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| Product | Description | |
|---|---|---|
| acyl-phosphate-hexose phosphotransferase | Phosphorylates D-glucose and D-mannose on O-6, and D-fructose on O-1 or O-6. Group: Enzymes. Synonyms: hexose phosphate:hexose phosphotransferase. Enzyme Commission Number: EC 2.7.1.61. CAS No. 37278-06-1. 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-3092; acyl-phosphate-hexose phosphotransferase; EC 2.7.1.61; 37278-06-1; hexose phosphate:hexose phosphotransferase. Cat No: EXWM-3092. |  |
| UDP-glucose-hexose-1-phosphate uridylyltransferase | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase. Other names in common use include uridyl transferase, hexose-1-phosphate uridylyltransferase, uridyltransferase, and hexose 1-phosphate uridyltransferase. This enzyme participates in galactose metabolism and nucleotide sugars metabolism. Group: Enzymes. Synonyms: uridyl transferase; hexose-1-phosphate uridylyltransferase; uridyltransferase; hexose 1-phosphate uridyltransferase; UDP-glucose:α-D-galactose-1-phosphate uridylyltransferase. Enzyme Commission Number: EC 2.7.7.12. CAS No. 9026-21-5. GALT. 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-3228; UDP-glucose-hexose-1-phosphate uridylyltransferase; EC 2.7.7.12; 9026-21-5; uridyl transferase; hexose-1-phosphate uridylyltransferase; uridyltransferase; hexose 1-phosphate uridyltransferase; UDP-glucose:α-D-galactose-1-phosphate uridylyltransferase. Cat No: EXWM-3228. | |
| UTP-hexose-1-phosphate uridylyltransferase | α-D-Glucose 1-phosphate can also act as acceptor, but more slowly. Group: Enzymes. Synonyms: galactose-1-phosphate uridylyltransferase; galactose 1-phosphate uridylyltransferase; α-D-galactose 1-phosphate uridylyltransferase; galactose 1-phosphate uridyltransferase; UDPgalactose pyrophosphorylase; uridine diphosphate galactose pyrophosphorylase; uridine diphosphogalactose pyrophosphorylase. Enzyme Commission Number: EC 2.7.7.10. CAS No. 9016-11-9. 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-3226; UTP-hexose-1-phosphate uridylyltransferase; EC 2.7.7.10; 9016-11-9; galactose-1-phosphate uridylyltransferase; galactose 1-phosphate uridylyltransferase; α-D-galactose 1-phosphate uridylyltransferase; galactose 1-phosphate uridyltransferase; UDPgalactose pyrophosphorylase; uridine diphosphate galactose pyrophosphorylase; uridine diphosphogalactose pyrophosphorylase. Cat No: EXWM-3226. | |
| 2-Deoxy-D-glucose-6-phosphate | 2-Deoxy-D-glucose-6-phosphate is an exquisite biochemical compound with prowess lying in the formidable suppression of glucose metabolism and cellular proliferation, thereby rendering it a promising harbinger for the research of specifically targeting malignant neoplasms. Synonyms: 2-Deoxy-D-arabino-hexose-6-phosphate. CAS No. 3573-50-0. Molecular formula: C6H13O8P. Mole weight: 244.14. |  |
| D-Fructose-1,6-diphosphate tetrasodium salt | D-Fructose-1,6-diphosphate tetrasodium salt is a crucial compound widely used in the pharmaceutical industry. It acts as a mediator in glycolysis, aiding glucose metabolism to produce energy. Additionally, it serves as a regulator in various biochemical pathways, making it valuable in treating metabolic disorders and enhancing cellular functions. Synonyms: D-Fructose, 1,6-bis(dihydrogen phosphate), tetrasodium salt; D-Fructose-1,6-diphosphate tetrasodium salt; D-fructose1,6-diphosphatesodiumsalt; tetrasodium; [(2R,3R,4S)-2,3,4-trihydroxy-5-oxo-6-phosphonatooxyhexyl] phosphate; D-Fructose, 1,6-bis(dihydrogen phosphate), trisodium salt; Sodium (3S,4R,5R)-6-((hydrogenphosphonato)oxy)-3,4,5-trihydroxy-2-oxohexyl phosphate; EINECS 245-884-0; 81028-91-3; Hexose diphosphate sodium salt; sodium fructose 1,6-bisphosphate; MFCD00135870; D-Fructose, 1,6-bis(dihydrogen phosphate), sodium salt (1:4); sodium (2R,3R,4S)-2,3,4-trihydroxy-5-oxohexane-1,6-diyl diphosphate. CAS No. 23784-19-2. Molecular formula: C6H10Na4O12P2. Mole weight: 428.04. | |
| Fructose 1,6-bisphosphatase from Human, Recombinant | Fructose 1,6-bisphosphatase (FBPase; EC 3.1.3.11) is an enzyme in the liver that converts fructose-1,6-bisphosphate to fructose 6-phosphate in gluconeogenesis. Fructose bisphosphatase catalyses the reverse of the reaction which is catalysed by phosphofructokinase, which is involved in the process of glycolysis. These enzymes only catalyse the reaction in one direction each, and are regulated by metabolites such as fructose 2,6-bisphosphate so that high activity of one of the two enzymes is accompanied by low activity of the other. It is involved in many different metabolic pathways and found in most organisms. FBPase requires metal ions for catalysis (Mg2+ and Mn2+ being preferred) and the enzyme is potently inhibited by Li+. Group: Enzymes. Synonyms: Fructose-bisphosphatase; EC 3.1.3.11; FBPase; Hexose diphosphatase. Enzyme Commission Number: EC 3.1.3.11. Purity: > 90% (densitometry). FBPase. Mole weight: 36.8 kDa. Activity: 1525 pmol/min/ug. Storage: Stable for > 6 months at -80°C. Form: Liquid. Storage Buffer: 50 mM potassium phosphate pH-7.4, 50 mM sodium chloride, 0.5 mM ethylenediaminetetraaceticacid, and 2.5% glycerol. Source: E. coli. Species: Human. Fructose-bisphosphatase; EC 3.1.3.11; FBPase; Hexose diphosphatase. Cat No: NATE-1576. | |
