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| Product | Description | |
|---|---|---|
| NADH dehydrogenase | A flavoprotein containing iron-sulfur centres. After preparations have been subjected to certain treatments, cytochrome c may act as an acceptor. Under normal conditions, two protons are extruded from the cytoplasm or the intramitochondrial or stromal compartment. Present in a mitochondrial complex as EC 1.6.5.3, NADH dehydrogenase (ubiquinone). Group: Enzymes. Synonyms: cytochrome c reductase; type 1 dehydrogenase; β-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine dinucleotide dehydrogenase; diphosphopyridine diaphorase; DPNH diaphorase; NADH diaphorase; NADH hydroge. Enzyme Commission Number: EC 1.6.99.3. CAS No. 9079-67-8. Diaphorase. 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-1601; NADH dehydrogenase; EC 1.6.99.3; 9079-67-8; cytochrome c reductase; type 1 dehydrogenase; β-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine dinucleotide dehydrogenase; diphosphopyridine diaphorase; DPNH diaphorase; NADH diaphorase; NADH hydrogenase; NADH oxidoreductase; NADH-menadione oxidoreductase; reduced diphosphopyridine nucleotide diaphorase; NADH:cytochrome c oxidoreductase; NADH2 dehydrogenase; NADH:(acceptor) oxidoreductase. Cat No: EXWM-1601. |  |
| NADH dehydrogenase (quinone) | Menaquinone can act as acceptor. Inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. Group: Enzymes. Synonyms: reduced nicotinamide adenine dinucleotide (quinone) dehydrogenase; NADH-quinone oxidoreductase; DPNH-menadione reductase; D-diaphorase; NADH2 dehydrogenase (quinone). Enzyme Commission Number: EC 1.6.5.11. CAS No. 37256-36-3. 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-1589; NADH dehydrogenase (quinone); EC 1.6.5.11; 37256-36-3; reduced nicotinamide adenine dinucleotide (quinone) dehydrogenase; NADH-quinone oxidoreductase; DPNH-menadione reductase; D-diaphorase; NADH2 dehydrogenase (quinone). Cat No: EXWM-1589. | |
| 3-Acetylpyridine Adenine Dinucleotide (APAD) | APAD is an NAD analog with higher oxidation potential than NAD. It can substitute for NAD as a hydrogen-accepting cofactor in many dehydrogenase reactions; e.g. lactate dehydrogenase from Toxoplasma, Clonorchis, and Plasmodium, bacterial lipoamide dehydrogenase, as well as mammalian dehydrogenases. It can also act as a proton acceptor in various transhydrogenation reactions with NADH or NADPH. Group: Biochemicals. Alternative Names: APAD; adenosine 5'-(trihydrogen diphosphate), P?5-ester with 3-acetyl-1- β -D-ribofuranosyl pyridinium , inner salt. Grades: Purified. CAS No. 86-08-8. Pack Sizes: 10mg, 25mg, 50mg, 100mg, 250mg. Molecular Formula: C22H28N6O14P2, Molecular Weight: 662.44. US Biological Life Sciences. |  Worldwide |
| 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. | |
| 3α-Hydroxysteroid Dehydrogenase from B. choshinensis, Recombinant | In enzymology, a 3alpha-hydroxysteroid dehydrogenase (B-specific) (EC 1.1.1.50) is an enzyme that catalyzes the chemical reaction: androsterone + NAD(P)+ <-> 5alpha-androstane-3,17-dione + NAD(P)H + H+. The 3 substRates of this enzyme are androsterone, NAD+, and NADP+, whereas its 4 products are 5alpha-androstane-3,17-dione, NADH, NADPH, 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, more specifically it is part of the group of hydroxysteroid dehydrogenases. Group: Enzymes. Synonyms: hydroxyprostaglandin dehydrogenase; 3α-hydroxysteroid oxidoreductase; sterognost 3α; 3α-hydroxysteroid dehydrogenas. Enzyme Commission Number: EC 1.1.1.50. CAS No. 9028-56-2. 3α-Hydroxysteroid Dehydrogenase. Mole weight: ca. 41 kDa. Activity: > 30 U/mg lyophilizate. Stability: stable at 37°C for at least four weeks. Appearance: White lyophilizate. Storage: at -20°C. Source: B. choshinensis. Species: B. choshinensis. hydroxyprostaglandin dehydrogenase; 3α-hydroxysteroid oxidoreductase; sterognost 3α; 3α-hydroxysteroid dehydrogenase (B-specific); 3α-hydroxysteroid 3-dehydrogenase (B-specific); 3α-hydroxysteroid:NAD(P)+ 3-oxidoreductase (B-specific); EC 1.1.1.50. Cat No: DIA-413. | |
| 3α-Hydroxysteroid Dehydrogenase, Recombinant | In enzymology, a 3alpha-hydroxysteroid dehydrogenase (B-specific) (EC 1.1.1.50) is an enzyme that catalyzes the chemical reaction: androsterone + NAD (P)+ ? 5alpha-androstane-3,17-dione + NAD (P)H + H+. The 3 substRates of this enzyme are androsterone, NAD+, and NADP+, whereas its 4 products are 5alpha-androstane-3,17-dione, NADH, NADPH, 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, more specifically it is part of the group of hydroxysteroid dehydrogenases. Applications: Bile acid is one of the substrates of 3α-hydroxy steroiddehydrogenase. 3α-hydroxy ste...3-dehydrogenase (B-specific); 3α-hydroxysteroid:NAD (P)+ 3-oxidoreductase (B-specific); EC 1.1.1.50. Enzyme Commission Number: EC 1.1.1.50. Purity: 90% (SDS-PAGE test). Mole weight: About 28 kDa (SDS-PAGE detection). Activity: About 50U/mg powder. Appearance: White powder, lyophilized. Storage: 4°C, store at -20°C for long-term preservation. Form: Freeze dried powder. hydroxyprostaglandin dehydrogenase; 3α-hydroxysteroid oxidoreductase; sterognost 3α; 3α-hydroxysteroid dehydrogenase (B-specific); 3α-hydroxysteroid 3-dehydrogenase (B-specific); 3α-hydroxysteroid:NAD (P)+ 3-oxidoreductase (B-specific); EC 1.1.1.50. Cat No: NATE-1138. | |
