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| Product | Description | |
|---|---|---|
| Phosphorylase b from rabbit muscle | Phosphorylase b from rabbit muscle. Uses: Designed for use in research and industrial production. Additional or Alternative Names: α-Glucan Phosphorylase. Appearance: Powder. CAS No. 9012-69-5. Product ID: ACM9012695-1. Alfa Chemistry ISO 9001:2015 Certified. |  |
| phosphorylase kinase | Requires Ca2+ and calmodulin for activity. The enzyme phosphorylates a specific serine residue in each of the subunits of the dimeric phosphorylase b. For muscle phosphorylase but not liver phosphorylase, this is accompaniedby a further dimerization to form a tetrameric phosphorylase. The enzyme couples muscle contraction with energy production via glycogenolysis-glycolysis by catalysing the Ca2+-dependent phosphorylation and activation of glycogen phosphorylase b. The γ subunit of the tetramericenzyme is the catalytic subunit. Group: Enzymes. Synonyms: dephosphophosphorylase kinase; glycogen phosphorylase kinase; PHK; phosphorylase b kinase; phosphorylase B kinase; phosphorylase kinase (phosphorylating); STK17. Enzyme Commission Number: EC 2.7.11.19. CAS No. 9001-88-1. 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-3138; phosphorylase kinase; EC 2.7.11.19; 9001-88-1; dephosphophosphorylase kinase; glycogen phosphorylase kinase; PHK; phosphorylase b kinase; phosphorylase B kinase; phosphorylase kinase (phosphorylating); STK17. Cat No: EXWM-3138. |  |
| Phosphorylase kinase | Phosphorylase kinase (PhK) is a biochemical reagent that can be used as a biological material or organic compound for life science related research. Uses: Scientific research. Group: Signaling pathways. Alternative Names: PhK. CAS No. 9001-88-1. Pack Sizes: 500 U; 1000 U. Product ID: HY-P2757. |  |
| Phosphorylase Kinase β-Subunit Fragment 420-436 | It is the β-subunit fragment (peptide 430-436) of phosphorylase kinase. Phosphokinase is a serine/threonine specific protein kinase that activates glycogen phosphorylase to release glucose-1-phosphate from glycogen. Synonyms: Lys-Arg-Asn-Pro-Gly-Ser-Gln-Lys-Arg-Phe-Pro-Ser-Asn-Cys-Gly-Arg-Asp; L-lysyl-L-arginyl-L-asparagyl-L-prolyl-glycyl-L-seryl-L-glutaminyl-L-lysyl-L-arginyl-L-phenylalanyl-L-prolyl-L-seryl-L-asparagyl-L-cysteinyl-glycyl-L-arginyl-L-aspartic acid; Phosphorylase Kinase b-Subunit Fragment (420-436). Grades: ≥95%. CAS No. 150829-21-3. Molecular formula: C79H131N31O25S. Mole weight: 1947.14. |  |
| 1,2-α-glucosylglycerol phosphorylase | The enzyme has been isolated from the bacterium Bacillus selenitireducens. In the absence of glycerol the enzyme produces α-D-glucopyranose and phosphate from β-D-glucopyranose 1-phosphate. In this reaction the glucosyl residue is transferred to a water molecule with an inversion of the anomeric conformation. Group: Enzymes. Synonyms: 2-O-α-D-glucopyranosylglycerol phosphorylase. Enzyme Commission Number: EC 2.4.1.332. 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-2570; 1,2-α-glucosylglycerol phosphorylase; EC 2.4.1.332; 2-O-α-D-glucopyranosylglycerol phosphorylase. Cat No: EXWM-2570. | |
| 1,2-β-oligoglucan phosphorylase | The enzyme has been isolated from the bacterium Listeria innocua. It catalyses the reversible phosphorolysis of β-(1?2)-D-glucans. The minimum length of the substrate for the phosphorolytic reaction is 3 D-glucose units. In the synthetic reaction starting from sophorose and α-D-glucose 1-phosphate the average polymerisation degree is 39. Group: Enzymes. Enzyme Commission Number: EC 2.4.1.333. 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-2571; 1,2-β-oligoglucan phosphorylase; EC 2.4.1.333. Cat No: EXWM-2571. | |
| 1,2-β-oligomannan phosphorylase | The enzyme, originally characterized from the thermophilic anaerobic bacterium Thermoanaerobacter sp. X514, catalyses a reversible reaction. In the synthetic direction it produces oligosaccharides with a degree of polymerization (DP) of 3, 4 and 5. The phosphorolysis reaction proceeds to completion, although activity is highest when the substrate has at least three residues. cf. EC 2.4.1.339, β-1,2-mannobiose phosphorylase. Group: Enzymes. Enzyme Commission Number: EC 2.4.1.340. 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-2579; 1,2-β-oligomannan phosphorylase; EC 2.4.1.340. Cat No: EXWM-2579. | |
| 1,3-α-oligoglucan phosphorylase | The enzyme, isolated from the bacterium Clostridium phytofermentans, catalyses a reversible reaction. Substrates for the phosphorolytic reaction are α-1,3-linked oligoglucans with a polymerisation degree of 3 or more. Nigerose (i.e. 3-O-α-D-glucopyranosyl-D-glucopyranose) is not phosphorylyzed but can serve as substrate in the reverse direction (cf. EC 2.4.1.279, nigerose phosphorylase). Group: Enzymes. Enzyme Commission Number: EC 2.4.1.334. 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-2572; 1,3-α-oligoglucan phosphorylase; EC 2.4.1.334. Cat No: EXWM-2572. | |
| 1,3-β-D-glucan phosphorylase | Acts on a range of β-1,3-oligoglucans, and on glucans of laminarin type. Different from EC 2.4.1.30 (1,3-β-oligoglucan phosphorylase) and EC 2.4.1.31 (laminaribiose phosphorylase). Group: Enzymes. Synonyms: laminarin phosphoryltransferase; 1,3-β-D-glucan:orthophosphate glucosyltransferase; 1,3-β-D-glucan:phosphate α-D-glucosyltransferase. Enzyme Commission Number: EC 2.4.1.97. CAS No. 37340-31-1. 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-2636; 1,3-β-D-glucan phosphorylase; EC 2.4.1.97; 37340-31-1; laminarin phosphoryltransferase; 1,3-β-D-glucan:orthophosphate glucosyltransferase; 1,3-β-D-glucan:phosphate α-D-glucosyltransferase. Cat No: EXWM-2636. | |
| 1,3-β-galactosyl-N-acetylhexosamine phosphorylase | Reaction also occurs with β-D-galactopyranosyl-(1?3)-N-acetyl-D-galactosamine as the substrate, giving N-acetyl-D-galactosamine as the product. Group: Enzymes. Synonyms: lacto-N-biose phosphorylase; LNBP; galacto-N-biose phosphorylase. Enzyme Commission Number: EC 2.4.1.211. CAS No. 224427-06-9. 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-2439; 1,3-β-galactosyl-N-acetylhexosamine phosphorylase; EC 2.4.1.211; 224427-06-9; lacto-N-biose phosphorylase; LNBP; galacto-N-biose phosphorylase. Cat No: EXWM-2439. | |