| Fructose-1,6-diphosphate barium salt | Fructose-1,6-diphosphate barium salt. Uses: Designed for use in research and industrial production. Additional or Alternative Names: d-fructose,1,6-bis(dihydrogenphosphate),bariumsalt(1:2);BARIUM FRUCTOSE-1,6-DIPHOSPHATE;HEXOSE DIPHOSPHATE BARIUM;FRUCTOSE-1,6-DIPHOSPHATE BARIUM SALT;D-FRUCTOSE-1,6-DIPHOSPHATE DIBARIUM SALT;fructose 1,6-bis(barium phosphate);Fructose-1,6-diphosphate ba. Product Category: Heterocyclic Organic Compound. CAS No. 6035-52-5. Molecular formula: C6H12BaO12P2. Mole weight: 610.74. Purity: N/A. IUPACName: barium(2+); [(2S,3S,4R)-2,3,4-trihydroxy-5-oxo-6-phosphonatooxyhexyl] phosphate. Canonical SMILES: C(C(C(C(C(=O)COP(=O)([O-])[O-])O)O)O)OP(=O)([O-])[O-].[Ba+2].[Ba+2]. ECNumber: 227-913-9. Product ID: ACM6035525. Alfa Chemistry ISO 9001:2015 Certified. |  |
| fructose-bisphosphatase | The animal enzyme also acts on sedoheptulose 1,7-bisphosphate. Group: Enzymes. Synonyms: hexose diphosphatase; FBPase; fructose 1,6-diphosphatase; fructose 1,6-diphosphate phosphatase; D-fructose 1,6-diphosphatase; fructose 1,6-bisphosphatase; fructose diphosphatase; fructose diphosphate phosphatase; fructose bisphosphate phosphatase; fructose 1,6-bisphosphate 1-phosphatase; fructose 1,6-bisphosphate phosphatase; hexose bisphosphatase; D-fructose-1,6-bisphosphate phosphatase. Enzyme Commission Number: EC 3.1.3.11. CAS No. 9001-52-9. FBPase. 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-3614; fructose-bisphosphatase; EC 3.1.3.11; 9001-52-9; hexose diphosphatase; FBPase; fructose 1,6-diphosphatase; fructose 1,6-diphosphate phosphatase; D-fructose 1,6-diphosphatase; fructose 1,6-bisphosphatase; fructose diphosphatase; fructose diphosphate phosphatase; fructose bisphosphate phosphatase; fructose 1,6-bisphosphate 1-phosphatase; fructose 1,6-bisphosphate phosphatase; hexose bisphosphatase; D-fructose-1,6-bisphosphate phosphatase. Cat No: EXWM-3614. | |
| glucose 1-dehydrogenase [NAD(P)+] | This enzyme has similar activity with either NAD+ or NADP+. cf. EC 1.1.1.118, glucose 1-dehydrogenase (NAD+) and EC 1.1.1.119, glucose 1-dehydrogenase (NADP+). Group: Enzymes. Synonyms: D-glucose dehydrogenase (NAD(P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD(P)+ 1-oxidoreductase; glucose 1-dehydrogenase. Enzyme Commission Number: EC 1.1.1.47. CAS No. 9028-53-9. Glucose Dehyrogenase. 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-0332; glucose 1-dehydrogenase [NAD(P)+]; EC 1.1.1.47; 9028-53-9; D-glucose dehydrogenase (NAD(P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD(P)+ 1-oxidoreductase; glucose 1-dehydrogenase. Cat No: EXWM-0332. | |
| glucose-6-phosphatase | Wide distribution in animal tissues. Also catalyses potent transphosphorylations from carbamoyl phosphate, hexose phosphates, diphosphate, phosphoenolpyruvate and nucleoside di- and triphosphates, to D-glucose, D-mannose, 3-methyl-D-glucose or 2-deoxy-D-glucose [cf. EC 2.7.1.62 (phosphoramidate-hexose phosphotransferase), EC 2.7.1.79 (diphosphate-glycerol phosphotransferase) and EC 3.9.1.1 (phosphoamidase)]. Group: Enzymes. Synonyms: glucose 6-phosphate phosphatase. Enzyme Commission Number: EC 3.1.3.9. CAS No. 9001-39-2. G6Pase. 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-3696; glucose-6-phosphatase; EC 3.1.3.9; 9001-39-2; glucose 6-phosphate phosphatase. Cat No: EXWM-3696. | |
| glucose-6-phosphate isomerase | Also catalyses the anomerization of D-glucose 6-phosphate. Group: Enzymes. Synonyms: phosphohexose isomerase; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; phosphoglucose isomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase. Enzyme Commission Number: EC 5.3.1.9. CAS No. 9001-41-6. PGI. 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-5480; glucose-6-phosphate isomerase; EC 5.3.1.9; 9001-41-6; phosphohexose isomerase; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; phosphoglucose isomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase. Cat No: EXWM-5480. | |
| Glucose Dehydrogenase (Crude Enzyme) | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD + or NADP + as acceptor. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Biotechnology; synthesis. Group: Enzymes. Synonyms: D-glucose dehydrogenase (NAD(P) + ); hexose phosphate dehydrogenase; β-D-glucose:NAD(P) + 1-oxidoreductase; glucose 1-dehydrogenase. Enzyme Commission Number: EC 1.1.1.47. CAS No. 9028-53-9. Glucose Dehyrogenase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. D-glucose dehydrogenase (NAD(P) + ); hexose phosphate dehydrogenase; β-D-glucose:NAD(P) + 1-oxidoreductase; glucose 1-dehydrogenase. Pack: 100ml. Cat No: NATE-1794. | |
| Glucose Dehydrogenase from E. coli, Recombiant | In enzymology, a glucose 1-dehydrogenase (EC 1.1.1.47) is an enzyme that catalyzes the chemical reaction:beta-D-glucose + NAD (P)+<-> D-glucono-1,5-lactone + NAD (P)H + H+. The 3 substrates of this enzyme are beta-D-glucose, NAD+, and NADP+, whereas its 4 products are D-glucono-1,5-lactone, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. Applications: This enzyme is useful for determination of glucose. Group: Enzymes. Synonyms: EC 1.1.1.47; D-glucose dehydrogenase (NAD (P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD (P)+ 1-oxidoreductase; glucose 1-dehydrogenase; Glucose dehydrogenase; 9028-53-9. Enzyme Commission Number: EC 1.1.1.47. CAS No. 9028-53-9. Glucose Dehyrogenase. Mole weight: ca. 126,000; Subunit molecular weight : ca. 31,500. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: E. coli. EC 1.1.1.47; D-glucose dehydrogenase (NAD (P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD (P)+ 1-oxidoreductase; glucose 1-dehydrogenase; Glucose dehydrogenase; 9028-53-9. Cat No: NATE-1902. | |
