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| Product | Description | |
|---|---|---|
| D-amino Acid Dehydrogenase | synthesis of D-amino acids from ketoacids. Group: Enzymes. Synonyms: D-amino Acid Dehydrogenase; D-AADH. Form: 1. Enzyme Powder: 17 items*50mg / item, or other quantity2. Screening Kit: 17 items*1mg / item. D-amino Acid Dehydrogenase; D-AADH; Screening Kit; library of enzyme; enzyme library. Cat No: ENLC-012. |  |
| D-amino acid dehydrogenase (quinone) | An iron-sulfur flavoprotein (FAD). The enzyme from the bacterium Helicobacter pylori is highly specific for D-proline, while the enzyme from the bacterium Escherichia coli B is most active with D-alanine, D-phenylalanine and D-methionine. This enzyme may be the same as EC 1.4.99.6. Group: Enzymes. Synonyms: DadA. Enzyme Commission Number: EC 1.4.5.1. 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-1486; D-amino acid dehydrogenase (quinone); EC 1.4.5.1; DadA. Cat No: EXWM-1486. | |
| D-Amino acid dehydrogenase, Recombinant | D-amino-acid dehydrogenase (EC 1.4.99.1) is a bacterial enzyme that catalyses the oxidation of D-amino acids into their corresponding oxoacids. It contains both flavin and nonheme iron as cofactors. The enzyme has a very broad specificity and can act on most D-amino acids. D-amino acid + H2O + acceptor <=> a 2-oxo acid + NH3 + reduced acceptor. This reaction is distinct from the oxidation reaction catalysed by D-amino acid oxidase that uses oxygen as a second substrate, as the dehydrogenase can use many different compounds as electron acceptors, with the physiological substrate being coenzyme Q. D-amino-acid dehydrogenase is used in enzyme assays to measure substrate specificity of D-amino acids, such as DauA. Applications: D-amino-acid dehydrogenase is a bacterial enzyme that catalyses the oxidation of d-amino acids into their corresponding oxoacids. it contains flavin and nonheme iron as cofactors and has a broad specificity thereby acting on most d-amino acids. Group: Enzymes. Synonyms: D-Amino acid dehydrogenase; EC 1.4.99.1; 37205-44-0. Enzyme Commission Number: EC 1.4.99.1. CAS No. 37205-44-0. D-Amino acid dehydrogenase. Activity: >26 U/g. Storage: Store at 2-8°C. Source: E. coli. D-Amino acid dehydrogenase; EC 1.4.99.1; 37205-44-0. Cat No: NATE-0825. | |
| L-amino-acid dehydrogenase | Acts on aliphatic amino acids. Group: Enzymes. Enzyme Commission Number: EC 1.4.1.5. CAS No. 9029-13-4. 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-1460; L-amino-acid dehydrogenase; EC 1.4.1.5; 9029-13-4. Cat No: EXWM-1460. | |
| (1R, 4R) -4-[[ (1, 1-Dimethylethoxy) carbonyl]amino]-2-cyclopentene-1-carboxylic Acid Methyl Ester | (1R, 4R) -4-[[ (1, 1-Dimethylethoxy) carbonyl]amino]-2-cyclopentene-1-carboxylic Acid Methyl Ester is an intermediate in synthesizing trans-Abacavir Dihydrochloride (A104995), which is an impurity of Abacavir. Abacavir (A104990) is a carbocyclic 2'-deoxyguanosine nucleoside reverse transcriptase inhibitor and an anti-HIV drug used to treat HIV infection (1). Intracellular enzymes convert Abacavir to its active form, carbovir-triphosphate (CBV-TP), which then selectively inhibits HIV reverse transcriptase by incorporating into viral DNA (2). Abacavir is metabolized in the liver by uridine diphosphate glucuronyltransferase and alcohol dehydrogenase resulting in inactive glucuronide and carboxylate metabolites, respectively. Group: Biochemicals. Grades: Highly Purified. CAS No. 168958-19-8. Pack Sizes: 10mg, 25mg. Molecular Formula: C12H19NO4. US Biological Life Sciences. |  Worldwide |
| 2,4-diaminopentanoate dehydrogenase | Also acts, more slowly, on 2,5-diaminohexanoate forming 2-amino-5-oxohexanoate, which then cyclizes non-enzymically to 1-pyrroline-2-methyl-5-carboxylate. Group: Enzymes. Synonyms: 2,4-diaminopentanoic acid C4 dehydrogenase. Enzyme Commission Number: EC 1.4.1.12. CAS No. 39346-26-4. 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-1445; 2,4-diaminopentanoate dehydrogenase; EC 1.4.1.12; 39346-26-4; 2,4-diaminopentanoic acid C4 dehydrogenase. Cat No: EXWM-1445. | |
| 2-Aminotetraline-2-carboxylic acid | 2-Aminotetraline-2-carboxylic acid is a potent and selective IDH1 (isocitrate dehydrogenase 1) mutant inhibitor for the treatment of acute myeloid leukemia. Synonyms: Atc-OH; 2-Amino-1,2,3,4-tetrahydronaphthalene-2-carboxylic acid; 2-Aminotetralin-2-carboxylic acid; D,L-2-Aminotetralin-2-carboxylic acid; 2-AMINOTETRALINE-2-CARBOXYLIC ACID; 2-Amino-1,2,3,4-tetrahydro-2-naphthalenecarboxylicacid; 2-amino-3,4-dihydro-1H-naphthalene-2-carboxylic acid; (R)-2-Amino-1,2,3,4-tetrahydronaphthalene-2-carboxylic acid; (+/-)-2-Amino-1,2,3,4-tetrahydro-2-naphthoic acid; GSK 321; Atc OH. Grades: ≥ 98% (HPLC). CAS No. 6331-63-1. Molecular formula: C11H13NO2. Mole weight: 191.22. |  |
