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| Product | Description | |
|---|---|---|
| Urea Phosphate | Urea Phosphate. We stock inventory in warehouses throughout the United States, allowing us to serve customers in all regions in a timely and cost effective manner. |  California |
| Urea phosphate salt | Urea phosphate salt. Group: Biochemicals. Grades: Highly Purified. CAS No. 4861-19-2. Pack Sizes: 100g, 250g, 500g, 1kg, 2kg. Molecular Formula: CH4N2O·H3O4P. US Biological Life Sciences. |  Worldwide |
| Aspartate Aminotransferase from Human, Recombinant | GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.GOT1 Human Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-413 a.a.) and having a molecular mass of 48.4 kDa. The GOT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Aspartate transaminase; AST; aspartate aminotransferase; sgot AspAT; ASAT; AAT; serum glutamic oxaloac. Purity: Greater than 95.0% as determined by SDS-PAGE. AST. Activity: > 50 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 colorless solution. Source: E.coli. Species: Human. Aspartate transaminase; AST; aspartate aminotransferase; sgot AspAT; ASAT; AAT; serum glutamic oxaloacetic transaminase; SGOT; pyridoxal phosphate PLP-dependent transaminase enzyme; EC 2.6.1.1; 9000-97-9; Aspartate aminotransferase 1; Transaminase A; GIG18. Cat No: DIA-128. |  |
| carbamoyl-phosphate synthase (ammonia) | The enzyme catalyses the first committed step in the urea cycle. The reaction proceeds via three separate chemical reactions: phosphorylation of hydrogencarbonate to carboxyphosphate; a nucleophilic attack of ammonia on carboxyphosphate yielding carbamate; and the phosphorylation of carbamate forming carbamoyl phosphate. Two moles of ATP are utilized for the synthesis of one molecule of carbamyl phosphate, making the reaction essentially irreversible. The enzyme requires the allosteric activator N-acetyl-L-glutamate. cf. EC 6.3.5.5, carbamoyl-phosphate synthase (glutamine-hydrolysing). Group: Enzymes. Synonyms: carbon-dioxide-ammonia ligase; carbamoylphosphate synthase; carbamylphosphate synthetase; carbamoylphosphate synthase (ammonia); carbamoylphosphate synthetase; carbamylphosphate s. Enzyme Commission Number: EC 6.3.4.16. CAS No. 9026-23-7. 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-5785; carbamoyl-phosphate synthase (ammonia); EC 6.3.4.16; 9026-23-7; carbon-dioxide-ammonia ligase; carbamoylphosphate synthase; carbamylphosphate synthetase; carbamoylphosphate synthase (ammonia); carbamoylphosphate synthetase; carbamylphosphate synthetase I; CPSI (gene name); carbon-dioxide:ammonia ligase (ADP-forming, carbamate-phosphorylating). Cat No: EXWM-5785. | |
| Fobrepodacin | Fobrepodacin is an orally active and potent phosphate prodrug of SPR719 and has potent bactericidal activities in vivo. Synonyms: 2-(5-{2-[(ethylcarbamoyl)amino]-6-fluoro-7-[(2R)-oxolan-2-yl]-1H-benzimidazol-5-yl}pyrimidin-2-yl)propan-2-yl dihydrogen phosphate; N-Ethyl-N'-(6-fluoro-5-(2-(1-methyl-1-(phosphonooxy)ethyl)-5-pyrimidinyl)-7-((2R)-tetrahydro-2-furanyl)-1H-benzimidazol-2-yl)urea; SPR720; SPR-720; SPR 720; pVXc-486; pVXc 486; pVXc486; (R)-2-(5-(2-(3-ethylureido)-6-fluoro-7-(tetrahydrofuran-2-yl)-1H-benzo[d]imidazol-5-yl)pyrimidin-2-yl)propan-2-yl dihydrogen phosphate. Grades: ≥98%. CAS No. 1384984-31-9. Molecular formula: C21H26FN6O6P. Mole weight: 508.44. |  |
| GLPG2938 | GLPG2938 is an antagonists of sphingosine-1-phosphate (S1P) receptor for prophylaxis and?/or treatment of diseases including fibrotic, inflammatory, autoimmune, metabolic, cardiovascular, and?/or proliferative diseases. GLPG2938 displayed S1P inhibitory activity.with EC50 value of 9.5 nM (S1P2 antagonist EC50)?. Group: Antagonists. Alternative Names: MUN96006; MUN-96006; MUN 96006; GLPG2938; GLPG-2938; GLPG 2938. CAS No. 2130996-00-6. Molecular formula: C20H19F6N7O2. Mole weight: 503.41. Appearance: Solid powder. Purity: >98%. IUPACName: 1-(2-ethoxy-6-(trifluoromethyl)pyridin-4-yl)-3-((5-methyl-6-(1-methyl-3-(trifluoromethyl)-1H-pyrazol-4-yl)pyridazin-3-yl)methyl)urea. Canonical SMILES: O=C (NCC1=NN=C (C2=CN (C)N=C2C (F) (F)F)C (C)=C1)NC3=CC (OCC)=NC (C (F) (F)F)=C3. Catalog: ACM2130996006. |  |
