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| Product | Description | |
|---|---|---|
| 5-(carboxyamino)imidazole ribonucleotide synthase | In Escherichia coli, this enzyme, along with EC 5.4.99.18, 5-(carboxyamino)imidazole ribonucleotide mutase, is required to carry out the single reaction catalysed by EC 4.1.1.21, phosphoribosylaminoimidazole carboxylase, in vertebrates. Belongs to the ATP grasp protein superfamily. Carboxyphosphate is the putative acyl phosphate intermediate. Involved in the late stages of purine biosynthesis. Group: Enzymes. Synonyms: N5-CAIR synthetase; N5-carboxyaminoimidazole ribonucleotide synthetase; PurK. Enzyme Commission Number: EC 6.3.4.18. CAS No. 255379-40-9. 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-5787; 5-(carboxyamino)imidazole ribonucleotide synthase; EC 6.3.4.18; 255379-40-9; N5-CAIR synthetase; N5-carboxyaminoimidazole ribonucleotide synthetase; PurK. Cat No: EXWM-5787. |  |
| Adenosine 3',5'-Bisphosphate Dicalcium Hydrate | Adenosine 3',5'-Bisphosphate Dicalcium Hydrate is a substrate for the amidohydrolase superfamily. Synonyms: Adenosine 3',5'-Diphosphate Dicalcium Hydrate; 3',5'-ADP Dicalcium Hydrate; 3',5'-Diphosphoadenosine Dicalcium Hydrate; 3'-Phosphoadenosine-5'-phosphate Dicalcium Hydrate; 3'-Phosphoryl-AMP Dicalcium Hydrate; A 3P5P; Adenosine 3',5'-bisphosphate Dicalcium Hydrate. Molecular formula: C10H27N5O18P2. Mole weight: 567.29. |  |
| Aluminum Phosphate Adjuvant | Aluminum phosphate adjuvant is a white hydrogel that sediments slowly and forms a clear supernatant. Synonyms: Adju-Phos; aluminum hydroxyphosphate; aluminium hydroxyphosphate; Rehydraphos. Product ID: PE0379. Molecular formula: Al(OH)x(PO4)y. Category: Adsorbents. Product Keywords: Pharmaceutical Excipients; Excipients for Solid Dosage Form; Filler Excipients; Absorbent; Aluminum Phosphate Adjuvant; PE0379. Chemical Name: Aluminum phosphate. Grade: Pharmceutical Excipients. Stability and Storage Conditions: Aluminum phosphate adjuvant is stable fwhen stored at 4-30°C in well-sealed inert containers. It must not be allowed to freeze as the hydrated colloid structure will be irreversibly damaged. Applications: Aluminum phosphate adjuvant is used in parenteral human and veterinary vaccines. Safety: Aluminum phosphate adjuvant is intended for use in parenteral vaccines and is generally regarded as safe. It may cause mild irritation, dryness, and dermatitis on skin contact. It may also cause redness, conjunctivitis, and short-term mild irritation on eye contact. Ingestion of large amounts of aluminum phosphate adjuvant may cause respiratory irritation with nausea, vomiting, and constipation. Inhalation is unlikely, although the dried product may cause respiratory irritation and cough. Type I hypersensitivity reactions following parenteral administration have also been reported. |  |
| Clindamycin | Clindamycin is produced by the strain of semi-synthetic lincomycin. The antibacterial spectrum of chloralincomycin is the same as that of Lincomycin, but its antibacterial activity is stronger, and its effect on anaerobic bacteria such as fragile Bacteroides is equivalent to 3-4 times of that of Lincomycin. It can be injected or administered orally, and oral absorption is obviously superior to lincomycin. Synonyms: Clindamycin phosphate EP Impurity E; Dalacine; Chlolincocin; Dalacin C; 7-Chlorolincomycin. Grade: >98%. CAS No. 18323-44-9. Molecular formula: C18H33ClN2O5S. Mole weight: 424.98. | |