| Glucose Dehydrogenase, Recombinant | In enzymology, a glucose 1-dehydrogenase (EC 1.1.1.47) is an enzyme that catalyzes the chemical reaction:beta-D-glucose + NAD (P)+? D-glucono-1,5-lactone + NAD (P)H + H+. The 3 substrates of this enzyme are beta-D-glucose, NAD+, and NADP+, whereas its 4 products are D-glucono-1,5-lactone, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. Applications: Gdh can be used as the raw material enzyme in clinic diagnostic of blood glucose. Group: Enzymes. Synonyms: EC 1.1.1.47; D-glucose dehydrogenase (NAD (P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD (P)+ 1-oxidoreductase; glucose 1-dehydrogenase; Glucose dehydrogenase; 9028-53-9. Enzyme Commission Number: EC 1.1.1.47. CAS No. 9028-53-9. Purity: 90% (SDS-PAGE test). Mole weight: About 28kDa (SDS-PAGE detection). Activity: About 200U/mg. Appearance: White powder, lyophilized. Storage: 4°C, store at -20°C for long-term preservation. Form: Freeze dried powder. EC 1.1.1.47; D-glucose dehydrogenase (NAD (P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD (P)+ 1-oxidoreductase; glucose 1-dehydrogenase; Glucose dehydrogenase; 9028-53-9. Cat No: NATE-1139. | |
| glutamine-fructose-6-phosphate transaminase (isomerizing) | Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination). Group: Enzymes. Synonyms: hexosephosphate aminotransferase; glucosamine-6-phosphate isomerase (glutamine-forming); glutamine-fructose-6-phosphate transaminase (isomerizing); D-fructose-6-phosphate amidotransferase; glucosaminephosphate isomerase; glucosamine 6-phosphate synthase; GlcN6P synthase. Enzyme Commission Number: EC 2.6.1.16. CAS No. 9030-45-9. 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-2856; glutamine-fructose-6-phosphate transaminase (isomerizing); EC 2.6.1.16; 9030-45-9; hexosephosphate aminotransferase; glucosamine-6-phosphate isomerase (glutamine-forming); glutamine-fructose-6-phosphate transaminase (isomerizing); D-fructose-6-phosphate amidotransferase; glucosaminephosphate isomerase; glucosamine 6-phosphate synthase; GlcN6P synthase. Cat No: EXWM-2856. | |
| Hexokinase-1 from Human, Recombinant | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Hk1 human recombinant produced in e. coli is a single, non-glycosylated, polypeptide chain fused to his tag a...ferase; EC 2.7.1.1; 9001-51-8. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. Hexokinase. Mole weight: 104.6 kDa. Activity: 7-8 units/ml. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles. Appearance: Sterile filtered colorless solution. Source: E. coli. Species: Human. Hexokinase-1; EC 2.7.1.1; Hexokinase type I; HK I; Brain form hexokinase; HK1-ta; HK1-tb; HXK1; HK1. Cat No: NATE-0844. | |
| Hexokinase-2 from Human, Recombinant | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Hk2 human recombinant produced in e. coli is a single, non-glycosylated, polypeptide chain fused to his tag a...rase; EC 2.7.1.1; 9001-51-8. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Purity: Greater than 90.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. Hexokinase. Mole weight: 104.1 kDa. Activity: 3-4 units/ml. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles. Appearance: Sterile filtered colorless solution. Source: E. coli. Species: Human. Hexokinase-2; EC 2.7.1.1; HK2; Hexokinase type II; HK II; Muscle form hexokinase; HXK2; DKFZp686M1669. Cat No: NATE-0845. | |
| Hexokinase-3 from Human, Recombinant | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Hk-3 human recombinant produced in e. coli is a single, non-glycosylated, polypeptide chain fused to his tag ...phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase; EC 2.7.1.1; 9001-51-8. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. Hexokinase. Mole weight: 101.1 kDa. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles. Appearance: Sterile filtered colorless solution. Source: E. coli. Species: Human. Hexokinase-3; EC 2.7.1.1; Hexokinase type III; HK III; HXK3; HK3. Cat No: NATE-0846. | |
| Hexokinase-4 from Human, Recombinant | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Glucokinase human recombinant produced in e. coli is a single, non-glycosylated, polypeptide chain fused to h...se; hexokinase; ATP:D-hexose 6-phosphotransferase; EC 2.7.1.1; 9001-51-8. Enzyme Commission Number: EC 2.7.1.2. CAS No. 9001-36-9. Purity: Greater than 95.0% as determined by SDS-PAGE. Hexokinase. Mole weight: 54.3 kDa. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles. Appearance: Sterile filtered colorless solution. Source: E. coli. Species: Human. Glucokinase; EC 2.7.1.2; Hexokinase-4; Hexokinase type IV; HK IV; HK4; Hexokinase-D; GCK; GK; GLK; HHF3; HKIV; HXKP; MODY2. Cat No: NATE-0847. | |
| Hexokinase from Kluyveromyces fragilis, Recombinant | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Group: Enzymes. Synonyms: hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase; EC 2.7.1.1. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Hexokinase. Mole weight: 54 Kd (SDS-PAGE). Activity: > 150 Units / mg. Storage: Below -20°C. Form: Lyophilized powder. Source: E. coli. Species: Kluyveromyces fragilis. hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase; EC 2.7.1.1. Cat No: NATE-1034. | |
| Hexokinase from Yeast, chemically modified | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Recombinant enzyme that converts hexose to hexose-6-phosphate. take advantage of the improved stability in liquid reagents. rely on the proven diagnostic quality of this product. Applications: Use hexokinase in diagnostic tests for blood glucose using the hexokinase method and for the determination of creatine kinase. Group: Enzymes. Synonyms: hexokinase type . Hexokinase. Mole weight: 57 kD (SDS-PAGE). Activity: > 40 U/mg lyophilizate. Stability: At +2 to +8°C within specification range for 18 months. Store dry. Appearance: White lyophilizate. Source: Yeast. hexokinase type IV glucokinase; hexokinase D; hexokinase type IV; hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase. Cat No: NATE-0989. | |
