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| Product | Description | |
|---|---|---|
| Alcohol Dehydrogenase (NADP+ dependent) from E. coli, Recombinant | Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an enzyme that in humans is encoded by the AKR1A1 gene. This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. This member, also known as aldehyde reductase, is involved in the reduction of biogenic and xenobiotic aldehydes and is present in virtually every tissue. Alternative splicing of this gene results in two transcript variants encoding the same protein. Group: Enzymes. Synonyms: EC 1.1.1.2; Aromatic Alcohol Dehydrogenase; Alcohol:NADP+ oxidoreductase; AKR1A1; ALDR1; ALR; . Enzyme Commission Number: EC 1.1.1.2. CAS No. 9028-12-0. ALR. Activity: >500 U/ml. Form: Liquid. Source: E. coli. Species: E. coli. EC 1.1.1.2; Aromatic Alcohol Dehydrogenase; Alcohol:NADP+ oxidoreductase; AKR1A1; ALDR1; ALR; ARM; DD3; HEL-S-6; aldehyde reductase; aldo-keto reductase family 1 member A1; alcohol dehydrogenase (NADP+); aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Cat No: NATE-1589. |  |
| Alcohol Dehydrogenase (NADP+ dependent) from Entamoeba species, Recombinant | NADP-dependent isopropanol dehydrogenase belongs to the superfamily of alcohol dehydrogenases with a preference for medium chain secondary alcohols, such as 2- butanol and isopropanol, while it has low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. It is also active with acetaldehyde and propionaldehyde. Group: Enzymes. Synonyms: EC 1.1.1.2; Aromatic Alcohol Dehy. Purity: > 95% by SDS-PAGE. ALR. Mole weight: ~40.9 kDa (SDS-PAGE). Activity: > 60U/mg. Storage: Aliquot and store at -20°C. Avoid repeated freeze thaw cycles. Form: Liquid, 1 mg/mL solution in 50 mM Tris-HCl buffer (pH 8.0) containing 100 mM NaCl and 50% glycerol. Source: E. coli. Species: Entamoeba species. EC 1.1.1.2; Aromatic Alcohol Dehydrogenase; Alcohol:NADP+ oxidoreductase; AKR1A1; ALDR1; ALR; ARM; DD3; HEL-S-6; aldehyde reductase; aldo-keto reductase family 1 member A1; alcohol dehydrogenase (NADP+); aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Cat No: NATE-1590. | |
| 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. | |
| Native Thermoanaerobium brockii Alcohol Dehydrogenase, NADP+ dependent | Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an enzyme that in humans is encoded by the AKR1A1 gene. This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. This member, also known as aldehyde reductase, is involved in the reduction of biogenic and xenobiotic aldehydes and is present in virtually every tissue. Alternative splicing of this gene results in two transcript variants encoding the same protein. Applications: Alcohol dehydrogenase may be used to synthesize enantiomerically pure stereoisomers of chiral alcohols. it may...ase; AKR1A1; ALDR1; ALR; ARM; DD3; HEL-S-6; aldehyde reductase; aldo-keto reductase family 1 member A1; alcohol dehydrogenase (NADP+); aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.2. CAS No. 9028-12-0. ALR. Activity: 5-15 units/mg protein; 30-90 units/mg protein. Stability: -20°C. Form: lyophilized powder. Source: Thermoanaerobium brockii. EC 1.1.1.2; Aro | |
| Native Thermoanaerobium sp. Aromatic Alcohol Dehydrogenase, NADP+ dependent | Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an enzyme that in humans is encoded by the AKR1A1 gene. This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. This member, also known as aldehyde reductase, is involved in the reduction of biogenic and xenobiotic aldehydes and is present in virtually every tissue. Alternative splicing of this gene results in two transcript variants encoding the same protein. Group: Enzymes. Synonyms: EC 1.1.1.2; Aromatic Alcohol Dehydrogenase; Alcohol. Enzyme Commission Number: EC 1.1.1.2. CAS No. 9028-12-0. ALR. Activity: 1-5 units/mg solid. Stability: -20°C. Form: lyophilized powder. Source: Thermoanaerobium sp. EC 1.1.1.2; Aromatic Alcohol Dehydrogenase; Alcohol:NADP+ oxidoreductase; AKR1A1; ALDR1; ALR; ARM; DD3; HEL-S-6; aldehyde reductase; aldo-keto reductase family 1 member A1; alcohol dehydrogenase (NADP+); aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Cat No: NATE-0063. | |
| phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating) | Highly specific for NAD+. The enzyme catalyses both the oxidation and decarboxylation of 6-phospho-D-gluconate. In the bacterium Methylobacillus flagellatus the enzyme participates in a formaldehyde oxidation pathway. cf. EC 1.1.1.44, phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating). Group: Enzymes. Synonyms: 6-PGDH (ambiguous); gntZ (gene name); GNDl. Enzyme Commission Number: EC 1.1.1.343. CAS No. 9073-95-4. 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-0258; phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating); EC 1.1.1.343; 9073-95-4; 6-PGDH (ambiguous); gntZ (gene name); GNDl. Cat No: EXWM-0258. | |
| phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating) | The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce NADPH and pentose for biosynthetic reactions. Highly specific for NADP+. cf. EC 1.1.1.343, phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating). Group: Enzymes. Synonyms: phosphogluconic acid dehydrogenase; 6-phosphogluconic dehydrogenase; 6-phosphogluconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase. Enzyme Commission Number: EC 1.1.1.44. CAS No. 9073-95-4. 6-Phosphogluconic Dehydrogenase. 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-0329; phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating); EC 1.1.1.44; 9073-95-4; phosphogluconic acid dehydrogenase; 6-phosphogluconic dehydrogenase; 6-phosphogluconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase. Cat No: EXWM-0329. | |
| phosphogluconate dehydrogenase [NAD(P)+-dependent, decarboxylating] | The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce reducing power and pentose for biosynthetic reactions. Unlike EC 1.1.1.44, phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating), it is not specific for NADP+ and can accept both cofactors with similar efficiency. cf. EC 1.1.1.343, phosphogluconate dehydrogenase [NAD+-dependent, decarboxylating]. Group: Enzymes. Enzyme Commission Number: EC 1.1.1.351. CAS No. 9073-95-4. 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-0267; phosphogluconate dehydrogenase [NAD(P)+-dependent, decarboxylating]; EC 1.1.1.351; 9073-95-4. Cat No: EXWM-0267. | |