| D-inositol-3-phosphate glycosyltransferase | The enzyme, which belongs to the GT-B fold superfamily, catalyses the first dedicated reaction in the biosynthesis of mycothiol. The substrate was initially believed to be inositol, but eventually shown to be D-myo-inositol 3-phosphate. A substantial conformational change occurs upon UDP binding, which generates the binding site for D-myo-inositol 3-phosphate. Group: Enzymes. Synonyms: mycothiol glycosyltransferases; MshA; UDP-N-acetyl-D-glucosamine:1D-myo-inositol 3-phosphate α-D-glycosyltransferase. Enzyme Commission Number: EC 2.4.1.250. 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-2480; D-inositol-3-phosphate glycosyltransferase; EC 2.4.1.250; mycothiol glycosyltransferases; MshA; UDP-N-acetyl-D-glucosamine:1D-myo-inositol 3-phosphate α-D-glycosyltransferase. Cat No: EXWM-2480. | |
| Glutathione S-Transferase from E.coli, Recombinant | Glutathione S-transferases (GSTs), previously known as ligandins, comprise a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies:the cytosolic, mitochondrial, and microsomal--also known as MAPEG--proteins. Members of the GST superfamily are extremely diverse in amino acid sequence, and a large fraction of the sequences deposited in public databases are of unknown function. The Enzyme Function Initiative (EFI) is using GSTs as a model superfamily to iden.ferase. Mole weight: 26kDa. Activity: >20 units/mg. 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).Avoid multiple freeze-thaw cycles. Form: Sterile Filtered clear solution in Phosphate Buffered Saline pH 7.4. Source: E.coli. Species: E.coli. Glutathione S-transferases; GSTs; GST; Glutathione S-alkenetransferase; Glutathione S-alkyltransferase; Glutathione S-aralkyltransferase; Glutathione S-aryltransferase; Glutathione S-epoxidetransferase; RX:Glutathione R-transferase; EC 2.5.1.18; 50812-37-8. Cat No: NATE-1945. | |
| m-3M3FBS | m-3M3FBS is a potent phospholipase C (PLC) activator. m-3M3FBS stimulates superoxide generation in human neutrophils, upregulates intracellular calcium concentration, and stimulates inositol phosphate generation in various cell lines. m-3M3FBS induces monocytic leukemia cell apoptosis[1][2][3]. Uses: Scientific research. Group: Signaling pathways. CAS No. 200933-14-8. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-19619. |  |
| Monosodium Phosphate | Monosodium Phosphate. Uses: Food industry: it is used as a food additive. chemical industry: it is used in the synthesis and manufacturing of other chemical products, such as detergents, cleaning products, fertilizers and personal care products. laboratory and analytical chemistry: it is used as a reagent and as a buffer in various chemical experiments and analyses. water treatment: to adjust ph and as a water conditioning agent. helps prevent corrosion of pipes and equipment and maintain chemical balance in water. cleaning products industry: it is used in the manufacture of cleaning products such as detergents, disinfectants and surface cleaners. ?pharmaceutical industry: it is used in the manufacture of medications and supplements as a buffering agent and ph stabilizer. it is also used in intravenous formulations and oral care products. Food grade. Group: Industrial Chemicals. CAS No. 7558-80-7. Pack Sizes: Bags, Super sacks. Molecular formula: Molecular formula: NaH2PO4. Categories: triglyceride. |  |