| 1,3-β-oligoglucan phosphorylase | Does not act on laminarin. Differs in specificity from EC 2.4.1.31 (laminaribiose phosphorylase) and EC 2.4.1.97 (1,3-β-D-glucan phosphorylase). Group: Enzymes. Synonyms: β-1,3-oligoglucan:orthophosphate glucosyltransferase II; β-1,3-oligoglucan phosphorylase; 1,3-β-D-oligoglucan:phosphate α-D-glucosyltransferase. Enzyme Commission Number: EC 2.4.1.30. CAS No. 37257-28-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2534; 1,3-β-oligoglucan phosphorylase; EC 2.4.1.30; 37257-28-6; β-1,3-oligoglucan:orthophosphate glucosyltransferase II; β-1,3-oligoglucan phosphorylase; 1,3-β-D-oligoglucan:phosphate α-D-glucosyltransferase. Cat No: EXWM-2534. | |
| 1,4-β-mannosyl-N-acetylglucosamine phosphorylase | The enzyme isolated from the anaerobic bacterium Bacteroides thetaiotaomicron is involved in the degradation of host-derived N-glycans. Group: Enzymes. Synonyms: BT1033. Enzyme Commission Number: EC 2.4.1.320. 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-2557; 1,4-β-mannosyl-N-acetylglucosamine phosphorylase; EC 2.4.1.320; BT1033. Cat No: EXWM-2557. | |
| 3-O-α-D-glucosyl-L-rhamnose phosphorylase | The enzyme does not phosphorylate α,α-trehalose, kojibiose, nigerose, or maltose. In the reverse phosphorolysis reaction the enzyme is specific for L-rhamnose as acceptor and β-D-glucose 1-phosphate as donor. Group: Enzymes. Synonyms: cphy1019 (gene name). Enzyme Commission Number: EC 2.4.1.282. 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-2515; 3-O-α-D-glucosyl-L-rhamnose phosphorylase; EC 2.4.1.282; cphy1019 (gene name). Cat No: EXWM-2515. | |
| 4-O-β-D-mannosyl-D-glucose phosphorylase | This enzyme forms part of a mannan catabolic pathway in the anaerobic bacterium Bacteroides fragilis NCTC 9343. Group: Enzymes. Synonyms: mannosylglucose phosphorylase. Enzyme Commission Number: EC 2.4.1.281. 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-2514; 4-O-β-D-mannosyl-D-glucose phosphorylase; EC 2.4.1.281; mannosylglucose phosphorylase. Cat No: EXWM-2514. | |
| α,α-trehalose phosphorylase | This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. Group: Enzymes. Synonyms: trehalose phosphorylase. Enzyme Commission Number: EC 2.4.1.64. CAS No. 37205-59-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2607; α,α-trehalose phosphorylase; EC 2.4.1.64; 37205-59-7; trehalose phosphorylase. Cat No: EXWM-2607. | |
| α,α-trehalose phosphorylase (configuration-retaining) | Unlike EC 2.4.1.64, α,α-trehalose phosphorylase, this enzyme retains its anomeric configuration. Vanadate is a strong competitive inhibitor of this reversible reaction. Group: Enzymes. Synonyms: trehalose phosphorylase[ambiguous]. Enzyme Commission Number: EC 2.4.1.231. 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-2461; α,α-trehalose phosphorylase (configuration-retaining); EC 2.4.1.231; trehalose phosphorylase[ambiguous]. Cat No: EXWM-2461. | |
| AMP phosphorylase | The enzyme from archaea is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes. The activity with CMP and UMP requires activation by cAMP. Group: Enzymes. Synonyms: AMPpase; nucleoside monophosphate phosphorylase; deoA (gene name). Enzyme Commission Number: EC 2.4.2.57. 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-2687; AMP phosphorylase; EC 2.4.2.57; AMPpase; nucleoside monophosphate phosphorylase; deoA (gene name). Cat No: EXWM-2687. | |
| β-1,2-mannobiose phosphorylase | The enzyme, originally characterized from the thermophilic anaerobic bacterium Thermoanaerobacter sp. X514, catalyses a reversible reaction. cf. EC 2.4.1.340, 1,2-β-oligomannan phosphorylase. Group: Enzymes. Enzyme Commission Number: EC 2.4.1.339. 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-2577; β-1,2-mannobiose phosphorylase; EC 2.4.1.339. Cat No: EXWM-2577. | |
| β-1,4-mannooligosaccharide phosphorylase | The enzyme, isolated from the ruminal bacterium Ruminococcus albus, catalyses the reversible phosphorolysis of β-1,4-mannooligosaccharide with a minimum size of three monomers. Group: Enzymes. Synonyms: RaMP2. Enzyme Commission Number: EC 2.4.1.319. 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-2555; β-1,4-mannooligosaccharide phosphorylase; EC 2.4.1.319; RaMP2. Cat No: EXWM-2555. | |
| β-D-galactosyl-(1?4)-L-rhamnose phosphorylase | The enzyme from Clostridium phytofermentans is also active towards towards β-D-galactosyl derivatives of L-mannose, L-lyxose, D-glucose, 2-deoxy-D-glucose, and D-galactose in this order. Differs from 1,3-β-galactosyl-N-acetylhexosamine phosphorylase (EC 2.4.1.211) in being active towards L-rhamnose and inactive towards N-acetyl hexosamine derivatives. Group: Enzymes. Synonyms: D-galactosyl-β1?4-L-rhamnose phosphorylase; GalRhaP. Enzyme Commission Number: EC 2.4.1.247. CAS No. 1236189-79-9. 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-2476; β-D-galactosyl-(1?4)-L-rhamnose phosphorylase; EC 2.4.1.247; 1236189-79-9; D-galactosyl-β1?4-L-rhamnose phosphorylase; GalRhaP. Cat No: EXWM-2476. | |
| cellobionic acid phosphorylase | The enzyme occurs in cellulolytic bacteria and fungi. It catalyses the reversible phosphorolysis of cellobionic acid. In the synthetic direction it produces 4-O-β-D-glucopyranosyl-D-glucuronate from α-D-glucose 1-phosphate and D-glucuronate with low activity. Group: Enzymes. Enzyme Commission Number: EC 2.4.1.321. 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-2558; cellobionic acid phosphorylase; EC 2.4.1.321. Cat No: EXWM-2558. | |
| cellobiose phosphorylase | This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is cellobiose:phosphate alpha-D-glucosyltransferase. This enzyme participates in starch and sucrose metabolism. Group: Enzymes. Enzyme Commission Number: EC 2.4.1.20. CAS No. 9030-20-0. 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-2428; cellobiose phosphorylase; EC 2.4.1.20; 9030-20-0. Cat No: EXWM-2428. | |