| 12α-hydroxysteroid dehydrogenase | Catalyses the oxidation of the 12α-hydroxy group of bile acids, both in their free and conjugated form. Also acts on bile alcohols. Group: Enzymes. Synonyms: 12α-hydroxy steroid dehydrogenase; NAD+-dependent 12α-hydroxysteroid dehydrogenase; NADP+-12α-hydroxysteroid dehydrogenase. Enzyme Commission Number: EC 1.1.1.176. CAS No. 61642-40-8. 12α-Hydroxysteroid Dehydrogenase. 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-0079; 12α-hydroxysteroid dehydrogenase; EC 1.1.1.176; 61642-40-8; 12α-hydroxy steroid dehydrogenase; NAD+-dependent 12α-hydroxysteroid dehydrogenase; NADP+-12α-hydroxysteroid dehydrogenase. Cat No: EXWM-0079. | |
| 15-hydroxyprostaglandin-D dehydrogenase (NADP+) | Specific for prostaglandins D [cf. EC 1.1.1.141 15-hydroxyprostaglandin dehydrogenase (NAD+) and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+)]. Group: Enzymes. Synonyms: prostaglandin-D 15-dehydrogenase (NADP); dehydrogenase, prostaglandin D2; NADP-PGD2 dehydrogenase; dehydrogenase, 15-hydroxyprostaglandin (nicotinamide adenine dinucleotide phosphate); 15-hydroxy PGD2 dehydrogenase; 15-hydroxyprostaglandin dehydrogenase (NADP); NADP-dependent 15-hydroxyprostaglandin dehydrogenase; prostaglandin . Enzyme Commission Number: EC 1.1.1.196. CAS No. 84399-95-1. 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-0099; 15-hydroxyprostaglandin-D dehydrogenase (NADP+); EC 1.1.1.196; 84399-95-1; prostaglandin-D 15-dehydrogenase (NADP); dehydrogenase, prostaglandin D2; NADP-PGD2 dehydrogenase; dehydrogenase, 15-hydroxyprostaglandin (nicotinamide adenine dinucleotide phosphate); 15-hydroxy PGD2 dehydrogenase; 15-hydroxyprostaglandin dehydrogenase (NADP); NADP-dependent 15-hydroxyprostaglandin dehydrogenase; prostaglandin D2 dehydrogenase; NADP-linked 15-hydroxyprostaglandin dehydrogenase; NADP-specific 15-hydroxyprostaglandin dehydrogenase; NADP-linked prostaglandin D2 dehydrogenase; 15-hydroxyprostaglandin-D dehydrogenase (NADP). Cat No: EXWM-0099. | |
| 15-hydroxyprostaglandin dehydrogenase (NAD+) | Acts on prostaglandin E2, F2α and B1, but not on prostaglandin D2. cf. EC 1.1.1.196 15-hydroxyprostaglandin-D dehydrogenase (NADP+) and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+). Group: Enzymes. Synonyms: NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type I); PGDH; 11α,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase; 15-OH-PGDH; 15-hydroxyprostaglandin dehydrogenase; 15-hydroxyprostanoic dehydrogenase; NAD+-specific 15-hydroxyprostaglandin dehydrogenase; prostaglandin dehydrogenase; 15-hydroxyprostaglandin dehydrogenase (NAD+); (5Z,13E)-(15S)-11α,15-dihydroxy-9-oxoprost-13. Enzyme Commission Number: EC 1.1.1.141. CAS No. 9030-87-9. 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-0045; 15-hydroxyprostaglandin dehydrogenase (NAD+); EC 1.1.1.141; 9030-87-9; NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type I); PGDH; 11α,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase; 15-OH-PGDH; 15-hydroxyprostaglandin dehydrogenase; 15-hydroxyprostanoic dehydrogenase; NAD+-specific 15-hydroxyprostaglandin dehydrogenase; prostaglandin dehydrogenase; 15-hydroxyprostaglandin dehydrogenase (NAD+); (5Z,13E)-(15S)-11α,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase. Cat No: EXWM-0045. | |
| 15-hydroxyprostaglandin dehydrogenase (NADP+) | Acts on prostaglandins E2, F2α and B1, but not on prostaglandin D2 [cf. EC 1.1.1.141 15-hydroxyprostaglandin dehydrogenase (NAD+) and EC 1.1.1.196 15-hydroxyprostaglandin-D dehydrogenase (NADP+)]. May be identical with EC 1.1.1.189 prostaglandin-E2 9-reductase. Group: Enzymes. Synonyms: NADP-dependent 15-hydroxyprostaglandin dehydrogenase; NADP-linked 15-hydroxyprostaglandin dehydrogenase; NADP-specific 15-hydroxyprostaglandin dehydrogenase; type II 15-hydroxyprostaglandin dehydrogenase; 15-hydroxyprostaglandin dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.197. CAS No. 54989-39-8. 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-0100; 15-hydroxyprostaglandin dehydrogenase (NADP+); EC 1.1.1.197; 54989-39-8; NADP-dependent 15-hydroxyprostaglandin dehydrogenase; NADP-linked 15-hydroxyprostaglandin dehydrogenase; NADP-specific 15-hydroxyprostaglandin dehydrogenase; type II 15-hydroxyprostaglandin dehydrogenase; 15-hydroxyprostaglandin dehydrogenase (NADP). Cat No: EXWM-0100. | |
| 15-hydroxyprostaglandin-I dehydrogenase (NADP+) | Specific for prostaglandin I2. Group: Enzymes. Synonyms: prostacyclin dehydrogenase; PG I2 dehydrogenase; prostacyclin dehydrogenase; NADP-linked 15-hydroxyprostaglandin (prostacyclin) dehydrogenase; NADP+-dependent PGI2-specific 15-hydroxyprostaglandin dehydrogenase; 15-hydroxyprostaglandin-I dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.231. CAS No. 79468-49-8. 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-0138; 15-hydroxyprostaglandin-I dehydrogenase (NADP+); EC 1.1.1.231; 79468-49-8; prostacyclin dehydrogenase; PG I2 dehydrogenase; prostacyclin dehydrogenase; NADP-linked 15-hydroxyprostaglandin (prostacyclin) dehydrogenase; NADP+-dependent PGI2-specific 15-hydroxyprostaglandin dehydrogenase; 15-hydroxyprostaglandin-I dehydrogenase (NADP). Cat No: EXWM-0138. | |
| 17b-Hydroxysteroid Dehydrogenase Type-3 Inhibitor (17b-HSD3 Inhibitor, 5-(3-Bromo-4-hydroxybenzylidene)-3-(4-methoxyphenyl)-2-thioxothiazolidin-4-one) | A cell-permeable benzylidine-thioxothiazolidinone compound that blocks the steroidogenesis of testosterone by directly inhibiting 17b-HSD3- (17b-hydroxysteroid dehydrogenase type 3) catalyzed, NADPH-dependent, reduction of delta4-dione C17 ketone in a delta4-dione- (4-androstene-3,17-dione) competitive, highly potent (IC50=0.6, 6.0, and 40nM, respectively, against momoset, human, and mouse 17b-HSD3 activity in testes homogenate), and selective manner, displaying no activity against 17b-HSD1 and 17b-HSD2 activity. Poor pharmacokinetic properties limit its use to culture treatments and cell-free assays only. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 10mg. US Biological Life Sciences. |  Worldwide |