| 3α(or 20β)-hydroxysteroid dehydrogenase | The 3α-hydroxy group or 20β-hydroxy group of pregnane and androstane steroids can act as donor. Group: Enzymes. Synonyms: cortisone reductase; (R)-20-hydroxysteroid dehydrogenase; dehydrogenase, 20β-hydroxy steroid; Δ4-3-ketosteroid hydrogenase; 20β-hydroxysteroid dehydrogenase; 3α,20β-hydroxysteroid:NAD+-oxidoreductase; NADH-20β-hydroxysteroid dehydrogenase; 20β-HSD. Enzyme Commission Number: EC 1.1.1.53. CAS No. 9028-42-6. 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-0338; 3α(or 20β)-hydroxysteroid dehydrogenase; EC 1.1.1.53; 9028-42-6; cortisone reductase; (R)-20-hydroxysteroid dehydrogenase; dehydrogenase, 20β-hydroxy steroid; Δ4-3-ketosteroid hydrogenase; 20β-hydroxysteroid dehydrogenase; 3α,20β-hydroxysteroid:NAD+-oxidoreductase; NADH-20β-hydroxysteroid dehydrogenase; 20β-HSD. Cat No: EXWM-0338. | |
| 3-(Aminocarbonyl)-1-(2,3,5-tri-O-acetyl- β-D-ribofuranosyl)-pyridinium-d4 Triflate | 3-(Aminocarbonyl)-1-(2,3,5-tri-O-acetyl- β-D-ribofuranosyl)-pyridinium-d4 Triflate is an intermediate in the synthesis of β-NADH-d5 (d5-major) Diammonium Salt (N201487). β-NADH-d4 is labelled β-NADH (N201480, Disodium salt). β-NADH is one of the biologically active forms of nicotinic acid. Serves as a coenzyme of hydrogenases and dehydrogenases. NAD usually acts as a hydrogen acceptor, forming NADH which then serves as a hydrogen donor in the respiratory chain. Present in living cells primarily in the reduced form (NADPH) and is involved in synthetic reactions. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 2.5mg, 25mg. Molecular Formula: C17H17D4N2O8+; CF3O3S-. US Biological Life Sciences. | Worldwide |
| 4-hydroxy-2-oxovalerate aldolase | Requires Mn2+ for maximal activity. The enzyme from the bacterium Pseudomonas putida is also stimulated by NADH. In some bacterial species the enzyme forms a bifunctional complex with EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase. Group: Enzymes. Synonyms: 4-hydroxy-2-ketovalerate aldolase; HOA; DmpG; 4-hydroxy-2-oxovalerate pyruvate-lyase; 4-hydroxy-2-oxopentanoate pyruvate-lyase; BphI; 4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming). Enzyme Commission Number: EC 4.1.3.39. CAS No. 37325-52-3. 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-4915; 4-hydroxy-2-oxovalerate aldolase; EC 4.1.3.39; 37325-52-3; 4-hydroxy-2-ketovalerate aldolase; HOA; DmpG; 4-hydroxy-2-oxovalerate pyruvate-lyase; 4-hydroxy-2-oxopentanoate pyruvate-lyase; BphI; 4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming). Cat No: EXWM-4915. | |
| 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 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. | |
| asparagusate reductase | Also acts on lipoate. Group: Enzymes. Synonyms: asparagusate dehydrogenase; asparagusic dehydrogenase; asparagusate reductase (NADH2); NADH2:asparagusate oxidoreductase. Enzyme Commission Number: EC 1.8.1.11. CAS No. 56126-52-4. 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-1637; asparagusate reductase; EC 1.8.1.11; 56126-52-4; asparagusate dehydrogenase; asparagusic dehydrogenase; asparagusate reductase (NADH2); NADH2:asparagusate oxidoreductase. Cat No: EXWM-1637. | |
| 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. | |
| butanoyl-CoA dehydrogenase (NAD+, ferredoxin) | This flavin containg enzyme, isolated from the bacteria Acidaminococcus fermentans and butanoate-producing Clostridia species, couples the exergonic reduction of (E)-but-2-enoyl-CoA to butanoyl-CoA with NADH to the endergonic reduction of ferredoxin by NADH, using electron bifurcation to overcome the steep energy barrier in ferredoxin reduction. Group: Enzymes. Synonyms: bifurcating butyryl-CoA dehydrogenase; butyryl-CoA dehydrogenase/Etf complex; Etf-Bcd complex; bifurcating butanoyl-CoA dehydrogenase; butanoyl-CoA dehydrogenase/Etf complex. Enzyme Commission Number: EC 1.3.1.109. 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-1281; butanoyl-CoA dehydrogenase (NAD+, ferredoxin); EC 1.3.1.109; bifurcating butyryl-CoA dehydrogenase; butyryl-CoA dehydrogenase/Etf complex; Etf-Bcd complex; bifurcating butanoyl-CoA dehydrogenase; butanoyl-CoA dehydrogenase/Etf complex. Cat No: EXWM-1281. | |
| 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. | |