| 2-Bromo-1,6-dimethyl Ester Hexanedioic Acid | 2-Bromo-1,6-dimethyl Ester Hexanedioic Acid is an intermediate in the synthesis of 2-Hydroxyhexanedioic Acid Disodium Salt (H943015). Accumulation and excretion of 2-Hydroxyhexanedioic Acid (with 2-ketoadipic and 2-aminoadipic) in urine can be caused by 2-ketoadipic acidemia, probably without adverse phenotypic effects, due to deficiency of 2-ketoadipic dehydrogenase. Group: Biochemicals. Grades: Highly Purified. CAS No. 3196-19-8. Pack Sizes: 100mg, 250mg. Molecular Formula: C8H13BrO4. US Biological Life Sciences. | Worldwide |
| 2-Hydroxy-4-(methylthio)butyric acid | 2-Hydroxy-4-(methylthio)butyric acid is a dietary essential amino acid which is converted to Methionine (HY-13694) by 2-hydroxy acid dehydrogenase and 2-hydroxy acid oxidase. 2-Hydroxy-4-(methylthio)butyric acid is promising for research of gut disease [1]. Uses: Scientific research. Group: Natural products. CAS No. 583-91-5. Pack Sizes: 10 mM * 1 mL; 10 g; 25 g; 50 g. Product ID: HY-116688. |  |
| 2-Hydroxyhexanedioic Acid Disodium Salt | Accumulation and excretion of 2-Hydroxyhexanedioic Acid (with 2-ketoadipic and 2-aminoadipic) in urine can be caused by 2-ketoadipic acidemia, probably without adverse phenotypic effects , due to deficiency of 2-ketoadipic dehydrogenase. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 50mg, 500mg. Molecular Formula: C6H8Na2O5. US Biological Life Sciences. | Worldwide |
| 2-NH2-6-Cl-5'-PuMP | 2-NH2-6-Cl-5'-PuMP is an analogue of guanosine-5'-O-monophosphate and an inhibitor of IMP dehydrogenase. It is often used as the precursor for 6-modified 5'-GMP derivatives. Synonyms: 2-Amino-6-chloropurine riboside-5'-O-monophosphate, sodium salt. Grades: ≥ 97% by HPLC. CAS No. 16321-98-5. Molecular formula: C10H13ClN5O7P (free acid). Mole weight: 381.67. | |
| 3-[[[3-[4-[ (Methylsulfonyl) amino]phenyl]-4-oxo-4H-chromen-7-yl]oxy]methyl]benzoic Acid | 3-[[[3-[4-[ (Methylsulfonyl) amino]phenyl]-4-oxo-4H-chromen-7-yl]oxy]methyl]benzoic Acid is a highly selective reversible aldehyde dehydrogenase 2 (ALDH-2) inhibitor that reduce alcohol and cocaine intake in rats. It also has anxiolytic properties as well as reduces excessive alcohol drinking. Group: Biochemicals. Grades: Highly Purified. CAS No. 1005334-57-5. Pack Sizes: 1mg, 5mg. Molecular Formula: C24H19NO7S, Molecular Weight: 465.48. US Biological Life Sciences. | Worldwide |
| 3-Amino-3-methylbutanoic Acid, 90% | 3-Amino-3-methylbutanoic Acid acts as a reagent in the preparation of arylsulfonyl methylbutanamides of cycloalkylamines, particularly adamantylamines, as selective inhibitors of human and murine 11 β-hydroxysteroid dehydrogenase type 1. Synthesis of acetylcholine and carbamoylcholine analogs as a functionally selective α4 β2 nicotinic acetylcholine receptor agonist. Phenamide preparation by coupling reaction. Group: Biochemicals. Grades: Highly Purified. CAS No. 625-05-8. Pack Sizes: 250mg, 1g. Molecular Formula: C5H11NO2. US Biological Life Sciences. | Worldwide |
| 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 |
| 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) | The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo-pentanoate, 2-oxobutyrate and 3-methylthiopropanamine. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.1, pyruvate synthase, and EC 1.2.7.3, 2-oxoglutarate synthase. Group: Enzymes. Synonyms: 2-ketoisovalerate ferredoxin reductase; 3-methyl-2-oxobutanoate synthase (ferredoxin); VOR; branched-chain ketoacid ferredoxin reductase; branched-chai. Enzyme Commission Number: EC 1.2.7.7. 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-1230; 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin); EC 1.2.7.7; 2-ketoisovalerate ferredoxin reductase; 3-methyl-2-oxobutanoate synthase (ferredoxin); VOR; branched-chain ketoacid ferredoxin reductase; branched-chain oxo acid ferredoxin reductase; keto-valine-ferredoxin oxidoreductase; ketoisovalerate ferredoxin reductase; 2-oxoisovalerate ferredoxin reductase. Cat No: EXWM-1230. | |
| Acyl-Coenzyme A Dehydrogenase 8 from Human, Recombinant | Acyl CoA dehydrogenase is the enzymeused to catalyzethe first step of β-oxidationin Fatty acid metabolism. Acyl-coenzyme A (CoA) dehydrogenases (ACADs) are a family of mitochondrial enzymes that catalyze the first dehydrogenation step in the bets-oxidation of fatty acyl-CoA derivatives. Several human ACADs exist and all ACADs catalyze the same initial dehydrogenation of the substrate at the beta-carbon atom and require electron transfer flavoprotein as an alectron acceptor. The predicted 415-amino acid ACAD8 protein contains many of the residues conserved in most other ACADs, including an active site glutamic acid residue and residues important for tetramer f...mber 8 mitochondrial; ACAD-8; Isobutyryl-CoA dehydrogenase; Activator-recruited cofactor 42 kDa component; ARC42; FLJ22590. Purity: Greater than 95.0% as determined by SDS-PAGE. ACAD-8. Mole weight: 47.7 kDa. Stability: ACAD8 although stable at 4°C for 1 week, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. Acyl-CoA dehydrogenase family member 8 mitochondrial; ACAD-8; Isobutyryl-CoA dehydrogenase; Activator-recruited cofactor 42 kDa component; ARC42; FLJ22590. Cat No: NATE-0801. | |