| Native Bacillus cereus Sphingomyelinase | Sphingomyelin phosphodiesterase is a hydrolase enzyme that is involved in sphingolipid metabolism reactions. SMase is a member of the DNase I superfamily of enzymes and is responsible for breaking sphingomyelin (SM) down into phosphocholine and ceramide. The activation of SMase has been suggested as a major route for the production of ceramide in response to cellular stresses. Applications: Sphingomyelinase has been used in a study to assess the interaction of actin with the hiv-1 accessory protein nef. sphingomyelinase has also been used in a study to investigate x-ray scattering as a quality-control tool for liposomal drug-delivery systems. Group: Enzymes. Synonyms: Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; SMase. Enzyme Commission Number: EC 3.1.4.12. CAS No. 9031-54-3. SMase. Activity: > 100 units/mg protein. Storage: 2-8°C. Form: Type I, buffered aqueous glycerol solution, Solution in 50% glycerol containing 50 mM Tris-HCl, pH 7.5; Type II, Lyophilized powder containing potassium phosphate buffer salts and stabilizer. Source: Bacillus cereus. Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; SMase. Cat No: NATE-0672. | |
| Native Bovine Xanthine Oxidase | Xanthine oxidase is a molybdenum-containing enzyme that is found in the cytosol, and may be strongly inhibited by flavonoids. It plays a vital role in the metabolism of some drugs, as well as purines and pyrimidines. It is also known to be a biological source of reactive oxygen species. Xanthine oxidase was shown to be involved in the reduction of cytochrome c by the generation of superoxide anions following the oxidation of xanthine. These free radicals are responsible for reducing cytochrome c. Formerly e.c. 1.1.3.22. Group: Enzymes. Synonyms: Xanthine oxidase; XO; xanthine oxidoreductase; EC 1.17.3.2; 9002-17-9; XOD; Xanthine:oxygen oxidoreductase; hypoxanthine oxidase; hyp.in. Storage: 2-8°C. Form: Type I, Type II, ammonium sulfate suspension; Suspension in 2.3 M (NH4)2SO4 containing 1 mM sodium salicylate; Type III, ammonium sulfate suspension, Suspension in 2.3 M (NH4)2SO4, 10 mM sodium phosphate buffer, pH 7.8, containing 1 mM EDTA and 1 mM sodium salicylate; Type IV, lyophilized powder, Contains 0.5% sodium salicylate. Source: Bovine milk. Species: Bovine. Xanthine oxidase; XO; xanthine oxidoreductase; EC 1.17.3.2; 9002-17-9; XOD; Xanthine:oxygen oxidoreductase; hypoxanthine oxidase; hypoxanthine:oxygen oxidoreductase; Schardinger enzyme; hypoxanthine-xanthine oxidase; xanthine:O2 oxidoreductase; xanthine:xanthine oxidase. Cat No: NATE-0732. | |
| Native Horseradish Superoxide Dismutase | Superoxide dismutases (SOD) are enzymes that alternately catalyze the dismutation (or partitioning) of the superoxide (O2-) radical into either ordinary molecular oxygen (O2) or hydrogen peroxide (H2O2). Superoxide is produced as a by-product of oxygen metabolism and, if not regulated, causes many types of cell damage. Hydrogen peroxide is also damaging, but less so, and is degraded by other enzymes such as catalase. Thus, SOD is an important antioxidant defense in nearly all living cells exposed to oxygen. One exception is Lactobacillus plantarum and related lactobacilli, which use a different mechanism to prevent damage from reactive (O2-). Applications: Superoxide dism.mutase and glutathione reductase, and environmental and xenobiotic stress tolerance in maize inbreds. superoxide dismutase from horseradish has also been used in a study to investigate chemiluminometric enzyme sensors for flow-injection analysis. Group: Enzymes. Synonyms: EC 1.15.1.1; 9054-89-1; SOD; Superoxide:superoxide oxidoreductase; Superoxide Dismutase. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Activity: 1,000-4,000 units/mg protein. Stability: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Horseradish. EC 1.15.1.1; 9054-89-1; SOD; Superoxide:superoxide oxidoreductase; Superoxide Dismutase. Cat No: NATE-0679. | |
