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| Product | Description | |
|---|---|---|
| glutamate dehydrogenase | 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; glutamate dehydrogenase (NAD); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD-dependent glutamate dehydrogenase; NAD-dependent glutamic dehydrogenase; NAD-glutamate dehydrogenase; NAD-linked glutamate dehydrogenase; NAD-linked glutamic dehydrogenase; NAD-specific glutamic dehydrogenase; NAD-specific glutamate dehydrogenase; N. Enzyme Commission Number: EC 1.4.1.2. CAS No. 9001-46-1. 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-1453; glutamate dehydrogenase; EC 1.4.1.2; 9001-46-1; glutamic dehydrogenase; glutamate dehydrogenase (NAD); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD-dependent glutamate dehydrogenase; NAD-dependent glutamic dehydrogenase; NAD-glutamate dehydrogenase; NAD-linked glutamate dehydrogenase; NAD-linked glutamic dehydrogenase; NAD-specific glutamic dehydrogenase; NAD-specific glutamate dehydrogenase; NAD:glutamate oxidoreductase; NADH-linked glutamate dehydrogenase. Cat No: EXWM-1453. |  |
| Glutamate dehydrogenase | Glutamate dehydrogenase. Group: Biochemicals. Grades: Highly Purified. CAS No. 9029-12-3. Pack Sizes: 25g. US Biological Life Sciences. |  Worldwide |
| Glutamate dehydrogenase | Glutamate dehydrogenase is an enzyme in both prokaryotes and eukaryotic mitochondria. Glutamate dehydrogenase can be used for the enzymatic determination of ammonia, alpha-ketoglutaric acid, L-glutamate and urease [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9001-46-1. Pack Sizes: 1 KU. Product ID: HY-E70003. |  |
| Glutamate Dehydrogenase from Thermophilic Bacterium, recombinant | GDH is an oxidoreductase enzyme which relates carbon and nitrogen metabolism. It catalyzes the reduction of α-ketoglutarate and ammonia to L-glutamate and vice versa. This enzyme is a robust and ideal candidate for research use, and industrial applications in the diagnostics and food industries. Group: Enzymes. Synonyms: glutamate dehydrogenase; glutamic dehydrogenase; glutamate dehydrogenase (NAD+); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD+-dependent glutamate dehydrogenase; NAD+-dependent glutamic dehyd. Enzyme Commission Number: EC 1.4.1.2. CAS No. 9001-46-1. GLDH. Mole weight: 270 kDa; Homohexameric ( 45 kDa per subunit). Activity: > 90 U/mg protein. Storage: at -20 °C. Form: Lyophilized powder. Source: E. coli. Species: Thermophilic Bacterium. glutamate dehydrogenase; glutamic dehydrogenase; glutamate dehydrogenase (NAD+); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD+-dependent glutamate dehydrogenase; NAD+-dependent glutamic dehydrogenase; NAD+-glutamate dehydrogenase; NAD+-linked glutamate dehydrogenase; NAD+-linked glutamic dehydrogenase; NAD+-specific glutamic dehydrogenase; NAD+-specific glutamate dehydrogenase; NAD+:glutamate oxidoreductase; NADH-linked glutamate dehydrogenase; GLDH; EC 1.4.1.2. Cat No: NATE-1701. | |
| 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)+] | 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; glutamate dehydrogenase [NAD(P)]. Enzyme Commission Number: EC 1.4.1.3. CAS No. 9029-12-3. 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-1458; glutamate dehydrogenase [NAD(P)+]; EC 1.4.1.3; 9029-12-3; glutamic dehydrogenase; glutamate dehydrogenase [NAD(P)]. Cat No: EXWM-1458. | |
| Glutamate dehydrogenase (NAD(P)) | Glutamate dehydrogenase NAD(P) (GLDH) can be found in hepatocytes, renal tissue, brain, muscle, and intestinal cells. Glutamate dehydrogenase NAD(P) is often used in biochemical studies. Glutamate dehydrogenase is a mitochondrial enzyme, it catalyzes the reversible oxidative deamination of glutamate to α-ketoglutarate (α-KG) as part of the urea cycle [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: GLDH. CAS No. 9029-12-3. Pack Sizes: 5 KU; 10 KU. Product ID: HY-P2911. | |
| 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. | |
| Glutamate dehydrogenase, 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. Glutamate dehydrogenase (gldh, ec 1.4.1.2) is the enzyme present in the mitochondrial matrix of the cell. it can convert glutamic acid to α-ketoglutarate and catalyze the re...ations: Except glutamate dehydrogenation, gldh can also catalytic the deaminase of other amino acids such as l-valine, l-2-aminobutyric acid and l-leucine. the main measuring method is continuous monitoring. moreover, gldh catalyzes the reaction of α-ketoglutarate, h+,ammonia and nadh to generating glutamic. since nadh is the color source of many biochemical assays, therefore the reaction catalyzed by the corresponding gldh is widely used to detect the final step of biochemical detection reagent. Group: Enzymes. Synonyms: glutamate dehydrogenase; glutamic dehydrogenase; glutamate dehydrogenase (NAD+); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate | |
| 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. | |
| L-Glutamate Dehydrogenase (Crude Enzyme) | 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 theurea 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. Glutamate dehydrogenase also has a very low affinity for ammonia (high Michaelis constant of about 1 mM), and therefore toxic levels of ammonia would have to be present in the bo...; diagnostics. Group: Enzymes. Synonyms: glutamic dehydrogenase; glutamate dehydrogenase (NAD); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD-dependent glutamate dehydrogenase; NAD-dependent glutamic dehydrogenase; NAD-glutamate dehydrogenase; NAD-linked glutamate dehydrogenase; NAD-linked glutamic dehydrogenase; NAD-specific glutamic dehydrogenase; NAD-specific glutamate dehydrogenase; NAD:glutamate oxidoreductase; NADH-linked glutamate dehydrogenase. Enzyme Commission Number: EC 1.4.1.2. CAS No. 9001-46-1. GLDH. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 mo | |