| aminomuconate-semialdehyde dehydrogenase | Also acts on 2-hydroxymuconate semialdehyde. Group: Enzymes. Synonyms: 2-aminomuconate semialdehyde dehydrogenase; 2-hydroxymuconic acid semialdehyde dehydrogenase; 2-hydroxymuconate semialdehyde dehydrogenase; α-aminomuconic ε-semialdehyde dehydrogenase; α-hydroxymuconic ε-semialdehyde dehydrogenase; 2-hydroxymuconic semialdehyde dehydrogenase. Enzyme Commission Number: EC 1.2.1.32. CAS No. 37250-95-6. 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-1139; aminomuconate-semialdehyde dehydrogenase; EC 1.2.1.32; 37250-95-6; 2-aminomuconate semialdehyde dehydrogenase; 2-hydroxymuconic acid semialdehyde dehydrogenase; 2-hydroxymuconate semialdehyde dehydrogenase; α-aminomuconic ε-semialdehyde dehydrogenase; α-hydroxymuconic ε-semialdehyde dehydrogenase; 2-hydroxymuconic semialdehyde dehydrogenase. Cat No: EXWM-1139. | |
| aspartate-semialdehyde dehydrogenase | In enzymology, an aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) is an enzyme that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. It forms an early branch point in the metabolic pathway forming lysine, methionine, leucine and isoleucine from aspartate. This pathway also produces diaminopimelate which plays an essential role in bacterial cell wall formation. There is particular interest in ASADH as disabling this enzyme proves fatal to the organism giving rise to the possibility of a new class of antibiotics, fungicides, and herbicides aimed at inhibiting it. Group: Enzymes. Synonyms: aspartate semialdehyde dehydrogenase; aspartic semialdehyde dehydrogenase; L-aspartate-β-semialdehyde:NADP+ oxidoreductase (phosphorylating); aspartic β-semialdehyde dehydrogenase; ASA dehydrogenase. Enzyme Commission Number: EC 1.2.1.11. CAS No. 9000-98-0. 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-1117; aspartate-semialdehyde dehydrogenase; EC 1.2.1.11; 9000-98-0; aspartate semialdehyde dehydrogenase; aspartic semialdehyde dehydrogenase; L-aspartate-β-semialdehyde:NADP+ oxidoreductase (phosphorylating); aspartic β-semialdehyde dehydrogenase; ASA dehydrogenase. Cat No: EXWM-1117. | |
| Az-33 | Az-33 is a lactate dehydrogenase A (LDHA) inhibitor, which is a key enzyme in anaerobic glycolysis process and is deregulated in human malignancies. Uses: Az-33 is a lactate dehydrogenase a (ldha) inhibitor. Synonyms: Az 33; Az33; 2-(4-(4-((3-((2-Methylbenzo[d]thiazol-6-yl)amino)-3-oxopropyl)amino)-4-oxobutyl)benzyl)malonic acid. Grades: ≥98%. CAS No. 1370290-34-8. Molecular formula: C25H27N3O6S. Mole weight: 497.56. | |
| BAY 1436032 | BAY-1436032 is a highly selective, potent and orally available inhibitor of mutant Isocitrate Dehydrogenase 1 (mIDH1). It is a double-digit nanomolar and selective pan-inhibitor of the enzymatic activity of various IDH1-R132X mutants in vitro and displays potent inhibition of 2-HG release (nanomolar range) in patient derived and engineered cell lines expressing different IDH1 mutants. BAY 1436032 strongly reduces 2-HG (2-hydroxyglutarate) levels in cells carrying IDH1-R132H, -R132C, -R132G, -R132S and -R132L mutations. BAY 1436032 showed a favourable selectivity profile against wtIDH1/2 and a large panel of off-targets in vitro. Synonyms: 3-(2-[[4-(Trifluoromethoxy)phenyl]amino]-1-[(1R,5R)-3,3,5-trimethylcyclohexyl]-1H-benzimidazol-5-yl)propanoic Acid; BAY-1436032. Grades: ≥98%. CAS No. 1803274-65-8. Molecular formula: C26H30F3N3O3. Mole weight: 489.53. | |
| BAY-1436032 | BAY-1436032 is a potent, selective and orally available inhibitor of mutant Isocitrate Dehydrogenase 1 (mIDH1). BAY 1436032 is a double-digit nanomolar and selective pan-inhibitor of the enzymatic activity of various IDH1-R132X mutants in vitro and displayed potent inhibition of 2-HG release (nanomolar range) in patient derived and engineered cell lines expressing different IDH1 mutants. In line with the proposed mode of action, a concentration-dependent lowering of 2-HG was observed in vitro accompanied by differentiation and maturation of mIDH1 tumor cells. Furthermore, BAY 1436032 showed a favourable selectivity profile against wtIDH1/2 and a large panel of off-targets in vitro. Group: Inhibitors. Alternative Names: BAY-1436032; BAY 1436032; BAY1436032. CAS No. 1803274-65-8. Molecular formula: C26H30F3N3O3. Mole weight: 489.54. Appearance: Solid powder. Purity: >98%. IUPACName: 3- (2- ( (4- (trifluoromethoxy)phenyl)amino)-1- ( (1R, 5R)-3, 3, 5-trimethylcyclohexyl)-1H-benzo[d]imidazol-5-yl)propanoic acid. Canonical SMILES: O=C (O)CCC1=CC=C2N ([C@H]3CC (C) (C)C[C@@H] (C)C3)C (NC4=CC=C (OC (F) (F)F)C=C4)=NC2=C1. Catalog: ACM1803274658. |  |
| 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. | |
