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| Product | Description | |
|---|---|---|
| acetylsalicylate deacetylase | Not identical with EC 3.1.1.1 (carboxylesterase), EC 3.1.1.2 (arylesterase), EC 3.1.1.7 (acetylcholinesterase) or EC 3.1.1.8 (cholinesterase). The activity of the liver cytosol enzyme is highest with acetyl esters of aryl alcohols, and thioesters are also hydrolysed; the microsomal enzyme also hydrolyses some other negatively charged esters, with highest activity on esters of salicylate with long-chain alcohols. Group: Enzymes. Synonyms: aspirin esterase; aspirin esterase; acetylsalicylic acid esterase; aspirin hydrolase. Enzyme Commission Number: EC 3.1.1.55. CAS No. 87348-04-7. 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-3483; acetylsalicylate deacetylase; EC 3.1.1.55; 87348-04-7; aspirin esterase; aspirin esterase; acetylsalicylic acid esterase; aspirin hydrolase. Cat No: EXWM-3483. |  |
| Alcohol dehydrogenase, Saccharomyces cerevisiae | Alcohol dehydrogenase, Saccharomyces cerevisiae is a dimeric protein in the cytosol of cells. Alcohol dehydrogenase, the key enzyme for alcohol consumption in the body, is the highest expressed in the liver and participates in the detoxification mechanism of environmental alcohol [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: EC 1.1.1.1. CAS No. 9031-72-5. Pack Sizes: 25 KU. Product ID: HY-P2740. |  |
| 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. | |
| argininosuccinate lyase | ASL (argininosuccinate lyase, also known as argininosuccinase) is an enzyme that catalyzes the reversible breakdown of argininosuccinate (ASA) producing the amino acid arginine and dicarboxylic acid fumarate. Located in liver cytosol, ASL is the fourth enzyme of the urea cycle and involved in the biosynthesis of arginine in all species and the production of urea in ureotelic species. Group: Enzymes. Synonyms: arginosuccinase; argininosuccinic acid lyase; arginine-succinate lyase; N-(L-argininosuccinate) arginine-lyase; ω-N-(L-arginino)succinate arginine-lyase; 2-(ω-N-L-arginino)succinate arginine-lyase (fumarate-forming). Enzyme Commission Number: EC 4.3.2.1. CAS No. 9027-34-3. 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-5296; argininosuccinate lyase; EC 4.3.2.1; 9027-34-3; arginosuccinase; argininosuccinic acid lyase; arginine-succinate lyase; N-(L-argininosuccinate) arginine-lyase; ω-N-(L-arginino)succinate arginine-lyase; 2-(ω-N-L-arginino)succinate arginine-lyase (fumarate-forming). Cat No: EXWM-5296. | |
| cytosol alanyl aminopeptidase | A puromycin-sensitive, Co2+-activated zinc-sialoglycoprotein that is generally cytosolic. Multiple forms are widely distributed in mammalian tissues and body fluids. In peptidase family M1 (membrane alanyl aminopeptidase family). Group: Enzymes. Synonyms: arylamidase; aminopolypeptidase; thiol-activated aminopeptidase; human liver aminopeptidase; puromycin-sensitive aminopeptidase; soluble alanyl aminopeptidase; cytosol aminopeptidase III; alanine aminopeptidase. Enzyme Commission Number: EC 3.4.11.14. CAS No. 243859-94-1. 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-4010; cytosol alanyl aminopeptidase; EC 3.4.11.14; 243859-94-1; arylamidase; aminopolypeptidase; thiol-activated aminopeptidase; human liver aminopeptidase; puromycin-sensitive aminopeptidase; soluble alanyl aminopeptidase; cytosol aminopeptidase III; alanine aminopeptidase. Cat No: EXWM-4010. | |
| 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 | |
| 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 Microorganism 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 d... 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. SDH. Mole weight: ca. 68,000; Subunit molecular weight : ca. 26,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Microorganism. 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-1909. | |
| 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 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. | |
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