| 2-oxoaldehyde dehydrogenase (NAD+) | Not identical with EC 1.2.1.49 2-oxoaldehyde dehydrogenase (NADP+). Group: Enzymes. Synonyms: α-ketoaldehyde dehydrogenase; methylglyoxal dehydrogenase; NAD+-linked α-ketoaldehyde dehydrogenase; 2-ketoaldehyde dehydrogenase; NAD+-dependent α-ketoaldehyde dehydrogenase. Enzyme Commission Number: EC 1.2.1.23. CAS No. 37250-91-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1129; 2-oxoaldehyde dehydrogenase (NAD+); EC 1.2.1.23; 37250-91-2; α-ketoaldehyde dehydrogenase; methylglyoxal dehydrogenase; NAD+-linked α-ketoaldehyde dehydrogenase; 2-ketoaldehyde dehydrogenase; NAD+-dependent α-ketoaldehyde dehydrogenase. Cat No: EXWM-1129. | |
| 2-oxoaldehyde dehydrogenase (NADP+) | Not identical with EC 1.2.1.23 2-oxoaldehyde dehydrogenase (NAD+). Group: Enzymes. Synonyms: α-ketoaldehyde dehydrogenase; methylglyoxal dehydrogenase; NADP+-linked α-ketoaldehyde dehydrogenase; 2-ketoaldehyde dehydrogenase; NADP+-dependent α-ketoaldehyde dehydrogenase. Enzyme Commission Number: EC 1.2.1.49. CAS No. 83588-97-0, 97162-76-0. 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-1152; 2-oxoaldehyde dehydrogenase (NADP+); EC 1.2.1.49; 83588-97-0, 97162-76-0; α-ketoaldehyde dehydrogenase; methylglyoxal dehydrogenase; NADP+-linked α-ketoaldehyde dehydrogenase; 2-ketoaldehyde dehydrogenase; NADP+-dependent α-ketoaldehyde dehydrogenase. Cat No: EXWM-1152. | |
| 3-Acetylpyridine-Adenine Dinucleotide, Oxidized (APAD) | 3-Acetylpyridine adenine dinucleotide is an NAD analog with higher oxidation potential than NAD. It can substitute for NAD as a hydrogen-accepting cofactor in many dehydrogenase reactions. For example lactate dehydrogenase from Toxoplasma, Clonorchis, and Plasmodium, bacterial lipoamide dehydrogenase, as well as mammalian dehydrogenases. This compound can also act as a proton acceptor in various transhydrogenation reactions with NADH or NADPH. Group: Coenzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NA. Enzyme Commission Number: EC 1.1.1.1. CAS No. 1986-8-8. Purity: Determined by increase in absorbance at 363 nm on enzymatic reduction with ADH* at pH 10.0 > 92% *ADH = Alcohol dehydrogenase (Horse liver) (EC 1.1.1.1.). APAD. Mole weight: 662.44. Storage: Keep tightly stoppered in the dark below 5°C. Moisture will reduce the purity. For prolonged storage, keep below-20°C. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1; APAD. Cat No: NATE-0077. | |
| 3-Acetylpyridine-Adenine Dinucleotide, Reduced (APADH) | Molecular Formula: C22H28N6O14P2. Group: Coenzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1; APADH. Enzyme Commission Number: EC 1.1.1.1. CAS No. 102029-93-6. Purity: Determined by decrease in absorbance at 363 nm on enzymatic oxidation with ADH* at pH 7.5 (> 92%) *ADH = Alcohol dehydrogenase (horse liver) (EC 1.1.1.1.). APADH. Mole weight: 708.42. Storage: Keep tightly stoppered in the dark below-20°C. Moisture will reduce the purity. For Prolonged storage, keep below-80°C. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1; APADH. Cat No: NATE-0078. | |
| 3-hydroxyisobutyrate dehydrogenase | 3-hydroxyisobutyrate dehydrogenase is a tetrameric mitochondrial enzyme that catalyzes the NAD+-dependent, reversible oxidation of 3-hydroxyisobutyrate, an intermediate of valine catabolism, to methylmalonate semialdehyde. Group: Enzymes. Synonyms: β-hydroxyisobutyrate dehydrogenase. Enzyme Commission Number: EC 1.1.1.31. CAS No. 9028-39-1. 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-0221; 3-hydroxyisobutyrate dehydrogenase; EC 1.1.1.31; 9028-39-1; β-hydroxyisobutyrate dehydrogenase. Cat No: EXWM-0221. | |
| 4-hydroxythreonine-4-phosphate dehydrogenase | The product of the reaction undergoes decarboxylation to give 3-amino-2-oxopropyl phosphate. The enzyme is part of the biosynthesis pathway of the coenzyme pyridoxal 5'-phosphate found in anaerobic bacteria. Group: Enzymes. Synonyms: NAD+-dependent threonine 4-phosphate dehydrogenase; L-threonine 4-phosphate dehydrogenase; 4-(phosphohydroxy)-L-threonine dehydrogenase; PdxA; 4-(phosphonooxy)-L-threonine:NAD+ oxidoreductase. Enzyme Commission Number: EC 1.1.1.262. CAS No. 230310-36-8. 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-0168; 4-hydroxythreonine-4-phosphate dehydrogenase; EC 1.1.1.262; 230310-36-8; NAD+-dependent threonine 4-phosphate dehydrogenase; L-threonine 4-phosphate dehydrogenase; 4-(phosphohydroxy)-L-threonine dehydrogenase; PdxA; 4-(phosphonooxy)-L-threonine:NAD+ oxidoreductase. Cat No: EXWM-0168. | |
| 6-Aminonicotinamide | 6-Aminonicotinamide (6-AN) is a well-established inhibitor of the NADP+-dependent enzyme, 6-phosphogluconate dehydrogenase (Ki = 0.46 μM). 6-Aminonicotinamide is a PGD inhibitor and apoptosis inducer. Uses: Teratogens. Synonyms: 6-aminopyridine-3-carboxamide. Grades: 95 %. CAS No. 329-89-5. Molecular formula: C6H7N3O. Mole weight: 137.14. |  |
| 7β-hydroxysteroid dehydrogenase (NADP+) | Catalyses the oxidation of the 7β-hydroxy group of bile acids such as ursodeoxycholate. Group: Enzymes. Synonyms: NADP-dependent 7β-hydroxysteroid dehydrogenase; 7β-hydroxysteroid dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.201. CAS No. 79393-83-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0106; 7β-hydroxysteroid dehydrogenase (NADP+); EC 1.1.1.201; 79393-83-2; NADP-dependent 7β-hydroxysteroid dehydrogenase; 7β-hydroxysteroid dehydrogenase (NADP). Cat No: EXWM-0106. | |
| alanine dehydrogenase | This enzyme participates in taurine and hypotaurine metabolism and reductive carboxylate cycle (CO2 fixation). Group: Enzymes. Synonyms: AlaDH; L-alanine dehydrogenase; NAD-linked alanine dehydrogenase; α-alanine dehydrogenase; NAD-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. 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-1442; alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; L-alanine dehydrogenase; NAD-linked alanine dehydrogenase; α-alanine dehydrogenase; NAD-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Cat No: EXWM-1442. | |