| Citrinin | Citrinin is a quinonemethine mycotoxin produced by diverse fungal genera, including Aspergillus and Penicillium. Citrinin has been extensively investigated. It is a potent nephrotoxin with hepatoxic and teratogenic activity. It is the causative agent of Balkan nephropathy and yellow rice fever in humans. At the molecular level, citrinin exhibits a range of effects including free radical damage to DNA and disruption to a wide variety of mitochrondrial membrane-bound enzymic activities and structural integrity. Specifically, citrinin is an inhibitor of NADH dehydrogenase in the mitochondrial electron transport chain and this action is responsible for recent reports of citrinin's apoptotic activity. Group: Biochemicals. Grades: Highly Purified. CAS No. 518-75-2. Pack Sizes: 1mg. US Biological Life Sciences. | Worldwide |
| D-2-hydroxyacid dehydrogenase (NADP+) | This enzyme, characterized from the halophilic archaeon Haloferax mediterranei and the mold Aspergillus oryzae, catalyses a stereospecific reduction of 2-oxocarboxylic acids into the corresponding D-2-hydroxycarboxylic acids. The enzyme prefers substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain, and can use NADH with much lower efficiency. cf. EC 1.1.1.345, (D)-2-hydroxyacid dehydrogenase (NAD+). Group: Enzymes. Synonyms: ddh (gene name). Enzyme Commission Number: EC 1.1.1.272. CAS No. 81210-65-3. 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-0179; D-2-hydroxyacid dehydrogenase (NADP+); EC 1.1.1.272; 81210-65-3; ddh (gene name). Cat No: EXWM-0179. | |
| D-3-hydroxybutyrate dehydrogenase from Microorganism | In enzymology, a 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) is an enzyme that catalyzes the chemical reaction: (R)-3-hydroxybutanoate + NAD+ ? acetoacetate + NADH + H+. Thus, the two substrates of this enzyme are (R)-3-hydroxybutanoate and NAD+, whereas its three products are acetoacetate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in synthesis and degradation of ketone bodies and butanoate metabolism. Group: Enzymes. Synonyms: (R)-3-hydroxybutanoate: NAD+ oxidoreductase; NAD+-beta-hydroxybutyrate dehydro. Enzyme Commission Number: EC 1.1.1.30. CAS No. 9028-38-0. Mole weight: 27.5 kDa (SDS-PAGE). Activity: >300U/mg. Storage: Store at -20°C. Form: Yellowish powder, lyophilized. Source: Microorganism. (R)-3-hydroxybutanoate: NAD+ oxidoreductase; NAD+-beta-hydroxybutyrate dehydrogenase; hydroxybutyrate oxidoreductase; beta-hydroxybutyrate dehydrogenase; D-beta-hydroxybutyrate dehydrogenase; D-3-hydroxybutyrate dehydrogenase; D-( - )-3-hydroxybutyrate dehydrogenase; beta-hydroxybutyric acid dehydrogenase; 3-D-hydroxybutyrate dehydrogenase; beta-hydroxybutyric dehydrogenase; EC 1.1.1.30; 9028-38-0; HBDH; β-Hydroxybutyrate Dehydrogenase; 3-Hydroxybutyrate Dehydrogenase. Cat No: NATE-1714. | |
| Diaphorase 22 from Recombinant E.coli | A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system (click here for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoami...(NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate dehydrogenase; lipoic acid dehydrogenase; lipoyl dehydrogenase; protein-6-N-(dihydrolipoyl)lysine:NAD+ oxidoreductase. Enzyme Commission Number: EC 1.8.1.4. CAS No. 9001-18-7. Diaphorase. Mole weight: ca. 110,000. Activity: >150 U/mg protein. Storage: Store at -20°C. Form: Lyophilized. Source: E. coli. LDP-Glc; LDP-Val; dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxidoreductase (NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate d | |
| Diaphorase from microorganism | Diaphorase from microorganism. Better stability and reactivity than dia-187. Group: Enzymes. Synonyms: dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxidoreductase (NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate dehydrogenase; lipoic acid dehydrogenase; lipoyl dehydrogenase; dihydrolipoyl dehydrogenase; Lipoamide Dehydrogenase. Enzyme Commission Number: EC 1.6.99.-. Diaphorase. Source: Microorganism. dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxidoreductase (NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate dehydrogenase; lipoic acid dehydrogenase; lipoyl dehydrogenase; dihydrolipoyl dehydrogenase; EC 1.8.1.4; 9001-18-7; Lipoamide Dehydrogenase. Cat No: DIA-275. | |
| dihydrolipoyl dehydrogenase | A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system (click here for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoamide or...tase (NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate dehydrogenase; lipoic acid dehydrogenase; lipoyl dehydrogenase; protein-6-N-(dihydrolipoyl)lysine:NAD+ oxidoreductase. Enzyme Commission Number: EC 1.8.1.4. CAS No. 9001-18-7. Diaphorase. 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-1648; dihydrolipoyl dehydrogenase; EC 1.8.1.4; 9001-18-7; LDP-Glc; LDP-Val; dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxido | |
| dihydroorotate dehydrogenase (NAD+) | Binds FMN, FAD and a [2Fe-2S] cluster. The enzyme consists of two subunits, an FMN binding catalytic subunit and a FAD and iron-sulfur binding electron transfer subunit. The reaction, which takes place in the cytosol, is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides. Other class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1) or NADP+ (EC 1.3.1.15) as electron acceptor. The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor. Group: Enzymes. Synonyms: orotate reductase (NADH); orotate reductase (NADH2); DHOdehase (ambiguous); DHOD (ambiguous); DHODase (ambiguous); dihydroorotate oxidase, pyrD (gene name). Enzyme Commission Number: EC 1.3.1.14. CAS No. 37255-26-8. 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-1288; dihydroorotate dehydrogenase (NAD+); EC 1.3.1.14; 37255-26-8; orotate reductase (NADH); orotate reductase (NADH2); DHOdehase (ambiguous); DHOD (ambiguous); DHODase (ambiguous); dihydroorotate oxidase, pyrD (gene name). Cat No: EXWM-1288. | |
| 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 | |
| (-)-endo-fenchol dehydrogenase | Isolated from the plant Foeniculum vulgare (fennel). NADH is slightly preferred to NADPH. Group: Enzymes. Synonyms: l-endo-fenchol dehydrogenase; FDH. Enzyme Commission Number: EC 1.1.1.322. 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-0235; (-)-endo-fenchol dehydrogenase; EC 1.1.1.322; l-endo-fenchol dehydrogenase; FDH. Cat No: EXWM-0235. | |
| 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. | |
| enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) | One of the activities of EC 2.3.1.86, fatty-acyl-CoA synthase, an enzyme found in yeasts (Ascomycota and the Basidiomycota). Catalyses the reduction of enoyl-acyl-[acyl-carrier protein] derivatives of carbon chain length from 4 to 16. The yeast enzyme is Si-specific with respect to NADP+. cf. EC 1.3.1.39, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH), which describes enzymes whose stereo-specificity towards NADPH is not known. See also EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH). Group: Enzymes. Synonyms: acy. Enzyme Commission Number: EC 1.3.1.10. CAS No. 37251-09-5. 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-1271; enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific); EC 1.3.1.10; 37251-09-5; acyl-ACP dehydrogenase (ambiguous); enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl acyl-carrier-protein reductase (ambiguous); enoyl-ACP reductase (ambiguous); acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (B-specific); acyl-[acyl-carrier protein]:NADP+ oxidoreductase (B-specific); enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific). Cat No: EXWM-1271. | |
| 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. | |
| 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 Dehydrogenases | recycling NADH. Group: Enzymes. Synonyms: Formate Dehydrogenases; FDH. Form: Enzyme Powder: 4 items*50mg / item, or other quantity. Formate Dehydrogenases; FDH; Screening Kit; library of enzyme; enzyme library. Cat No: ENLC-016. | |
| fumarate reductase (CoM/CoB) | The enzyme, isolated from the archaeon Methanobacterium thermoautotrophicum, is very oxygen sensitive. It cannot use reduced flavins, reduced coenzyme F420, or NAD(P)H as an electron donor. Distinct from EC 1.3.1.6 [fumarate reductase (NADH)], EC 1.3.5.1 [succinate dehydrogenase (ubiquinone)], and EC 1.3.5.4 [fumarate reductase (quinol)]. Group: Enzymes. Synonyms: thiol:fumarate reductase; Tfr. Enzyme Commission Number: EC 1.3.4.1. 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-1384; fumarate reductase (CoM/CoB); EC 1.3.4.1; thiol:fumarate reductase; Tfr. Cat No: EXWM-1384. | |
| 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 Dehydrogenase from E. coli, Recombiant | In enzymology, a glucose 1-dehydrogenase (EC 1.1.1.47) is an enzyme that catalyzes the chemical reaction:beta-D-glucose + NAD (P)+<-> D-glucono-1,5-lactone + NAD (P)H + H+. The 3 substrates of this enzyme are beta-D-glucose, NAD+, and NADP+, whereas its 4 products are D-glucono-1,5-lactone, NADH, NADPH, 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. Applications: This enzyme is useful for determination of glucose. Group: Enzymes. Synonyms: EC 1.1.1.47; D-glucose dehydrogenase (NAD (P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD (P)+ 1-oxidoreductase; glucose 1-dehydrogenase; Glucose dehydrogenase; 9028-53-9. Enzyme Commission Number: EC 1.1.1.47. CAS No. 9028-53-9. Glucose Dehyrogenase. Mole weight: ca. 126,000; Subunit molecular weight : ca. 31,500. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: E. coli. EC 1.1.1.47; D-glucose dehydrogenase (NAD (P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD (P)+ 1-oxidoreductase; glucose 1-dehydrogenase; Glucose dehydrogenase; 9028-53-9. Cat No: NATE-1902. | |
