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| Product | Description | |
|---|---|---|
| 4-hydroxy-2-oxoglutarate aldolase | The enzymes from rat liver and bovine liver act on both enantiomers of 4-hydroxy-2-oxoglutarate. cf. EC 4.1.3.42, L-4-hydroxy-2-oxoglutarate aldolase. Group: Enzymes. Synonyms: 2-oxo-4-hydroxyglutarate aldolase; hydroxyketoglutaric aldolase; 4-hydroxy-2-ketoglutaric aldolase; 2-keto-4-hydroxyglutaric aldolase; 4-hydroxy-2-ketoglutarate aldolase; 2-keto-4-hydroxyglutarate aldolase; 2-oxo-4-hydroxyglutaric aldolase; DL-4-hydroxy-2-ketoglutarate aldolase; hydroxyketoglutarate aldolase; 2-keto-4-hydroxybutyrate aldolase; 4-hydroxy-2-oxoglutarate glyoxylate-lyase; KHGA. Enzyme Commission Number: EC 4.1.3.16. CAS No. 9030-81-3. 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-4901; 4-hydroxy-2-oxoglutarate aldolase; EC 4.1.3.16; 9030-81-3; 2-oxo-4-hydroxyglutarate aldolase; hydroxyketoglutaric aldolase; 4-hydroxy-2-ketoglutaric aldolase; 2-keto-4-hydroxyglutaric aldolase; 4-hydroxy-2-ketoglutarate aldolase; 2-keto-4-hydroxyglutarate aldolase; 2-oxo-4-hydroxyglutaric aldolase; DL-4-hydroxy-2-ketoglutarate aldolase; hydroxyketoglutarate aldolase; 2-keto-4-hydroxybutyrate aldolase; 4-hydroxy-2-oxoglutarate glyoxylate-lyase; KHGA. Cat No: EXWM-4901. |  |
| Acaterin | Acarbose is an acyl-CoA isolated from Pseudomonas species. A92. In the presence of oxidized low-density lipoprotein in macrophages J744, the synthesis of cholesterol enzymes is inhibited, with an IC50 of 45 μmol/L, and the IC50 for inhibiting ACAT in rat liver microsomes is 120 μmol/L. Inhibition of ACAT is non-competitive Sexual. Synonyms: (2R)-4-[(1R)-1-hydroxyoctyl]-2-methyl-2H-furan-5-one; 3-(1-Hydroxyoctyl)-5-methyl-2(5H)-furanone. Grades: >98%. CAS No. 144398-20-9. Molecular formula: C13H22O3. Mole weight: 226.31. |  |
| Alanine Aminotransferase from Human, Recombinant | Alanine transaminase (ALT) is a transaminase enzyme. It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate-pyruvate transaminase (SGPT) or serum glutamic-pyruvic transaminase (SGPT). ALT is found in plasma and in various body tissues, but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Alanine aminotransferase human recombinant produced in e. coli is a homodimer, nonglycosylated, polypeptide chain containing 495a.a...inotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. CAS No. 9000-86-6. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. ALT. Mole weight: 54,479 Da. Activity: 1,000 U/mg. Stability: AAT1 although stable at 10°C for 5 days, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile liquid formulation. Source: E. coli. Species: Human. ALT1; Glutamic-pyruvic transaminase 1; GPT 1; Glutamic-alanine transaminase 1; AAT1; ALT; ALAT; SGPT; Alanine transaminase; alanine aminotransferase; GPT; β-alanine aminotransferase; alanine-α | |
| Aldehyde Dehydrogenase 2 from Human, Recombinant | ALDH2 is part of the aldehyde dehydrogenase family of proteins which catalyze the chemical transformation from acetaldehyde to acetic acid. ALDH2 is the second enzyme of the major oxidative pathway of alcohol metabolism. ALDH2 has 2 major liver isoforms: cytosolic and mitochondrial, which differ by their electrophoretic mobilities, kinetic properties, and subcellular localizations. Nearly all Caucasians have 2 major isozymes, whereas roughly 50% of Orientals have only the cytosolic isozyme, omitting the mitochondrial isozyme. The extremely higher rate of acute alcohol intoxication with Orientals compared to Caucasians is due to the fact of the absence of mitochondrial... & having a molecular mass of 54.5 kda. the aldh2 is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: ALDM; ALDHI; ALDH-E2; MGC1806; ALDH2; Aldehyde dehydrogenase mitochondrial; ALDH class 2. Purity: Greater than 90.0% as determined by SDS-PAGE. ALDH2. Mole weight: 54.5 kDa. Activity: > 0.14 units/ml. Stability: Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. ALDM; ALDHI; ALDH-E2; MGC1806; ALDH2; Aldehyde dehydrogenase mitochondrial; ALDH class 2. Cat No: NATE-0804. | |
| Aspartate Transaminase (Crude Enzyme) | (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or serum glutamic oxaloacetic transaminase(SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme (EC 2. 6. 1. 1) that was first described by Arthur Karmen and colleagues in 1954. AST catalyzes the reversible transfer of an α-amino group between aspartate and glutamate and, as such, is an important enzyme in amino acid metabolism. AST is found in the liver, heart, skeletal muscle, kidneys, brain, and red blood cells. Serum AST level, serum ALT (alanine transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; medicine; biotechnology. Group: Enzymes. Synonyms: glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutarate-glutamate aminotransferase; aspartate α-ketoglutarate transaminase; aspartate aminotransferase; aspartate-2-oxoglutarate transaminase; aspartic a. Enzyme Commission Number: EC 2.6.1.1. CAS No. 9000-97-9. AST. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. glutamic-oxaloacetic transamina | |