| Alanine Dehydrogenase (Crude Enzyme) | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH 2 group of donors with NAD + or NADP + as acceptor. This enzyme participates in taurine and hypotaurine metabolism and reductive carboxylate cycle (CO 2 fixation). This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; synthesis; biotechnology; nutrition. Group: Enzymes. Synonyms: AlaDH; L-alanine dehydrogenase; NAD-linked alanine dehydrogenase; α-alanine dehydrogenase; NAD-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. AlaDH; L-alanine dehydrogenase; NAD-linked alanine dehydrogenase; α-alanine dehydrogenase; NAD-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Pack: 100ml. Cat No: NATE-1801. | |
| Alanine Dehydrogenase from Bacillus cereus, Recombinant | L-Alanine dehydrogenase is an A-stereospecific dehydrogenase that catalyzes the reversible deamination of L-alanine to pyruvate and ammonium. It is important for the geneRation of pyruvate during sporulation. L-Alanine dehydrogenase from Bacillus subtilis has a predominately ordered kinetic mechanism in which NAD binds before L-alanine. Subsequently, ammonia, pyruvate, and NADH are released in that specific order. Optimal pH for the amination reaction is 8.8-9.0, whereas it is 10-10.5 for the deamination reaction. The enzyme is inactivated by divalent metal ions and p-chloromercuribenzoate, mercuric ion being most effective. The inactivation may be reversed by L-or D-cysteine. Group: Enzymes. Synonyms: L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alan. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. Activity: > 350 units/ml. Storage: -20°C. Source: E. coli. Species: Bacillus cereus. L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Cat No: NATE-0044. | |
| alcohol dehydrogenase | A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols. Group: Enzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. 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-0001; alcohol dehydrogenase; EC 1.1.1.1; 9031-72-5; aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase. Cat No: EXWM-0001. | |
| Alcohol Dehydrogenase (Crude Enzyme) | This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; medicine. Group: Enzymes. Synonyms: aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP + -aldehyde reductase; NADP + -dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.2. CAS No. 9028-12-0. ALR. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP + -aldehyde reductase; NADP + -dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Pack: 100ml. Cat No: NATE-1792. | |
| Alcohol dehydrogenase from E. coli, Recombinant | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Applications: High purity recombinant alcohol dehyd...l dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. Mole weight: ~ 38,642 Da. Activity: 6.7 U/mg protein at pH 8.5 and 25°C. Storage: Store at 4°C. Do not store the enzyme in presence of sodium azide. Form: In 3.2 M ammonium sulphate. Source: E. coli. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Cat No: NATE-0803. | |
| Alcohol dehydrogenase from Equine, Recombinant | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Group: Enzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcoh. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. Activity: >0.5 U/mg. Storage: Store at -20°C. Source: E. coli. Species: Equine. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Cat No: NATE-1584. | |
| Alcohol dehydrogenase from Human, Recombinant | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Group: Enzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcoh. Enzyme Commission Number: EC 1.1.1.2. Alcohol dehydrogenase. Mole weight: 36573.0 Da. Source: Human. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.2. Cat No: NATE-1197. | |
| alcohol dehydrogenase (NADP+) | A zinc protein. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. May be identical with EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate reductase (NADPH)] and EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. Re-specific with respect to NADPH. Group: Enzymes. Synonyms: aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.2. CAS No. 9028-12-0. ALR. 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-0103; alcohol dehydrogenase (NADP+); EC 1.1.1.2; 9028-12-0; aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Cat No: EXWM-0103. | |
| alcohol dehydrogenase (nicotinoprotein) | Contains Zn2+. Nicotinoprotein alcohol dehydrogenases are unique medium-chain dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a tightly bound NAD+/NADH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro.The enzyme from the Gram-positive bacterium Amycolatopsis methanolica can accept many primary alcohols as substrates, including benzylalcohol. Group: Enzymes. Synonyms: NDMA-dependent alcohol dehydrogenase; nicotinoprotein alcohol dehydrogenase; np-ADH; ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase. Enzyme Commission Number: EC 1.1.99.36. 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-0464; alcohol dehydrogenase (nicotinoprotein); EC 1.1.99.36; NDMA-dependent alcohol dehydrogenase; nicotinoprotein alcohol dehydrogenase; np-ADH; ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase. Cat No: EXWM-0464. | |
| aldehyde dehydrogenase (NAD+) | Wide specificity, including oxidation of D-glucuronolactone to D-glucarate. Group: Enzymes. Synonyms: CoA-independent aldehyde dehydrogenase; m-methylbenzaldehyde dehydrogenase; NAD-aldehyde dehydrogenase; NAD-dependent 4-hydroxynonenal dehydrogenase; NAD-dependent aldehyde dehydrogenase; NAD-linked aldehyde dehydrogenase; propionaldehyde dehydrogenase; aldehyde dehydrogenase (NAD). Enzyme Commission Number: EC 1.2.1.3. CAS No. 9028-86-8. 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-1136; aldehyde dehydrogenase (NAD+); EC 1.2.1.3; 9028-86-8; CoA-independent aldehyde dehydrogenase; m-methylbenzaldehyde dehydrogenase; NAD-aldehyde dehydrogenase; NAD-dependent 4-hydroxynonenal dehydrogenase; NAD-dependent aldehyde dehydrogenase; NAD-linked aldehyde dehydrogenase; propionaldehyde dehydrogenase; aldehyde dehydrogenase (NAD). Cat No: EXWM-1136. | |