| Glucose Dehydrogenase, Recombinant | In enzymology, a glucose 1-dehydrogenase (EC 1.1.1.47) is an enzyme that catalyzes the chemical reaction:beta-D-glucose + NAD (P)+? D-glucono-1,5-lactone + NAD (P)H + H+. The 3 substrates of this enzyme are beta-D-glucose, NAD+, and NADP+, whereas its 4 products are D-glucono-1,5-lactone, NADH, NADPH, 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. Applications: Gdh can be used as the raw material enzyme in clinic diagnostic of blood glucose. Group: Enzymes. Synonyms: EC 1.1.1.47; D-glucose dehydrogenase (NAD (P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD (P)+ 1-oxidoreductase; glucose 1-dehydrogenase; Glucose dehydrogenase; 9028-53-9. Enzyme Commission Number: EC 1.1.1.47. CAS No. 9028-53-9. Purity: 90% (SDS-PAGE test). Mole weight: About 28kDa (SDS-PAGE detection). Activity: About 200U/mg. Appearance: White powder, lyophilized. Storage: 4°C, store at -20°C for long-term preservation. Form: Freeze dried powder. EC 1.1.1.47; D-glucose dehydrogenase (NAD (P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD (P)+ 1-oxidoreductase; glucose 1-dehydrogenase; Glucose dehydrogenase; 9028-53-9. Cat No: NATE-1139. | |
| Glucose Dehydrogenases | recycling NADPH and NADH. Group: Enzymes. Synonyms: Glucose Dehydrogenases; GDH. Form: Enzyme Powder: 9 items*50mg / item, or other quantity. Glucose Dehydrogenases; GDH; Screening Kit; library of enzyme; enzyme library. Cat No: ENLC-015. | |
| 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, 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 | |
| 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 (phosphorylating) | Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate. Group: Enzymes. Synonyms: 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. Enzyme Commission Number: EC 1.2.1.12. CAS No. 9001-50-7. Glyceraldehyde-3-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-1118; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); EC 1.2.1.12; 9001-50-7; 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. Cat No: EXWM-1118. | |
| glycerol-3-phosphate dehydrogenase | This flavin-dependent dehydrogenase is an essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis. In bacteria, the enzyme is localized to the cytoplasmic membrane, while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane. In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8, glycerol-3-phosphate dehydrogenase (NAD+), forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD+ by the mitochondrial electron-transport chain.This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix. Insect flight muscle uses only CoQ10 as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ9. The enzyme is activated by calcium. Group: Enzymes. Synonyms: α-glycerophosphate dehydrogenase; α-glycerophosphate dehydrogenase (acceptor); anaerobic glycerol-3-phosphate dehydrogenase; DL-glycerol 3-phosphate oxidase (misleading); FAD-dependent glycerol-3-phosphate dehydrogenase; FAD-dependent sn-glycerol-3-phosphate dehydrogenase; FAD-GPDH; FAD-linked glycerol 3-phosphate dehydrogenase; FAD-linked L-glycerol-3-phosphate dehydrogenase; flavin-linked glycerol-3-phosphate dehydrogenas | |
| Glycerol-3-Phosphate Dehydrogenase from E. coli, Recombinant | α-glycerophosphate dehydrogenase catalyzes the conversion of dihydroxyacetone to glycerol phosphate. Applications: The enzyme is useful for enzymatic determination of glycerol and triglyceride when coupled with glycerokinase. Group: Enzymes. Synonyms: α-glycerol phosphate dehydrogenase (NAD); α-glycerophosphate dehydrogenase (NAD. Enzyme Commission Number: EC 1.1.1.8. CAS No. 9075-65-4. GPDH. Mole weight: ca. 73,600; Subunit molecular weight : ca. 36,800. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: E. coli. α-glycerol phosphate dehydrogenase (NAD); α-glycerophosphate dehydrogenase (NAD); glycerol 1-phosphate dehydrogenase; glycerol phosphate dehydrogenase (NAD); glycerophosphate dehydrogenase (NAD); hydroglycerophosphate dehydrogenase; L-α-glycerol phosphate dehydrogenase; L-α-glycerophosphate dehydrogenase; L-glycerol phosphate dehydrogenase; L-glycerophosphate dehydrogenase; NAD-α-glycerophosphate dehydrogenase; NAD-dependent glycerol phosphate dehydrogenase; NAD-dependent glycerol-3-phosphate dehydrogenase; NAD-L-glycerol-3-phosphate dehydrogenase; NAD-linked glycerol 3-phosphate dehydrogenase; NADH-dihydroxyacetone phosphate reductase; glycerol-3-phosphate dehydrogenase (NAD); EC 1.1.1.8; 9075-65-4; α-GDH. Cat No: NATE-1904. | |