| cellodextrin phosphorylase | This enzyme belongs to GH (glycoside hydrolases) family 94. The systematic name of this enzyme class is 1,4-beta-D-oligo-D-glucan:phosphate alpha-D-glucosyltransferase. This enzyme is also called beta-1,4-oligoglucan:orthophosphate glucosyltransferase. Group: Enzymes. Synonyms: β-1,4-oligoglucan:orthophosphate glucosyltransferase; 1,4-β-D-oligo-D-glucan:phosphate α-D-glucosyltransferase. Enzyme Commission Number: EC 2.4.1.49. CAS No. 37277-58-0. 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-2595; cellodextrin phosphorylase; EC 2.4.1.49; 37277-58-0; β-1,4-oligoglucan:orthophosphate glucosyltransferase; 1,4-β-D-oligo-D-glucan:phosphate α-D-glucosyltransferase. Cat No: EXWM-2595. | |
| GDP-D-glucose phosphorylase | The enzyme may be involved in prevention of misincorporation of glucose in place of mannose residues into glycoconjugates i.e. to remove accidentally produced GDP-α-D-glucose. Activities with GDP-L-galactose, GDP-D-mannose and UDP-D-glucose are all less than 3% that with GDP-D-glucose. Group: Enzymes. Enzyme Commission Number: EC 2.7.7.78. 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-3290; GDP-D-glucose phosphorylase; EC 2.7.7.78. Cat No: EXWM-3290. | |
| GDP-L-galactose phosphorylase | The enzyme catalyses a reaction of the Smirnoff-Wheeler pathway, the major route to ascorbate biosynthesis in plants. Group: Enzymes. Synonyms: VTC2; VTC5. Enzyme Commission Number: EC 2.7.7.69. 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-3280; GDP-L-galactose phosphorylase; EC 2.7.7.69; VTC2; VTC5. Cat No: EXWM-3280. | |
| [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase | This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2, glutamine synthetase. The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42, [glutamine synthetase] adenylyltransferase). The two activities are present on separate domains. Group: Enzymes. Synonyms: adenylyl-[glutamine-synthetase]-deadenylase; [L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine:phosphate adenylyltransferase; [glutamate-ammonia ligase]-adenylyl-L-tyrosine phosphorylase. Enzyme Commission Number: EC 2.7.7.89. 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-3302; [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase; EC 2.7.7.89; adenylyl-[glutamine-synthetase]-deadenylase; [L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine:phosphate adenylyltransferase; [glutamate-ammonia ligase]-adenylyl-L-tyrosine phosphorylase. Cat No: EXWM-3302. | |
| 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 | |
| Glycogen Phosphorylase Inhibitor | Glycogen phosphorylase inhibitor is a cell-permeable inhibitor of human liver glycogen phosphorylase with an IC50 value of 53 nM. It has been used in biological studies to study glycogen utilization in human liver HepG2 cells, retinal explants, and human T lymphocyte Kit 225 cells. Synonyms: GPI; 2-chloro-4, 5-difluoro-N- [ [ [2-methoxy-5- [ [ (methylamino) carbonyl] amino] phenyl] amino] carbonyl] -benzamide. Grades: ≥98%. CAS No. 648926-15-2. Molecular formula: C17H15ClF2N4O4. Mole weight: 412.8. | |
| Glycogen Phosphorylase Inhibitor | Glycogen Phosphorylase Inhibitor is used in biological studies to to evaluate glycogen utilization in human liver HepG2 cells. Group: Biochemicals. Grades: Highly Purified. CAS No. 648926-15-2. Pack Sizes: 1mg, 5mg. Molecular Formula: C17H15ClF2N4O4, Molecular Weight: 412.78. US Biological Life Sciences. |  Worldwide |
| guanosine phosphorylase | Also acts on deoxyguanosine. Group: Enzymes. Enzyme Commission Number: EC 2.4.2.15. CAS No. 9030-28-8. 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-2642; guanosine phosphorylase; EC 2.4.2.15; 9030-28-8. Cat No: EXWM-2642. | |
| kojibiose phosphorylase | The enzyme from Thermoanaerobacter brockii can act with α-1,2-oligoglucans, such as selaginose, as substrate, but more slowly. The enzyme is inactive when dissaccharides with linkages other than α-1,2 linkages, such as sophorose, trehalose, neotrehalose, nigerose, laminaribiose, maltose, cellobiose, isomaltose, gentiobiose, sucrose and lactose, are used as substrates. Group: Enzymes. Enzyme Commission Number: EC 2.4.1.230. CAS No. 206566-36-1. 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-2460; kojibiose phosphorylase; EC 2.4.1.230; 206566-36-1. Cat No: EXWM-2460. | |
| laminaribiose phosphorylase | Also acts on 1,3-β-D-oligoglucans. Differs in specificity from EC 2.4.1.30 (1,3-β-oligoglucan phosphorylase) and EC 2.4.1.97 (1,3-β-D-glucan phosphorylase). Group: Enzymes. Enzyme Commission Number: EC 2.4.1.31. CAS No. 37257-29-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2545; laminaribiose phosphorylase; EC 2.4.1.31; 37257-29-7. Cat No: EXWM-2545. | |
| maltose phosphorylase | This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is maltose:phosphate 1-beta-D-glucosyltransferase. This enzyme participates in starch and sucrose metabolism. Group: Enzymes. Enzyme Commission Number: EC 2.4.1.8. CAS No. 9030-19-7. MP. 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-2620; maltose phosphorylase; EC 2.4.1.8; 9030-19-7. Cat No: EXWM-2620. | |
| Maltose phosphorylase | Maltose phosphorylase is a dimerase which catalyzes the transformation of maltose and inorganic phosphate into β-D-glucose-1-phosphate and glucose. Maltose phosphorylases have been classified in family 65 of the glycoside hydrolases [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: E.C. 2.4.1.8. CAS No. 9030-19-7. Pack Sizes: 50 U; 250 U. Product ID: HY-P2741. | |
| Maltose Phosphorylase from E. coli, Recombinant | Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes maltose and inorganic phosphate into β-D-glucose-1-phosphate and glucose. Group: Enzymes. Synonyms: maltose phosphorylase; maltose:phosphate 1-β-D-glucosyltransferase; EC 2.4.1.8; 9030-19-7; MP. Enzyme Commission Number: EC 2.4.1.8. CAS No. 9030-19-7. MP. Mole weight: ca. 220 kDa. Activity: > 10 U/mg lyophilizate. Stability: Stability (liquid form) stable at 37°C for at least one week Stability (powder form) stable at 30°C for at least four weeks. Appearance: White lyophilizate. Storage: at -20°C. Source: E. coli. Species: E. coli. maltose phosphorylase; maltose:phosphate 1-β-D-glucosyltransferase; EC 2.4.1.8; 9030-19-7; MP. Cat No: NATE-1250. | |