| aldehyde dehydrogenase (NADP+) | 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 aldehyde:NADP+ oxidoreductase. Other names in common use include NADP+-acetaldehyde dehydrogenase, NADP+-dependent aldehyde dehydrogenase, and aldehyde dehydrogenase (NADP+). This enzyme participates in caprolactam degradation. Group: Enzymes. Synonyms: NADP-acetaldehyde dehydrogenase; NADP-dependent aldehyde dehydrogenase; aldehyde dehydrogenase (NADP). Enzyme Commission Number: EC 1.2.1.4. CAS No. 9028-87-9. 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-1144; aldehyde dehydrogenase (NADP+); EC 1.2.1.4; 9028-87-9; NADP-acetaldehyde dehydrogenase; NADP-dependent aldehyde dehydrogenase; aldehyde dehydrogenase (NADP). Cat No: EXWM-1144. | |
| arogenate dehydrogenase (NADP+) | Arogenate dehydrogenases may utilize NAD+ (EC 1.3.1.43), NADP+ (EC 1.3.1.78), or both (EC 1.3.1.79). NADP+-dependent enzymes usually predominate in higher plants.The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 and the TyrAAT1 isoform of the plant Arabidopsis thaliana cannot use prephenate as a substrate, while the Arabidopsis isoform TyrAAT2 can use it very poorly. Group: Enzymes. Synonyms: arogenic dehydrogenase (ambiguous); pretyrosine dehydrogenase (ambiguous); TyrAAT1; TyrAAT2; TyrAa. Enzyme Commission Number: EC 1.3.1.78. CAS No. 64295-75-6. 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-1347; arogenate dehydrogenase (NADP+); EC 1.3.1.78; 64295-75-6; arogenic dehydrogenase (ambiguous); pretyrosine dehydrogenase (ambiguous); TyrAAT1; TyrAAT2; TyrAa. Cat No: EXWM-1347. | |
| aspartate dehydrogenase | The enzyme is strictly specific for L-aspartate as substrate. Catalyses the first step in NAD biosynthesis from aspartate. The enzyme has a higher affinity for NAD+ than NADP+. Group: Enzymes. Synonyms: NAD-dependent aspartate dehydrogenase; NADH2-dependent aspartate dehydrogenase; NADP+-dependent aspartate dehydrogenase. Enzyme Commission Number: EC 1.4.1.21. CAS No. 37278-97-0. 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-1455; aspartate dehydrogenase; EC 1.4.1.21; 37278-97-0; NAD-dependent aspartate dehydrogenase; NADH2-dependent aspartate dehydrogenase; NADP+-dependent aspartate dehydrogenase. Cat No: EXWM-1455. | |
| β-Galactose Dehydrogenase S from Pseudomonas fluorescens, Recombinant | In enzymology, a galactose 1-dehydrogenase (EC 1.1.1.48) is an enzyme that catalyzes the chemical reaction: D-galactose + NAD+ rightleftharpoons D-galactono-1,4-lactone + NADH + H+. Thus, the two substrates of this enzyme are D-galactose and NAD+, whereas its 3 products are D-galactono-1,4-lactone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in galactose metabolism. Applications: Β-galactose dehydrogenase s has been used in the colorimetric microassay method to determine the level of galactose and galactose-1-phosphate in blood. Group: Enzymes. Synonyms: D-galactose:NAD+ 1-oxidoreductase; D-galactose dehydrogenase; beta-galactose dehydrogenase; NAD+-dependent D-galactose dehydrogenase; galactose 1-dehydrogenase; EC 1.. Enzyme Commission Number: EC 1.1.1.48. Galactose dehydrogenase. Activity: 80 U/mg protein. Storage: Store at -20°C. Form: Suspension in 3.2 M ammonium sulfate solution, pH approximately 6. Source: E. coli. Species: Pseudomonas fluorescens. D-galactose:NAD+ 1-oxidoreductase; D-galactose dehydrogenase; beta-galactose dehydrogenase; NAD+-dependent D-galactose dehydrogenase; galactose 1-dehydrogenase; EC 1.1.1.48; Galactose dehydrogenase. Cat No: NATE-1710. | |
| β-NADH, Reduced Disodium Salt (Nicotinamide Adenine Dinucleotide) | Beta-nicotinamide adenine dinucleotide hydrate. Can be used as a cofactor in reactions with NAD-dependent histone deacetylase enzymes.NAD is a coenzyme formed from the nucleotide, nicotinamide, adenosine monophosphateand a phosphate group joining the first two components. NADP has the same structure with the addition of an extra phosphate group to AMP. NAD can be reduced to NADH during coupling with reactions which oxidize various organic substrates. For example, the reaction catalyzed by glyceraldehyde phosphate dehydrogenase during glycolysis. NADH then passes to the inside of mitochondria where it donates the electrons it is carrying to the electron tran...accomplished by the removal of hydrogen atoms. Both of these coenzymes play crucial roles in this. Each molecule of NAD+ (or NADP+) can acquire two electrons; that is, be reduced by two electrons. However, only one proton accompanies the reduction. The other proton produced as two hydrogen atoms are removed from the molecule being oxidized is liberated into the surrounding medium. Group: Biochemicals. Alternative Names: β-DPNH; β-NADH; DPNH; Diphosphopyridine nucleotide, reduced form; NADH. Grades: Highly Purified. CAS No. 606-68-8. Pack Sizes: 1g, 5g, 10g. Molecular Formula: C21H27N7O14P2Na2, Molecular Weight: 709.41. US Biological Life Sciences. | Worldwide |
| β-Nicotinamide-Adenine Dinucleotide, Reduced Form (β-NADH) | NADH is a coenzyme that functions as a regenerating electron donor in catabolic processes including glycolysis, beta-oxidation and the citric acid cycle (Krebs cycle, TCA cycle). It participates in cell signaling events as well, for example as a substrate for the poly (ADP-ribose) polymerases (PARPs) during the DNA damage response. The NAD+/NADH dependent sirtuins play key roles in stress responses during events involving energy metabolism, with implications in cancer biology, diabetes and neurodegenerative disease. Group: Coenzymes. Synonyms. Enzyme Commission Number: EC 1.1.1.1. CAS No. 606-68-8. Purity: Dertermined by decrease in absorbance at 340 nm on enzymatic oxidation with ADH* at pH 10.0 > 95% *ADH = Alcohol dehydrogenase (yeast) (EC 1.1.1.1.). β-NADH. Mole weight: 709.41. Storage: Keep tightly stoppered in the dark below 5°C. Moisture will reduce the purity. For prolonged storage, keep below-20°C. Unstable in acids, but relatively stable at pH 10-11. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1; β-NADH. Cat No: NATE-0786. | |