| glycerol-3-phosphate dehydrogenase (NAD+) | Also acts on propane-1,2-diol phosphate and glycerone sulfate (but with a much lower affinity). Group: Enzymes. Synonyms: α-glycerol phosphate dehydrogenase (NAD+); α-glycerophosphate dehydrogenase (NAD+); glycerol 1-phosphate dehydrogenase; glycerol phosphate dehydrog. Enzyme Commission Number: EC 1.1.1.8. CAS No. 9075-65-4. GPDH. 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-0363; glycerol-3-phosphate dehydrogenase (NAD+); EC 1.1.1.8; 9075-65-4; α-glycerol phosphate dehydrogenase (NAD+); α-glycerophosphate dehydrogenase (NAD+); glycerol 1-phosphate dehydrogenase; glycerol phosphate dehydrogenase (NAD+); glycerophosphate dehydrogenase (NAD+); hydroglycerophosphate dehydrogenase; L-α-glycerol phosphate dehydrogenase; L-α-glycerophosphate dehydrogenase; L-glycerol phosphate dehydrogenase; L-glycerophosphate dehydrogenase (ambiguous); NAD+-α-glycerophosphate dehydrogenase; NAD+-dependent glycerol phosphate dehydrogenase; NAD+-dependent glycerol-3-phosphate dehydrogenase; NAD+-L-glycerol-3-phosphate dehydrogenase; NAD+-linked glycerol 3-phosphate dehydrogenase; NADH-dihydroxyacetone phosphate reductase; glycerol-3-phosphate dehydrogenase (NAD+); L-glycerol-3-phosphate dehydrogenase (ambiguous). Cat No: EXWM-0363. | |
| hydroxylamine reductase (NADH) | Also acts on some hydroxamates. Group: Enzymes. Synonyms: hydroxylamine reductase; ammonium dehydrogenase; NADH-hydroxylamine reductase; N-hydroxy amine reductase; hydroxylamine reductase (NADH2); NADH2:hydroxylamine oxidoreductase. Enzyme Commission Number: EC 1.7.1.10. CAS No. 9032-6-8. 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-1603; hydroxylamine reductase (NADH); EC 1.7.1.10; 9032-06-8; hydroxylamine reductase; ammonium dehydrogenase; NADH-hydroxylamine reductase; N-hydroxy amine reductase; hydroxylamine reductase (NADH2); NADH2:hydroxylamine oxidoreductase. Cat No: EXWM-1603. | |
| hydroxypyruvate reductase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glycerate:NADP+ 2-oxidoreductase. Other names in common use include beta-hydroxypyruvate reductase, NADH:hydroxypyruvate reductase, and D-glycerate dehydrogenase. This enzyme participates in glycine, serine and threonine metabolism and glyoxylate and dicarboxylate metabolism. Group: Enzymes. Synonyms: β-hydroxypyruvate reductase; NADH:hydroxypyruvate reductase; D-glycerate dehydrogenase. Enzyme Commission Number: EC 1.1.1.81. CAS No. 9059-44-3. 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-0365; hydroxypyruvate reductase; EC 1.1.1.81; 9059-44-3; β-hydroxypyruvate reductase; NADH:hydroxypyruvate reductase; D-glycerate dehydrogenase. Cat No: EXWM-0365. | |
| Isocitrate dehydrogenase (NAD+) from Bacteria, Recombinant | Isocitrate dehydrogenase (IDH) is an enzyme that catalyzes the oxidative decarboxylation of Isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2. This is a two-step process, which involves oxidation of Isocitrate (a secondary alcohol) to oxalosuccinate (a ketone), followed by the decarboxylation of the carboxyl group beta to the ketone, forming alpha-ketoglutarate. In humans, IDH exists in three isoforms:IDH3 catalyzes the third step of the citric acid cycle while converting NAD+ to NADH in the mitochondria. The isoforms IDH1 and IDH2 catalyze the same reaction outside the context of the citric acid cycle and use NADP+ as a cofactor instead o...namide adenine dinucleotide Isocitrate dehydrogenase; EC 1.1.1.41. Enzyme Commission Number: EC 1.1.1.41. CAS No. 9001-58-5. IDH. Mole weight: 40 kD (SDS-PAGE). Activity: > 40 Units / mg. Storage: Below -20°C. Form: Lyophilized powder. Source: E. coli. Species: Bacteria. Beta-ketoglutaric-isocitric carboxylase; IDH; Isocitrate dehydrogenase (NAD); Isocitric acid dehydrogenase; Isocitric dehydrogenase; NAD dependent Isocitrate dehydrogenase; NAD Isocitrate dehydrogenase; NAD isocitric dehydrogenase; NAD-linked Isocitrate dehydrogenase; NAD-specific Isocitrate dehydrogenase; Nicotinamide adenine dinucleotide Isocitrate dehydrogenase; EC 1.1.1.41. Cat No: NATE-1041. | |
| Isocitrate Dehydrogenase (NADP+) from Bacteria, Recombinant | Isocitrate dehydrogenase (IDH) (EC 1.1.1.42) is an enzyme that catalyzes the oxidative decarboxylation of Isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2. This is a two-step process, which involves oxidation of Isocitrate (a secondary alcohol) to oxalosuccinate (a ketone), followed by the decarboxylation of the carboxyl group beta to the ketone, forming alpha-ketoglutarate. In humans, IDH exists in three isoforms:IDH3 catalyzes the third step of the citric acid cycle while converting NAD+ to NADH in the mitochondria. The isoforms IDH1 and IDH2 catalyze the same reaction outside the context of the citric acid cycle and use NADP+ as a cof...rogenase (NADP+); EC 1.1.1.42; IDH; Isocitrate Dehydrogenase; Dual-cofactor-specific Isocitrate dehydrogenase; IDP; Isocitrate (NADP) dehydrogenase; Isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; Isocitrate dehydrogenase (NADP); Isocitrate dehydrogenase (NADP-dependent); NADP isocitric dehydrogenase; NADP (+)-ICDH; NADP (+)-IDH; NADP (+)-linked Isocitrate dehydrogenase; NADP-dependent Isocitrate dehydrogenase; NADP-dependent isocitric dehydrogenase; NADP-linked Isocitrate dehydrogenase; NADP-specific Isocitrate dehydrogenase; Oxalosuccinate decarboxylase; Oxalsuccinic decarboxylase; Triphosphopyridine nucleotide-linked Isocitrate dehydrog | |