| mannitol-1-phosphate 5-dehydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-mannitol-1-phosphate:NAD+ 2-oxidoreductase. Other names in common use include hexose reductase, mannitol 1-phosphate dehydrogenase, D-mannitol-1-phosphate dehydrogenase, and fructose 6-phosphate reductase. This enzyme participates in fructose and mannose metabolism. Group: Enzymes. Synonyms: hexose reductase; mannitol 1-phosphate dehydrogenase; D-mannitol-1-phosphate dehydrogenase; fructose 6-phosphate reductase. Enzyme Commission Number: EC 1.1.1.17. CAS No. 9028-24-4. 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-0073; mannitol-1-phosphate 5-dehydrogenase; EC 1.1.1.17; 9028-24-4; hexose reductase; mannitol 1-phosphate dehydrogenase; D-mannitol-1-phosphate dehydrogenase; fructose 6-phosphate reductase. Cat No: EXWM-0073. | |
| Native Bacillus sp. Hexokinase | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Applications: This enzyme is useful for enzymatic determination of glucose or creatinine kinase activity when coupled with glucose-6-phosphate dehydrogenase. Group: Enzymes. Synonyms: hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Hexokinase. Mole weight: 68 kDa (gel filtration). Activity: More than 250 U/mg solid. Appearance: White amorphous powder, lyophilized. Storage: Storage at -20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Bacillus sp. hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase; EC 2.7.1.1. Cat No: NATE-1157. | |
| Native Bacillus stearothermophilus Phosphoglucose isomerase | Glucose-6-phosphate isomerase is an enzyme that catalyzes the conversion of glucose-6-phosphate into fructose 6-phosphate in the second step of glycolysis. The human variant of this enzyme is encoded by the GPI gene. Native glucose-6-phosphate isomerase (ec 5.3.1.9) was purified from bacillus stearothermophilus. Group: Enzymes. Synonyms: Glucose-6-phosphate isomerase; phosphoglucose isomerase; phosphohexose isomerase; EC 5.3.1.9; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase. Enzyme Commission Number: EC 5.3.1.9. CAS No. 9001-41-6. PGI. Activity: > 250 U/mg. Appearance: White powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus stearothermophilus. Glucose-6-phosphate isomerase; phosphoglucose isomerase; phosphohexose isomerase; EC 5.3.1.9; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase. Cat No: DIA-162. | |
| Native Baker's yeast (S. cerevisiae) Phosphoglucose Isomerase | Phosphoglucose Isomerase (PGI) is an enzyme crucial for the interconversion of D-glucose 6-phosphate and D-fructose 6-phosphate. PGI is responsible for the second step of glycolysis and is involved in glucogenesis. It is highly conserved in bacteria and eukaryotes. Applications: Isomerization of ketoses to aldoses. Group: Enzymes. Synonyms: Glucose-6-phosphate isomerase; EC 5.3.1.9; phosphohexose isomerase; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; phosphoglucose isomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase; 9001-41-6; PGI. Enzyme Commission Number: EC 5.3.1.9. CAS No. 9001-41-6. PGI. Mole weight: 145 kDa. Activity: 350 U/mg at +25°C with F6P as substrate. Storage: Stable at +2 to +8°C. Source: Baker's yeast (S. cerevisiae). Glucose-6-phosphate isomerase; EC 5.3.1.9; phosphohexose isomerase; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; phosphoglucose isomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase; 9001-41-6; PGI. Cat No: NATE-0554. | |
| Native Galactose-adapted yeast Galactose-1-phosphate Uridyltransferase | Galactose-1-phosphate uridyltransferase (GALT) facilitates the simultaneous conversion of uridine diphosphoglucose (UDP-glucose) and galactose-1-phosphate (gal-1P) to uridine diphosphogalactose (UDP-galactose) and glucose-1-phosphate. Classic Galactosemia (CG) is an inherited metabolic condition caused by deficiency of GALT activity. Group: Enzymes. Synonyms: EC 2.7.7.12; UDP-glucose-hexose-1-phosphate uridylyltransferase; uridyl transferase; hexose-1-phosphate uridylyltransferase; uridyltransferase; hexose 1-phosphate uridyltransferase; UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase; 9016-11-9. Enzyme Commission Number: EC 2.7.7.12. CAS No. 9026-21-5. GALT. Activity: 20-60 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: lyophilized powder; Contains buffer salts as Citrate and reduced glutathione. Source: Galactose-adapted yeast. EC 2.7.7.12; UDP-glucose-hexose-1-phosphate uridylyltransferase; uridyl transferase; hexose-1-phosphate uridylyltransferase; uridyltransferase; hexose 1-phosphate uridyltransferase; UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase; 9016-11-9. Cat No: NATE-0277. | |
| Native Microorganism Hexokinase | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Applications: The enzyme is useful for enzymatic determination of glucose, adenosine-5'-triphosphate (atp) and creatine phosphokinase when coupled with glucose-6-phosphate dehydrogenase. Group: Enzymes. Synonyms: Hexokinase; EC 2.7.1.1; hexokinase type IV glucokinase; hexokinase D; hexokinase type IV; hexokinase (phosphorylating); ATP-dependen. Enzyme Commission Number: EC 2.7.1.1. Mole weight: approx. 82 kDa (by gel filtration). Activity: 150U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Hexokinase; EC 2.7.1.1; hexokinase type IV glucokinase; hexokinase D; hexokinase type IV; hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; ATP: D-hexose 6-phosphotransferase. Cat No: DIA-202. | |