| Maltose Phosphorylase from Enterococcus sp., Recombinant | Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes maltose and inorganic phosphate into β-D-glucose-1-phosphate and glucose. Maltose phosphorylase (mp) is a dimeric enzyme that catalyzes maltose and inorganic phosphate into β-d-glucose-1-phosphate and glucose. Applications: Maltose phosphorylase from enter oc occus has been used in a study to describe a new pathway for maltose utilization in lactic acid bacteria. it has also been used in a study to describe the transfer of glucosyl moiety of maltose to acceptors with alcoholic oh groups. Group: Enzymes. Synonyms: maltose phosphorylase; maltose:phosphate 1-β-D-glucosyltransferase; EC 2.4.1.8; 9030-19-7; MP. Enzyme Commission Number: EC 2.4.1.8. CAS No. 9030-19-7. MP. Mole weight: mol wt 90 kDa by SDS-PAGE. Storage: -20°C. Form: lyophilized powder. Source: E. coli. Species: Enterococcus sp. maltose phosphorylase; maltose:phosphate 1-β-D-glucosyltransferase; EC 2.4.1.8; 9030-19-7; MP. Cat No: NATE-0456. | |
| Native Bacillus sp. Purine Nucleoside Phosphorylase | Purine nucleoside phosphorylase (also known as PNPase) is an enzyme (EC 2.4.2.1) involved in purine metabolism. PNP metabolizes adenosine into adenine, inosine into hypoxanthine, and guanosine into guanine, in each case creating ribose phosphate. NP encodes the enzyme purine nucleoside phosphorylase that together with adenosine deaminase (ADA) serves a key role in purine catabolism, referred to as the salvage pathway. Mutations in either enzyme result in a severe combined immunodeficiency (SCID). Confusingly, the same abbreviation (PNPase), is also used for another, otherwise unrelated, enzyme, namely Polynucleotide Phosphorylase. Purine nucleoside phosphorylase produced in microorganism has a molecular mass of 32 kda. Applications: Useful for enzymatic determination of inorganic phosphate. Group: Enzymes. Synonyms: inos. Enzyme Commission Number: EC 2.4.2.1. CAS No. 9030-21-1. PNPase. Activity: > 500U/mL. Appearance: Colourless to light brown solution. Storage: -20°C. Form: Liquid. Source: Bacillus sp. inosine phosphorylase; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase; purine ribonucleoside phosphorylase; purine-nucleoside: phosphate ribosyltransferase; EC 2.4.2.1. Cat No: DIA-164. | |
| Native Bacillus stearothermophilus Polynucleotide Phosphorylase | Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity. It is also involved in mRNA processing and degradation in bacteria, plants, and humans. Applications: The enzyme is useful for the preparation of polyribonucleotide. Group: Enzymes. Synonyms: PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Enzyme Commission Number: EC 2.7.7.8. CAS No. 9014-12-4. Polynucleotide phosphorylase. Mole weight: 300,000 - 340,000; Subunit molecular weight : ca. 85,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Bacillus stearothermophilus. PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Cat No: NATE-1908. | |
| Native Bacteria Maltose phosphorylase | Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes maltose and inorganic phosphate into β-D-glucose-1-phosphate and glucose. Group: Enzymes. Synonyms: maltose phosphorylase; maltose:phosphate 1-β-D-glucosyltransferase; EC 2.4.1.8; 9030-19-7; MP. Enzyme Commission Number: EC 2.4.1.8. CAS No. 9030-19-7. MP. Activity: > 5 units/mg protein (at 25°C and pH 7.5). Storage: 0 -5°C. Form: Ammonium sulfate suspension. Source: Bacteria. maltose phosphorylase; maltose:phosphate 1-β-D-glucosyltransferase; EC 2.4.1.8; 9030-19-7; MP. Cat No: NATE-1031. | |
| Native Baker's yeast Uridine-5'-diphosphoglucose pyrophosphorylase | UTP-glucose-1-phosphate uridylyltransferase is an enzyme associated with glycogenesis. It synthesizes UDP-glucose from glucose-1-phosphate and UTP; i.e., glucose-1-phosphate + UTP<-> UDP-glucose + pyrophosphate. Applications: Uridine-5?-diphosphoglucose pyrophosphorylase has been used in assays to determine the concentration of pyrophosphate in human urine samples. Group: Enzymes. Synonyms: UDP glucose pyrophosphorylase; glucose-1-phosphate uridylyltransferase; UDPG phosphorylase; UDPG pyrophosphorylase; uridine 5'-diphosphoglucose pyrophosphorylase; uridine diphosphoglucose pyrophosphorylase; uridine diphosphate-D-glucose pyrophosphorylase; uridine-diphosphate glucose pyrophosphorylase; EC 2.7.7.9; 9026-22-6. Enzyme Commission Number: EC 2.7.7.9. CAS No. 9026-22-6. UDPG pyrophosphorylase. Activity: > 50 units/mg protein. Storage: -20°C. Form: Lyophilized, sulfate-free powder containing Citrate buffer salt. Source: Baker's yeast. UDP glucose pyrophosphorylase; glucose-1-phosphate uridylyltransferase; UDPG phosphorylase; UDPG pyrophosphorylase; uridine 5'-diphosphoglucose pyrophosphorylase; uridine diphosphoglucose pyrophosphorylase; uridine diphosphate-D-glucose pyrophosphorylase; uridine-diphosphate glucose pyrophosphorylase; EC 2.7.7.9; 9026-22-6. Cat No: NATE-0728. | |
| Native Brewer's bottom yeast Orotidine-5'-monophosphate pyrophosphorylase | Orotate phosphoribosyltransferase (OPRTase) or Orotic acid phosphoribosyltransferase is an enzyme involved in pyrimidine biosynthesis. It catalyzes the formation of orotidine 5'-monophosphate (OMP) from orotate and phosphoribosyl pyrophosphate. In yeast and bacteria, orotate phosphoribosyltransferase is an independent enzyme with a unique gene coding for the protein, whereas in mammals and other multicellular organisms, the catalytic function is carried out by a domain of the bifunctional enzyme UMP synthase. Applications: This is the preferred enzyme for assaying orotidine 5?-monophosphate and for the production of omp analogs from the corresponding orot...ty: ~25 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: Lyophilized powder containing approx. 50% buffer salts. Source: Brewer's bottom yeast. orotidylic acid phosphorylase; orotidine-5'-phosphate pyrophosphorylase; OPRTase; orotate phosphoribosyl pyrophosphate transferase; orotic acid phosphoribosyltransferase; orotidine 5'-monophosphate pyrophosphorylase; orotidine monophosphate pyrophosphorylase; orotidine phosphoribosyltransferase; orotidylate phosphoribosyltransferase; orotidylate pyrophosphorylase; orotidylic acid pyrophosphorylase; orotidylic phosphorylase; orotidylic pyrophosphorylase; EC 2.4.2.10; 9030-25-5. Cat No: NATE-0498. | |