| Native Human Superoxide Dismutase | Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice by preventing the conversion of NO to peroxynitrate, an inducer of apoptosis. Applications: Superoxide dismutase from human erythr ocytes has been used in a study to identify in vitro glycated sites of hu.-3; SOD-4; hemocuprein; erythrocuprein; cytocuprein; cuprein ; hepatocuprein; 9054-89-1. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Activity: > 2,500 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Human erythrocytes. Species: Human. Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuperoxide dismutase; superoxide dismutase I; superoxide dismutase II; SOD; Cu,Zn-SOD; Mn-SOD; Fe-SOD; SODF; SODS; SOD-1; SOD-2; SOD-3; SOD-4; hemocuprein; erythrocuprein; cytocuprein; cuprein ; hepatocuprein; 9054-89-1. Cat No: NATE-0680. | |
| Native Human Topoisomerase I | Topoisomerase I relaxes supercoiled DNA molecules. The enzyme initiates transient breakages and rejoins of phosphodiester bonds in superhelical turns of closed-circular DNA. Enzyme activity is independent of right-and left-handed superhelices. Cellular topoisomerase i is present in retroviral particles and enhances viral cdna synthesis. Applications: Topoisomerase i has been used in a study to assess implications for the regulation of hiv-1 replication. topoisomerase i has also been used in a study to investigate the tumor suppressor protein kinase chk2 is a mediator of anoikis of intestinal epithelial cells. Group: Enzymes. Synonyms: Topoisomerase I; EC 5.99.1.2; type I DNA topoisomerase; untwisting enzyme; relaxing enzyme; nicking-c. Enzyme Commission Number: EC 5.99.1.2. CAS No. 80449-01-0. TOPO I. Mole weight: mol wt 100 kDa. Activity: > 2 units/μL. Storage: -70°C. Form: buffered aqueous glycerol solution; Solution containing 20 mM sodium phosphate, pH 7.4, 300 mM NaCl, 50 μg/mL BSA, 50% glycerol, and between 25-100 mM imidazole (concentration will be lot dependent). Source: Human. Topoisomerase I; EC 5.99.1.2; type I DNA topoisomerase; untwisting enzyme; relaxing enzyme; nicking-closing enzyme; swivelase; ω-protein; deoxyribonucleate topoisomerase; topoisomerase; type I DNA topoisomerase; DNA topoisomerase; TOPO I. Cat No: NATE-0707. | |
| Native Staphylococcus aureus Sphingomyelinase | Sphingomyelin phosphodiesterase is a hydrolase enzyme that is involved in sphingolipid metabolism reactions. SMase is a member of the DNase I superfamily of enzymes and is responsible for breaking sphingomyelin (SM) down into phosphocholine and ceramide. The activation of SMase has been suggested as a major route for the production of ceramide in response to cellular stresses. Group: Enzymes. Synonyms: Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; SMase. Enzyme Commission Number: EC 3.1.4.12. CAS No. 9031-54-3. SMase. Activity: 100-300 units/mg protein (Lowry). Storage: 2-8°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 0.25 M phosphate buffer, pH 7.5. Source: Staphylococcus aureus. Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; SMase. Cat No: NATE-0673. | |