| Native Porcine Cytochrome c Reductase | Cytochrome c reductase is a flavoprotein that completes the oxidation-reduction chain between hexosemonophosphate and cytochrome c. The molecular weight of cytochrome c reductase is found to be approximately 78 kDa Da. The prosthetic group of cytochrome c reductase is alloxazine mononucleotide. The enzyme is very unstable with respect to low pH and to denaturation by heat. Group: Enzymes. Synonyms: EC 1.6.99.3; cytochrome c reductase; type 1 dehydrogenase; β-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine . Enzyme Commission Number: EC 1.6.99.3. CAS No. 9027-14-9. Cytochrome c Reductase. Activity: > 1.0 units/mg protein. Storage: -20°C. Form: lyophilized powder. Crude, lyophilized powder containing potassium phosphate, pH approx. 7.0. Source: Porcine heart. Species: Porcine. EC 1.6.99.3; cytochrome c reductase; type 1 dehydrogenase; β-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine dinucleotide dehydrogenase; diphosphopyridine diaphorase; DPNH diaphorase; NADH diaphorase; NADH hydrogenase; NADH oxidoreductase; NADH-menadione oxidoreductase; reduced diphosphopyridine nucleotide diaphorase; NADH:cytochrome c oxidoreductase; NADH2 dehydrogenase; NADH: (acceptor) oxidoreductase; 9027-14-9. Cat No: NATE-0179. | |
| Native Porcine Diamine Oxidase | Diamine oxidase from porcine kidney is a homodimer consisting of 2 equal subunits with a molecular weight of 87 kDa each. Each subunit contains one molecule of pyridoxal phosphate and one atom of copper. The molecular mass of the enzyme is found to be 170 kDa. The enzyme is a glycoprotein containing 5% hexose, 3.3% glucosamine, 2.6% N-acetylglucosamine, and 0.25% N-acetylneuraminic acid. The enzyme exhibits a high affinity for concanavalin A. It catalyzes the oxidation of monoamines, diamines, and histamine to aldehydes, ammonia, and hydrogen peroxide. Optimum pH with cadverine and histamine as substrates is found to be 6.3-7.4.2 The enzyme is classified as a copper amine oxid...a luminescence-based test for determining ornithine decarboxylase activity. diamine oxidase from porcine kidney has also been used in a study to investigate n-linked oligosaccharide structures in diamine oxidase. Group: Enzymes. Synonyms: EC 1.4.3.6; 9001-53-0; Amine:oxygen oxidoreductase (deaminating) (pyridoxal-containing); Diamine Oxidase; Amine oxidase (copper-containing). Enzyme Commission Number: EC 1.4.3.6. CAS No. 9001-53-0. Diamine Oxidase. Activity: > 0.05 unit/mg solid. Storage: -20°C. Source: Porcine kidney. Species: Porcine. EC 1.4.3.6; 9001-53-0; Amine:oxygen oxidoreductase (deaminating) (pyridoxal-containing); Diamine Oxidase; Amine oxidase (copper-containing). | |
| Native Pseudomonas sp. Glucose dehydrogenase | In enzymology, a glucose 1-dehydrogenase (EC 1.1.1.47) is an enzyme that catalyzes the chemical reaction:beta-D-glucose + NAD (P)+<-> D-glucono-1,5-lactone + NAD (P)H + H+. The 3 substrates of this enzyme are beta-D-glucose, NAD+, and NADP+, whereas its 4 products are D-glucono-1,5-lactone, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. Group: Enzymes. Synonyms: EC 1.1.1.47; D-glucose dehydrogenase (NAD (P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD (P)+ 1-oxidoreductase; glucose 1-dehydrogenase; Glucose dehydrogenase; 9028-53-9. Enzyme Commission Number: EC 1.1.1.47. CAS No. 9028-53-9. Glucose Dehyrogenase. Activity: > 200 units/mg. Storage: -20°C. Form: powder; white. Source: Pseudomonas sp. EC 1.1.1.47; D-glucose dehydrogenase (NAD (P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD (P)+ 1-oxidoreductase; glucose 1-dehydrogenase; Glucose dehydrogenase; 9028-53-9. Cat No: NATE-0305. | |
| Native Rabbit Phosphoglucose Isomerase | Phosphoglucose Isomerase (PGI) is an enzyme crucial for the interconversion of D-glucose 6-phosphate and D-fructose 6-phosphate. PGI is responsible for the second step of glycolysis and is involved in glucogenesis. It is highly conserved in bacteria and eukaryotes. Applications: Phosphoglucose isomerase (pgi) is an enzyme crucial for the interconversion of d-glucose 6-phosphate and d-fructose 6-phosphate. pgi is responsible for the second step of glycolysis and is involved in glucogenesis. it is highly conserved in bacteria and eukaryotes. it is used in sugar assays to convert fructose to glucose. this product is type xi and is from rabbit muscle. it is useful in enzyme systems requiring low sulfate. Group: Enzymes. Synonyms: Glucose-6-phosphate isomerase. Enzyme Commission Number: EC 5.3.1.9. CAS No. 9001-41-6. PGI. Activity: > 200 units/mg protein. Storage: -20°C. Form: lyophilized powder; Essentially sulfate-free powder containing Citrate buffer salts. Source: Rabbit muscle. Species: Rabbit. Glucose-6-phosphate isomerase; EC 5.3.1.9; phosphohexose isomerase; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; phosphoglucose isomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase; 9001-41-6; PGI. Cat No: NATE-0555. | |