| β-cyano-L-alanine | β-cyano-L-alanine is a reversible inhibitor of the H2S-synthesizing enzyme CSE. It blocks H2S synthesis in rat liver preparations with an IC50 value of 6.5 μM and increases blood pressure in anaesthetized rats induced with hemorrhagic shock by inhibiting endogenous H2S synthesis. Synonyms: BCA; beta-cyano-L-alanine; 3-Cyano-L-alanine; L-3-Cyanoalanine. Grades: ≥ 98% (TLC). CAS No. 6232-19-5. Molecular formula: C4H6N2O2. Mole weight: 114.1. | |
| CP-640186 | CP-640186 is an orally active and cell-permeable Acetyl-CoA carboxylase ( ACC ) inhibitor with IC 50 s of 53 nM and 61 nM for rat liver ACC1 and rat skeletal muscle ACC2 respectively. Acetyl-CoA carboxylase (ACC) is a key enzyme of fatty acid metabolism that enables the synthesis of malonyl-CoA. CP-640186 can also stimulate muscle fatty acid oxidation [1] [2]. Uses: Scientific research. Group: Signaling pathways. CAS No. 591778-68-6. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg. Product ID: HY-15259. |  |
| CP-640186 hydrochloride | CP-640186 hydrochloride is an orally active and cell-permeable Acetyl-CoA carboxylase ( ACC ) inhibitor with IC 50 s of 53 nM and 61 nM for rat liver ACC1 and rat skeletal muscle ACC2 respectively. Acetyl-CoA carboxylase (ACC) is a key enzyme of fatty acid metabolism that enables the synthesis of malonyl-CoA. CP-640186 hydrochloride can also stimulate muscle fatty acid oxidation [1] [2]. Uses: Scientific research. Group: Signaling pathways. CAS No. 591778-70-0. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-15259A. | |
| D-Eritadenine | D-Eritadenine is an adenosine analog and a potent, reversible inhibitor of S-adenosylhomocysteine hydrolase. Dietary administration of D-eritadenine (50 mg/kg) increases liver microsomal phosphatidylethanolamine concentration and decreases liver microsomal Δ6 desaturase activity and plasma cholesterol levels in rats. Uses: Enzyme inhibitors. Synonyms: (αR,βR)-6-Amino-α,β-dihydroxy-9H-purine-9-butanoic Acid; 4-(6-Amino-9H-purin-9-yl)-4-deoxy-D-erythronic Acid; 4-(6-Aminopurin-9-yl)-4-deoxy-D-erythronic Acid; Lentinacin; Lentysine; 4-(9-Adenyl)-D-erythro-2,3-dihydroxybutyric Acid; Eritadenine; Lentysine; Lentinacin. Grades: ≥95%. CAS No. 23918-98-1. Molecular formula: C9H11N5O4. Mole weight: 253.21. | |
| dihydroorotate dehydrogenase (quinone) | This Class 2 dihydroorotate dehydrogenase enzyme contains FMN. The enzyme is found in eukaryotes in the mitochondrial membrane, in cyanobacteria, and in some Gram-negative and Gram-positive bacteria associated with the cytoplasmic membrane. The reaction is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides. The best quinone electron acceptors for the enzyme from bovine liver are ubiquinone-6 and ubiquinone-7, although simple quinones, such as benzoquinone, can also act as acceptor at lower rates. Methyl-, ethyl-, tert-butyl and benzyl (S)-dihydroorotates are also substrates, but methyl esters of (S)-1-methyl and (S)-3-methyl and (S)-1,3-dimethyldihydroorotates are not. Class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1), NAD+ (EC 1.3.1.14) or NADP+ (EC 1.3.1.15) as electron acceptor. Group: Enzymes. Synonyms: dihydroorot. Enzyme Commission Number: EC 1.3.5.2. CAS No. 59088-23-2. 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-1386; dihydroorotate dehydrogenase (quinone); EC 1.3.5.2; 59088-23-2; dihydroorotate:ubiquinone oxidoreductase; (S)-dihydroorotate:(acceptor) oxidoreductase; (S)-dihydroorotate:acceptor oxidoreductase; DHOdehase (ambiguous); DHOD (ambiguous); DHODase (ambiguous); DHODH. Cat No: EXWM-1386. | |
| DL-Propargyl glycine hydrochloride | DL-Propargyl glycine (PAG) is an irreversible inhibitor of the H2S synthesizing enzyme cystathionine-γ-lyase (CSE). PAG blocks H2S synthesis activity in rat liver preparations with an IC50 value of 55 μM and abolishes the rise in plasma H2S in anaesthetized rats induced with hemorrhagic shock. Synonyms: PAG; 2-Aminopent-4-ynoic acid hydrochloride; AK323755; AK110719. Grades: ≥95%. CAS No. 16900-57-5. Molecular formula: C5H7NO2·HCl. Mole weight: 149.6. | |
| DT Diaphorase from human, Recombinant | DT Diaphorase is a flavoenzyme that catalyzes the oxidation of reduced di-and triphosphopyridine nucleotides. It contains one mole of FAD per mole of enzyme. The enzyme found in rat liver catalyzes the oxidation of NADH and NADPH by various dyes and quinones. The molecular weight is found to be approximately 48 kDa Da. The pH optimum of the enzyme purified from rat liver is found to be 5.0. It is a cytosolic enzyme that catalyzes the two-electron reduction of various quinones. It catalyzes the conversion of vitamin K to vitamin K hydroquinone for utilization in the post-translational γ-glutamyl carboxylation reactions. These reactions are necessary for several proteins involved in blood coagulation. Applications: Human dt diaphorase has been used in a study to assess the development of novel quinone phosphorodiamidate prodrugs. human dt diaphorase has also been used to investigate its crystal structure for the development of a model for its interaction with the cytotoxic prodrug 5-(aziridin-1-yl)-2,4-dinitrobenzamide (cb1954). Group: Enzymes. Synonyms: menadione reductase; phylloquinone reductase; quinone reductase; dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone); DT-diaphorase; flavoprotein NAD (P)H-q. Enzyme Commission Number: EC 1.6.99.2. Diaphorase. Mole weight: monomer mol wt 31 kDa. Storage: 2-8°C. F | |