| L-glutamate γ-semialdehyde dehydrogenase | This enzyme catalyses the irreversible oxidation of glutamate-γ-semialdehyde to glutamate as part of the proline degradation pathway. (S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2, proline dehydrogenase) is in spontaneous equilibrium with its tautomer L-glutamate γ-semialdehyde. In many bacterial species, both activities are carried out by a single bifunctional enzyme.The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1-pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)-1-pyrroline-5-carboxylate is converted into D-glutamate. NADP+ can also act as acceptor, but with lower activity. Group: Enzymes. Synonyms: 1-pyrroline-5-carbo. Enzyme Commission Number: EC 1.2.1.88. CAS No. 9054-82-4. 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-1191; L-glutamate γ-semialdehyde dehydrogenase; EC 1.2.1.88; 9054-82-4; 1-pyrroline-5-carboxylate dehydrogenase; Δ1-pyrroline-5-carboxylate dehydrogenase; 1-pyrroline dehydrogenase; pyrroline-5-carboxylate dehydrogenase; pyrroline-5-carboxylic acid dehydrogenase; L-pyrroline-5-carboxylate-NAD+ oxidoreductase; 1-pyrroline-5-carboxylate:NAD+ oxidoreductase; Δ1-pyrroline-5-carboxylic acid dehydrogenase. Cat No: EXWM-1191. | |
| methylglutamate dehydrogenase | A number of N-methyl-substituted amino acids can act as donor; 2,6-dichloroindophenol is the best acceptor. Group: Enzymes. Synonyms: N-methylglutamate dehydrogenase; N-methyl-L-glutamate:(acceptor) oxidoreductase (demethylating). Enzyme Commission Number: EC 1.5.99.5. CAS No. 37217-26-8. 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-1572; methylglutamate dehydrogenase; EC 1.5.99.5; 37217-26-8; N-methylglutamate dehydrogenase; N-methyl-L-glutamate:(acceptor) oxidoreductase (demethylating). Cat No: EXWM-1572. | |
| Native Bovine Glutamate Dehydrogenase | 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 [NAD(P)+]; EC 1.4.1.3; GLDH; glutamic dehydrogenase; glutamate dehydrogenase [NAD(P)]; L-glutamate: NAD(P)+ oxidoreductase (deaminating); L-GLDH; Glutamate Dehydrogenase from bovine liver; L-Glutamic Dehydrogenase; glutamate dehydrogenase. Enzyme Commission Number: EC 1.4.1.3. CAS No. 9001-46-1. GLDH. Mole weight: 260 kDa (gel). Activity: > 500U /mg protein. Appearance: White/off white powder. Storage: -20°C. Form: Freeze dried powder. Source: Bovine liver. Species: Bovine. glutamate dehydrogenase [NAD(P)+]; EC 1.4.1.3; GLDH; glutamic dehydrogenase; glutamate dehydrogenase [NAD(P)]; L-glutamate: NAD(P)+ oxidoreductase (deaminating); L-GLDH; Glutamate Dehydrogenase from bovine liver; L-Glutamic Dehydrogenase; glutamate dehydrogenase. Cat No: DIA-146. | |
| 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 Microorganism Glutamate Dehydrogenase (NAD-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...ating); EC 1.4.1.2; GLDH. Enzyme Commission Number: EC 1.4.1.2. CAS No. 9001-46-1. Mole weight: approx. 260 kDa. Activity: 100 U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Glutamate Dehydrogenase; glutamic dehydrogenase; glutamate dehydrogenase (NAD); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD-dependent glutamate dehydrogenase; NAD-dependent glutamic dehydrogenase; NAD-glutamate dehydrogenase; NAD-linked glutamate dehydrogenase; NAD-linked glutamic dehydrogenase; NAD-specific glutamic dehydrogenase; NAD-specific glutamate dehydrogenase; NAD: gluta | |
| 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. | |
| saccharopine dehydrogenase (NAD+, L-glutamate-forming) | The activities of this enzyme along with EC 1.5.1.8, saccharopine dehydrogenase (NADP+, L-lysine-forming), occur on a single protein. Group: Enzymes. Synonyms: dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, glutamate-forming); saccharopin dehydrogenase; NAD+ oxidoreductase (L-2-aminoadipic-Δ-semialdehyde and glutamate forming); aminoadipic semialdehyde synthase; 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-glutamate-forming). Enzyme Commission Number: EC 1.5.1.9. CAS No. 37256-26-1. 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-1536; saccharopine dehydrogenase (NAD+, L-glutamate-forming); EC 1.5.1.9; 37256-26-1; dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, glutamate-forming); saccharopin dehydrogenase; NAD+ oxidoreductase (L-2-aminoadipic-Δ-semialdehyde and glutamate forming); aminoadipic semialdehyde synthase; 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-glutamate-forming). Cat No: EXWM-1536. | |
| saccharopine dehydrogenase (NADP+, L-glutamate-forming) | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in lysine biosynthesis and lysine degradation. Group: Enzymes. Synonyms: saccharopine (nicotinamide adenine dinucleotide phosphate, glutamate-forming) dehydrogenase; aminoadipic semialdehyde-glutamic reductase; aminoadipate semialdehyde-glutamate reductase; aminoadipic semialdehyde-glutamate reductase; ε-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase (L-2-aminoadipate-semialdehyde forming); saccharopine reductase; 6-N-(L-1,3-dicar. Enzyme Commission Number: EC 1.5.1.10. CAS No. 9033-55-0. 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-1494; saccharopine dehydrogenase (NADP+, L-glutamate-forming); EC 1.5.1.10; 9033-55-0; saccharopine (nicotinamide adenine dinucleotide phosphate, glutamate-forming) dehydrogenase; aminoadipic semialdehyde-glutamic reductase; aminoadipate semialdehyde-glutamate reductase; aminoadipic semialdehyde-glutamate reductase; ε-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase (L-2-aminoadipate-semialdehyde forming); saccharopine reductase; 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-glutamate-forming). Cat No: EXWM-1494. | |