| CVT10216 | CVT10216 is a potent and selective, reversible inhibitor of aldehyde dehydrogenase 2 (ALDH2) with IC50 value of 29nM, thereby inhibiting dopamine synthesis. It is active in suppressing alcohol and cocaine use, and anxiety. It has been shown to produce anxiolytic effects in four different rodent models, including a model of repeated alcohol withdrawal-induced anxiety. It increases acetaldehyde after alcohol gavage and inhibits 2-bottle choice alcohol intake in heavy drinking rodents. It prevents operant self-administration and eliminates cue-induced reinstatement of alcohol seeking. It also prevents alcohol-induced increases in NAc DA without changing basal levels. Uses: Cvt10216 is active in suppressing alcohol and cocaine use, and anxiety. Synonyms: CVT-10216; CVT 10216; CVT10216. 3-[[[3-[4-[(Methylsulfonyl)amino]phenyl]-4-oxo-4H-chromen-7-yl]oxy]methyl]benzoic acid;GS 455534. Grades: >98 %. CAS No. 1005334-57-5. Molecular formula: C24H19NO7S. Mole weight: 465.48. | |
| CVT 10216 | Potent and selective, reversible inhibitor of aldehyde dehydrogenase 2 (ALDH2) (IC50 values are 29 and 1300 nM for ALDH2 and ALDH1, respectively). Exhibits anxiolytic effects in rat models. Group: Biochemicals. Alternative Names: 3-[[[3-[4-[ (Methylsulfonyl) amino]phenyl]-4-oxo-4H-1-benzopyran-7-yl]oxy]methyl]benzoic acid. Grades: Highly Purified. CAS No. 1005334-57-5. Pack Sizes: 10mg, 50mg. US Biological Life Sciences. | Worldwide |
| D-Amino Acid Oxidase (Crude Enzyme) | D-Amino Acid Oxidase (DAAO; also DAO, OXDA, DAMOX) is a peroxisomal enzyme containing FAD as cofactor that is expressed in a wide range of species from yeasts to human. It is not present in plants or in bacteria which instead use D-amino acid dehydrogenase. Its function is to oxidize D-amino acids to the corresponding imino acids, producing ammonia and hydrogen peroxide. DAAO is a candidate susceptibility gene and together with G72 may play a role in the glutamatergic mechanisms of schizophrenia. Risperidone andsodium benzoate are inhibitors of DAAO. DAAO is used as a biocatalyst in several biotechnological applications, such as the oxidation of cephalosporin C, the deracem...n may use the morpheein model of allosteric regulation. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Biotechnology; industry; drug development; medicine; pharmacology; analysis; diagnostics; synthesis. Group: Enzymes. Synonyms: ophio-amino-acid oxidase; L-amino acid:O 2 oxidoreductase; new yellow enzyme. Enzyme Commission Number: EC 1.4.3.3. CAS No. 9000-88-8. DAAO. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. ophio-amino-acid oxidase; L-amino acid:O 2 oxidoreductase; new yellow enzyme. Pack: 100ml. Cat No: NATE-1807. | |
| D-arginine dehydrogenase | Contains a non-covalent FAD cofactor. The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, is a catabolic enzyme that is part of a two-enzyme complex involved in the racemization of D and L-arginine. The enzyme has a broad substrate range and can act on most D-amino acids with the exception of D-glutamate and D-aspartate. However, activity is maximal with D-arginine and D-lysine. Not active on glycine. Group: Enzymes. Synonyms: D-amino-acid:(acceptor) oxidoreductase (deaminating); D-amino-acid dehydrogenase; D-amino-acid:acceptor oxidoreductase (deaminating). Enzyme Commission Number: EC 1.4.99.6. CAS No. 37205-44-0. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1492; D-arginine dehydrogenase; EC 1.4.99.6; 37205-44-0; D-amino-acid:(acceptor) oxidoreductase (deaminating); D-amino-acid dehydrogenase; D-amino-acid:acceptor oxidoreductase (deaminating). Cat No: EXWM-1492. | |
| 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 | |
| Dihydrofolate Reductase from human, Recombinant | Dihydrofolate reductase, or DHFR, is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as electron donor, which can be converted to the kinds of tetrahydrofolate cofactors used in 1-carbon transfer chemistry. In humans, the DHFR enzyme is encoded by the DHFR gene. It is found in the q11?q22 region of chromosome 5. Bacterial species possesses distinct DHFR enzymes (based on their pattern of binding diaminoheterocyclic molecules), but mammalian DHFRs are highly similar. Human dhfr is an 186 amino acid protein with an apparent molecular weight of 25 kda. it is 30% homologous to the e. coli protein and up to 70% homologous to vertebrate protein... from mycobacterium smegmatis. human dihydrofolate reductase has been used in a study to investigate the stable expression of green fluorescent protein and the targeted disruption of thioredoxin peroxidase-1 gene in babesia bovis. human dihydrofolate reductase has also been used in a study to investigate the structural analysis of human dihydrofolate reductase as a binary complex. Group: Enzymes. Synonyms: DHFR; dihydrofolate reductase; DYR; DHFRP1; Tetrahydrofolate NADP+ oxidoreductase; EC 1.5.1.3; tetrahydrofolate dehydrogenase; pteridine reductase:dihydrofolate reductase; dihydrofolate reductase:thymidylate synthase; thymidylate synthetase-dihydrofolate reductase; f | |
| 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 | |