| carbonyl reductase (NADPH) | Acts on a wide range of carbonyl compounds, including quinones, aromatic aldehydes, ketoaldehydes, daunorubicin and prostaglandins E and F, reducing them to the corresponding alcohol. Si-specific with respect to NADPH [cf. EC 1.1.1.2 alcohol dehydrogenase (NADP+)]. Group: Enzymes. Synonyms: aldehyde reductase 1; prostaglandin 9-ketoreductase; xenobiotic ketone reductase; NADPH-dependent carbonyl reductase; ALR3; carbonyl reductase; nonspecific NADPH-dependent carbonyl reductase; carbonyl reductase (NADPH2). Enzyme Commission Number: EC 1.1.1.184. CAS No. 89700-36-7. 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-0086; carbonyl reductase (NADPH); EC 1.1.1.184; 89700-36-7; aldehyde reductase 1; prostaglandin 9-ketoreductase; xenobiotic ketone reductase; NADPH-dependent carbonyl reductase; ALR3; carbonyl reductase; nonspecific NADPH-dependent carbonyl reductase; carbonyl reductase (NADPH2). Cat No: EXWM-0086. | |
| CBR 5884 | CBR 5884 is a 3-Phosphoglycerate dehydrogenase (PHGDH) inhibitor (IC50 = 33 μM), does not affect other NAD+-dependent dehydrogenases. Uses: 3-phosphoglycerate dehydrogenase (phgdh) inhibitor. Synonyms: CBR-5884; CBR 5884; CBR5884. Ethyl 5-[(2-furanylcarbonyl)amino]-3-methyl-4-thiocyanato-2-thiophenecarboxylate. Grades: ≥98%. CAS No. 681159-27-3. Molecular formula: C14H12N2O4S2. Mole weight: 336.39. | |
| Chemically modified Glucose-6-phosphate Dehydrogenase from Leuconostoc mesenteroides | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Applications: Use glucose-6-phosphate dehydrogenase for the determination of blood glucose or creatine kinase. Group: Enzymes. Synonyms: D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glu. Glucose-6-phosphate dehydrogenase. Mole weight: 110 kD (2 identical subunits 55,000 D). Activity: >30 U/mg lyophilizate. Stability: At +2 to +8°C within specification range for 18 months. Store dry. Appearance: White lyophilizate. Source: E. coli. Species: Leuconostoc mesenteroides. EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase; 9001-40-5. Cat No: DIA-280. | |
| 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. | |
| cis-2-enoyl-CoA reductase (NADPH) | Not identical with EC 1.3.1.38 trans-2-enoyl-CoA reductase (NADPH) [cf. EC 1.3.1.8 acyl-CoA dehydrogenase (NADP+)]. Group: Enzymes. Synonyms: NADPH-dependent cis-enoyl-CoA reductase; reductase, cis-2-enoyl coenzyme A; cis-2-enoyl-coenzyme A reductase; cis-2-enoyl-CoA reductase (NADPH). Enzyme Commission Number: EC 1.3.1.37. CAS No. 72841-00-0. 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-1309; cis-2-enoyl-CoA reductase (NADPH); EC 1.3.1.37; 72841-00-0; NADPH-dependent cis-enoyl-CoA reductase; reductase, cis-2-enoyl coenzyme A; cis-2-enoyl-coenzyme A reductase; cis-2-enoyl-CoA reductase (NADPH). Cat No: EXWM-1309. | |
| D-2-Hydroxyglutarate Dehydrogenase from Acidaminococcus fermentans, Recombinant | D-2-hydroxyglutarate (D2HG) level is significantly increased in metabolic diseases and various cancers such as acute myeloid leukemia. Studies suggest that the detection of D2HG serves as a biomarker assay related to IDH (isocitrate dehydrogenase) mutations. D2HGDH is a special NAD-dependent enzyme which reacts with D2HG specifically and converts D2HG to α-ketoglutarate. D2HGDH is a key enzyme to distinguish between two metabolites, D2HG and L-2-hydroxyglutarate (L2HG), during biomarker assays. Group: Enzymes. Synonyms: D-2-hydroxyglutarate dehydrogenase; D2HGDH; D2HGD. Enzyme Commission Number: EC 1.1.99.39. Purity: > 99% by SDS - PAGE. Mole weight: 39 kDa. Activity: > 90,000 mU/mg. Storage: Can be stored at 4°C up to 2 weeks. For long term storage, aliquot and store at -20°C. Avoid repeated freezing and thawing cycles. Form: Lyophilized in 50mM Tris, pH 8 without any additives. Source: E. coli. Species: Acidaminococcus fermentans. D-2-hydroxyglutarate dehydrogenase; D2HGDH; D2HGD. Cat No: NATE-1660. | |
| D-arabinitol dehydrogenase (NADP+) | The enzyme from the rust fungus Uromyces fabae can use D-arabinitol and D-mannitol as substrates in the forward direction and D-xylulose, D-ribulose and, to a lesser extent, D-fructose as substrates in the reverse direction. This enzyme carries out the reactions of both EC 1.1.1.11, D-arabinitol 4-dehydrogenase and EC 1.1.1.250, D-arabinitol 2-dehydrogenase, but unlike them, uses NADP+ rather than NAD+ as cofactor. D-Arabinitol is capable of quenching reactive oxygen species involved in defense reactions of the host plant. Group: Enzymes. Synonyms: NADP+-dependent D-arabitol dehydrogenase; ARD1p; D-arabitol dehydrogenase 1. Enzyme Commission Number: EC 1.1.1.287. 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-0195; D-arabinitol dehydrogenase (NADP+); EC 1.1.1.287; NADP+-dependent D-arabitol dehydrogenase; ARD1p; D-arabitol dehydrogenase 1. Cat No: EXWM-0195. | |
| D-galactose 1-dehydrogenase | This enzyme is part of the De Ley-Doudoroff pathway, which is used by some bacteria during growth on D-galactose. Group: Enzymes. Synonyms: D-galactose dehydrogenase; β-galactose dehydrogenase (ambiguous); NAD+-dependent D-galactose dehydrogenase. Enzyme Commission Number: EC 1.1.1.48. CAS No. 9028-54-0. Galactose dehydrogenase. 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-0333; D-galactose 1-dehydrogenase; EC 1.1.1.48; 9028-54-0; D-galactose dehydrogenase; β-galactose dehydrogenase (ambiguous); NAD+-dependent D-galactose dehydrogenase. Cat No: EXWM-0333. | |
| D-xylulose reductase | Also acts as an L-erythrulose reductase. Group: Enzymes. Synonyms: NAD+-dependent xylitol dehydrogenase; xylitol dehydrogenase (ambiguous); erythritol dehydrogenase; 2,3-cis-polyol(DPN) dehydrogenase (C3-5); pentitol-DPN dehydrogenase (ambiguous); xylitol-2-dehydrogenase. Enzyme Commission Number: EC 1.1.1.9. CAS No. 9028-16-4. 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-0373; D-xylulose reductase; EC 1.1.1.9; 9028-16-4; NAD+-dependent xylitol dehydrogenase; xylitol dehydrogenase (ambiguous); erythritol dehydrogenase; 2,3-cis-polyol(DPN) dehydrogenase (C3-5); pentitol-DPN dehydrogenase (ambiguous); xylitol-2-dehydrogenase. Cat No: EXWM-0373. | |