| succinylglutamate-semialdehyde dehydrogenase | This is the fourth enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.11 (acetylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase). Group: Enzymes. Synonyms: succinylglutamic semialdehyde dehydrogenase; N-succinylglutamate 5-semialdehyde dehydrogenase; SGSD; AruD; AstD. Enzyme Commission Number: EC 1.2.1.71. 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-1173; succinylglutamate-semialdehyde dehydrogenase; EC 1.2.1.71; succinylglutamic semialdehyde dehydrogenase; N-succinylglutamate 5-semialdehyde dehydrogenase; SGSD; AruD; AstD. Cat No: EXWM-1173. | |
| 2-Ketoglutaric Acid-d2 Cacium Salt (d3 major) | 2-Ketoglutaric Acid-d2 Cacium Salt is a isotope labelled derivative of glutaric acid and is an intermediate in the krebs cycle catalyzed by glutamate dehydrogenase enzyme on glutamate. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 5mg, 25mg. Molecular Formula: C5H2D2CaO5. US Biological Life Sciences. | Worldwide |
| 3-Acetylpyridine-adenine dinucleotide phosphate, reduced form, tetrasodium salt (APADPH) | Molecular Formula: C22H32N6O17P3. Group: Coenzymes. Synonyms: APADPH. Enzyme Commission Number: EC 1.1.1.1. Purity: > 92% when determined by enzymatic analysis with glutamate dehydrogenase at pH 7.5. APADPH. Mole weight: 745.45 (as anhydrous free acid) 886.41 (APADPH.Na4.3H2O). Storage: Keep tightly stoppered in the dark below 5°C. Moisture will accelerate the purity reduction. For prolonged storage keep below - 20°C. APADPH. Cat No: NATE-0080. | |
| Adaptaquin | Adaptaquin is an inhibitor of hypoxia-inducible factor (HIF) prolyl hydroxylase 2 (PHD2) with IC50 value of 2 μM in a reporter assay using SH-SY5Y-ODD-Luc cells. It displays neuroprotective effects and enhances functional recovery in rodent intracerebral hemorrhage models by inhibition of ATF4 dependent genes. It reduces neuronal death and behavioral deficits after intracerebral hemorrhage (ICH) in several rodent models. It blocks glutamate induced ROS production in HT-22 cells, independent of MnSOD. It stabilizes HIF-1α protein and induces expression of the HIF1-regulated genes EPO and VEGF in SH-SY5Y human neuroblastoma cells. It is used in ischemic injury research, renal anemia, and used as an antioxidant. It is also used in pyruvate dehydrogenase (PDH) related research. Synonyms: 7-[(4-Chlorophenyl)[(3-hydroxy-2-pyridinyl)amino]methyl]-8-quinolinol. Grades: ≥97% by HPLC. CAS No. 385786-48-1. Molecular formula: C21H16ClN3O2. Mole weight: 377.82. |  |
| Adenosine 5'-diphosphate Disodium salt | Adenosine 5'-diphosphate (ADP) is used in the determination of creatine kinase, glutamate dehydrogenase, urea and ammonia. Group: Coenzymes. Synonyms: Adenosine 5'-diphosphate; ADP; Adenosine 5'-diphosphate Disodium salt; ADP Disodium salt; ADP-Na2. Mole weight: 507.2. Storage: Store at -20° C. Form: Crystalline powder. Adenosine 5'-diphosphate; ADP; Adenosine 5'-diphosphate Disodium salt; ADP Disodium salt; ADP-Na2. Cat No: COEC-120. | |
| arginine N-succinyltransferase | Also acts on L-ornithine. This is the first enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.81 (succinylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase). Group: Enzymes. Synonyms: arginine succinyltransferase; AstA; arginine and ornithine N2-succinyltransferase; AOST; AST; succinyl-CoA:L-arginine 2-N-succinyltransferase. Enzyme Commission Number: EC 2.3.1.109. CAS No. 99676-48-9. 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-2047; arginine N-succinyltransferase; EC 2.3.1.109; 99676-48-9; arginine succinyltransferase; AstA; arginine and ornithine N2-succinyltransferase; AOST; AST; succinyl-CoA:L-arginine 2-N-succinyltransferase. Cat No: EXWM-2047. | |
| Chemically modified Porcine L-Lactate Dehydrogenase | Dehydrogenase that catalyzes the interconversion of L(+)-lactate to pyruvate. Take advantage of the enhanced liquid stability of this enzyme. Rely on the proven diagnostic quality of this product. Applications: Use l-lactate dehydrogenase (l-ldh), chemically modified, in a variety of diagnostic tests for the removal of pyruvate in determinations working with nadh (i.e., triglycerides, lipase, aldolase, aminotransferases, glutamate dehydrogenase). Group: Enzymes. Synonyms: lactic acid dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; L-lactate dehydrogenase; L-LDH; LAD; LD; Lactate. LDH. Activity: >25 U/mg lyophilizate; >150 U/mg protein. Stability: At +2 to +8°C within specification range for 12 months. Appearance: White lyophilizate. Source: Porcine heart. Species: Porcine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: DIA-279. | |