| glutamate-5-semialdehyde dehydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating). Other names in common use include beta-glutamylphosphate reductase, gamma-glutamyl phosphate reductase, beta-glutamylphosphate reductase, glutamate semialdehyde dehydrogenase, and glutamate-gamma-semialdehyde dehydrogenase. This enzyme participates in urea cycle and metabolism of amino groups. Group: Enzymes. Synonyms: β-glutamylphosphate reductase; γ-glutamyl phosphate reductase; β-glutamylphosphate reductase; glutamate semialdehyde dehydrogenase; glutamate-γ-semialdehyde dehydrogenase. Enzyme Commission Number: EC 1.2.1.41. CAS No. 54596-29-1. 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-1145; glutamate-5-semialdehyde dehydrogenase; EC 1.2.1.41; 54596-29-1; β-glutamylphosphate reductase; γ-glutamyl phosphate reductase; β-glutamylphosphate reductase; glutamate semialdehyde dehydrogenase; glutamate-γ-semialdehyde dehydrogenase. Cat No: EXWM-1145. | |
| glutamate dehydrogenase (NADP+) | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. Group: Enzymes. Synonyms: glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP). Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. 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-1459; glutamate dehydrogenase (NADP+); EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP). Cat No: EXWM-1459. | |
| Glutamate Dehydrogenase (NAD(P)) from E.coli, Recombinant | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Applications: Use recombinant glutamate dehydrogenase in diagnostic tests for the determination of ammonia, urea, l-glutamate, glutamate pyruvate transaminase and leucine aminopeptidase. Group: Enzymes. Synonyms: glu. CAS No. 9029-12-3. GLDH. Mole weight: ~2 200 kD for the associated enzyme with 8 subunits; 280 kD for one subunit. Activity: >80 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White lyophilizate. Source: E.coli. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: NATE-0981. | |
| JTE-013 | JTE-013 is a potent and selective sphingosine-1-phosphate (S1P) receptor 2 (S1P2) antagonist (IC50=17.6 nM). Synonyms: 1-(2,6-dichloropyridin-4-yl)-3-[(1,3-dimethyl-4-propan-2-ylpyrazolo[3,4-b]pyridin-6-yl)amino]urea; JTE-013; JTE 013; JTE013. Grades: >98%. CAS No. 383150-41-2. Molecular formula: C17H19Cl2N7O. Mole weight: 408.287. | |
| L-Citrulline | L-Citrulline is a non-essential amino acid that is synthesized from ornithine and carbamoyl phosphate in the urea cycle. It is first isolated from watermelon. It can act as a nitric oxide synthase inhibitor. Nutritional supplement in health care products. Uses: Ingredient of health care products. Synonyms: Citrulline; H-Cit-OH; Delta-Ureidonorvaline; Sitrulline; (2S)-2-amino-5-(carbamoylamino)pentanoic acid. Grades: 98%. CAS No. 372-75-8. Molecular formula: C6H13N3O3. Mole weight: 175.19. | |
| N-acetyl-γ-glutamyl-phosphate reductase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in urea cycle and metabolism of amino groups. Group: Enzymes. Synonyms: reductase, acetyl-γ-glutamyl phosphate; N-acetylglutamate 5-semialdehyde dehydrogenase; N-acetylglutamic γ-semialdehyde dehydrogenase; N-acetyl-L-glutamate γ-semialdehyde:NADP+ oxidoreductase (phosphorylating). Enzyme Commission Number: EC 1.2.1.38. CAS No. 37251-00-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1142; N-acetyl-γ-glutamyl-phosphate reductase; EC 1.2.1.38; 37251-00-6; reductase, acetyl-γ-glutamyl phosphate; N-acetylglutamate 5-semialdehyde dehydrogenase; N-acetylglutamic γ-semialdehyde dehydrogenase; N-acetyl-L-glutamate γ-semialdehyde:NADP+ oxidoreductase (phosphorylating). Cat No: EXWM-1142. | |