| EC 1.1.1.47 | EC 1.1.1.47. Synonyms: glucose dehydrogenase F. bacillus mega-terium;Dehydrogenase, glucose;GLUCOSE DEHYDROGENASE THERMOPLASMA,*ACID OPHILUM REC;BETA-D-GLUCOSE: NADP+ 1-OXIDOREDUCTASE;GLUCOSE DEHYDROGENASE;GLUCOSE DEHYDROGENASE, NADP DEPENDENT;GDH;EC 1.1.1.47. CAS No. 9028-53-9. Product ID: CDF4-0056. Category: Enzyme Preparations. Product Keywords: Food Ingredients; Enzyme Preparations; EC 1.1.1.47; CDF4-0056; 9028-53-9; 232-836-9; 9028-53-9. Purity: 0.99. Color: White. EC Number: 232-836-9. Physical State: Powder. Storage: -20°C. Application: Diagnostics and cofactor regeneration of NAD(P)H in reductive processes. Product Description: This product has been enhanced for energy efficiency and waste prevention when used in biofuel cell research. |  |
| enoyl-[acyl-carrier-protein] reductase (NADPH) | The enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to the acyl-carrier protein, in an NADPH-dependent manner. This entry stands for enzymes whose stereo-specificity with respect to NADP+ is not known. [cf. EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific), EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH)]. Group: Enzymes. Synonyms: acyl-ACP dehydrogenase (ambiguous); enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl-ACP reductase (ambiguous); fabL (gene name). Enzyme Commission Number: EC 1.3.1.104. 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-1276; enoyl-[acyl-carrier-protein] reductase (NADPH); EC 1.3.1.104; acyl-ACP dehydrogenase (ambiguous); enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl-ACP reductase (ambiguous); fabL (gene name). Cat No: EXWM-1276. | |
| FAD-dependent glucose dehydrogenase | FAD-dependent glucose dehydrogenase (EC 1.1.5.9), or glucose dehydrogenase (FAD)/Pseudomonas glucose dehydrogenase. Glucose 1-dehydrogenase is an enzyme used as a regeneration cofactor to convert glucose and NAD(P) into NAD(P)H and gluconic acid [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: FAD-GDH; Glucose 1-dehydrogenase. CAS No. 37250-84-3. Pack Sizes: 1 KU. Product ID: HY-E70014. |  |
| flavin reductase (NADPH) | The enzyme reduces riboflavin, and, less efficiently, FMN and FAD. NADH is oxidized less efficiently than NADPH. Group: Enzymes. Synonyms: NADPH:flavin oxidoreductase; riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide phosphate) reductase; flavin mononucleotide reductase; flavine mononucleotide reductase; FMN reductase (NADPH); NADPH-dependent FMN reductase; NADPH-flavin reductase; NADPH-FMN reductase; NADPH-specific FMN reductase; riboflavin mononucleotide reductase; riboflavine mononucleotide reductase; NADPH2 dehydrogenase (flavin); NADPH2:riboflavin oxidoreductase. Enzyme Commission Number: EC 1.5.1.30. CAS No. 56626-29-0. 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-1512; flavin reductase (NADPH); EC 1.5.1.30; 56626-29-0; NADPH:flavin oxidoreductase; riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide phosphate) reductase; flavin mononucleotide reductase; flavine mononucleotide reductase; FMN reductase (NADPH); NADPH-dependent FMN reductase; NADPH-flavin reductase; NADPH-FMN reductase; NADPH-specific FMN reductase; riboflavin mononucleotide reductase; riboflavine mononucleotide reductase; NADPH2 dehydrogenase (flavin); NADPH2:riboflavin oxidoreductase. Cat No: EXWM-1512. | |
| formaldehyde 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 formaldehyde:NAD+ oxidoreductase. Other names in common use include NAD+-linked formaldehyde dehydrogenase, s-nitrosoglutathione reductase (GSNO reductase) and NAD+-dependent formaldehyde dehydrogenase. This enzyme participates in methane metabolism. Group: Enzymes. Synonyms: NAD-linked formaldehyde dehydrogenase; NAD-dependent formaldehyde dehydrogenase. Enzyme Commission Number: EC 1.2.1.46. CAS No. 9028-84-6. Formaldehyde Dehydrogenase. 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-1149; formaldehyde dehydrogenase; EC 1.2.1.46; 9028-84-6; NAD-linked formaldehyde dehydrogenase; NAD-dependent formaldehyde dehydrogenase. Cat No: EXWM-1149. | |
| formate dehydrogenase | The enzyme from most aerobic organisms is devoid of redox-active centres but that from the proteobacterium Methylosinus trichosporium contains iron-sulfur centres, flavin and a molybdenum centre. Together with EC 1.12.1.2 hydrogen dehydrogenase, forms a system previously known as formate hydrogenlyase. Group: Enzymes. Synonyms: formate-NAD oxidoreductase; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Enzyme Commission Number: EC 1.2.1.2. CAS No. 9028-85-7. FDH. 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-1125; formate dehydrogenase; EC 1.2.1.2; 9028-85-7; formate-NAD oxidoreductase; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Cat No: EXWM-1125. | |
| Formate Dehydrogenase (Crude Enzyme) | Formate Dehydrogenases are a set of enzymes that catalyse the oxidation of formate to carbon dioxide, donating the electrons to a second substrate, such as NAD + in formate:NAD + oxidoreductase (EC 1. 2. 1. 2) or to a cytochrome in formate:ferricytochrome-b1 oxidoreductase (EC 1. 2. 2. 1). This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; biotechnology; medicine; analysis. Group: Enzymes. Synonyms: formate-NAD oxidoreductase; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Enzyme Commission Number: EC 1.2.1.2. CAS No. 9028-85-7. FDH. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. formate-NAD oxidoreductase; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Pack: 100ml. Cat No: NATE-1799. | |
| Formate Dehydrogenase from Recombinant E. coli | Formate dehydrogenase is involved in the stress response of plants and catalyzes the reduction of NAD+ to NADH. Group: Enzymes. Synonyms: EC 1.2.1.2; 9028-85-7; formate-NAD oxidoreductase; FDH; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Enzyme Commission Number: EC 1.2.1.2. CAS No. 9028-85-7. Purity: 5% - 25%. FDH. Activity: 0.5-2.0 u/mg. Storage: 0-10°C. Form: Powder. Source: E. coli. EC 1.2.1.2; 9028-85-7; formate-NAD oxidoreductase; FDH; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Cat No: NATE-1783. | |