| Native Leuconostoc Mesenteroides Sucrose Phosphorylase | Sucrose phosphorylase (EC. 2.4.1.7) is an important enzyme in the metabolism of sucrose and regulation of other metabolic intermediates. Sucrose phosphorylase is in the class of hexosyltransferases. More specifically it has been placed in the retaining glycoside hydrolases family although it catalyzes a transglycosidation rather than hydrolysis. Sucrose phosphorylase catalyzes the conversion of sucrose to D-fructose and α-D-glucose-1-phosphate. It has been shown in multiple experiments that the enzyme catalyzes this conversion by a double displacement mechanism. Group: Enzymes. Synonyms: Sucrose Phosphorylase; EC 2.4.1.7; sucrose glucosyltransferase; disaccharide glucosyltransferase; Sucrose:orthophosphate α-D-glucosytransferase. Enzyme Commission Number: EC. 2.4.1.7. CAS No. 9074-06-0. Sucrose Phosphorylase. Activity: > 100 units/mg protein. Storage: Store at -20°C. Form: Lyophilized powder. Source: Leuconostoc Mesenteroides. Sucrose Phosphorylase; EC 2.4.1.7; sucrose glucosyltransferase; disaccharide glucosyltransferase; Sucrose:orthophosphate α-D-glucosytransferase. Cat No: NATE-0890. | |
| Native Microorganism Purine-nucleoside phosphorylase | In enzymology, a purine-nucleoside phosphorylase (EC 2.4.2.1) is an enzyme that catalyzes the chemical reaction: purine nucleoside + phosphate <-> purine + alpha-D-ribose 1-phosphate. Thus, the two substrates of this enzyme are purine nucleoside and phosphate, whereas its two products are purine and alpha-D-ribose 1-phosphate. This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. Applications: This enzyme is useful for enzymatic determination of inorganic phosphorus, 5'-nucleotidase and adenosine deaminase when coupled with xanthine oxidase and uricase. Group: Enzymes. Synonyms: EC 2.4.2.1; inosine phosphorylase; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynuc. Enzyme Commission Number: EC 2.4.2.1. CAS No. 9030-21-1. PNPase. Mole weight: approx. 120 kDa. Activity: Grade? 15U/mg-solid or more. Stability: Stable at-20°C for at least 12 months. Appearance: White amorphous powder, lyophilized. Source: Microorganism. EC 2.4.2.1; inosine phosphorylase; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase; purine ribonucleoside phosphorylase; purine-nucleoside: phosphate ribosyltransferase. Cat No: DIA-216. | |
| Native Microorganisms Nucleoside Phosphorylase | In enzymology, a purine-nucleoside phosphorylase (EC 2.4.2.1) is an enzyme that catalyzes the chemical reaction:purine nucleoside + phosphate<-> purine + alpha-D-ribose 1-phosphate. Thus, the two substrates of this enzyme are purine nucleoside and phosphate, whereas its two products are purine and alpha-D-ribose 1-phosphate. This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. This enzyme participates in 3 metabolic pathways:purine metabolism, pyrimidine metabolism, and nicotinate and nicotinamide metabolism. Applications: Nucleoside phosphorylase is used in coupled enzyme systems to measure protein dephosphorylation. this e...osphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase; purine ribonucleoside phosphorylase; 9030-21-1; EC 2.4.2.1. Enzyme Commission Number: EC 2.4.2.1. CAS No. 9030-21-1. PNPase. Mole weight: mol wt ~120 kDa. Activity: > 10 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium gluconate, mannitol and EDTA. Source: Microorganisms. purine-nucleoside phosphorylase; inosine phosphorylase; PNP; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; pu | |
| 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 Rabbit Phosphorylase Kinase | Phosphorylase kinase (PhK) is a serine/threonine-specific protein kinase which activates glycogen phosphorylase to release glucose-1-phosphate from glycogen. PhK phosphorylates glycogen phosphorylase at two serine residues, triggering a conformational shift which favors the more active glycogen phosphorylase a form over the less active glycogen phosphorylase b. Phosphorylase kinase contains four subunits each containing an α, β, γ, and creative enzymes component. the creative enzymes component binds 4 calcium molecules and is termed calmodulin while the γ unit acts as the catalytic subunit. Applications: Phosphorylase kinase from rabbit muscle has be...osphorylase kinase; glycogen phosphorylase kinase; PHK; phosphorylase b kinase; phosphorylase B kinase; phosphorylase kinase (phosphorylating); STK17; EC 2.7.11.19; EC 2.7.1.38; 9001-88-1. Enzyme Commission Number: EC 2.7.1.38. CAS No. 9001-88-1. PHK. Activity: > 60 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing (NH4)2SO4, sucrose, β-glycerophosphate and dithioerythritol. Source: Rabbit muscle. Species: Rabbit. Phosphorylase Kinase; dephosphophosphorylase kinase; glycogen phosphorylase kinase; PHK; phosphorylase b kinase; phosphorylase B kinase; phosphorylase kinase (phosphorylating); STK17; EC 2.7.11.19; EC 2.7.1.38; 9001-88-1. Cat No: NATE-0559. | |
| nigerose phosphorylase | The enzymes from Clostridium phytofermentans is specific for nigerose, and shows only 0.5% relative activity with kojibiose (cf. EC 2.4.1.230, kojibiose phosphorylase). Group: Enzymes. Synonyms: cphy1874 (gene name). Enzyme Commission Number: EC 2.4.1.279. 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-2511; nigerose phosphorylase; EC 2.4.1.279; cphy1874 (gene name). Cat No: EXWM-2511. | |