| Phosphoglycerate mutase 1 from Human, Recombinant | Phosphoglycerate mutase (PGM) is an enzyme that catalyzes step 8 of glycolysis. It catalyzes the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme (EC 5.4.2.11) is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM (EC 5.4.2.12) class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase. Group: Enzymes. Synonyms: Pgam-1; PGAM1. Enzyme Commission Number: EC 5.4.2.1. Purity: > 90% by SDS-PAGE. Mole weight: 30.9 kDa. Activity: >300 units/mg. Storage: Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles. Form: Liquid. Source: E. coli and fused to His-tag at N-terminus. Species: Human. Pgam-1; PGAM1; Phosphoglycerate mutase 1; Phosphoglycerate mutase. Cat No: NATE-1647. | |
| Phosphoglycerate mutase 1 from Mouse, Recombinant | Phosphoglycerate mutase (PGM) is an enzyme that catalyzes step 8 of glycolysis. It catalyzes the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme (EC 5.4.2.11) is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM (EC 5.4.2.12) class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase. Group: Enzymes. Synonyms: Pgam-1; PGAM1. Enzyme Commission Number: EC 5.4.2.1. Purity: > 95% by SDS-PAGE. Mole weight: 31.4 kDa. Activity: >150 units/mg. Storage: Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles. Form: Liquid. Source: E. coli and fused to His-tag at N-terminus. Species: Mouse. Pgam-1; PGAM1; Phosphoglycerate mutase 1; Phosphoglycerate mutase. Cat No: NATE-1646. | |
| Phosphoglycerate mutase 2 from Human, Recombinant | Phosphoglycerate mutase (PGM) is an enzyme that catalyzes step 8 of glycolysis. It catalyzes the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme (EC 5.4.2.11) is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM (EC 5.4.2.12) class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase. Group: Enzymes. Synonyms: GSD10; PGAM-M; PGAMM; PGAM2. Enzyme Commission Number: EC 5.4.2.11. Purity: > 95% by SDS-PAGE. Mole weight: 30.9 kDa. Activity: >100 units/mg. Storage: Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles. Form: Liquid. Source: E. coli and fused to His-tag at N-terminus. Species: Human. GSD10; PGAM-M; PGAMM; PGAM2; Phosphoglycerate mutase 2; Phosphoglycerate mutase. Cat No: NATE-1643. | |
| phosphonopyruvate hydrolase | Highly specific for phosphonopyruvate as substrate. The reaction is not inhibited by phosphate but is inhibited by the phosphonates phosphonoformic acid, hydroxymethylphosphonic acid and 3-phosphonopropanoic acid. The enzyme is activated by the divalent cations Co2+, Mg2+ and Mn2+. This enzyme is a member of the phosphoenolpyruvate mutase/isocitrate lyase superfamily. Group: Enzymes. Synonyms: PPH. Enzyme Commission Number: EC 3.11.1.3. 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-3776; phosphonopyruvate hydrolase; EC 3.11.1.3; PPH. Cat No: EXWM-3776. | |
| Pseudo-UTP, 100mM Solution | Pseudo-UTP is a building block for the polymerase-mediated synthesis of RNA molecules. RNA molecules, especially messenger RNAs (mRNAs), have widespread applications in therapeutic and diagnostic areas, and have demonstrated their superiority over plasmid DNA techniques in both gene and vaccination therapy. Compared with uridine-containing unmodified mRNAs, the application of pseudouridine-containing modified mRNAs exhibits better nuclease stability, immunogenicity, and translational properties. Thus, pseudo-UTP could be used to develop drugable mRNAs with improved properties, by replacing the standard bases by modified ones. Alternative Names: Pseudouridine-5'-Triphosphate, 5-Ribosyl Uracil. Pseudouridine-5'-triphosphate, Sodium Salt. [[(2R,3S,4R,5S)-5-(2,4-dioxo-1H-pyrimidin-5-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] phosphono hydrogen phosphate. ((2R,3S,4R,5S)-5-(2,4-Dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl tetrahydrogen triphosphate. CAS No. 1175-34-4. Product ID: PIPB-0467. Molecular formula: C9H15N2O15P3 (free acid). Mole weight: 484.1 (free acid). SMILES: C1=C(C(=O)NC(=O)N1)[C@H]2[C@@H]([C@@H]([C@H](O2)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O. Appearance: clear aqueous solution. Category: Modified Nucleotides. |  |