| formate dehydrogenase (NADP+) | A tungsten-selenium-iron protein. Group: Enzymes. Synonyms: NADP-dependent formate dehydrogenase; formate dehydrogenase (NADP). Enzyme Commission Number: EC 1.2.1.43. CAS No. 51377-43-6. 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-1147; formate dehydrogenase (NADP+); EC 1.2.1.43; 51377-43-6; NADP-dependent formate dehydrogenase; formate dehydrogenase (NADP). Cat No: EXWM-1147. | |
| Galactose dehydrogenase from recombinant E. coli | In enzymology, a galactose 1-dehydrogenase (EC 1.1.1.48) is an enzyme that catalyzes the chemical reaction: D-galactose + NAD+ rightleftharpoons D-galactono-1,4-lactone + NADH + H+. Thus, the two substrates of this enzyme are D-galactose and NAD+, whereas its 3 products are D-galactono-1,4-lactone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in galactose metabolism. Group: Enzymes. Synonyms: D-galactose:NAD+ 1-oxidoreductase; D-galactose dehydrogenase; beta-galactose dehydrogenase; NAD+-dependent D-galactose dehydrogenase; galactose 1-dehydrogenase; EC 1.1.1.48; Galactose dehydrogenase. Enzyme Commission Number: EC 1.1.1.48. CAS No. 9028-54-0. Galactose dehydrogenase. Mole weight: ca. 33,800. Activity: more than 80 U/mg protein. Stability: Stable at 4 °C for at least one year. Storage: Store at 4 to 10 °C (Do not freeze). Form: Ammonium sulphate suspension. Source: E. coli. D-galactose:NAD+ 1-oxidoreductase; D-galactose dehydrogenase; beta-galactose dehydrogenase; NAD+-dependent D-galactose dehydrogenase; galactose 1-dehydrogenase; EC 1.1.1.48; Galactose dehydrogenase. Cat No: NATE-1931. | |
| glucose 1-dehydrogenase (NADP+) | Also oxidizes D-mannose, 2-deoxy-D-glucose and 2-amino-2-deoxy-D-mannose. Group: Enzymes. Synonyms: nicotinamide adenine dinucleotide phosphate-linked aldohexose dehydrogenase; NADP-linked aldohexose dehydrogenase; NADP-dependent glucose dehydrogenase; glucose 1-dehydrogenase (NADP). Enzyme Commission Number: EC 1.1.1.119. CAS No. 37250-50-3. 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-0022; glucose 1-dehydrogenase (NADP+); EC 1.1.1.119; 37250-50-3; nicotinamide adenine dinucleotide phosphate-linked aldohexose dehydrogenase; NADP-linked aldohexose dehydrogenase; NADP-dependent glucose dehydrogenase; glucose 1-dehydrogenase (NADP). Cat No: EXWM-0022. | |
| glucose-6-phosphate dehydrogenase (coenzyme-F420) | The enzyme is very specific for D-glucose 6-phosphate. No activity with NAD+, NADP+, FAD and FMN. Group: Enzymes. Synonyms: coenzyme F420-dependent glucose-6-phosphate dehydrogenase; F420-dependent glucose-6-phosphate dehydrogenase; FGD1; Rv0407; F420-dependent glucose-6-phosphate dehydrogenase 1. Enzyme Commission Number: EC 1.1.98.2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0439; glucose-6-phosphate dehydrogenase (coenzyme-F420); EC 1.1.98.2; coenzyme F420-dependent glucose-6-phosphate dehydrogenase; F420-dependent glucose-6-phosphate dehydrogenase; FGD1; Rv0407; F420-dependent glucose-6-phosphate dehydrogenase 1. Cat No: EXWM-0439. | |
| Glucose-6-phosphate Dehydrogenase from E. coli, Recombinant | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Group: Enzymes. Synonyms: EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate . Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Mole weight: ~ 56,770. Activity: 172 U/mg. Stability: > 2 years. Storage: 4°C. Form: In 3.2 M ammonium sulphate. Source: E. coli. Species: E. coli. EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase; 9001-40-5. Cat No: DIA-407. | |
| glucose-6-phosphate dehydrogenase (NADP+) | The enzyme catalyses a step of the pentose phosphate pathway. The enzyme is specific for NADP+. cf. EC 1.1.1.363, glucose-6-phosphate dehydrogenase [NAD(P)+] and EC 1.1.1.388, glucose-6-phosphate dehydrogenase (NAD+). Group: Enzymes. Synonyms: NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. 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-0334; glucose-6-phosphate dehydrogenase (NADP+); EC 1.1.1.49; 9001-40-5; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase. Cat No: EXWM-0334. | |
| 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 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)) 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 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. | |
| Glyceraldehyde-3-phosphate dehydrogenase from Human, Recombinant | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a tetramer of 36 kDa subunits, is a catalytic enzyme involved in glycolysis. GAPDH catalyzes the reversible reduction of glyceraldehyde-3-phosphate to 3-phosphoglycerol phosphate in the presence of NAD+. Besides functioning as a glycolytic enzyme in the cytoplasm, mammalian GAPDH is also involved in a variety of intracellular processes such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication, and DNA repair. Glyceraldehyde-3-phosphate dehydrogenase was also found to bind to mutant polyglutamine proteins formed in neurodegenerative diseases such as Huntingto...horylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phosphate dehydrogenase (NAD+); glyceraldehyde-3-phosphate dehydrogenase (NAD+); NADH-glyceraldehyde phosphate dehydrogenase; glyceraldehyde-3-P-dehydrogenase; 9001-50-7. Glyceraldehyde-3-phosphate Dehydrogenase. Mole weight: 37,984 Da. Activity: > 80 units/mg protein. Stability: Store at -20°C. Form: Lyophilized from a buffered solution with stabilizers. Source: E. coli. Species: Human. EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate | |
| glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) | NAD+ and NADP+ can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and EC 1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating), which are NAD+- and NADP+-dependent, respectively. Group: Enzymes. Synonyms: triosephosphate dehydrogenase (NAD(P)); glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating). Enzyme Commission Number: EC 1.2.1.59. CAS No. 39369-25-0. 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-1161; glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating); EC 1.2.1.59; 39369-25-0; triosephosphate dehydrogenase (NAD(P)); glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating). Cat No: EXWM-1161. | |
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