| N-Acetyl-L-Glutamic acid | N-Acety-L-Glutamic acid is a biologically active compound that is found in the cells. It is a product of the urea cycle and has been shown to inhibit the activity of enzymes such as ester hydrochloride synthetase, which catalyzes the conversion of arginine and citrulline to ornithine and carbamoyl phosphate. N-Acetylglutamic acid also plays an important role in cellular physiology, such as transcriptional regulation and protein synthesis. Deficiency can lead to glutamate accumulation and neurological disorders such as epilepsy. The biochemical properties of N-acetylglutamic acid are still not well known, but it has been shown to react with ammonia to form glutamine. CAS No. 1188-37-0. Product ID: PAP-0020. Molecular formula: C7H11NO5. Category: Amino acid. Product Keywords: Amino Acid Series; N-Acetyl-L-Glutamic acid; PAP-0020; Amino acid; C7H11NO5; 1188-37-0. Color: White. EC Number: 214-708-4. Physical State: Solid. Solubility: 36g/l (Lit.). Storage: 2-8°C. Applications: N-Acetyl-L-Glutamic acid is a product of the urea cycle and has been shown to inhibit the activity of enzymes such as ester hydrochloride synthetase, which catalyzes the conversion of arginine and citrulline to ornithine and carbamoyl phosphate. N-Acetylglutamic acid also plays an important role in cellular physiology, such as transcriptional regulation and protein synthesis. Deficiency can lead to glutamate accumulation and neurological |  |
| Native Baker's yeast (S. cerevisiae) Triosephosphate Isomerase | Triose-phosphate isomerase (TPI or TIM) is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. Applications: Triosephosphate isomerase has been used in a study to assess differential expression of fourteen proteins of uveal melanoma. triosephosphate isomerase has also been used in a study to investigate the use of sigmoid ph gradients in free-flow isoelectric f ocusing of human endothelial cell proteins. Group: Enzymes. Synonyms: Triose-. Enzyme Commission Number: EC 5.3.1.1. CAS No. 9023-78-3. TPI. Activity: ~10,000 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension; Crystalline suspension in 2.7 M (NH4)2SO4, 0.5 mM EDTA, pH 6.5. Source: Baker's yeast (S. cerevisiae). Triose-phosphate isomerase; phosphotriose isomerase; triose phosphoisomerase; triose phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3. Cat No: NATE-0711. | |
| Native Glutamate dehydrogenase (NADP+) from Yeast | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Group: Enzymes. Synonyms: glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate d. Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. Activity: > 10 U/mg protein. Storage: Below -20°C. Form: Lyophilized Powder. Source: Yeast. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: NATE-1037. | |
| Native Human Aspartate Aminotransferase | Aspartate Aminotransferase (AST), also known as Glutamate Oxaloacetate Transaminase (GOT), is a pyridoxal phosphate-dependant enzyme which exists in two isoenzymes; mitochondrial and cytosolic forms. The AST enzyme plays an important role in amino acid metabolism and in the urea and tricarboxylic acid cycles. In liver about 80% of the enzyme activity is mitochondrial in origin, whereas in serum the enzyme activity is largely cytosolic. In hepatic disease, serum levels are used to assess liver necrosis and for determining prognosis. In patients with acute Myocardial infarction, measurement of AST isoenzymes provides diagnostic information that differs from that obtained by determination of other marker proteins. Creative Enzymes products are not intended for use in pharmaceutical applications. Applications: Research life science elisa assay clinical chemistry. 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 aminotransferas. Enzyme Commission Number: EC 2.6.1.1. CAS No. 9000-97-9. AST. Activity: >50U/ml. Storage: -20°C. Source: Human Cardiac Tissue. Species: Human. EC 2.6.1.1; glutamic-oxaloa | |
| Native Proteus sp. Glutamate Dehydrogenase (NADP-dependent) | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Applications: This enzyme is useful for enzymatic determination of nh3, α-ketoglutaric acid and l-glutamic acid, and for assay of leucine aminopeptidase and urea...lutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Enzyme Commission Number: EC 1.4.1.4. Mole weight: approx. 300 kDa. Activity: 300U/mg-protein or more (9,000U/ml or more). Appearance: Solution with 50mM Tris-HCl buffer containing 0.05% NaN3 and 5.0mM EDTA, pH 7.8. Form: Freeze dried powder. Source: Proteus sp. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: DIA-196. | |