| D-Amino Acid Oxidase (Crude Enzyme) | D-Amino Acid Oxidase (DAAO; also DAO, OXDA, DAMOX) is a peroxisomal enzyme containing FAD as cofactor that is expressed in a wide range of species from yeasts to human. It is not present in plants or in bacteria which instead use D-amino acid dehydrogenase. Its function is to oxidize D-amino acids to the corresponding imino acids, producing ammonia and hydrogen peroxide. DAAO is a candidate susceptibility gene and together with G72 may play a role in the glutamatergic mechanisms of schizophrenia. Risperidone andsodium benzoate are inhibitors of DAAO. DAAO is used as a biocatalyst in several biotechnological applications, such as the oxidation of cephalosporin C, the deracem...n may use the morpheein model of allosteric regulation. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Biotechnology; industry; drug development; medicine; pharmacology; analysis; diagnostics; synthesis. Group: Enzymes. Synonyms: ophio-amino-acid oxidase; L-amino acid:O 2 oxidoreductase; new yellow enzyme. Enzyme Commission Number: EC 1.4.3.3. CAS No. 9000-88-8. DAAO. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. ophio-amino-acid oxidase; L-amino acid:O 2 oxidoreductase; new yellow enzyme. Pack: 100ml. Cat No: NATE-1807. | |
| D-arginine dehydrogenase | Contains a non-covalent FAD cofactor. The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, is a catabolic enzyme that is part of a two-enzyme complex involved in the racemization of D and L-arginine. The enzyme has a broad substrate range and can act on most D-amino acids with the exception of D-glutamate and D-aspartate. However, activity is maximal with D-arginine and D-lysine. Not active on glycine. Group: Enzymes. Synonyms: D-amino-acid:(acceptor) oxidoreductase (deaminating); D-amino-acid dehydrogenase; D-amino-acid:acceptor oxidoreductase (deaminating). Enzyme Commission Number: EC 1.4.99.6. CAS No. 37205-44-0. 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-1492; D-arginine dehydrogenase; EC 1.4.99.6; 37205-44-0; D-amino-acid:(acceptor) oxidoreductase (deaminating); D-amino-acid dehydrogenase; D-amino-acid:acceptor oxidoreductase (deaminating). Cat No: EXWM-1492. | |
| (-)-Epigallocatechin Gallate | (-)-Epigallocatechin Gallate (EGCG) is a major polyphenol in green tea, which can inhibit cell proliferation and induce cell apoptosis. (-)-Epigallocatechin Gallate inhibits glutamate dehydrogenase 1/2 (GDH1/2, GLUD1/2) activity. (-)-Epigallocatechin Gallate has a potent anticancer, antioxidant and anti-inflammatory properties against various types of cancers such as colorectal cancer, myeloid leukemia, thyroid carcinoma [1] [2] [3] [4]. Uses: Scientific research. Group: Natural products. Alternative Names: EGCG; Epigallocatechol Gallate. CAS No. 989-51-5. Pack Sizes: 10 mM * 1 mL; 50 mg; 100 mg. Product ID: HY-13653. | |
| Etiroxate Carboxylic Acid | Thyroxin derivative inhibiting glutamate dehydrogenase, isocitrate dehydrogenase, alcohol dehydrogenase, rat liver mitochondrial phosphorylation and electron transfer. Administration also induces hypothyroid state. Group: Biochemicals. Alternative Names: O-(4-Hydroxy-3,5-diiodophenyl)-3,5-diiodo-α-methyl-tyrosine; α-Methyl-DL-thyroxine. Grades: Highly Purified. CAS No. 3414-34-4. Pack Sizes: 25mg. US Biological Life Sciences. | Worldwide |
| glutamate synthase (NADPH) | Binds FMN, FAD, 2 [4Fe-4S] clusters and 1 [3Fe-4S] cluster. The reaction takes place in the opposite direction to that shown. The protein is composed of two subunits, α and &beta. The α subunit is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.4, glutamate dehydrogenase [NADP+]). The β subunit transfers electrons to the cosubstrate. The NH3 is channeled through a 31 ? channel in the active protein. In the absence of the β subunit, coupling between the two domains of the α subunit...mmission Number: EC 1.4.1.13. CAS No. 37213-53-9. 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-1446; glutamate synthase (NADPH); EC 1.4.1.13; 37213-53-9; glutamate (reduced nicotinamide adenine dinucleotide phosphate) synthase; L-glutamate synthase; L-glutamate synthetase; glutamate synthetase (NADP); NADPH-dependent glutamate synthase; glutamine-ketoglutaric aminotransferase; NADPH-glutamate synthase; NADPH-linked glutamate synthase; glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP); L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing; GOGAT. Cat No: EXWM-1446. | |
| Glutamine Metabolism Compound Library | A unique collection of 455 glutamine metabolism related compounds can be used for high throughput screening (HTS) and high content screening (HCS), and also is an effective tool for research in glutamine metabolism and cancer; - Targets include glutaminase?GLS??ASCT2?glutamate dehydrogenase?c-Myc, etc. - Some compounds have been approved by the FDA; - Structurally diverse, medicinally active, and cell permeable; - Detailed compound information with structure, target, IC50 value, and bioactivity information; - NMR and HPLC/LCMS validated to ensure high purity. Uses: Scientific use. Product Category: L2550. Categories: Glutamine Metabolism Compounds Libraries. |  |
| glutathione dehydrogenase (ascorbate) | This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a quinone or similar compound as acceptor. This enzyme participates in 3 metabolic pathways: ascorbate and aldarate metabolism, glutamate metabolism, and glutathione metabolism. Group: Enzymes. Synonyms: dehydroascorbic reductase; dehydroascorbic acid reductase; glutathione dehydroascorbate reductase; DHA reductase dehydroascorbate reductase; GDOR; glutathione:dehydroascorbic acid oxidoreductase. Enzyme Commission Number: EC 1.8.5.1. CAS No. 9026-38-4. 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-1676; glutathione dehydrogenase (ascorbate); EC 1.8.5.1; 9026-38-4; dehydroascorbic reductase; dehydroascorbic acid reductase; glutathione dehydroascorbate reductase; DHA reductase dehydroascorbate reductase; GDOR; glutathione:dehydroascorbic acid oxidoreductase. Cat No: EXWM-1676. | |