| N,N'-diacetylchitobiose phosphorylase | The enzyme is specific for N,N'-diacetylchitobiose and does not phosphorylate other N-acetylchitooligosaccharides, cellobiose, trehalose, lactose, maltose or sucrose. Group: Enzymes. Synonyms: chbP (gene name). Enzyme Commission Number: EC 2.4.1.280. 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-2513; N,N'-diacetylchitobiose phosphorylase; EC 2.4.1.280; chbP (gene name). Cat No: EXWM-2513. | |
| NUCLEOSIDE PHOSPHORYLASE | NUCLEOSIDE PHOSPHORYLASE. Synonyms: Nucleoside Phosphorylase bacterial,PNP, Purine nucleoside phosphorylase, Purine nucleoside:orthophosphate ribosyltransferase;Purine nucleoside phosphorylase [ >=200 units/mg];Deoxyribonucleoside phosphorylase;Purine deoxynucleoside phosphorylase;Purine deoxyribonucleoside phosphorylase;Purine ribonucleoside phosphorylase;PNP/Purine-nucleoside phosphorylase;Nucleoside Phosphorylase from microorganisms. CAS No. 9030-21-1. Pack Sizes: 1 kg. Product ID: CDF4-0059. Molecular formula: C10H12N4O4. Category: Enzyme Preparations. Product Keywords: Food Ingredients; Enzyme Preparations; NUCLEOSIDE PHOSPHORYLASE; CDF4-0059; 9030-21-1; C10H12N4O4; 232-857-3; 9030-21-1. Purity: 0.98. EC Number: 232-857-3. Physical State: lyophilized Powder. Storage: -20°C. |  |
| Nucleoside Phosphorylase from bacterial, Recombinant | In enzymology, a purine-nucleoside phosphorylase (EC 2.4.2.1) is an enzyme that catalyzes the chemical reaction:purine nucleoside + phosphate<-> purine + alpha-D-ribose 1-phosphate. Thus, the two substrates of this enzyme are purine nucleoside and phosphate, whereas its two products are purine and alpha-D-ribose 1-phosphate. This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. This enzyme participates in 3 metabolic pathways:purine metabolism, pyrimidine metabolism, and nicotinate and nicotinamide metabolism. Applications: Nucleoside phosphorylase is used in coupled enzyme systems to measure protein dephosphorylation. bac...eoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase; purine ribonucleoside phosphorylase; 9030-21-1; EC 2.4.2.1. Enzyme Commission Number: EC 2.4.2.1. CAS No. 9030-21-1. PNPase. Activity: > 10 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: E. coli. Species: Bacterial. purine-nucleoside phosphorylase; inosine phosphorylase; PNP; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase; purine ribonucleoside phosphorylase; 9030-21-1; EC 2.4.2.1. Cat No: NATE-0607. | |
| [phosphorylase] phosphatase | This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. Group: Enzymes. Synonyms: PR-enzyme; phosphorylase a phosphatase; glycogen phosphorylase phosphatase; protein phosphatase C; type 1 protein phosphatase. Enzyme Commission Number: EC 3.1.3.17. CAS No. 9025-74-5. 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-3619; [phosphorylase] phosphatase; EC 3.1.3.17; 9025-74-5; PR-enzyme; phosphorylase a phosphatase; glycogen phosphorylase phosphatase; protein phosphatase C; type 1 protein phosphatase. Cat No: EXWM-3619. | |
| Polynucleotide Phosphorylase from Escherichia coli, Recombinant | Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity. It is also involved in mRNA processing and degradation in bacteria, plants, and humans. Applications: Polynucleotide phosphorylase (pnp) has been used in a study to show that spontaneous mutations resulting from replication errors are reduced in a pnp-deficient strain. it has also been used in a study to show that the absence of pnpase makes e. coli cells sensitive to uv, which suggests pnp has a role in survival of uv damage. Group: Enzymes. Synonyms: PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Enzyme Commission Number: EC 2.7.7.8. CAS No. 9014-12-4. Polynucleotide phosphorylase. Storage: -70°C. Form: Supplied as a solution in 20 mM Hepes buffer pH 7.9, 0.1 mM EDTA, 2 mM DTT, 12.5 mM MgCl2, 200 mM KCl, 21.4% (w/v) Glycerol. Source: E. coli. Species: Escherichia coli. PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Cat No: NATE-0608. | |
| Polynucleotide phosphorylase from Human, Recombinant | Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity. It is also involved in mRNA processing and degradation in bacteria, plants, and humans. Group: Enzymes. Synonyms: PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Enzyme Commission Number: EC 2.7.7.8. CAS No. 9014-12-4. Polynucleotide phosphorylase. Storage: -70°C. Form: supplied as a solution in 20 mM HEPES buffer, pH 7.9, with 0.1 mM EDTA, 2 mM DTT, 12.5 mM MgCl2, ~130 mM KCl, and 20% (w/v) glycerol. Source: E. coli. Species: Human. PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Cat No: NATE-0609. | |
| Polynucleotide phosphorylase from Synechocystis sp., Recombinant | Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity. It is also involved in mRNA processing and degradation in bacteria, plants, and humans. Polynuclotide phosphorlyase in spinach chloroplasts acts as a exonuclease and a poly (a) polymerase. Applications: Polynucleotide phosphorylase has been used in a study to discover that a major function of pnpase is the synthesis of cdp. it has also been used in a study to investigate the enzyme responsible for rna 3?-tail synthesis in s. coelicolor. Group: Enzymes. Synonyms: PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Enzyme Commission Number: EC 2.7.7.8. CAS No. 9014-12-4. Polynucleotide phosphorylase. Storage: -70°C. Source: E. coli. Species: Synechocystis sp. PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase; EC 2.7.7.8; 9014-12-4. Cat No: NATE-0610. | |
| purine-nucleoside phosphorylase | Specificity not completely determined. Can also catalyse ribosyltransferase reactions of the type catalysed by EC 2.4.2.5, nucleoside ribosyltransferase. Group: Enzymes. Synonyms: inosine phosphorylase; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase; purine ribonucleoside phosphorylase. Enzyme Commission Number: EC 2.4.2.1. CAS No. 9030-21-1. PNPase. 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-2638; purine-nucleoside phosphorylase; EC 2.4.2.1; 9030-21-1; inosine phosphorylase; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase; purine ribonucleoside phosphorylase. Cat No: EXWM-2638. | |