| DT Diaphorase from rat, Recombinant | DT Diaphorase is a flavoenzyme that catalyzes the oxidation of reduced di-and triphosphopyridine nucleotides. It contains one mole of FAD per mole of enzyme. The enzyme found in rat liver catalyzes the oxidation of NADH and NADPH by various dyes and quinones. The molecular weight is found to be approximately 48 kDa Da. The pH optimum of the enzyme purified from rat liver is found to be 5.0. It is a cytosolic enzyme that catalyzes the two-electron reduction of various quinones. It catalyzes the conversion of vitamin K to vitamin K hydroquinone for utilization in the post-translational γ-glutamyl carboxylation reactions. These reactions are necessary for several proteins involved in blood coagulation. Applications: Dt diaphorase from rat has been used in a study to investigate the two-electron reduction of quinones by rat liver. dt diaphorase from rat has also been used in a study to investigate colon cancer chemopreventive efficacy of silibinin through perturbation of xenobiotic metabolizing enzymes. Group: Enzymes. Synonyms: menadione reductase; phylloquinone reductase; quinone reductase; dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone); DT-diaphorase; flavoprotein NAD (P)H-qui. Enzyme Commission Number: EC 1.6.99.2. Purity: ~90% (SDS-PAGE). Diaphorase. Mole weight: monomer mol wt 31 kDa. Storage: 2-8°C. Form | |
| Eniluracil | Eniluracil, also known as GW776 and GW776C85, is an orally active and irreversible inhibitor of dihydropyrimidine dehydrogenase. Eniluracil inhibits dihydropyrimidine dehydrogenase, the rate-limiting enzyme that catabolizes and inactivates 5-fluorouracil (5-FU) in the liver. Co-administration of ethynyluracil permits the oral administration of 5-FU. Uses: Enzyme inhibitors. Synonyms: 5-ethynyluracil; 5-ethynylpyrimidine-2,4(1H,3H)-dione; 5-Ethynyl-2-hydroxypyrimidin-4(1H)-one; GW776; GW-776; GW 776. CAS No. 59989-18-3. Molecular formula: C6H4N2O2. Mole weight: 136.11. | |
| Enniatin B | Enniatin B is a Fusarium mycotoxin. Enniatin B inhibits acyl-CoA: cholesterol acyltransferase ( ACAT ) activity with an IC 50 of 113 μM in an enzyme assay using rat liver microsomes [1]. Enniatins B decreases the activation of ERK (p44/p42) [2]. Uses: Scientific research. Group: Natural products. CAS No. 917-13-5. Pack Sizes: 1 mg. Product ID: HY-N3806. | |
| Entacapone | Entacapone is a potent, reversible, peripherally acting and orally active catechol-O-methyltransferase (COMT) inhibitor. Entacapone inhibits COMT from rat brain, erythrocytes and liver with IC 50 values of 10 nM, 20 nM, and 160 nM, respectively. Entacapone is selective for COMT over other catecholamine metabolizing enzymes, including MAO-A, MAO-B, phenolsulphotransferase M (PST-M) and PST-P (IC 50 s>50 μM). Entacapone can be used for the research of Parkinson's disease [1]. Entacapone serves as a inhibitor of FTO demethylation with an IC 50 of 3.5 μM, can be used for the research of metabolic disorders [2]. Uses: Scientific research. Group: Signaling pathways. CAS No. 130929-57-6. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 50 mg; 100 mg. Product ID: HY-14280. | |
| glycine N-methyltransferase | This enzyme is thought to play an important role in the regulation of methyl group metabolism in the liver and pancreas by regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine. It is inhibited by 5-methyltetrahydrofolate pentaglutamate. Sarcosine, which has no physiological role, is converted back into glycine by the action of EC 1.5.8.3, sarcosine dehydrogenase. Group: Enzymes. Synonyms: glycine methyltransferase; S-adenosyl-L-methionine:glycine methyltransferase; GNMT. Enzyme Commission Number: EC 2.1.1.20. CAS No. 37228-72-1. 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-1800; glycine N-methyltransferase; EC 2.1.1.20; 37228-72-1; glycine methyltransferase; S-adenosyl-L-methionine:glycine methyltransferase; GNMT. Cat No: EXWM-1800. | |
| leucine transaminase | A pyridoxal-phosphate protein. This enzyme differs from EC 2.6.1.42, branched-chain-amino-acid transaminase, in that it does not act on L-valine or L-isoleucine, although it does act on L-methionine. The mitochondrial form from rat liver differs in physical characteristics from the cytoplasmic form. Group: Enzymes. Synonyms: L-leucine aminotransferase; leucine 2-oxoglutarate transaminase; leucine aminotransferase; leucine-α-ketoglutarate transaminase. Enzyme Commission Number: EC 2.6.1.6. CAS No. 9030-37-9. 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-2901; leucine transaminase; EC 2.6.1.6; 9030-37-9; L-leucine aminotransferase; leucine 2-oxoglutarate transaminase; leucine aminotransferase; leucine-α-ketoglutarate transaminase. Cat No: EXWM-2901. | |