| D-lysopine dehydrogenase | In the reverse reaction, a number of L-amino acids can act instead of L-lysine, and 2-oxobutanoate and, to a lesser extent, glyoxylate can act instead of pyruvate. Group: Enzymes. Synonyms: D-lysopine synthase; lysopine dehydrogenase; D(+)-lysopine dehydrogenase; 2-N-(D-1-carboxyethyl)-L-lysine:NADP+ oxidoreductase (L-lysine-forming). Enzyme Commission Number: EC 1.5.1.16. CAS No. 65187-41-9. 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-1497; D-lysopine dehydrogenase; EC 1.5.1.16; 65187-41-9; D-lysopine synthase; lysopine dehydrogenase; D(+)-lysopine dehydrogenase; 2-N-(D-1-carboxyethyl)-L-lysine:NADP+ oxidoreductase (L-lysine-forming). Cat No: EXWM-1497. | |
| D-proline dehydrogenase | A flavoprotein (FAD). The enzyme prefers D-proline and acts on other D-amino acids with lower efficiency. Group: Enzymes. Synonyms: D-Pro DH; D-Pro dehydrogenase; dye-linked D-proline dehydrogenase. Enzyme Commission Number: EC 1.5.99.13. 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-1567; D-proline dehydrogenase; EC 1.5.99.13; D-Pro DH; D-Pro dehydrogenase; dye-linked D-proline dehydrogenase. Cat No: EXWM-1567. | |
| Enasidenib mesylate | Enasidenib mesylate is a first-in-class, oral, potent, reversible, selective inhibitor of the IDH2 mutant enzymes indicated for the treatment of adult patients with replased or refractory acute myeloid leukemia (AML) with an isocitrate dehydrogenase-2 (IDH2) mutation. Synonyms: methanesulfonic acid;2-methyl-1-[[4-[6-(trifluoromethyl)pyridin-2-yl]-6-[[2-(trifluoromethyl)pyridin-4-yl]amino]-1,3,5-triazin-2-yl]amino]propan-2-ol; Enasidenib (mesylate); AG-221 mesylate; Enasidenib mesilate; Enasidenib methanesulfonate; Enasidenib mesylate [USAN]. CAS No. 1650550-25-6. Molecular formula: C20H21F6N7O4S. Mole weight: 569.48. | |
| Farudodstat | Farudodstat is an orally active and potent inhibitor of DHODH (human dihydroorotate dehydrogenase). It inhibits the proliferation of MOLM-14 and KG-1 acute myeloid leukemia (AML) cells (IC50s = 0.582 and 0.382 μM, respectively), as well as induces apoptosis in the same cells when used at concentrations of 0.5 and 1 μM. Synonyms: 2-[(3,5-difluoro-3'-methoxy-[1,1'-biphenyl]-4-yl)amino]pyridine-3-carboxylic acid; ASLAN003; 2-[(3,5-Difluoro-3'-methoxy-4-biphenylyl)amino]nicotinic Acid; 3-Pyridinecarboxylic acid, 2-[(3,5-difluoro-3'-methoxy-[1,1'-biphenyl]-4-yl)amino]-; 2-((3,5-Difluoro-3'-methoxy-[1,1'-biphenyl]-4-yl)amino)nicotinic acid; 2-[(3,5-difluoro-3'-methoxy[1,1'-biphenyl]-4-yl)amino]-3-pyridinecarboxylic acid. Grades: ≥98%. CAS No. 1035688-66-4. Molecular formula: C19H14F2N2O3. Mole weight: 356.32. | |
| Glutamate Dehydrogenase (NAD(P)) from E.coli, Recombinant | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Applications: Use recombinant glutamate dehydrogenase in diagnostic tests for the determination of ammonia, urea, l-glutamate, glutamate pyruvate transaminase and leucine aminopeptidase. Group: Enzymes. Synonyms: glu. CAS No. 9029-12-3. GLDH. Mole weight: ~2 200 kD for the associated enzyme with 8 subunits; 280 kD for one subunit. Activity: >80 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White lyophilizate. Source: E.coli. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: NATE-0981. | |
| Glutamate dehydrogenase, Recombinant | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Glutamate dehydrogenase (gldh, ec 1.4.1.2) is the enzyme present in the mitochondrial matrix of the cell. it can convert glutamic acid to α-ketoglutarate and catalyze the re...ations: Except glutamate dehydrogenation, gldh can also catalytic the deaminase of other amino acids such as l-valine, l-2-aminobutyric acid and l-leucine. the main measuring method is continuous monitoring. moreover, gldh catalyzes the reaction of α-ketoglutarate, h+,ammonia and nadh to generating glutamic. since nadh is the color source of many biochemical assays, therefore the reaction catalyzed by the corresponding gldh is widely used to detect the final step of biochemical detection reagent. Group: Enzymes. Synonyms: glutamate dehydrogenase; glutamic dehydrogenase; glutamate dehydrogenase (NAD+); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate | |
| Glutaryl coenzyme A lithium salt | Glutaryl coenzyme A is an intermediate in the metabolism (catabolism) of the amino acids lysine and tryptophan. Glutaryl CoA is used as a substrate to study the specificity and kinetics of glutaryl-CoA dehydrogenases. Applications: An intermediate in the metabolism (catabolism) of the amino acids lysine and tryptophan. Group: Coenzymes. Synonyms: Glutaryl CoA. CAS No. 103192-48-9. Purity: ≥90%. Mole weight: 881.63. Appearance: Powder. Form: Solid. Glutaryl CoA; Glutaryl coenzyme A lithium salt; 103192-48-9. Cat No: COEC-053. | |
| GSK2837808A | GSK2837808A is a potent and specific lactate dehydrogenase A (LDHA) with IC50 values of 1.9 and 14 nM for LDHA and LDHB, respectively and inhibits lactate production in selected cancer cell lines. Synonyms: GSK2837808A; GSK-2837808A; GSK 2837808A; GSK2837808; GSK-2837808; GSK 2837808. 3-[[3-(cyclopropylsulfamoyl)-7-(2,4-dimethoxypyrimidin-5-yl)quinolin-4-yl]amino]-5-(3,5-difluorophenoxy)benzoic acid. CAS No. 1445879-21-9. Molecular formula: C31H25F2N5O7S. Mole weight: 649.62. | |