| Isocitrate Dehydrogenase (NADP+) from Yeast, Recombinant | Isocitrate dehydrogenase (IDH) (EC 1.1.1.42) is an enzyme that catalyzes the oxidative decarboxylation of Isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2. This is a two-step process, which involves oxidation of Isocitrate (a secondary alcohol) to oxalosuccinate (a ketone), followed by the decarboxylation of the carboxyl group beta to the ketone, forming alpha-ketoglutarate. In humans, IDH exists in three isoforms:IDH3 catalyzes the third step of the citric acid cycle while converting NAD+ to NADH in the mitochondria. The isoforms IDH1 and IDH2 catalyze the same reaction outside the context of the citric acid cycle and use NADP+ as a cofactor instead of NAD+. They localize to the cytosol as well as the mitochondrion and peroxisome. Group: Enzymes. Synonyms: Isocitrate Dehydrogenase (NADP+); EC 1.1.1.42; IDH; Isocitrate . Enzyme Commission Number: EC 1.1.1.42. CAS No. 9028-48-2. IDH. Activity: r-ICDH activity = 100%. Storage: -20°C. Form: Liquid. Source: Pichia pastoris. Species: Yeast. Isocitrate Dehydrogenase (NADP+); EC 1.1.1.42; IDH; Isocitrate Dehydrogenase; Dual-cofactor-specific Isocitrate dehydrogenase; IDP; Isocitrate (NADP) dehydrogenase; Isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; Isocitrate dehydrogenase (NADP); Isocitrate dehydrogenase (NADP-dependent); NADP | |
| (-)-isopiperitenone reductase | The reaction occurs in the opposite direction to that shown above. The enzyme participates in the menthol-biosynthesis pathway of Mentha plants. (+)-Pulegone, (+)-cis-isopulegone and (-)-menthone are not substrates. The enzyme has a preference for NADPH as the reductant, with NADH being a poor substitute. The enzyme is highly regioselective for the reduction of the endocyclic 1,2-double bond, and is stereoselective, producing only the 1R-configured product. It is a member of the short-chain dehydrogenase/reductase superfamily. Group: Enzymes. Enzyme Commission Number: EC 1.3.1.82. 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-1351; (-)-isopiperitenone reductase; EC 1.3.1.82. Cat No: EXWM-1351. | |
| L-2-hydroxycarboxylate dehydrogenase [NAD(P)+] | The enzyme from the archaeon Methanocaldococcus jannaschii catalyses the reversible oxidation of (2R)-3-sulfolactate and (S)-malate to 3-sulfopyruvate and oxaloacetate, respectively (note that (2R)-3-sulfolactate has the same stereochemical configuration as (2S)-2-hydroxycarboxylates). The enzyme can use both NADH and NADPH, although activity is higher with NADPH. The oxidation of (2R)-3-sulfolactate was observed only in the presence of NADP+. The same organism also possesses an NAD+-specific enzyme with similar activity, cf. EC 1.1.1.337, L-2-hydroxycarboxylate dehydrogenase (NAD+). Group: Enzymes. Synonyms: MdhII; lactate/malate dehydrogenase. Enzyme Commission Number: EC 1.1.1.375. 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-0293; L-2-hydroxycarboxylate dehydrogenase [NAD(P)+]; EC 1.1.1.375; MdhII; lactate/malate dehydrogenase. Cat No: EXWM-0293. | |
| Lactaldehyde dehydrogenase from Escherichia coli, Recombinant | In enzymology, a lactaldehyde dehydrogenase (EC 1.2.1.22) is an enzyme that catalyzes the chemical reaction: (S)-lactaldehyde + NAD+ + H2O <-> (S)-lactate + NADH + 2 H+. The 3 substrates of this enzyme are (S)-lactaldehyde, NAD+, and H2O, whereas its 3 products are (S)-lactate, NADH, and H+. 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. Group: Enzymes. Synonyms: E.C. 1.2.1.22; lactaldehyde dehydrogenase; L-lactaldehyde:NAD oxidoreductase; nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase; (S)-lactaldehyde:NAD+ oxidoreductase. Enzyme Commission Number: EC 1.2.1.22. CAS No. 37250-90-1. Lactaldehyde dehydrogenase. Mole weight: 53337.9 Da. Source: Escherichia coli. E.C. 1.2.1.22; lactaldehyde dehydrogenase; L-lactaldehyde:NAD oxidoreductase; nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase; (S)-lactaldehyde:NAD+ oxidoreductase. Cat No: NATE-1213. | |