| Lipase Feed Grade Enzymes | It can promote the digestion and absorption of fat in the daily diets, increase feed conversion ratio and meet the requirements for high energy rations. 1.Supplying the endogenous digestive enzyme (Perfecting the digestive enzyme system of animals), meeting the demand of animals for daily diets of high energy. 2. Improving nutrition of the feed, especially digestion and utilization of fat, increasing the feed conversion rate. 3. Reducing weanling stress of piglets, obviously reducing its diarrhea and alimentary canal diseases and improving survival rate. 4. Enhancing bait percentage in aquiculture, improving fat utilization and reducing formation of fatty liver. 5.Protecting animal health, increasing average daily gain and production capacity, improving meat quality. 6. Boosting absorption and utilization of fat-soluble vitamin and other micro element. Applications: Fish, piglet, fowl,others. Group: Enzymes. Synonyms: Lipase Feed Grade Enzymes; digestion and utilization of fat; for Fish; piglet; fowl; Feed;Lipase; Feed Grade Enzymes; Lipase Feed Grade Enzymes; FEED-2321. CAS No. 9001-62-1. Lipase. Appearance: powder. Lipase Feed Grade Enzymes; digestion and utilization of fat; for Fish; piglet; fowl; Feed;Lipase; Feed Grade Enzymes; Lipase Feed Grade Enzymes; FEED-2321. Pack: 25kg/barrel or subject to client requirement. Cat No: FEED-2321. | |
| long-chain acyl-CoA dehydrogenase | Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 6 to at least 16 carbon atoms. The highest activity was found with C12, and the rates with C8 and C16 were 80 and 70%, respectively. The enzyme from rat can accept substrates with C8-C22. It is most active with C14 and C16, and has no activity with C4, C6 or C24. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase. Group: Enzymes. Synonyms: palmitoyl-CoA dehydrogenase; palmitoyl-coenzyme A dehydrogenase; long-chain acyl-coenzyme A dehydrogenase; long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase; ACADL (gene name). Enzyme Commission Number: EC 1.3.8.8. CAS No. 59536-74-2. 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-1415; long-chain acyl-CoA dehydrogenase; EC 1.3.8.8; 59536-74-2; palmitoyl-CoA dehydrogenase; palmitoyl-coenzyme A dehydrogenase; long-chain acyl-coenzyme A dehydrogenase; long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase; ACADL (gene name). Cat No: EXWM-1415. | |
| medium-chain acyl-CoA dehydrogenase | Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 4 to 16 carbon atoms, but is most active with C8 to C12 compounds. The enzyme from rat does not accept C16 at all and is most active with C6-C8 compounds. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase. Group: Enzymes. Synonyms: fatty acyl coenzyme A dehydrogenase (ambiguous); acyl coenzyme A dehydrogenase (ambiguous); acyl dehydrogenase (ambiguous); fatty-acyl-CoA dehydrogenase (ambiguous); acyl CoA dehydrogenase (ambiguous); general acyl CoA dehydrog. Enzyme Commission Number: EC 1.3.8.7. 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-1414; medium-chain acyl-CoA dehydrogenase; EC 1.3.8.7; fatty acyl coenzyme A dehydrogenase (ambiguous); acyl coenzyme A dehydrogenase (ambiguous); acyl dehydrogenase (ambiguous); fatty-acyl-CoA dehydrogenase (ambiguous); acyl CoA dehydrogenase (ambiguous); general acyl CoA dehydrogenase (ambiguous); medium-chain acyl-coenzyme A dehydrogenase; acyl-CoA:(acceptor) 2,3-oxidoreductase (ambiguous); ACADM (gene name). Cat No: EXWM-1414. | |
| Nafenopin | Nafenopin is a hypolipidemic agent, a peroxisome proliferator, on the activities of rat liver glutathione-requiring enzymes and catalase in comparison to the action of phenobarbital. Uses: A hypolipidemic agent. Synonyms: 2-Methyl-2-[4-(1,2,3,4-tetrahydronaphthalen-1-yl)phenoxy]propanoic acid. Grades: ≥98%. CAS No. 3771-19-5. Molecular formula: C20H22O3. Mole weight: 310.39. | |
| Native Bacillus licheniformis Proteinase | Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 kda. Applications: The enzyme from creative enzymes has been used to optimize release of all mit ochondrial populations from homogenized ventricular tissue of rat heart. it has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax-embedded liver specimens for detecting human and viral dna. this is a proteolytic enzyme isolated from th...ls to study the silencing of cardiac mit ochondrial nhe1. Group: Enzymes. Synonyms: protease; peptidase; proteinase; EC 3.4.21.62; 9014-01-1; Alkaline Protease; Protease from Bacillus licheniformis; Proteinase from Bacillus licheniformis; Subtilo peptidase A. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9001-92-7. Purity: crystallization. Proteinase. Mole weight: 27 KDa. Activity: 7.0-14.0 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Bacillus licheniformis. protease; peptidase; proteinase; EC 3.4.21.62; 9014-01-1; Alkaline Protease; Protease from Bacillus licheniformis; Proteinase from Bacillus licheniformis; Subtilo peptidase A. Cat No: NATE-0639. | |