| Hydroxypyruvic acid | Hydroxypyruvic acid (β-Hydroxypyruvic acid) is an intermediate in the metabolism of glycine, serine and threonine. Hydroxypyruvic acid is a substrate for serine-pyruvate aminotransferase and glyoxylate reductase/hydroxypyruvate reductase. Hydroxypyruvic acid is involved in the metabolic disorder which is the dimethylglycine dehydrogenase deficiency pathway. Uses: Scientific research. Group: Natural products. Alternative Names: β-Hydroxypyruvic acid; 3-Hydroxypyruvic acid. CAS No. 1113-60-6. Pack Sizes: 1 mg; 5 mg. Product ID: HY-113013. | |
| indolepyruvate ferredoxin oxidoreductase | Contains thiamine diphosphate and [4Fe-4S] clusters. Preferentially utilizes the transaminated forms of aromatic amino acids and can use phenylpyruvate and p-hydroxyphenylpyruvate as substrates. This enzyme, which is found in archaea, is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin). Group: Enzymes. Synonyms: 3-(indol-3-yl)pyruvate synthase (ferredoxin); IOR. Enzyme Commission Number: EC 1.2.7.8. CAS No. 158886-06-7. 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-1231; indolepyruvate ferredoxin oxidoreductase; EC 1.2.7.8; 158886-06-7; 3-(indol-3-yl)pyruvate synthase (ferredoxin); IOR. Cat No: EXWM-1231. | |
| Isoguanosine Hydrate | A useful synthetic intermedate. A naturally occuring, biologically active isomer of guanosine. Reported to stimulate the accumulation of cyclic-AMP in the brain. It is an inhibitor of IMP pyrophosphorylase, and its 5'-di and -tri-phosphates inhibit glutamic acid dehydrogenase. May contain approximately 0.6 moles of water. Synonyms: 2-Hydroxy adenosine hydrate; 1,2-Dihydro-2-oxo-adenosine Hydrate; Crotonosid Hydrate; Isoguanine riboside Hydrate; NSC 1216 Hydrate; 2,3-Dihydro-2-oxoadenosine Hydrate; 6-Amino-9-β-D-ribofuranosyl-9H-Purin-2-ol Hydrate. Grades: ≥95%. CAS No. 359436-55-8. Molecular formula: C10H13N5O5. Mole weight: 283.24. | |
| methylglutamate dehydrogenase | A number of N-methyl-substituted amino acids can act as donor; 2,6-dichloroindophenol is the best acceptor. Group: Enzymes. Synonyms: N-methylglutamate dehydrogenase; N-methyl-L-glutamate:(acceptor) oxidoreductase (demethylating). Enzyme Commission Number: EC 1.5.99.5. CAS No. 37217-26-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1572; methylglutamate dehydrogenase; EC 1.5.99.5; 37217-26-8; N-methylglutamate dehydrogenase; N-methyl-L-glutamate:(acceptor) oxidoreductase (demethylating). Cat No: EXWM-1572. | |
| Mutant Isocitrate Dehydrogenase 1 R132H from Human, Recombinant | Mutations of the cytosolic IDH 1 are a common feature in primary human brain cancers. Arginine 132 (R132) of IDH is highly conserved among different isoforms of IDH and is most commonly mutated to Histidine. Mutation of IDH1 R132H leads to accumulation of R(-)-2-hydroxyglutarate (2HG), which correlates with an increased risk for malignant brain tumors. Full-length human idh1 (452 amino acids) with n-terminal hattag. arginine 132 is mutated to histidine. Group: Enzymes. Synonyms: Isocitrate dehydrogenase [NADP] cytoplasmic mutant, R132H; IDH 1 R132H. Purity: > 90% by SDS-PAGE. IDH. Mole weight: 50.9 kDa. Activity: >500 mU/mg. Storage: Lyophilized protein is stable for 1 year at -20°C. Once reconstituted aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. Form: Lyophilized powder with additives. Source: E. coli. Species: Human. Isocitrate dehydrogenase [NADP] cytoplasmic mutant, R132H; IDH 1 R132H; Isocitrate dehydrogenase; Isocitrate Dehydrogenase (NADP+). Cat No: NATE-1649. | |
| Native Bovine L-Glutamic Dehydrogenase | L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate. Mammalian forms of this enzyme, including this bovine form, can use either NADP (H) or NAD (H) as coenzymes. L-glutamic dehydrogenase plays a unique role in mammalian metabolism. The reverse reaction catalyzed by this enzyme is the only pathway by which ammonia can become bound to the α-carbon atom of an α-carboxylic acid and thus, is the only source of de novo amino acid synthesis in mammalian species. Group: Enzymes. Synonyms: glutamic dehydrogenase; glutamate dehydrogenase [NAD (P)]; 9029-12-3; glutamate dehydrogenase [NAD (P)+]; EC 1.4.1.3; L-GLDH; L-Glutamate:NAD[P]+ Oxidoreductase (deaminating). Enzyme Commission Number: EC 1.4.1.3. CAS No. 9029-12-3. GLDH. Activity: Type I, > 40 units/mg protein; Type II, > 20 units/mg protein; Type III, > 35 units/mg protein. Storage: 2-8°C. Form: Type I, ammonium sulfate suspension, Suspension in 2.0 M (NH4)2SO4 solution; Type II, lyophilized powder, Contains primarily Citrate buffer salt; Type III, aqueous glycerol solution, Solution in 50% glycerol, pH 7.3. Source: Bovine liver. Species: Bovine. glutamic dehydrogenase; glutamate dehydrogenase [NAD (P)]; 9029-12-3; glutamate dehydrogenase [NAD (P)+]; EC 1.4.1.3; L-GLDH; L-Glutamate:NAD[P]+ Oxidoreductase (deaminating). Cat No: NATE-0392. | |