| isocitrate-homoisocitrate dehydrogenase | Requires Mn2+ and K+ or NH4+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+) and EC 1.1.1.87, homoisocitrate dehydrogenase, this enzyme, from Pyrococcus horikoshii, can use both isocitrate and homoisocitrate as substrates. The enzyme may play a role in both the lysine and glutamate biosynthesis pathways. Group: Enzymes. Synonyms: homoisocitrate-isocitrate dehydrogenase; PH1722. Enzyme Commission Number: EC 1.1.1.286. 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-0194; isocitrate-homoisocitrate dehydrogenase; EC 1.1.1.286; homoisocitrate-isocitrate dehydrogenase; PH1722. Cat No: EXWM-0194. | |
| L-glutamate oxidase | A flavoprotein (FAD).The enzyme from Azotobacter previously listed under this number, which did not produce H2O2, was a crude cell-free extract that probably contained catalase. Group: Enzymes. Synonyms: glutamate (acceptor) dehydrogenase; glutamate oxidase; glutamic acid oxidase; glutamic dehydrogenase (acceptor); L-glutamic acid oxidase. Enzyme Commission Number: EC 1.4.3.11. CAS No. 39346-34-4. L-Glutamate Oxidase. 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-1467; L-glutamate oxidase; EC 1.4.3.11; 39346-34-4; glutamate (acceptor) dehydrogenase; glutamate oxidase; glutamic acid oxidase; glutamic dehydrogenase (acceptor); L-glutamic acid oxidase. Cat No: EXWM-1467. | |
| L-Glutamate Oxidase (Crude Enzyme) | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH 2 group of donors with oxygen as acceptor. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Analysis; food industry; medicine; biotechnology. Group: Enzymes. Synonyms: glutamate (acceptor) dehydrogenase; glutamate oxidase; glutamic acid oxidase; glutamic dehydrogenase (acceptor); L-glutamic acid oxidase. Enzyme Commission Number: EC 1.4.3.11. CAS No. 39346-34-4. L-Glutamate Oxidase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. glutamate (acceptor) dehydrogenase; glutamate oxidase; glutamic acid oxidase; glutamic dehydrogenase (acceptor); L-glutamic acid oxidase. Pack: 100ml. Cat No: NATE-1806. | |
| L-Glutamate Oxidase from Streptomyces sp., Recombinant | In enzymology, a L-glutamate oxidase is an enzyme that catalyzes the chemical reaction:L-glutamate + O2 + H2O<-> 2-oxoglutarate + NH3 + H2O2. The 3 substrates of this enzyme are L-glutamate, O2, and H2O, whereas its 3 products are 2-oxoglutarate, NH3, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. It employs one cofactor, FAD. Group: Enzymes. Synonyms: L-glutamate oxidase; EC 1.4.3.11; 39346-34-4; glutamate (acceptor) dehydrogenase; glutamate oxidase; glutamic acid oxidase; glutamic dehydrogenase (acceptor); L-glutamic acid oxidase. Enzyme Commission Number: EC 1.4.3.11. CAS No. 39346-34-4. L-Glutamate Oxidase. Activity: > 5.0 unit/mg solid. Storage: 2-8°C. Form: lyophilized powder. Source: E. coli. Species: Streptomyces sp. L-glutamate oxidase; EC 1.4.3.11; 39346-34-4; glutamate (acceptor) dehydrogenase; glutamate oxidase; glutamic acid oxidase; glutamic dehydrogenase (acceptor); L-glutamic acid oxidase. Cat No: NATE-0393. | |
| 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. | |
| Native Bacillus licheniformis NADH Oxidase | NADH Oxidase from Bacillus licheniformis was shown to display hydrogen peroxide-forming activity. Nadh oxidase is a surface enzyme with increased oxidative activity in polymorphonuclear leukocytes during phagocytosis. Applications: Nadh oxidase from bacillus licheniformis has been used in a study to assess nitrogen assimilation by bacillus licheniformis growing in chemostat cultures. it has also been used in a study to investigate the role of glutamate dehydrogenase in ammonia assimilation in bacillus macerans. Group: Enzymes. Synonyms: NADH Oxidase; 9032-21-7. CAS No. 9032-21-7. NADH Oxidase. Activity: > 35 units/mg protein. Form: lyophilized powder. Source: Bacillus licheniformis. NADH Oxidase; 9032-21-7. Pack: vial of > 15 units. Cat No: NATE-0473. | |
| Native Bovine L-Glutamic Dehydrogenase | L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate. Mammalian forms of this enzyme, including this bovine form, can use either NADP (H) or NAD (H) as coenzymes. L-glutamic dehydrogenase plays a unique role in mammalian metabolism. The reverse reaction catalyzed by this enzyme is the only pathway by which ammonia can become bound to the α-carbon atom of an α-carboxylic acid and thus, is the only source of de novo amino acid synthesis in mammalian species. Group: Enzymes. Synonyms: glutamic dehydrogenase; glutamate dehydrogenase [NAD (P)]; 9029-12-3; glutamate dehydrogenase [NAD (P)+]; EC 1.4.1.3; L-GLDH; L-Glutamate:NAD[P]+ Oxidoreductase (deaminating). Enzyme Commission Number: EC 1.4.1.3. CAS No. 9029-12-3. GLDH. Activity: Type I, > 40 units/mg protein; Type II, > 20 units/mg protein; Type III, > 35 units/mg protein. Storage: 2-8°C. Form: Type I, ammonium sulfate suspension, Suspension in 2.0 M (NH4)2SO4 solution; Type II, lyophilized powder, Contains primarily Citrate buffer salt; Type III, aqueous glycerol solution, Solution in 50% glycerol, pH 7.3. Source: Bovine liver. Species: Bovine. glutamic dehydrogenase; glutamate dehydrogenase [NAD (P)]; 9029-12-3; glutamate dehydrogenase [NAD (P)+]; EC 1.4.1.3; L-GLDH; L-Glutamate:NAD[P]+ Oxidoreductase (deaminating). Cat No: NATE-0392. | |