| Purine nucleoside phosphorylase, Microorganism | Purine nucleoside phosphorylase, Microorganism (PNP) is a key enzyme in purine metabolism, which is involved in the purine rescue pathway. The deficiency of Purine nucleoside phosphorylase resulted in impaired T cell function. In the presence of inorganic orthophosphate as the second substrate, Purine nucleoside phosphorylase catalyzes the breaking of the glycosidic bond between ribose and deoxyribonucleoside to generate purine base and ribose (deoxyribose) -1-phosphate [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: PNP. CAS No. 9030-21-1. Pack Sizes: 100 U. Product ID: HY-P2724. | |
| Purine nucleoside phosphorylase, Recombinant | Purine nucleoside phosphorylase is an enzyme involved in purine metabolism. PNP metabolizes adenosine into adenine, inosine into hypoxanthine, and guanosine into guanine. Mutations in the PNP gene are responsible for purine nucleoside phosphorylase deficiency. Applications: Purine nucleoside phosphorylase is used to study nucleotide salvage pathways and purine metabolism. it is used to study purine nucleoside phosphorylase deficiency and responsible pnp genetic mutations. this product is recombinant and expressed in e. coli. Group: Enzymes. Synonyms: purine-nucleoside phosphorylase; inosine phosphorylase; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase; purine ribonucleoside phosp. Enzyme Commission Number: EC 2.4.2.1. CAS No. 9030-21-1. PNPase. Activity: > 120 U/mL. Storage: -20°C. Form: buffered aqueous solution (100 mM phosphate buffer with 1 mM MgCl2. Source: E. coli. purine-nucleoside phosphorylase; inosine phosphorylase; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase; purine ribonucleoside phosphorylase; EC 2.4.2.1; 9030-21-1. Cat No: NATE-0644. | |
| pyrimidine-nucleoside phosphorylase | Unlike EC 2.4.2.3, uridine phosphorylase, and EC 2.4.2.4, thymidine phosphorylase, this enzyme can accept both the ribonucleoside uridine and the 2'-deoxyribonucleosides 2'-deoxyuridine and thymidine. The reaction is reversible, and the enzyme does not distinguish between α-D-ribose 1-phosphate and 2-deoxy-α-D-ribose 1-phosphate in the synthetic direction. Group: Enzymes. Synonyms: Py-NPase; pdp (gene name). Enzyme Commission Number: EC 2.4.2.2. CAS No. 9055-35-0. PyNPase. 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-2647; pyrimidine-nucleoside phosphorylase; EC 2.4.2.2; 9055-35-0; Py-NPase; pdp (gene name). Cat No: EXWM-2647. | |
| Pyrimidine nucleoside phosphorylase, Recombinant | Pyrimidine nucleoside phosphorylase (PyNPase) is a glycosyltransferase that catalyzes the conversion of pyrimidine nucleoside and phosphate to a pyrimidine base and α-D-ribose 1-phosphate. PyNPase plays a significant role in breast cancer angiogenesis. Applications: Pyrimidine nucleoside phosphorylase (pynpase) may be used as a marker to predict the malignant potential of breast cancer, especially lymph node metastasis. pynpase is used to study breast cancer, specifically its role in angiogenesis. Group: Enzymes. Synonyms: Pyrimidine nucleoside phosphorylase; EC 2.4.2.2; Py-NPase; 9055-35-0; pdp (gene name); PyNPase. Enzyme Commission Number: EC 2.4.2.2. CAS No. 9055-35-0. PyNPase. Activity: > 1300 U/mL. Storage: -20°C. Source: E. coli. Pyrimidine nucleoside phosphorylase; EC 2.4.2.2; Py-NPase; 9055-35-0; pdp (gene name); PyNPase. Cat No: NATE-0646. | |
| Recombinant mutant (Met62Val) purine nucleoside phosphorylase from E. coli | Purine nucleoside phosphorylase is an enzyme involved in purine metabolism. PNP metabolizes adenosine into adenine, inosine into hypoxanthine, and guanosine into guanine. Mutations in the PNP gene are responsible for purine nucleoside phosphorylase deficiency. Applications: These enzymes are widely used for the synthesis of modified nucleotides (virasol, cladribine, fludarabine) which are efficient antiviral and antitumor drugs. Group: Enzymes. Synonyms: purine-nucleoside phosphorylase; inosine phosphorylase; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase;. Enzyme Commission Number: EC 2.4.2.1. CAS No. 9030-21-1. Purity: > 95 %. PNPase. Mole weight: 156 kDa. Activity: 27 U/mg. Appearance: Colourless clear liquid. Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C. Source: E. coli. Species: E. coli. purine-nucleoside phosphorylase; inosine phosphorylase; PNPase; PUNPI; PUNPII; inosine-guanosine phosphorylase; nucleotide phosphatase; purine deoxynucleoside phosphorylase; purine deoxyribonucleoside phosphorylase; purine nucleoside phosphorylase; purine ribonucleoside phosphorylase; EC 2.4.2.1; 9030-21-1. Cat No: NATE-1000. | |
| Recombinant uridine phosphorylase from E. coli | Uridine phosphorylase catalyzes the reversible phosphorolysis of uridine with the formation of ribose-1-phosphate and uracil. Applications: These enzymes are widely used for the synthesis of modified nucleotides (virasol, cladribine, fludarabine) which are efficient antiviral and antitumor drugs. Group: Enzymes. Synonyms: Uridine phosphorylase; EC 2.4.2.3; UrdPase; Upase; StUP. Enzyme Commission Number: EC 2.4.2.3. CAS No. 9030-22-2. Purity: > 85 %. Upase. Mole weight: 27.3 kDa (163.5 kDa - hexamer). Activity: more than 20 u/mg. Appearance: Colourless clear liquid. Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C. Source: E. coli. Species: E. coli. Uridine phosphorylase; EC 2.4.2.3; UrdPase; Upase; StUP. Cat No: NATE-0999. | |
| S-methyl-5'-thioadenosine phosphorylase | Also acts on 5'-deoxyadenosine and other analogues having 5'-deoxy groups. Group: Enzymes. Synonyms: 5'-deoxy-5'-methylthioadenosine phosphorylase; MTA phosphorylase; MeSAdo phosphorylase; MeSAdo/Ado phosphorylase; methylthioadenosine phosphorylase; methylthioadenosine nucleoside phosphorylase; 5'-methylthioadenosine:phosphate methylthio-D-ribosyl-transferase; S-methyl-5-thioadenosine phosphorylase; S-methyl-5-thioadenosine:phosphate S-methyl-5-thio-α-D-ribosyl-transferase. Enzyme Commission Number: EC 2.4.2.28. CAS No. 61970-06-7. MTAP. 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-2655; S-methyl-5'-thioadenosine phosphorylase; EC 2.4.2.28; 61970-06-7; 5'-deoxy-5'-methylthioadenosine phosphorylase; MTA phosphorylase; MeSAdo phosphorylase; MeSAdo/Ado phosphorylase; methylthioadenosine phosphorylase; methylthioadenosine nucleoside phosphorylase; 5'-methylthioadenosine:phosphate methylthio-D-ribosyl-transferase; S-methyl-5-thioadenosine phosphorylase; S-methyl-5-thioadenosine:phosphate S-methyl-5-thio-α-D-ribosyl-transferase. Cat No: EXWM-2655. | |