| Native Candida boidinii Formate Dehydrogenase | Formate dehydrogenase is involved in the stress response of plants and catalyzes the reduction of NAD+ to NADH. Fdh is an abundant enzyme from yeast candida boidinii (cbfdh) that plays an important role in the energy supply of methylotrophic microorganisms and in the stress response of plants. Applications: Formate dehydrogenase (fdh) is used for diagnostics in large scale industrial pr ocesses. its used in the production of an unnatural amino acid, tert-l-leucine, a component of some hiv protease and matrix metalloprotease inhibitors. 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. Enzyme Commission Number: EC 1.2.1.2. CAS No. 9028-85-7. FDH. Activity: Type I, 5.0-15.0 units/mg protein; Type II, 0.3-0.6 units/mg; Type III, ~50 U/mL. Storage: -20°C. Form: Type I, lyophilized powder; Type II, powder; Type III, clear brown liquid. Source: Candida boidinii. 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-0254. | |
| Native Gluconobacter sp. D-Fructose Dehydrogenase | D-fructose dehydrogenase is a heterotrimeric membrane-bound enzyme commonly seen in various Gluconobacter sp. especially in Gluconobacter japonicus (Gluconobacter industrius). It has a molecular mass of ca. 140 kDa, consisting of subunits I (67kDa), II (51 kDa), and III (20 kDa) and catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose. The enzyme is a flavoprotein-cytochrome c complex with subunits I and II covalently bound to flavin adenine dinucleotide (FAD) and heme C as prosthetic groups, respectively. Applications: D-fructose dehydrogenase is used as a biosensor to detect the presence of d-fructose. this enzyme is also used in a number of basic res...tic determination of d-fructose in clinical analysis. Group: Enzymes. Synonyms: EC 1.1.99.11; fructose 5-dehydrogenase; D-fructose dehydrogenase; D-fructose: (acceptor) 5-oxidoreductase; 37250-85-4. Enzyme Commission Number: EC 1.1.99.11. CAS No. 37250-85-4. D-Fructose Dehydrogenase. Mole weight: mol wt ~140 kDa. Activity: > 20 units/mg solid; 400-1,200 units/mg protein. Storage: -20°C. Form: lyophilized powder. supplied as a lyophilized powder containing approx 80% stabilizers, sugars, amino acids and BSA. Source: Gluconobacter sp. EC 1.1.99.11; fructose 5-dehydrogenase; D-fructose dehydrogenase; D-fructose: (acceptor) 5-oxidoreductase; 37250-85-4. Cat No: NATE-0185. | |
| 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 Porcine Malate Dehydrogenase, IFCC Quality | Dehydrogenase that catalyzes the interconversion of malate to oxaloacetate. Rely on the proven diagnostic quality of this product. Tested according to the recommendations of the International Federation of Clinical Chemistry (IFCC). Applications: Use malate dehydrogenase in diagnostic tests for the determination of aspartate aminotransferase or in applications for citric and acetic acid testing. Group: Enzymes. Synonyms: Malate Dehydrogenase, IFCC Quality; malic dehydrogenase; L-malate dehydrogenase; malic acid dehydrogenase; MDH. MDH. Mole weight: 70 kDa. Activity: >70 U/mg lyophilizate. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White lyophilizate. Source: Porcine heart. Species: Porcine. Malate Dehydrogenase, IFCC Quality; malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; S-malate: NAD+ oxidoreductase; EC 1.1.1.37; Malate Dehydrogenase. Cat No: DIA-278. | |
| Native Proteus sp. Glutamate Dehydrogenase (NADP-dependent) | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Applications: This enzyme is useful for enzymatic determination of nh3, α-ketoglutaric acid and l-glutamic acid, and for assay of leucine aminopeptidase and urea...lutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Enzyme Commission Number: EC 1.4.1.4. Mole weight: approx. 300 kDa. Activity: 300U/mg-protein or more (9,000U/ml or more). Appearance: Solution with 50mM Tris-HCl buffer containing 0.05% NaN3 and 5.0mM EDTA, pH 7.8. Form: Freeze dried powder. Source: Proteus sp. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: DIA-196. | |
| Native Proteus sp. L-Glutamic Dehydrogenase (NADP) | L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate. Applications: This enzyme is useful for enzymatic determination of nh3, α-ketoglutaric acid and l-glutamic acid, and for assay of leucine aminopeptidase and urease. this enzyme is also used for enzymatic determination of urea when coupled with urease (urh-201) in clinical analysis. Group: Enzymes. Synonyms: L-Glutamic Dehydrogenase; EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD (P)-glutamate dehydrogenase; NAD (P)H-dependent glutamate de. Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. Mole weight: mol wt ~300 kDa. Activity: > 400 units/mg protein (biuret). Storage: 2-8°C. Form: buffered aqueous solution; Solution in 50 mM Tris HCl, pH 7.8, 5 mM Na2EDTA containing 0.05% sodium azide. Source: Proteus sp. L-Glutamic Dehydrogenase; EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD (P)-glutamate dehydrogenase; NAD (P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP). Cat No: NATE-0395. | |