| Native Bovine Deoxyribonuclease II | Deoxyribonuclease II, also called as acid DNAse, hydrolyzes deoxyribonucleotide linkages in native and denatured DNA yielding products with 3'-phosphates. In vitro, its optimum pH range is 4.5-5.0. It also acts upon p-nitrophenyl-phosphodiesters at pH 5.6-5.9. The molecular weight is approximately 38 kDa Da. Applications: Dnase ii from creative enzymes has been used in the dissociation medium during the preparation of embryonic cardiac myocytes from rat heart. deoxyribonuclease ii from bovine spleen has been used in a study that conducted a partial purification of deoxyribonucleases from eggs and liver of xenopus laevis. deoxyribonuclease ii from bovine spleen has also been used in a study to investigate nucleic acid and protein synthesis of splenic lymphocytes. Group: Enzymes. Synonyms: DNASE2; deoxyribonuclease II; EC 3.1.22.1; 9025-64-3; DNase II; pancreatic DNase II; deoxyribonucleate 3'-nucleotidohydrolase; DNase II; pancreati. Enzyme Commission Number: EC 3.1.22.1. CAS No. 9025-64-3. DNASE2. Activity: > 1,000 units/mg protein. Storage: -20°C. Form: essentially salt-free, lyophilized powder. Source: Bovine spleen. Species: Bovine. DNASE2; deoxyribonuclease II; EC 3.1.22.1; 9025-64-3; DNase II; pancreatic DNase II; deoxyribonucleate 3'-nucleotidohydrolase; DNase II; pancreatic DNase II; acid deoxyribonuclease; acid Dnase. Cat No: NATE-0201. | |
| Native Bovine Liver Alkaline Phosphatase | Alkaline phosphatases (APs) are highly ubiquitous enzymes, present in all species from bacteria to man. In humans, APs are encoded by a multi-gene family composed of four loci; i.e., tissue-nonspecific AP, also called bone/liver/kidney AP, intestinal. The sequence and complexity of the AP genes from other vertebrates and lower species are now being elucidated. The biological function of AP isozymes is still unknown. In vitro, the enzymes behave as phosphotransferases at neutral pH. The use of phosphate acceptor molecules (diethanolamine, tris, 2-amino-2-methyl-1-propanol) in the buffered substrate solutions increases the reaction rates and, thus, the sensitivity of assays based on AP determinations. Group: Enzymes. Synonyms: Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Enzyme Commission Number: EC 3.1.3.1. CAS No. 9001-78-9. Activity: 100 U/mg protein. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Bovine Liver. Species: Bovine. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase; AP. Cat No: NATE-1871. | |
| Native Candida Rugosa Cholesterol Esterase | Cholesterol esterase (CE) is also known as cholesterol ester hydrolase. This enzyme catalyzes the following reaction: Sterol Ester --------> Sterol + Fatty Acid.Cholesterol esterase activity has been demonstrated in pancreas, intestine, liver and kidney. The enzyme is inactivated by proteolytic enzymes but stabilized by proteolytic enzyme inhibitors and by bile salts. CE from rat pancreas has a molecular weight of 65,000-69,000. In the presence of bile salts, it aggregates to a hexamer which is possibly the active form of the enzyme. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; sterol esterase; CE. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Purity: 0.9. Cholesterol Esterase. Activity: 25-100 U/mg. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Candida Rugosa. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; sterol esterase; CE. Cat No: NATE-1679. | |
| Native E. coli Alanine Aminotransferase | Alanine transaminase (ALT) is a transaminase enzyme (EC 2.6.1.2). It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate-pyruvate transaminase (SGPT) or serum glutamic-pyruvic transaminase (SGPT). ALT is found in plasma and in various body tissues, but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Group: Enzymes. Synonyms: Alanine transami. Enzyme Commission Number: EC 2.6.1.2. CAS No. 9000-86-6. Purity: > 95% (SDS-PAGE). ALT. Mole weight: 54,479 of subunit deduced from gene sequence. Activity: > 1,000 U/mL. Storage: -20°C. Form: Liquid. Source: E. coli. Alanine transaminase; ALT; EC 2.6.1.2; alanine aminotransferase; ALAT; glutamic-pyruvic transaminase; glutamic-alanine transaminase; GPT; β-alanine aminotransferase; alanine-α-ketoglutarate aminotransferase; alanine-pyruvate aminotransferase; glutamic acid-pyruvic acid transaminase; glutamic-pyruvic aminotransferase; L-alanine aminotransferase; L-alanine transaminase; L-alanine-α-ketoglutarate aminotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. Cat No: NATE-0064. | |