| Native Rhodothermus obamensis Hexokinase | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Applications: This enzyme is useful for enzymatic determination of glucose or creatinine kinase activity when coupled with glucose-6-phosphate dehydrogenase. Group: Enzymes. Synonyms: hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Hexokinase. Mole weight: 140 kDa (gel filtration). Activity: 100 - 400 U/mg. Appearance: White to light grayish lyophilized powder. Storage: Storage at -20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Rhodothermus obamensis. hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase; EC 2.7.1.1. Cat No: NATE-1156. | |
| Native Saccharomyces cerevisiae Hexokinase | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Group: Enzymes. Synonyms: hexokinase type IV glucokinase; hexokinase D; hexokinase type IV. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Hexokinase. Mole weight: ~ 54 kDa (monomer); ~110 kDa (dimer). Activity: Type I, > 350 units/mg protein; Type II, > 25 units/mg protein (biuret); Type III, > 130 units/mg protein (biuret). Storage: -20°C. Form: Type I, Lyophilized powder containing phosphate/Citrate pH approx. 7.0; Type II, Type III, Lyophilized powder containing approx. 15% sodium Citrate. Source: Saccharomyces cerevisiae. hexokinase type IV glucokinase; hexokinase D; hexokinase type IV; hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase; EC 2.7.1.1; 9001-51-8. Cat No: NATE-0342. | |
| Native Yeast 6-Phosphogluconic Dehydrogenase | In enzymology, a phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) is an enzyme that catalyzes the chemical reaction:6-phospho-D-gluconate + NADP+<-> D-ribulose 5-phosphate + CO2 + NADPH. Thus, the two substRates of this enzyme are 6-phospho-D-gluconate and NADP+, whereas its 3 products are D-ribulose 5-phosphate, CO2, and NADPH. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. Applications: 6-phosphoglyconic dehydrogenase (6pgd) is a key enzyme in the oxidative portion of the hexose monophosphate shunt. it is specific for oxidized nicotinamide adenine dinucleotide ph...luconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase; EC 1.1.1.44; phosphogluconate dehydrogenase; decarboxylating; 9073-95-4. Enzyme Commission Number: EC 1.1.1.44. CAS No. 9073-95-4. 6-Phosphogluconic Dehydrogenase. Activity: 3.0-6.0 units/mg solid. Storage: 2-8°C. Form: lyophilized powder. Source: Yeast. 6-Phosphogluconic Dehydrogenase; phosphogluconic acid dehydrogenase; 6-phosphogluconic dehydrogenase; 6-phosphogluconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase; EC 1.1.1.44; phosphogluconate dehydrogenase; decarboxylating; 9073-95-4. Cat No: NATE-0009. | |
| nucleoside-triphosphate-aldose-1-phosphate nucleotidyltransferase | In decreasing order of activity, guanosine, inosine and adenosine diphosphate hexoses are substrates in the reverse reaction, with either glucose or mannose as the sugar. Group: Enzymes. Synonyms: NDP hexose pyrophosphorylase; hexose 1-phosphate nucleotidyltransferase; hexose nucleotidylating enzyme; nucleoside diphosphohexose pyrophosphorylase; hexose-1-phosphate guanylyltransferase; GTP:α-D-hexose-1-phosphate guanylyltransferase; GDP hexose pyrophosphorylase; guanosine diphosphohexose pyrophosphorylase; nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase; NTP:he. Enzyme Commission Number: EC 2.7.7.28. CAS No. 37278-26-5. 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-3239; nucleoside-triphosphate-aldose-1-phosphate nucleotidyltransferase; EC 2.7.7.28; 37278-26-5; NDP hexose pyrophosphorylase; hexose 1-phosphate nucleotidyltransferase; hexose nucleotidylating enzyme; nucleoside diphosphohexose pyrophosphorylase; hexose-1-phosphate guanylyltransferase; GTP:α-D-hexose-1-phosphate guanylyltransferase; GDP hexose pyrophosphorylase; guanosine diphosphohexose pyrophosphorylase; nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase; NTP:hexose-1-phosphate nucleotidyltransferase. Cat No: EXWM-3239. | |
| phosphoglucomutase (α-D-glucose-1,6-bisphosphate-dependent) | Maximum activity is only obtained in the presence of α-D-glucose 1,6-bisphosphate. This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. The enzyme also catalyses (more slowly) the interconversion of 1-phosphate and 6-phosphate isomers of many other α-D-hexoses, and the interconversion of α-D-ribose 1-phosphate and 5-phosphate. cf. EC 5.4.2.5, phosphoglucomutase (glucose-cofactor). Group: Enzymes. Synonyms: glucose phosphomutase; phosphoglucose mutase. Enzyme Commission Number: EC 5.4.2.2. CAS No. 9001-81-4. Phosphoglucomutase. 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-5524; phosphoglucomutase (α-D-glucose-1,6-bisphosphate-dependent); EC 5.4.2.2; 9001-81-4; glucose phosphomutase; phosphoglucose mutase. Cat No: EXWM-5524. | |
| phosphoramidate-hexose phosphotransferase | Activity is observed with several hexoses; of these glucose is the best substrate and the product from it is α-D-glucose 1-phosphate. The phosphoramidate donor can be replaced by N-phosphoglycine and by an N-phosphohistidine. May be identical with EC 3.1.3.9 glucose-6-phosphatase. Group: Enzymes. Synonyms: phosphoramidate-hexose transphosphorylase; phosphoramidic-hexose transphosphorylase; phosphoramidate:hexose 1-phosphotransferase. Enzyme Commission Number: EC 2.7.1.62. CAS No. 9031-45-2. 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-3093; phosphoramidate-hexose phosphotransferase; EC 2.7.1.62; 9031-45-2; phosphoramidate-hexose transphosphorylase; phosphoramidic-hexose transphosphorylase; phosphoramidate:hexose 1-phosphotransferase. Cat No: EXWM-3093. | |
