, 150 mM NaCl, pH 8.0.Sample contains maltodextrin. Source: E. coli. Species: Rabbit. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide: | |
| Transglutaminase 2 from Rat, Recombinant | Transglutaminase 2 is based on clone IRBPp993H102D. It is N-terminally fused to a hexahistidine-tag resulting in the encoded N-terminal amino acid sequence MHHHHHHAEELNL. Transglutaminase 2 is produced in E. coli and purified by ion metal chelating chromatography to more than 95 % purity. Applications: The transglutaminase 2 catalyzes acyl transfer reactions from glutamine residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. the transglutaminase 2 may also be used ...d monodansylcadaverine-incorporation into N,N-dimethylated casein according to Lorand et al., Anal. Biochem. 44 (271-231). Appearance: White lyophilized solid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing.Delivery is possible at ambient temperature. Form: The transglutaminase is lyophilized from 50 mM NaH2PO4, 150 mM NaCl, pH 8. Sample contains maltodextrin. Source: E. coli. Species: Rat. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine &gamm | |
| Transglutaminase 4 from Human prostate, Recombinant | This enzyme is based on clone IMAGp958A10818Q2. It is N-terminally fused to a hexahistidine-tag resulting in the encoded N-terminal amino acid sequence MHHHHHHAEELLL . This enzyme is produced in E. coli and purified by ion metal chelating chromatography to more than 95 % purity. Applications: The transglutaminase 4 catalyzes acyl transfer reactions from glutamine residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. the transglutaminase 4 may also be used for ...verine-incorporation into N,N-dimethylated casein according to Lorand et al., Anal. Biochem. 44 (221-231). Appearance: White lyophilized solid. Storage: Store at -20 °C in working aliquots. Repeated freezing and thawing is not recommended.Delivery is possible at ambient temperature. Form: The transglutaminase is lyophilized from 10 mM Tris-HCl pH 8.1, 150 mM NaCl, 5 mM DTT, 1 mM EDTA. Sample contains maltodextrin. Source: E. coli. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-gluta | |
| Transglutaminase from Cynomolgus, Recombinant | Transglutaminases are a family of enzymes that catalyze the posttranslational modification of proteins by inserting an isopeptide bond within or between polypeptide chains. These enzymes catalyze the acyl transfer reaction between the γ-carboxyamide groups of peptide-bound glutamine residues and a variety of primary amines, particularly the ε-amino group of lysine. The resulting crosslink is of great significance, since it is highly stable and also resistant to mechanical and proteolytic degradation. Applications: Labeling, immobilisation, conjugation and modification of proteins. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transg... casein according to Lorand et al., Anal. Biochem. 44 (221-231). Appearance: White lyophilized solid. Storage: Store at -20°C in working aliquots. Repeated freezing and thawing is not recommended.Delivery is possible at ambient temperature. Form: The purified transglutaminase is lyophilized from 20 mM Tris-HCl pH 7.5, 150 mM NaCl, 1 mM DTT, 1 mM EDTA, contains maltodextrin. Source: Insect cells. Species: Cynomolgus. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutam | |
| Transglutaminase from Guinea pig, Recombinant | Catalyzes acyl transfer reactions from glutamine residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. Group: Enzymes. Enzyme Commission Number: EC 2.3.2.13. CAS No. 80146-85-6. Purity: >95% (SDS-PAGE). Mole weight: ~77kDa. Activity: >8 U/mg. Storage: Store at -20°C. After reconstitution, prepare aliquots and store at -20°C. Avoid freeze/thaw cycles. Form: Lyophilized from 50mM NaH2PO4, pH 8.0, containing 150mM sodium chloride. Sample contains maltodextrin. Source: E.coli. Species: Guinea pig liver. Cat No: NATE-1721. | |
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