| Native Proteus sp. L-Glutamic Dehydrogenase (NADP) | L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate. Applications: This enzyme is useful for enzymatic determination of nh3, α-ketoglutaric acid and l-glutamic acid, and for assay of leucine aminopeptidase and urease. this enzyme is also used for enzymatic determination of urea when coupled with urease (urh-201) in clinical analysis. Group: Enzymes. Synonyms: L-Glutamic Dehydrogenase; EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD (P)-glutamate dehydrogenase; NAD (P)H-dependent glutamate de. Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. Mole weight: mol wt ~300 kDa. Activity: > 400 units/mg protein (biuret). Storage: 2-8°C. Form: buffered aqueous solution; Solution in 50 mM Tris HCl, pH 7.8, 5 mM Na2EDTA containing 0.05% sodium azide. Source: Proteus sp. L-Glutamic Dehydrogenase; EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD (P)-glutamate dehydrogenase; NAD (P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP). Cat No: NATE-0395. | |
| Native Rabbit Triosephosphate Isomerase | Triose-phosphate isomerase (TPI or TIM) is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. Applications: Triosephosphate isomerase has been used in a study to assess molecular characterizations of cryptosporidium, giardia, and enter ...e phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3. Enzyme Commission Number: EC 5.3.1.1. CAS No. 9023-78-3. TPI. Activity: Type I, > 4,000 units/mg protein; Type II, > 3,500 units/mg protein. Storage: -20°C. Form: Type I, ammonium sulfate suspension; Crystalline suspension in 3.2 M (NH4)2SO4 solution, pH 6.0; Type II, lyophilized powder, Sulfate-free, contains EDTA and borate buffer salts. Source: Rabbit muscle. Species: Rabbit. Triose-phosphate isomerase; phosphotriose isomerase; triose phosphoisomerase; triose phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3. Cat No: NATE-0712. | |
| Native Streptococcus faecalis Ornithine Transcarbamylase | Ornithine transcarbamylase (OTC) is an enzyme that catalyzes the reaction between carbamoyl phosphate (CP) and ornithine (Orn) to form citrulline (Cit) and phosphate (Pi). In plants and microbes, OTC is involved in arginine (Arg) biosynthesis, whereas in mammals it is located in the mitochondria and is part of the urea cycle. Group: Enzymes. Synonyms: Ornithine transcarbamylase; EC 2.1.3.3; citrulline phosphorylase; ornithine transcarbamylase; OTC; OTCase; carbamylphosphate-ornithine transcarbamylase; L-ornithine carbamoyltransferase; L-ornithine carbamyltransferase; L-ornithine transcarbamylase; ornithine carbamyltransferase; 9001-69-8. Enzyme Commission Number: EC 2.1.3.3. CAS No. 9001-69-8. OTC. Activity: > 600 units/mg protein. Storage: -20°C. Form: Lyophilized powder contains Tris buffer salts. Source: Streptococcus faecalis. Ornithine transcarbamylase; EC 2.1.3.3; citrulline phosphorylase; ornithine transcarbamylase; OTC; OTCase; carbamylphosphate-ornithine transcarbamylase; L-ornithine carbamoyltransferase; L-ornithine carbamyltransferase; L-ornithine transcarbamylase; ornithine carbamyltransferase; 9001-69-8. Cat No: NATE-0499. | |
| 1-(3,5-Dichloropyridin-4-yl)-3-[(1,3-dimethyl-4-propylpyrazolo[3,4-b]pyridin-6-yl)amino]urea | JTE 013 has been found to be an antagonist of Sphingosine-1-Phosphate Receptor-2 (S1P2R). Synonyms: JTE 013; JTE013; JTE-013; 1-[1,3-Dimethyl-4-(2-methylethyl)-1H-pyrazolo[3,4-b]pyridin-6-yl]-4-(3,5-dichloro-4-pyridinyl)-semicarbazide; N-(2,6-Dichloro-4-pyridinyl)-2-[1,3-dimethyl-4-(1-methylethyl)-1H-pyrazolo[3,4-b]pyridin-6-yl]hydrazinecarboxamide. Grades: ≥98% by HPLC. CAS No. 547756-93-4. Molecular formula: C17H19N7OCl2. Mole weight: 408.29. | |
| Suramin | Suramin, also called as Germanin, has been demonstrated to inhibit a large variety of enzymes including urease, hexokinase, succinic dehydrogenase, p-glucuronidase, acid phosphatase, lysozyme, thrombin, plasma kallikrein, (Na'-K')-activated ATPase, plasmi. Uses: Antineoplastic agents. Synonyms: suramin; Germanin; Naganol; Naphuride; Belganyl; Suramine. Grades: 95%. CAS No. 145-63-1. Molecular formula: C51H40N6O23S6. Mole weight: 1297.29. | |
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