| sucrose-phosphate phosphatase | Requires Mg2+ for maximal activity. This is the final step in the sucrose-biosynthesis pathway. The enzyme is highly specific for sucrose 6-phosphate, with fructose 6-phosphate unable to act as a substrate. Belongs in the haloacid dehydrogenase (HAD) superfamily. The F of sucrose 6F-phosphate is used to indicate that the fructose residue of sucrose carries the substituent. Group: Enzymes. Synonyms: sucrose 6-phosphate hydrolase; sucrose-phosphate hydrolase; sucrose-phosphate phosphohydrolase; sucrose-6-phosphatase; sucrose phosphatase; sucrose-6-phosphate phosphatase; SPP. Enzyme Commission Number: EC 3.1.3.24. CAS No. 9059-33-0. 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-3627; sucrose-phosphate phosphatase; EC 3.1.3.24; 9059-33-0; sucrose 6-phosphate hydrolase; sucrose-phosphate hydrolase; sucrose-phosphate phosphohydrolase; sucrose-6-phosphatase; sucrose phosphatase; sucrose-6-phosphate phosphatase; SPP. Cat No: EXWM-3627. | |
| TDCPP | Tris(1,3-dichloro-2-propyl)phosphate is a clear colorless viscous liquid. Generally a super-cooled liquid at room temperature but may occasionally solidify when held at low temperatures for prolonged periods. (NTP, 1992);Liquid. Group: Plastic additives. CAS No. 13674-87-8. Product ID: tris(1,3-dichloropropan-2-yl) phosphate. Molecular formula: 430.9g/mol. Mole weight: C9H15Cl6O4P. C (C (CCl)OP (=O) (OC (CCl)CCl)OC (CCl)CCl)Cl. InChI=1S/C9H15Cl6O4P/c10-1-7 (2-11)17-20 (16, 18-8 (3-12)4-13)19-9 (5-14)6-15/h7-9H, 1-6H2. ASLWPAWFJZFCKF-UHFFFAOYSA-N. |  |
| Tri(2,3-dichloropropyl) Phosphate | Tris(1,3-dichloro-2-propyl)phosphate is a clear colorless viscous liquid. Generally a super-cooled liquid at room temperature but may occasionally solidify when held at low temperatures for prolonged periods. (NTP, 1992);Liquid. Group: Polymers. CAS No. 13674-87-8. Product ID: tris(1,3-dichloropropan-2-yl) phosphate. Molecular formula: 430.9g/mol. Mole weight: C9H15Cl6O4P. C (C (CCl)OP (=O) (OC (CCl)CCl)OC (CCl)CCl)Cl. InChI=1S/C9H15Cl6O4P/c10-1-7 (2-11)17-20 (16, 18-8 (3-12)4-13)19-9 (5-14)6-15/h7-9H, 1-6H2. ASLWPAWFJZFCKF-UHFFFAOYSA-N. | |
| Tris(1,3-dichloro-2-propyl) Phosphate | Tris(1,3-dichloro-2-propyl)phosphate is a clear colorless viscous liquid. Generally a super-cooled liquid at room temperature but may occasionally solidify when held at low temperatures for prolonged periods. (NTP, 1992);Liquid. Group: Battery materials electronic materials plastic additivesplasticizers. Alternative Names: Phosphoric Acid Tris(1,3-dichloro-2-propyl) Ester. CAS No. 13674-87-8. Product ID: tris(1,3-dichloropropan-2-yl) phosphate. Molecular formula: 430.89. Mole weight: C9H15Cl6O4P. C (C (CCl)OP (=O) (OC (CCl)CCl)OC (CCl)CCl)Cl. InChI=1S/C9H15Cl6O4P/c10-1-7 (2-11)17-20 (16, 18-8 (3-12)4-13)19-9 (5-14)6-15/h7-9H, 1-6H2. ASLWPAWFJZFCKF-UHFFFAOYSA-N. >93.0%(GC). | |
| Vinyl Carbamate. | A potent promutagen. Also mutagenic to Salmonella typhimurium TA 1535 and TA 100 in the presence of reduced nicotinamide adenine dinucleotide phosphate-fortified rat or mouse liver mitochondrial supernatant fractions. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 10mg. US Biological Life Sciences. |  Worldwide |
| 1,3-Dimethylimidazolium dimethyl phosphate | ?98.0% (HPLC). Group: Supercapacitors. |  |