| S-methyl-5'-thioadenosine phosphorylase from Human, Recombinant | MTAP expression is crucial for the catabolism of methylthioadenosine, which is a by-product of polyamine biosynthesis in the methionine salvage pathway. Protein expression is decreased by homozygous deletion and promoter hypermethylation. N-terminal gst-tagged 57 kda protein containing amino acids 2-end. Applications: S-methyl-5?-thioadenosine phosphorylase human (mtap) is an enzyme used in cancer research that is deficient in many types of cancer. decreased mtap expression may be used as a potential indicator of disease progression of gastrointestinal stromal tumors. mtap may be a used to develop potential therapeutic strategies for hepat ocellular carcinoma ...CAS No. 61970-06-7. MTAP. Mole weight: 57 kDa. Storage: -70°C. Form: Supplied as a solution in 25 mM Tris-HCl, pH 8.0,100 mM NaCl, 0.05% Tween-20, 10% glycerol,and 3 mM DTT. Source: E. coli. Species: Human. S-methyl-5'-thioadenosine phosphorylase; EC 2.4.2.28; 5'-deoxy-5'-methylthioadenosine phosphorylase; MTA phosphorylase; MeSAdo phosphorylase; MeSAdo/Ado phosphorylase; methylthioadenosine phosphorylase; methylthioadenosine nucleoside phosphorylase; 5'-methylthioadenosine:phosphate methylthio-D-ribosyl-transferase; S-methyl-5-thioadenosine phosphorylase; S-methyl-5-thioadenosine:phosphate S-methyl-5-thio-α-D-ribosyl-transferase; MTAP. Cat No: NATE-0462. | |
| S-methyl-5'-thioinosine phosphorylase | No activity with S-methyl-5'-thioadenosine. The catabolism of of 5'-methylthioadenosine in Pseudomonas aeruginosa involves deamination to S-methyl-5'-thioinosine (EC 3.5.4.31, S-methyl-5'-thioadenosine deaminase) and phosphorolysis to hypoxanthine. Group: Enzymes. Synonyms: MTIP; MTI phosphorylase; methylthioinosine phosphorylase. Enzyme Commission Number: EC 2.4.2.44. 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-2673; S-methyl-5'-thioinosine phosphorylase; EC 2.4.2.44; MTIP; MTI phosphorylase; methylthioinosine phosphorylase. Cat No: EXWM-2673. | |
| sucrose 6F-phosphate phosphorylase | The enzyme, isolated from the thermophilic bacterium Thermoanaerobacterium thermosaccharolyticum, catalyses the reversible phosphorolysis of sucrose 6F-phosphate. It also acts on sucrose with lower activity. Group: Enzymes. Synonyms: sucrose 6'-phosphate phosphorylase. Enzyme Commission Number: EC 2.4.1.329. 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-2566; sucrose 6F-phosphate phosphorylase; EC 2.4.1.329; sucrose 6'-phosphate phosphorylase. Cat No: EXWM-2566. | |
| sucrose phosphorylase | In the forward reaction, arsenate may replace phosphate. In the reverse reaction, various ketoses and L-arabinose may replace D-fructose. Group: Enzymes. Synonyms: sucrose glucosyltransferase; disaccharide glucosyltransferase. Enzyme Commission Number: EC 2.4.1.7. CAS No. 9074-06-0. Sucrose Phosphorylase. 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-2613; sucrose phosphorylase; EC 2.4.1.7; 9074-06-0; sucrose glucosyltransferase; disaccharide glucosyltransferase. Cat No: EXWM-2613. | |
| Sucrose phosphorylase 13 A from Bifidobacterium adolescentis, Recombinant | Sucrose phosphorylase (EC. 2.4.1.7) is an important enzyme in the metabolism of sucrose and regulation of other metabolic intermediates. Sucrose phosphorylase is in the class of hexosyltransferases. More specifically it has been placed in the retaining glycoside hydrolases family although it catalyzes a transglycosidation rather than hydrolysis. Sucrose phosphorylase catalyzes the conversion of sucrose to D-fructose and α-D-glucose-1-phosphate. It has been shown in multiple experiments that the enzyme catalyzes this conversion by a double displacement mechanism. Group: Enzymes. Synonyms: Sucrose Phosphorylase; EC 2.4.1.7; sucrose glucosyltransferase; disaccharide glucosyltransferase; Sucrose:orthophosphate α-D-glucosytransferase. Enzyme Commission Number: EC. 2.4.1.7. CAS No. 9074-06-0. Purity: >90% as judged by SDS-PAGE. Sucrose Phosphorylase. Mole weight: 58.2 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: Bifidobacterium adolescentis. Sucrose Phosphorylase; EC 2.4.1.7; sucrose glucosyltransferase; disaccharide glucosyltransferase; Sucrose:orthophosphate α-D-glucosytransferase. Cat No: NATE-1532. | |
| Sucrose Phosphorylase, Recombinant | Sucrose phosphorylase (E.C. 2.4.1.7) is an important enzyme in the metabolism of sucrose and regulation of other metabolic intermediates. Sucrose phosphorylase is in the class of hexosyltransferases. More specifically it has been placed in the retaining glycoside hydrolases family although it catalyzes a transglycosidation rather than hydrolysis. Sucrose phosphorylase catalyzes the conversion of sucrose to D-fructose and α-D-glucose-1-phosphate. It has been shown in multiple experiments that the enzyme catalyzes this conversion by a double displacement mechanism. Sucrose phosphorylase catalyzes the reversible conversion of sucrose (α-d-glucopyranosyl-1,2-β-d...stigate the novel transglucosylating reaction with carboxylic compounds. Group: Enzymes. Synonyms: Sucrose Phosphorylase; EC 2.4.1.7; 9074-06-0; sucrose glucosyltransferase; disaccharide glucosyltransferase; Sucrose:orthophosphate α-D-glucosytransferase. Enzyme Commission Number: EC 2.4.1.7. CAS No. 9074-06-0. Sucrose Phosphorylase. Mole weight: mol wt 56 kDa by SDS-PAGE. Activity: > 45 units/mg solid. Storage: -20°C. Form: lyophilized powder; Contains sucrose as stabilizer. Source: E. coli. Sucrose Phosphorylase; EC 2.4.1.7; 9074-06-0; sucrose glucosyltransferase; disaccharide glucosyltransferase; Sucrose:orthophosphate α-D-glucosytransferase. Cat No: NATE-0684. | |
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