| Native Human Alanine Aminotransferase | Alanine transaminase (ALT) is a transaminase enzyme (EC 2.6.1.2). It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate-pyruvate transaminase (SGPT) or serum glutamic-pyruvic transaminase (SGPT). ALT is found in plasma and in various body tissues, but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Alanine transaminase, also commonly known as serum glutamate pyruvate transaminase is an enzyme involved in the synthesis o...oup: Enzymes. Synonyms: Alanine transaminase; ALT; EC 2.6.1.2; alanine aminotransferase; ALAT; glutamic-pyruvic transaminase; glutamic-alanine transaminase; GPT; β-alanine aminotransferase; alanine-α-ketoglutarate aminotransferase; alanine-pyruvate aminotransferase; glutamic acid-pyruvic acid transaminase; glutamic-pyruvic aminotransferase; L-alanine aminotransferase; L-alanine transaminase; L-alanine-α-ketoglutarate aminotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. Enzyme Commission Number: EC 2.6.1.2. CAS No. 9000-86-6. ALT. Activity: >5 U /mg. Storage: -20°C. Source: Human Liver. Species: Human. | |
| Native Human Cathepsin B | Cathepsin B has been found to cleave procaspase 1 and procaspase 11 and to induce apoptosis in digitonin-permeabilized cells. Translocation of cathepsin B from the cytoplasm to the nucleus contributes to bile salt induced apoptosis of rat hepatocytes. Levels of cathepsin B in PC12 cells significantly decrease 12 to 24 hours after apoptosis is induced. Group: Enzymes. Synonyms: CTSB; cathepsin B; cathepsin B1; APPS; CPSB; EC 3.4.22.1; 9047-22-7; cathepsin II; CatB. Enzyme Commission Number: EC 3.4.22.1. CAS No. 9047-22-7. Cathepsin B. Activity: > 2 ,000 units/mg protein (E1%/280). Storage: -20°C. Form: buffered aqueous solution. Solution in 50 mM sodium acetate, pH 5.0, with 1 mM EDTA. Source: Human liver. Species: Human. CTSB; cathepsin B; cathepsin B1; APPS; CPSB; EC 3.4.22.1; 9047-22-7; cathepsin II; CatB. Cat No: NATE-0168. | |
| Native Porcine Glutamic-Oxalacetic Transaminase | Aspartate transaminase (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or serum glutamic oxaloacetic transaminase (SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme (EC 2.6.1.1). AST catalyzes the reversible transfer of an α-amino group between aspartate and glutamate and, as such, is an important enzyme in amino acid metabolism. AST is found in the liver, heart, skeletal muscle, kidneys, brain, and red blood cells. Serum AST level, serum ALT (alanine transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Group: Enzymes. Synonyms: EC 2.6.1.1; glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutaRate-glutamate aminotransferase; aspartate α-ketoglutaRate transaminase; aspartate aminotransferase; aspartate-2-oxoglutaRate transaminase; aspartic acid aminotr. Enzyme Commission Number: EC 2.6.1.1. CAS No. 9000-97-9. Activity: > 100 U/mg. Storage: 2-8°C. Source: Porcine heart. Species: Porcine. EC 2.6.1.1; glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutaRate-glutamate aminotransferase; aspartate α-ketoglutaRate transaminase; aspartate aminotransferase; aspartate-2-oxoglutaRate transa | |
| Native Porcine Glutamic-Pyruvic Transaminase | Alanine transaminase (ALT) is a transaminase enzyme (EC 2.6.1.2). It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate-pyruvate transaminase (SGPT) or serum glutamic-pyruvic transaminase (SGPT). ALT is found in plasma and in various body tissues, but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Group: Enzymes. Synonyms: Alanine transaminase; ALT; EC 2.6.1.2; alanine aminotransferase; ALA. Enzyme Commission Number: EC 2.6.1.2. CAS No. 9000-86-6. Activity: 100 U/mg. Storage: -20°C. Form: Freeze dried powder. Source: Porcine heart. Species: Porcine. Alanine transaminase; ALT; EC 2.6.1.2; alanine aminotransferase; ALAT; glutamic-pyruvic transaminase; glutamic-alanine transaminase; GPT; β-alanine aminotransferase; alanine-α-ketoglutarate aminotransferase; alanine-pyruvate aminotransferase; glutamic acid-pyruvic acid transaminase; glutamic-pyruvic aminotransferase; L-alanine aminotransferase; L-alanine transaminase; L-alanine-α-ketoglutarate aminotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. Cat No: NATE-0068. | |
| Native Porcine NAD(P)H Dehydrogenase (quinone) | DT Diaphorase is a flavoenzyme that catalyzes the oxidation of reduced di-and triphosphopyridine nucleotides. It contains one mole of FAD per mole of enzyme. The enzyme found in rat liver catalyzes the oxidation of NADH and NADPH by various dyes and quinones. The molecular weight is found to be approximately 48 kDa Da. The pH optimum of the enzyme purified from rat liver is found to be 5.0. It is a cytosolic enzyme that catalyzes the two-electron reduction of various quinones. It catalyzes the conversion of vitamin K to vitamin K hydroquinone for utilization in the post-translational γ-glutamyl carboxylation reactions. These reactions are necessary for several pr...hydrogenase; NAD (P)H menadione reductase; NAD (P)H-quinone dehydrogenase; NAD (P)H-quinone oxidoreductase; NAD (P)H: (quinone-acceptor)oxidoreductase. CAS No. 9032-20-6. Diaphorase. Activity: >25 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Appearance: Yellow suspension in ammonium sulfate, 3.2 mol/l. Source: Porcine heart. Species: Porcine. menadione reductase; phylloquinone reductase; quinone reductase; dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone); DT-diaphorase; flavoprotein NAD (P)H-quinone reductase; menadione oxidoreductase; NAD (P)H dehydrogenase; NAD (P)H menadione reductase; NAD (P)H-quinone dehydro | |