| 1-Ethyl-3-methylimidazolium dibutyl phosphate | ?97.0% (HPLC). Group: Supercapacitors. | |
| 1-Ethyl-3-methylimidazolium diethyl phosphate | ?98.0%. Group: Supercapacitors. | |
| FMN hydrolase | Requires Mg2+. The enzyme, found in many isoforms purified from both bacteria and plants, is a member of the haloacid dehalogenase superfamily. Most of the isoforms have a wide substrate specificity, but isoforms specific for FMN also exist. Group: Enzymes. Synonyms: FMN phosphatase; AtcpFHy1. Enzyme Commission Number: EC 3.1.3.102. 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-3611; FMN hydrolase; EC 3.1.3.102; FMN phosphatase; AtcpFHy1. Cat No: EXWM-3611. | |
| Native Sphingomyelinase from Streptomyces sp. | Sphingomyelin phosphodiesterase is a hydrolase enzyme that is involved in sphingolipid metabolism reactions. SMase is a member of the DNase I superfamily of enzymes and is responsible for breaking sphingomyelin (SM) down into phosphocholine and ceramide. The activation of SMase has been suggested as a major route for the production of ceramide in response to cellular stresses. Applications: This enzyme is useful for enzymatic determination of sphingomyelin when coupled with alkaline phosphatase and choline oxidase. Group: Enzymes. Synonyms: Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; Smase. Enzyme Commission Number: EC 3.1.4.12. CAS No. 9031-54-3. SMase. Mole weight: 37.5 kDa (SDS-PAGE). Activity: > 500 U/mg. Stability: At least one year at ?20°C. Appearance: White to brownish amorphous powder?lyophilized. Storage: Storage at ?20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Streptomyces sp. Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; Smase. Cat No: NATE-1160. | |
| Phospholipase D, Streptomyces chromofuscus | Phospholipase D, Streptomyces chromofuscus (PLD) is an enzyme of the phospholipase superfamily, which widely exists in bacteria, yeast, plants, animals and viruses, and is often used in biochemical research. Phospholipase D can catalyze the hydrolysis of phosphodiester bonds in glycerophospholipids to produce phosphatidic acid and soluble choline. Phospholipase D is involved in a variety of disease-related processes, including diabetes, atherogenesis, obesity, tumorigenesis, immune response, and neuroendocrine function [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: PLD. CAS No. 9001-87-0. Pack Sizes: 1 KU; 5 KU. Product ID: HY-P2812. | |
| phosphonoacetate hydrolase | A zinc-dependent enzyme. Belongs to the alkaline phosphatase superfamily of zinc-dependent hydrolases. Group: Enzymes. Enzyme Commission Number: EC 3.11.1.2. CAS No. 153570-68-4. 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-3775; phosphonoacetate hydrolase; EC 3.11.1.2; 153570-68-4. Cat No: EXWM-3775. | |
| Soybean Phosphatidylcholine | Fluidlecithin Super is used as a refatting agent in shower gels and as a co-emulsifier in creams and is particularly suitable for dry, sensitive skin and skin in need of care. Alternative Names: LECITHIN. PC(16:0/18:2(9E,12E)). 1,2-Diacyl-sn-glycero-3-phosphocholine. L-alpha-Lecithin. LMGP01010592. CAS No. 97281-47-5. Product ID: PIE-0386. Molecular formula: C42H80NO8P. Mole weight: 758.1. EINECS: 232-307-2. SMILES: CCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)([O-])OCC[N+](C)(C)C)OC(=O)CCCCCCC/C=C/C/C=C/CCCCC. Appearance: Waxy solid or thick liquid. Category: Emulsifiers. | |
| Tributylmethylammonium dibutyl phosphate | ?97.0% (T). Group: Supercapacitors. | |
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