| Lactate Dehydrogenase A Inhibitor, FX11 (LDHA Inhibitor I, LDH-A Inhibitor I, LDH-M Inhibitor I, LDHM Inhibitor I) | A cell permeable, gossypol analog that acts as a selective, reversible, and NADH competitive inhibitor of lactate dehhydrogenase A (LDHA; Ki = 8uM for human liver LDHA). Does not affect the activities of LDHB and glyceraldehyde-3-phosphate dehydrogenase even at higher concentrations. Shown to increase oxygen consumption, reactive oxygen species production, and cell death in P493 human lymphoma B cells. Also shown to reduce mitochondrial transmembrane potential and ATP levels and increase AMP kinase activity. Exhibits synergistic toxicity in P493 cells when combined with FK866. Blocks the progression of human lymphoma and pancreatic cancer xenografts and when used in combination with FK866 it induces lymphoma regression. Group: Biochemicals. Grades: Highly Purified. CAS No. 213971-34-7. Pack Sizes: 10mg. US Biological Life Sciences. | Worldwide |
| Lactate Dehydrogenase from Chicken Heart, Recombinant | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. Purity: > 96% (SDS-PAGE). LDH. Activity: >90%. (>200U/mL). Storage: -20°C. Form: Lyophilized. Source: E. coli. Species: Chicken Heart. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0383. | |
| Lactic Dehydrogenase, Recombinant | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Group: Enzymes. Synonyms: 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; LDH; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Source: E. coli. 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; LDH; Lactate. Cat No: NATE-0381. | |
| Leucine dehydrogenase from Microorganism | In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction: L-leucine + H2O + NAD+ ? 4-methyl-2-oxopentanoate + NH3 + NADH + H+. The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis. Group: Enzymes. Synonyms: EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH. Enzyme Commission Number: EC 1.4.1.9. CAS No. 9082-71-7. Mole weight: 43 kDa (SDS-PAGE). Activity: >500U/mg protein. Storage: Store at -20°C. Form: White powder, lyophilized. Source: Microorganism. EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH; LEDH. Cat No: NATE-1715. | |
| 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-Lactate Dehydrogenase (Crude Enzyme) | Lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion oflactate to pyruvic acid and back, as it converts NAD + to NADH and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. LDH is expressed extensively in body tissues, such as blood cells and heart muscle. Because it is released during tissue damage, it is a marker of common injuries and disease such as heart failure. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Medicine; synthesis; biotechnology; drug development. Group: Enzymes. Synonyms: lactic acid dehydrogenase; L(+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. 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. Pack: 100ml. Cat No: NATE-1793. | |
| L-Lactate Dehydrogenase from Porcine, Recombinant | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: High purity l-lactate dehydrogenase (porcine) for use in research, biochemical enzyme assays and in vitro diagnostic analysis. Group: Enzymes. Synonyms: 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. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. Activity: ~ 330 U/mg. Storage: > 2 years at 4°C. Form: In 3.2 M ammonium sulphate. Source: 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: NATE-1105. | |
| L-Lactate dehydrogenase, Microorganism | L-Lactate dehydrogenase, Microorganism (LAD) is a redox enzyme. L-Lactate dehydrogenase catalyzes the reduction of pyruvate to L-lactate by NADH in vivo with absolute enantiospecificity [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: LAD. CAS No. 9001-60-9. Pack Sizes: 5 mg; 10 mg; 25 mg. Product ID: HY-P2807. |  |
| L-Lactic Dehydrogenase from Bacillus stearothermophilus, Recombinant | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Recombinant, expressed in e. coli, lyophilized powder, > 200 units/mg protein (lowry). Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: > 200 units/mg protein (Lowry). Stability: 2-8°C. Form: lyophilized powder. Source: E. coli. Species: Bacillus stearothermophilus. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0382. | |
| methylglyoxal reductase (NADH) | This mammalian enzyme differs from the yeast enzyme, EC 1.1.1.283, methylglyoxal reductase (NADPH-dependent), by its coenzyme requirement, reaction direction, and enantiomeric preference. Group: Enzymes. Synonyms: methylglyoxal reductase; D-lactaldehyde dehydrogenase; methylglyoxal reductase (NADH-dependent). Enzyme Commission Number: EC 1.1.1.78. CAS No. 37250-16-1. 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-0361; methylglyoxal reductase (NADH); EC 1.1.1.78; 37250-16-1; methylglyoxal reductase; D-lactaldehyde dehydrogenase; methylglyoxal reductase (NADH-dependent). Cat No: EXWM-0361. | |
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