| Native Rat Arginase | Arginase (EC 3.5.3.1, arginine amidinase, canavanase, L-arginase, arginine transamidinase) is a manganese-containing enzyme. The reaction catalyzed by this enzyme is:arginine + H2O ? ornithine + urea. It is the final enzyme of the urea cycle. It is ubiquitous to all domains of life. Group: Enzymes. Synonyms: Arginase; arginine amidinase; canavanase; L-arginase; arginine transamidinase; EC 3.5.3.1. Enzyme Commission Number: EC 3.5.3.1. CAS No. 9000-96-8. Purity: Purified. Arginase. Activity: > 200 U/mg. Storage: -20°C. Form: Lyophilized. Source: Rat Liver. Species: Rat. Arginase; arginine amidinase; canavanase; L-arginase; arginine transamidinase; EC 3.5.3.1. Cat No: NATE-0086. | |
| Native Rat Glutathione-S-Transferase | 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 identify new GST functions. Group: Enzymes. Synonyms: Glutathione S-transferases; GSTs; GST; Glutathione S-alkenetransferase; Glutathione S-alkyltransferase; Glutathione S-aralkyltransferase; Glutathione S-aryltransferase;. Enzyme Commission Number: EC 2.5.1.18. CAS No. 50812-37-8. Purity: Purified. Glutathione S-Transferase. Activity: > 10 U/mg. Storage: -20°C. Form: Lyophilized. Source: Rat Liver. Species: Rat. 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-0327. | |
| Native Rat Sorbitol Dehydrogenase | Sorbitol dehydrogenase (or SDH) is a cytosolic enzyme. In humans this protein is encoded by the SORD gene. Sorbitol dehydrogenase is an enzyme in carbohydrate metabolism converting sorbitol, the sugar alcohol form of glucose, into fructose. Together with aldose reductase, it provides a way for the body to produce fructose from glucose without using ATP. Sorbitol dehydrogenase uses NAD+ as a cofactor; its reaction is sorbitol + NAD+--> fructose + NADH + H+. A zinc ion is also involved in catalysis. Organs that use it most frequently include the liver and seminal vesicle; it is found in all kinds of organisms from bacteria to humans. A secondary use is the metabolism of dietar...5-oxidoreductase; L-iditol (sorbitol) dehydrogenase; glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase. Enzyme Commission Number: EC 1.1.1.14. CAS No. 9028-21-1. Purity: Purified. SDH. Activity: Reported in U/mg. Storage: -20°C. Form: Lyophilized. Source: Rat Liver. Species: Rat. Sorbitol Dehydrogenase; SDH; EC 1.1.1.14; 9028-21-1; L-iditol 2-dehydrogenase; polyol dehydrogenase; sorbitol dehydrogenase; L-iditol:NAD+ 5-oxidoreductase; L-iditol (sorbitol) dehydrogenase; glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase. Cat No: NATE-0667. | |
| Native Rat Thioredoxin Reductase | Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide. Applications: Thioredoxin reductase from rat liver can be used for studying the uptake and reduction of a-lipoic acid... NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR; 9074-14-0. Enzyme Commission Number: EC 1.8.1.9. CAS No. 9074-14-0. TrxR. Activity: > 100 units/mg protein (Bradford). Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 1 mM EDTA, and 10% glycerol. Source: Rat liver. Species: Rat. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR; 9074-14-0. Cat No: NATE-0713. | |
| N-formylmethionyl-peptidase | Highly specific for N-formylmethionyl peptides. Will not cleave methionyl peptides or N-formyl derivatives of amino acids other than methionine. Isolated from rat liver. Inhibited by heavy metals and activated by Cl-. Group: Enzymes. Synonyms: (fMet)-releasing enzyme; formylmethionine aminopeptidase. Enzyme Commission Number: EC 3.4.19.7. CAS No. 76106-80-4. 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-4091; N-formylmethionyl-peptidase; EC 3.4.19.7; 76106-80-4; (fMet)-releasing enzyme; formylmethionine aminopeptidase. Cat No: EXWM-4091. | |
| Phenacetin | Phenacetin (Acetophenetidin) is a non-opioid analgesic/antipyretic agent. Phenacetin is a selective COX-3 inhibitor. Phenacetin is used as probe of cytochrome P450 enzymes CYP1A2 in human liver microsomes and in rats [1] [2] [3]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Acetophenetidin. CAS No. 62-44-2. Pack Sizes: 10 mM * 1 mL; 500 mg; 1 g; 5 g. Product ID: HY-B0476. | |
| Phenacetin (Standard) | Phenacetin (Standard) is the analytical standard of Phenacetin. This product is intended for research and analytical applications. Phenacetin (Acetophenetidin) is a non-opioid analgesic/antipyretic agent. Phenacetin is a selective COX-3 inhibitor. Phenacetin is used as probe of cytochrome P450 enzymes CYP1A2 in human liver microsomes and in rats [1] [2] [3]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Acetophenetidin (Standard). CAS No. 62-44-2. Pack Sizes: 25 mg; 50 mg; 100 mg. Product ID: HY-B0476R. | |