| Native Candida utilis L-Glutamic Dehydrogenase (NADP) | L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate. 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 dehydrogenase; glutamate dehydrogenase (NADP). Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. Activity: 50-200 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salt. Source: Candida utilis. 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-0394. | |
| Native Microorganism Creatinine Deiminase | In enzymology, a creatinine deaminase (EC 3.5.4.21) is an enzyme that catalyzes the chemical reaction: creatinine + H2O <-> N-methylhydantoin + NH3. Thus, the two substrates of this enzyme are creatinine and H2O, whereas its two products are N-methylhydantoin and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is creatinine iminohydrolase. Applications: This enzyme is useful for enzymatic determination of creatinine when coupled with glutamate dehydrogenase in clinical analysis. Group: Enzymes. Synonyms: Creatinine hydrolase; Creatinine deaminase; EC 3.5.4.21. Enzyme Commission Number: EC 3.5.4.21. CAS No. 37289-15-9. Creatinine Deiminase. Mole weight: approx. 260 kDa. Activity: Grade? 10U/mg-solid or more (containing approx. 30% of stabilizer). Stability: Stable at-20°C for at least one year. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Creatinine hydrolase; Creatinine deaminase; EC 3.5.4.21. Cat No: DIA-186. | |
| 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 Sporosarcina sp. L-Phenylalanine Dehydrogenase | Phenylalanine dehydrogenase is a member of a large family of amino-acid dehydrogenases, which includes glutamate dehydrogenase, alanine dehydrogenase, leucine dehydrogenase, lysine EUR-dehydrogenase, and meso-a,EUR-diaminopimelate D-dehydrogenase. The three known gene sequences are octomers. It has a two-domain, three-dimensional structure. Applications: L-phenylalanine dehydrogenase is a nad+-dependent oxidoreductase that catalyzes the reversible, oxidative deamination of l-phenylalanine which results in its degradation. l-phenylalanine dehydrogenase is used to study phenylalanine metabolism and phenylalanine, tyrosine and tryptophan biosynthesis. Group: Enzymes. Synonyms: phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Enzyme Commission Number: EC 1.4.1.20. CAS No. 69403-12-9. PHD. Activity: > 6 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Sporosarcina sp. phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Cat No: NATE-0558. | |
| Native Thermoactinomyces intermedius Phenylalanine Dehydrogenase | Phenylalanine dehydrogenase is a member of a large family of amino-acid dehydrogenases, which includes glutamate dehydrogenase, alanine dehydrogenase, leucine dehydrogenase, lysine EUR-dehydrogenase, and meso-a,EUR-diaminopimelate D-dehydrogenase. The three known gene sequences are octomers. It has a two-domain, three-dimensional structure. Group: Enzymes. Synonyms: phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Enzyme Commission Number: EC 1.4.1.20. CAS No. 69403-12-9. PHD. Mole weight: ca. 380,000; Subunit molecular weight : ca. 40,000. Appearance: Ammonium sulphate suspension. Storage: Stable at 0 to 4 °C for at least six months (Do not freeze). Source: Thermoactinomyces intermedius. phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Cat No: NATE-1906. | |
| Nicotinamide 1,N6-Ethenoadenine Dinucleotide | A fluorescent analog of Nicotinamide Adenine Dinucleotide as a coenzyme for glutamate dehydrogenase. Group: Biochemicals. Alternative Names: 3- (Aminocarbonyl) -1-[5-O-[hydroxy (phosphonooxy) phosphinyl]- β -D-ribofuranosyl] pyridinium Inner Salt P'5'-Ester with 3- β-D-Ribofuranosyl-3H-imidazo[2,1-i]purine; 1,N6-Ethenonicotinamide Adenine Dinucleotide; ε-NAD. Grades: Highly Purified. CAS No. 38806-38-1. Pack Sizes: 5mg. Molecular Formula: C??H??N?O??P?, Molecular Weight: 687.45. US Biological Life Sciences. | Worldwide |
| N-succinylarginine dihydrolase | Arginine, N2-acetylarginine and N2-glutamylarginine do not act as substrates. This is the second enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.81 (succinylornithine transaminase), EC 1.2.1.71 (succinylglutamate semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase). Group: Enzymes. Synonyms: N2-succinylarginine dihydrolase; arginine succinylhydrolase; SADH; AruB; AstB; 2-N-succinyl-L-arginine iminohydrolase (decarboxylating). Enzyme Commission Number: EC 3.5.3.23. 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-4525; N-succinylarginine dihydrolase; EC 3.5.3.23; N2-succinylarginine dihydrolase; arginine succinylhydrolase; SADH; AruB; AstB; 2-N-succinyl-L-arginine iminohydrolase (decarboxylating). Cat No: EXWM-4525. | |
| Octanoyl coenzyme A lithium | Octanoyl coenzyme A lithium is a fatty acyl coenzyme A derivative. Octanoyl coenzyme A lithium can inhibit citrate synthase (CS) and glutamate dehydrogenase (GDH) with IC 50 values of 0.4-1.6 mM [1]. Uses: Scientific research. Group: Biochemical assay reagents. CAS No. 324518-20-9. Pack Sizes: 1 mg; 5 mg. Product ID: HY-134136A. | |
| Oxalomalic acid sodium salt | Oxalomalic acid is an inhibitor of both aconitase and NADP-dependent isocitrate dehydrogenase, At 5 mM, oxalomalic acid inhibition of aconitase leads to a decrease in the binding activity of IRP1 and a decrease in glutamate secretion in cultured lens epithelial cells, retinal pigment epithelial cells, and neurons. Synonyms: Oxalomalic acid trisodium salt. Grades: ≥95%. CAS No. 89304-26-7. Molecular formula: C6H6O8·3Na. Mole weight: 275. | |