| [protein-PII] uridylyltransferase | The enzyme uridylylates and de-uridylylates the small trimeric protein PII. The enzymes from Escherichia coli and Salmonella typhimurium have been wrongly identified, in some databases, as EC 2.7.7.12 (UDP-glucose-hexose-1-phosphate uridylyltransferase), from which it differs greatly in both reaction catalysed and sequence. Group: Enzymes. Synonyms: PII uridylyl-transferase; uridyl removing enzyme. Enzyme Commission Number: EC 2.7.7.59. CAS No. 57657-57-5. 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-3270; [protein-PII] uridylyltransferase; EC 2.7.7.59; 57657-57-5; PII uridylyl-transferase; uridyl removing enzyme. Cat No: EXWM-3270. | |
| Rucaparib | Rucaparib (AG014699) is an orally active, potent inhibitor of PARP proteins (PARP-1, PARP-2 and PARP-3) with a K i of 1.4 nM for PARP1. Rucaparib is a modest hexose-6-phosphate dehydrogenase (H6PD) inhibitor. Rucaparib has the potential for castration-resistant prostate cancer (CRPC) research [1] [2] [3] [4]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: AG014699; PF-01367338. CAS No. 283173-50-2. Pack Sizes: 5 mg; 10 mg; 50 mg; 100 mg. Product ID: HY-10617A. |  |
| Rucaparib monocamsylate | Rucaparib (AG014699) monocamsylate is an orally active, potent inhibitor of PARP proteins (PARP-1, PARP-2 and PARP-3) with a K i of 1.4 nM for PARP1. Rucaparib monocamsylate is a modest hexose-6-phosphate dehydrogenase (H6PD) inhibitor. Rucaparib monocamsylate has the potential for castration-resistant prostate cancer (CRPC) research [1] [2] [3] [4]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: AG014699 monocamsylate; PF-01367338 monocamsylate. CAS No. 1859053-21-6. Pack Sizes: 10 mM * 1 mL; 10 mg; 25 mg; 50 mg; 100 mg; 250 mg; 500 mg. Product ID: HY-102003. | |
| Rucaparib phosphate | Rucaparib (AG014699) phosphate is an orally active, potent inhibitor of PARP proteins (PARP-1, PARP-2 and PARP-3) with a K i of 1.4 nM for PARP1. Rucaparib phosphate is a modest hexose-6-phosphate dehydrogenase (H6PD) inhibitor. Rucaparib phosphate has the potential for castration-resistant prostate cancer (CRPC) research [1] [2] [3] [4]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: AG-014699 phosphate; PF-01367338 phosphate. CAS No. 459868-92-9. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 50 mg; 100 mg; 200 mg. Product ID: HY-10617. | |
| sorbitol-6-phosphatase | Acts, very slowly, on hexose 6-phosphates. Group: Enzymes. Synonyms: sorbitol-6-phosphate phosphatase. Enzyme Commission Number: EC 3.1.3.50. CAS No. 80449-21-4. 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-3655; sorbitol-6-phosphatase; EC 3.1.3.50; 80449-21-4; sorbitol-6-phosphate phosphatase. Cat No: EXWM-3655. | |
| 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. | |
| Chondroitinase AC from Flavobacterium heparinum, Recombinant | Chondroitinase AC from Flavobacteriun heparinum is an eliminase that degrades chondroitin sulfates A and C, but not chondroitin sulfate B. The enzyme cleaves, via an elimination mechanism, both sulfated and non-sulfated polysaccharide chains that contain (1?4)-linkages between hexosamines and glucuronic acid residues. The reaction yields oligosaccharide products, mainly disaccharides, with unsaturated uronic acids that can be detected by UV spectroscopy at 232 nm. Applications: Chondroitinase ac was shown to inhibit melanoma invasion and proliferation, endothelial proliferation, and angiogenesis. chondroitinase ac, but not chondroitinase b, has also been shown t..., and protease activities. ChnAC. Activity: >200 units/mg protein. Appearance: Powder. Storage: Store the product at -20?C. When stored properly and unopened at -20?C, the enzyme has a recommended retest date of 2 years. After reconstitution, the product may be kept at 4?C for 4 days, but it is recommended to store the solution in working aliquots at -20 ?C. Form: The enzyme is supplied as a lyophilized powder containing potassium phosphate, NaCl, and a stabilizer. Source: E. coli. Species: Flavobacterium heparinum. chondroitinase (ambiguous); chondroitin sulfate lyase; chondroitin AC eliminase; chondroitinase AC; ChnAC; 9047-57-8; EC 4.2.2.5. Cat No: NATE-1738. | |
| Chondroitinase B from Flavobacterium heparinum, Recombinant | In enzymology, a chondroitin B lyase (EC 4.2.2.19) is an enzyme that catalyzes the chemical reaction:Eliminative cleavage of dermatan sulfate containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucurosonyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (deltaUA-GalNAc-4S). This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The enzyme cleaves, via an elimination mechanism, polysaccharide chains containing 1-4 linkages between hexosamines and iduronic acid residues in dermatan sulfate (chondroit...preparation of di-and oligo-saccharides of dermatan sulfate. Group: Enzymes. Synonyms: Chondroitinase B; EC 4.2.2.19; chondroitin B lyase; ChonB; ChnB. Enzyme Commission Number: EC 4.2.2.19. CAS No. 52227-83-5. Purity: > 90 % by reversed phase HPLC analysis. ChonB. Mole weight: 54,779 Da. Activity: > 550 IU/mg (substrate: dermatan sulfate). Stability: Expiration is 30 months from manufacturing date, frozen at -70°C in aqueous buffers containing Sodium Chloride, Sodium Phosphate and Sucrose 5%. Source: Flavobacterium heparinum. Species: Flavobacterium heparinum. Chondroitinase B; EC 4.2.2.19; chondroitin B lyase; ChonB; ChnB. Pack: vial of 5 ug. Cat No: NATE-0130. | |
| 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. | |