| short-chain acyl-CoA dehydrogenase | Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme catalyses the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R-hydrogen atoms. The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms. The highest activity was reported with either butanoyl-CoA or pentanoyl-CoA. The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA. cf. EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC ...name). Enzyme Commission Number: EC 1.3.8.1. CAS No. 9027-88-7. 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-1405; short-chain acyl-CoA dehydrogenase; EC 1.3.8.1; 9027-88-7; butyryl-CoA dehydrogenase; butanoyl-CoA dehydrogenase; butyryl dehydrogenase; unsaturated acyl-CoA reductase; ethylene reductase; enoyl-coenzyme A reductase; unsaturated acyl coenzyme A reductase; butyryl coenzyme A dehydrogenase; short-chain acyl CoA dehydrogenase; short-chain acyl-coenzyme A dehydrogenase; 3-hydroxyacyl CoA reductase; butanoyl-CoA:(acceptor) 2,3-oxidoreductase; ACADS (gene name). Cat No: EXWM-1405. | |
| stearoyl-CoA 9-desaturase | An iron protein. The rat liver enzyme is an enzyme system involving cytochrome b5 and EC 1.6.2.2, cytochrome-b5 reductase. The ferricytochrome b5 produced is reduced by NADH and cytochrome-b5 reductase (EC 1.6.2.2). Group: Enzymes. Synonyms: Δ9-desaturase; acyl-CoA desaturase; fatty acid desaturase; stearoyl-CoA, hydrogen-donor:oxygen oxidoreductase. Enzyme Commission Number: EC 1.14.19.1. CAS No. 9014-34-0. 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-0971; stearoyl-CoA 9-desaturase; EC 1.14.19.1; 9014-34-0; Δ9-desaturase; acyl-CoA desaturase; fatty acid desaturase; stearoyl-CoA, hydrogen-donor:oxygen oxidoreductase. Cat No: EXWM-0971. | |
| tryptophan 2,3-dioxygenase | A protohemoprotein. In mammals, the enzyme appears to be located only in the liver. This enzyme, together with EC 1.13.11.52, indoleamine 2,3-dioxygenase, catalyses the first and rate-limiting step in the kynurenine pathway, the major pathway of tryptophan metabolism. The enzyme is specific for tryptophan as substrate, but is far more active with L-tryptophan than with D-tryptophan. Group: Enzymes. Synonyms: tryptophan pyrrolase (ambiguous); tryptophanase; tryptophan oxygenase; tryptamine 2,3-dioxygenase; tryptophan peroxidase; indoleamine 2,3-dioxygenase (ambiguous); indolamine 2,3-dioxygenase (ambiguous); L-tryptophan pyrrolase; TDO; L-tryptophan 2,3-dioxygenase; L-tryptophan:oxygen 2,3-oxidoreductase (decyclizing). Enzyme Commission Number: EC 1.13.11.11. CAS No. 9014-51-1. 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-0531; tryptophan 2,3-dioxygenase; EC 1.13.11.11; 9014-51-1; tryptophan pyrrolase (ambiguous); tryptophanase; tryptophan oxygenase; tryptamine 2,3-dioxygenase; tryptophan peroxidase; indoleamine 2,3-dioxygenase (ambiguous); indolamine 2,3-dioxygenase (ambiguous); L-tryptophan pyrrolase; TDO; L-tryptophan 2,3-dioxygenase; L-tryptophan:oxygen 2,3-oxidoreductase (decyclizing). Cat No: EXWM-0531. | |
| TUG-770 | TUG-770 displayed excellent physicochemical and in vitro ADME properties, with good aqueous solubility, good chemical stability, low lipophilicity, and decreased plasma protein binding (PPB). TUG-770 furthermore showed excellent stability toward human liver microsomes (HLM), no inhibition of selected CYP-enzymes implicated in drug-drug interactions, no P-glycoprotein (P-gp) inhibition, and good permeability in the Caco-2 cell assay. Examination of TUG-770 in an acute intraperitoneal glucose tolerance test (IPGTT) in normal mice revealed a good dose dependent response with maximal reduction in glucose level reached at 50 mg/kg. The effect of TUG-770 was fully sustained after 29 days of daily oral treatment. Additional evaluation of TUG-770 in rats confirmed a significant glucose lowering effect for the high doses already after 10 min and for all doses after 30 min. Synonyms: TUG-770; TUG 770; TUG770. Grades: >98%. CAS No. 1402601-82-4. Molecular formula: C19H14FNO2. Mole weight: 307.32. | |
| YM-53601 | YM-53601 is a squalene synthase inhibitor with IC50s of 79 and 90 nM in HepG2 cells and rat liver microsomes, respectively. It is a lipid lowering agent that can reduce plasma cholesterol and triglyceride levels in vivo and inhibit cholesterol biosynthesis in rats (ED50 = 32 mg/kg). It is also an inhibitor of farnesyl-diphosphate farnesyltransferase 1 (FDFT1) enzyme activity and can inhibit the proliferation of HCV. Synonyms: 9H-Carbazole, 2-[(2E)-2-(1-azabicyclo[2.2.2]oct-3-ylidene)-2-fluoroethoxy]-, hydrochloride (1:1); (E)-3-[2-(Carbazol-2-yloxy)-1-fluoroethylidene]quinuclidine hydrochloride; 2-[(2E)-2-(1-azabicyclo[2.2.2]oct-3-ylidene)-2-fluoroethoxy]-9H-carbazole, monohydrochloride. Grades: ≥98%. CAS No. 182959-33-7. Molecular formula: C21H21FN2O.HCl. Mole weight: 372.86. | |
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