| Perphenazine | D2 dopamine receptor antagonist; α-adrenergic receptor antagonist and ?-receptor agonist; phenothiazine antipsychotic. Inhibits glutamate dehydrogenase in vitro. Antipsychotic. Group: Biochemicals. Grades: Highly Purified. CAS No. 58-39-9. Pack Sizes: 100mg. US Biological Life Sciences. | Worldwide |
| Perphenazine-d8 Dihydrochloride | Labeled Perphenazine. D2 dopamine receptor antagonist; α-adrenergic receptor antagonist and ?-receptor agonist; phenothiazine antipsychotic. Inhibits glutamate dehydrogenase in vitro. Antipsychotic. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 1mg. US Biological Life Sciences. | Worldwide |
| proline dehydrogenase | A flavoprotein (FAD). The electrons from L-proline are transferred to the FAD cofactor, and from there to a quinone acceptor. In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.2.1.88, L-glutamate γ-semialdehyde dehydrogenase. Both activities are carried out by the same enzyme in enterobacteria. Group: Enzymes. Synonyms: L-proline dehydrogenase; L-proline:(acceptor) oxidoreductase. Enzyme Commission Number: EC 1.5.5.2. CAS No. 9050-70-8. 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-1557; proline dehydrogenase; EC 1.5.5.2; 9050-70-8; L-proline dehydrogenase; L-proline:(acceptor) oxidoreductase. Cat No: EXWM-1557. | |
| R162 | R162 is a potent, selective inhibitor of glutamate dehydrogenase 1 (GDH1) (Ki = 28.6 μM), with anti-cancer properties. It does not inhibit the activity of other NADPH enzymes such as 6-phosphogluconate dehydrogenase and fumarate hydratase. Synonyms: R 162; R-162; 2-allyl-1-hydroxy-anthraquinone; 2-allyl-1-hydroxyanthra-9,10-quinone. CAS No. 64302-87-0. Molecular formula: C17H12O3. Mole weight: 264.28. | |
| Saccharopine | Saccharopine (L-Saccharopine), a lysine degradation intermediate, is a mitochondrial toxin. Lysine and α-ketoglutarate are converted into Saccharopine by the lysine-ketoglutarate reductase. Saccharopine is then oxidized to α-aminoapidate semialdehyde and glutamate by the saccharopine dehydrogenase. Saccharopine impairs development by disrupting mitochondrial homeostasis [1] [2] [3]. Uses: Scientific research. Group: Natural products. Alternative Names: L-Saccharopine. CAS No. 997-68-2. Pack Sizes: 1 mg. Product ID: HY-W040307. | |
| succinate-semialdehyde dehydrogenase (NAD+) | This enzyme participates in the degradation of glutamate and 4-aminobutyrate. It is similar to EC 1.2.1.79 [succinate-semialdehyde dehydrogenase (NADP+)], and EC 1.2.1.16 [succinate-semialdehyde dehydrogenase (NAD(P)+)], but is specific for NAD+. Group: Enzymes. Synonyms: succinate semialdehyde dehydrogenase (NAD+); succinic semialdehyde dehydrogenase (NAD+); succinyl semialdehyde dehydrogenase (NAD+); succinate semialdehyde:NAD+ oxidoreductase. Enzyme Commission Number: EC 1.2.1.24. CAS No. 9028-95-9. 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-1130; succinate-semialdehyde dehydrogenase (NAD+); EC 1.2.1.24; 9028-95-9; succinate semialdehyde dehydrogenase (NAD+); succinic semialdehyde dehydrogenase (NAD+); succinyl semialdehyde dehydrogenase (NAD+); succinate semialdehyde:NAD+ oxidoreductase. Cat No: EXWM-1130. | |
| succinate-semialdehyde dehydrogenase (NADP+) | This enzyme participates in the degradation of glutamate and 4-aminobutyrate.It is similar to EC 1.2.1.24 [succinate-semialdehyde dehydrogenase (NAD+)], and EC 1.2.1.16 [succinate-semialdehyde dehydrogenase (NAD(P)+)], but is specific for NADP+. The enzyme from Escherichia coli is 20-fold more active with NADP+ than NAD+. Group: Enzymes. Synonyms: succinic semialdehyde dehydrogenase (NADP+); succinyl semialdehyde dehydrogenase (NADP+); succinate semialdehyde:NADP+ oxidoreductase; NADP-dependent succinate-semialdehyde dehydrogenase; GabD. Enzyme Commission Number: EC 1.2.1.79. 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-1181; succinate-semialdehyde dehydrogenase (NADP+); EC 1.2.1.79; succinic semialdehyde dehydrogenase (NADP+); succinyl semialdehyde dehydrogenase (NADP+); succinate semialdehyde:NADP+ oxidoreductase; NADP-dependent succinate-semialdehyde dehydrogenase; GabD. Cat No: EXWM-1181. | |
| succinate-semialdehyde dehydrogenase [NAD(P)+] | 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 succinate-semialdehyde:NAD(P)+ oxidoreductase. Other names in common use include succinate semialdehyde dehydrogenase (nicotinamide adenine, dinucleotide (phosphate)), and succinate-semialdehyde dehydrogenase [NAD(P)+]. This enzyme participates in 3 metabolic pathways: glutamate metabolism, tyrosine metabolism, and butanoate metabolism. Group: Enzymes. Synonyms: succinate semialdehyde dehydrogenase (nicotinamide adenine dinucleotide (phosphate)); succinate-semialdehyde dehydrogenase [NAD(P)]. Enzyme Commission Number: EC 1.2.1.16. CAS No. 37250-88-7. 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-1121; succinate-semialdehyde dehydrogenase [NAD(P)+]; EC 1.2.1.16; 37250-88-7; succinate semialdehyde dehydrogenase (nicotinamide adenine dinucleotide (phosphate)); succinate-semialdehyde dehydrogenase [NAD(P)]. Cat No: EXWM-1121. | |
| succinylglutamate desuccinylase | Requires Co2+ for maximal activity. N2-Acetylglutamate is not a substrate. This is the final enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.11 (acetylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase). Group: Enzymes. Synonyms: N2-succinylglutamate desuccinylase; SGDS; AstE. Enzyme Commission Number: EC 3.5.1.96. CAS No. 99676-40-1. 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-4488; succinylglutamate desuccinylase; EC 3.5.1.96; 99676-40-1; N2-succinylglutamate desuccinylase; SGDS; AstE. Cat No: EXWM-4488. | |