| N-acetylhexosamine 1-kinase from Bifidobacterium longum, Recombinant | N-acetylhexosamine 1-kinase (EC 2.7.1.162, NahK, LnpB, N-acetylgalactosamine/N-acetylglucosamine 1-kinase) is an enzyme with systematic name ATP:N-acetyl-D-hexosamine 1-phosphotransferase. This enzyme catalyses the following chemical reaction: ATP + N-acetyl-D-hexosamine ? ADP + N-acetyl-alpha-D-hexosamine 1-phosphate. This enzyme is involved in the lacto-N-biose I/galacto-N-biose degradation pathway in the probiotic bacterium Bifidobacterium longum. Group: Enzymes. Synonyms: EC 2.7.1.162; NahK; LnpB; N-acetylgalactosamine/N-acetylglucosamine 1-kinase; ATP:N-acetyl-D-hexosamine 1-phosphotransferase. Enzyme Commission Number: EC 2.7.1.162. Purity: min 95% by SDS-PAGE. N-Acetylhexosamine 1-Kinase. Mole weight: 40 kDa. Source: E. coli. Species: Bifidobacterium longum. N-acetylhexosamine 1-kinase; EC 2.7.1.162; NahK; LnpB; N-acetylgalactosamine/N-acetylglucosamine 1-kinase; ATP:N-acetyl-D-hexosamine 1-phosphotransferase. Cat No: NATE-1481. | |
| Native Flavobacterium heparinum Chondroitinase B | Chondroitinase B cleaves, via an elimination mechanism, polysaccharide chains containing 1-4 linkages between hexosamines and iduronic acid residues in dermatan sulfate (chondroitin B).The reaction yields oligosaccharide products (mainly disaccharides) containing unsaturated uronic acids which can be detected by UV spectroscopy at 232 nm. Applications: Research reagent (glycobiology, preparation of oligosaccharide libraries from dermatan sulfate).determination of contents of chondrotin sulfates by hplc. Group: Enzymes. Synonyms: Chondroitinase B; EC 4.2.2.19; chondroitin B lyase; ChonB; ChnB. Enzyme Commission Number: EC 4.2.2.19. CAS No. 52227-83-5. ChonB. Mole weight: 55 kDa. Activity: >200 IU/mg (substrate: dermatan sulfate). Stability: 12 months frozen at -20°C in aqueous buffers containing sodium phosphate and sucrose 5%. Source: Flavobacterium heparinum. Chondroitinase B; EC 4.2.2.19; chondroitin B lyase; ChonB; ChnB. Cat No: NATE-1950. | |
| Native Human β-N-Acetylglucosaminidase | This enzyme, sometimes called β-N-acetylhexosaminidase, is reported to liberate terminal β-linked N-acetylglucosamine and N-acetylgalactosamine from a variety of substrates. The activity of β-N-actylglucosaminidase may be determined with the chromogenic substrate p-nitrophenyl-N-acetyl-β-D-glucosaminide. β-N-actylglucosaminidase hydrolyzes the terminal nonreducing N-acetyl-D-hexosamine residues. This enzyme contains two predominant isozymes, Hex A, a heterodimer, and Hex B, a homodimer. N-acetylglucosamine, acetamide, N-2-acetamido-2-deoyglucosylamine, N-acetylnojirimycin, and N-acetyldeoxynojirmycin are known inhibitors. Applications: Β-n-...etylhexosaminidase; β-D-hexosaminidase; 9012-33-3; EC 3.2.1.52. Enzyme Commission Number: EC 3.2.1.52. CAS No. 9012-33-3. β-N-Acetylhexosaminidase. Activity: 6-20 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 2.4 M (NH4)2SO4 containing 0.15 M NaCl and 0.1 M sodium phosphate, pH 6.0. Source: Human placenta. Species: Human. hexosaminidase; β-acetylaminodeoxyhexosidase; N-acetyl-β-D-hexosaminidase; N-acetyl-beta-hexosaminidase; β-hexosaminidase; β-acetylhexosaminidinase; β-D-N-acetylhexosaminidase; β-N-acetyl-D-hexosaminidase; β-N-acetylglucosaminidase; hexosaminidase A; N-acetylhexosaminidase | |
| 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. | |
| phosphatidylinositol α-mannosyltransferase | This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. Group: Enzymes. Synonyms: GDP mannose-phosphatidyl-myo-inositol α-mannosyltransferase; GDPmannose:1-phosphatidyl-myo-inositol α-D-mannosyltransferase; guanosine diphosphomannose-phosphatidyl-inositol α-mannosyltransferase; phosphatidyl-myo-inositol α-mannosyltransferase. Enzyme Commission Number: EC 2.4.1.57. CAS No. 37277-65-9. 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-2602; phosphatidylinositol α-mannosyltransferase; EC 2.4.1.57; 37277-65-9; GDP mannose-phosphatidyl-myo-inositol α-mannosyltransferase; GDPmannose:1-phosphatidyl-myo-inositol α-D-mannosyltransferase; guanosine diphosphomannose-phosphatidyl-inositol α-mannosyltransferase; phosphatidyl-myo-inositol α-mannosyltransferase. Cat No: EXWM-2602. | |
| poly(glycerol-phosphate) α-glucosyltransferase | This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. Group: Enzymes. Synonyms: UDP glucose-poly(glycerol-phosphate) α-glucosyltransferase; uridine diphosphoglucose-poly(glycerol-phosphate) α-glucosyltransferase. Enzyme Commission Number: EC 2.4.1.52. CAS No. 37277-60-4. 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-2598; poly(glycerol-phosphate) α-glucosyltransferase; EC 2.4.1.52; 37277-60-4; UDP glucose-poly(glycerol-phosphate) α-glucosyltransferase; uridine diphosphoglucose-poly(glycerol-phosphate) α-glucosyltransferase. Cat No: EXWM-2598. | |
| poly(ribitol-phosphate) β-glucosyltransferase | This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. Group: Enzymes. Synonyms: UDP glucose-poly(ribitol-phosphate) β-glucosyltransferase; uridine diphosphoglucose-poly(ribitol-phosphate) β-glucosyltransferase; UDP-D-glucose polyribitol phosphate glucosyl transferase; UDP-D-glucose:polyribitol phosphate glucosyl transferase. Enzyme Commission Number: EC 2.4.1.53. CAS No. 37277-61-5. 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-2599; poly(ribitol-phosphate) β-glucosyltransferase; EC 2.4.1.53; 37277-61-5; UDP glucose-poly(ribitol-phosphate) β-glucosyltransferase; uridine diphosphoglucose-poly(ribitol-phosphate) β-glucosyltransferase; UDP-D-glucose polyribitol phosphate glucosyl transferase; UDP-D-glucose:polyribitol phosphate glucosyl transferase. Cat No: EXWM-2599. | |
| 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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