| succinylornithine transaminase | A pyridoxal-phosphate protein. Also acts on N2-acetyl-L-ornithine and L-ornithine, but more slowly. In Pseudomonas aeruginosa, the arginine-inducible succinylornithine transaminase, acetylornithine transaminase (EC 2.6.1.11) and ornithine aminotransferase (EC 2.6.1.13) activities are catalysed by the same enzyme, but this is not the case in all species. This is the third enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.81 (succinylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase). Group: Enzymes. Synonyms: succinylornithine aminotr. Enzyme Commission Number: EC 2.6.1.81. 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-2922; succinylornithine transaminase; EC 2.6.1.81; succinylornithine aminotransferase; N2-succinylornithine 5-aminotransferase; AstC; SOAT; 2-N-succinyl-L-ornithine:2-oxoglutarate 5-aminotransferase. Cat No: EXWM-2922. | |
| Acyl-Coenzyme A Dehydrogenase 8 from Human, Recombinant | Acyl CoA dehydrogenase is the enzymeused to catalyzethe first step of β-oxidationin Fatty acid metabolism. Acyl-coenzyme A (CoA) dehydrogenases (ACADs) are a family of mitochondrial enzymes that catalyze the first dehydrogenation step in the bets-oxidation of fatty acyl-CoA derivatives. Several human ACADs exist and all ACADs catalyze the same initial dehydrogenation of the substrate at the beta-carbon atom and require electron transfer flavoprotein as an alectron acceptor. The predicted 415-amino acid ACAD8 protein contains many of the residues conserved in most other ACADs, including an active site glutamic acid residue and residues important for tetramer f...mber 8 mitochondrial; ACAD-8; Isobutyryl-CoA dehydrogenase; Activator-recruited cofactor 42 kDa component; ARC42; FLJ22590. Purity: Greater than 95.0% as determined by SDS-PAGE. ACAD-8. Mole weight: 47.7 kDa. Stability: ACAD8 although stable at 4°C for 1 week, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. Acyl-CoA dehydrogenase family member 8 mitochondrial; ACAD-8; Isobutyryl-CoA dehydrogenase; Activator-recruited cofactor 42 kDa component; ARC42; FLJ22590. Cat No: NATE-0801. | |
| Dimethyl dicarbonate | Dimethyl dicarbonate (DMDC) is an organic compound which is a Colorless liquid with a sharp odor at room temperature. It is primarily used as a beverage preservative, processing aid, or sterilant (INS No. 242), and acts by inhibiting the enzymes acetate kinase and L-glutamic acid decarboxylase. It has also been proposed that DMDC inhibits the enzymes alcohol dehydrogenase and glyceraldehyde 3-phosphate dehydrogenase by causing the methoxycarbonylation of their histidine components. Uses: Designed for use in research and industrial production. Additional or Alternative Names: methoxycarbonyl methyl carbonate;DMPC Dimethyl pyrocarbonate Pyrocarbonic acid dimethyl ester. Product Category: Heterocyclic Organic Compound. CAS No. 4525-33-1. Molecular formula: C4H6O5. Mole weight: 134.09. IUPACName: methoxycarbonyl methyl carbonate. Canonical SMILES: COC(=O)OC(=O)OC. Density: 1.242 g/cm³. Product ID: ACM4525331. Alfa Chemistry ISO 9001:2015 Certified. |  |
| 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 | |
| Isoguanosine Hydrate | A useful synthetic intermedate. A naturally occuring, biologically active isomer of guanosine. Reported to stimulate the accumulation of cyclic-AMP in the brain. It is an inhibitor of IMP pyrophosphorylase, and its 5'-di and -tri-phosphates inhibit glutamic acid dehydrogenase. May contain approximately 0.6 moles of water. Synonyms: 2-Hydroxy adenosine hydrate; 1,2-Dihydro-2-oxo-adenosine Hydrate; Crotonosid Hydrate; Isoguanine riboside Hydrate; NSC 1216 Hydrate; 2,3-Dihydro-2-oxoadenosine Hydrate; 6-Amino-9-β-D-ribofuranosyl-9H-Purin-2-ol Hydrate. Grades: ≥95%. CAS No. 359436-55-8. Molecular formula: C10H13N5O5. Mole weight: 283.24. | |
| 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 | |
| phosphoserine transaminase | A pyridoxal-phosphate protein. This enzyme catalyses the second step in the phosphorylated pathway of serine biosynthesis in Escherichia coli. It also catalyses the third step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate in Escherichia coli (using Reaction 2 above). In Escherichia coli, pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72 (erythrose-4-phosphate dehydrogenase), EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate). ...ransaminase; 3-O-phospho-L-serine:2-oxoglutarate aminotransferase; SerC; PdxC; 3PHP transaminase. Enzyme Commission Number: EC 2.6.1.52. CAS No. 9030-90-4. 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-2894; phosphoserine transaminase; EC 2.6.1.52; 9030-90-4; PSAT; phosphoserine aminotransferase; 3-phosphoserine aminotransferase; hydroxypyruvic phosphate-glutamic transaminase; L-phosphoserine aminotransferase; phosphohydroxypyruvate transaminase; phosphohydroxypyruvic-glutamic transaminase; 3-O-phospho-L-serine:2-oxoglutarate aminotransferase; SerC; PdxC; 3PHP transaminase. Cat No: EXWM-2894. | |
| QL9 | QL9 (QLSPFPFDL), derived from the enzyme 2-oxoglutarate dehydrogenase, is a high-affinity alloantigen for the 2C T cell receptor (TCR). Synonyms: L-Leucine, L-glutaminyl-L-leucyl-L-seryl-L-prolyl-L-phenylalanyl-L-prolyl-L-phenylalanyl-L-α-aspartyl-; Gln-Leu-Ser-Pro-Phe-Pro-Phe-Asp-Leu; QL 9; QL-9. Grades: ≥95%. CAS No. 159646-83-0. Molecular formula: C52H74N10O14. Mole weight: 1063.21. | |
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