| Native Sporosarcina sp. L-Phenylalanine Dehydrogenase | Phenylalanine dehydrogenase is a member of a large family of amino-acid dehydrogenases, which includes glutamate dehydrogenase, alanine dehydrogenase, leucine dehydrogenase, lysine EUR-dehydrogenase, and meso-a,EUR-diaminopimelate D-dehydrogenase. The three known gene sequences are octomers. It has a two-domain, three-dimensional structure. Applications: L-phenylalanine dehydrogenase is a nad+-dependent oxidoreductase that catalyzes the reversible, oxidative deamination of l-phenylalanine which results in its degradation. l-phenylalanine dehydrogenase is used to study phenylalanine metabolism and phenylalanine, tyrosine and tryptophan biosynthesis. Group: Enzymes. Synonyms: phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Enzyme Commission Number: EC 1.4.1.20. CAS No. 69403-12-9. PHD. Activity: > 6 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Sporosarcina sp. phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Cat No: NATE-0558. | |
| Native Thermoactinomyces intermedius Phenylalanine Dehydrogenase | Phenylalanine dehydrogenase is a member of a large family of amino-acid dehydrogenases, which includes glutamate dehydrogenase, alanine dehydrogenase, leucine dehydrogenase, lysine EUR-dehydrogenase, and meso-a,EUR-diaminopimelate D-dehydrogenase. The three known gene sequences are octomers. It has a two-domain, three-dimensional structure. Group: Enzymes. Synonyms: phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Enzyme Commission Number: EC 1.4.1.20. CAS No. 69403-12-9. PHD. Mole weight: ca. 380,000; Subunit molecular weight : ca. 40,000. Appearance: Ammonium sulphate suspension. Storage: Stable at 0 to 4 °C for at least six months (Do not freeze). Source: Thermoactinomyces intermedius. phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Cat No: NATE-1906. | |
| opine dehydrogenase | In the forward direction, the enzyme from Arthrobacter sp. acts also on secondary amine dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine. Dehydrogenation forms an imine, which dissociates to the amino acid and pyruvate. In the reverse direction, the enzyme acts also on neutral amino acids as an amino donor. They include L-amino acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, phenylalanine, leucine and alanine. The amino acceptors include 2-oxoacids such as pyruvate, oxaloacetate, glyoxylate and 2-oxobutyrate. Group: Enzymes. Synonyms: (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate dehydrogenase (NAD+, L-aminopentanoate-forming). Enzyme Commission Number: EC 1.5.1.28. CAS No. 108281-02-3. 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-1510; opine dehydrogenase; EC 1.5.1.28; 108281-02-3; (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate dehydrogenase (NAD+, L-aminopentanoate-forming). Cat No: EXWM-1510. | |
| Oxalacetic Acid (Oxaloacetic acid) | A four carbon dicarboxylic acid that is an intermediate in the citric acid cycle and glucogenesis. It has been shown to inhibit succinate dehydrogenase. Oxaloacetic acid, in the form of its conjugate base oxaloacetate, is a metabolic intermediate in many processes that occur in animals. It takes part in the: gluconeogenesis, urea cycle, glyoxylate cycle, amino acid synthesis, fatty acid synthesis and citric acid cycle. Gluconeogenesis[1] is a metabolic pathway consisting of a series of eleven enzyme-catalyzed reactions, resulting in the generation of glucose from non-carbohydrates substrates. The beginning of this process takes place in the mitochondrial matrix, where pyruvate molecules are found. A pyruvate molecule is carboxylated by a pyruvate carboxylase enzyme, activated by a molecule each of ATP and water. This reaction results in the formation of oxaloacetate. NADH reduces oxaloacetate to malate. This transformation is needed to transport the molecule out of the mitochondria. On Group: Biochemicals. Alternative Names: Oxobutanedioic Acid; Oxalacetic Acid; 2-Ketosuccinic acid; 2-Oxobutanedioic acid; 2-Oxosuccinic Acid; Ketosuccinic Acid; NSC 284205; NSC 77688; OAA; Oxaloacetic Acid; Oxaloethanoic Acid; Oxosuccinic Acid; α-Ketosuccinic Acid. Grades: Reagent Grade. CAS No. 328-42-7. Pack Sizes: 25g, 50g, 100g, 250g. Molecular Formula: C?H?O?, Molecular Weight: 132.07. US Biological Life Sciences. | Worldwide |
| Palifosfamide | Palifosfamide is a synthetic mustard compound with potential antineoplastic activity. An active metabolite of ifosfamide covalently linked to the amino acid lysine for stability, palifosfamide irreversibly alkylates and cross-links DNA through GC base pairs, resulting in irreparable 7-atom inter-strand cross-links; inhibition of DNA replication and cell death follow. Unlike ifosfamide, this agent is not metabolized to acrolein or chloroacetaldehyde, metabolites associated with bladder and CNS toxicities. In addition, because palifosfamide does not require activation by aldehyde dehydrogenase, it may overcome the tumor resistance seen with ifosfamide. Synonyms: Isophosphamide mustard; Isophosphoramide mustard; IPAM; bis(2-chloroethylamino)phosphinic acid. Grades: ≥ 98%. CAS No. 31645-39-3. Molecular formula: C4H11Cl2N2O2P. Mole weight: 221.018. | |
| PF 915275 | PF-915275 is a selective and potent and inhibitor of human 11β-hydroxysteroid dehydrogenase type 1(11βHSD1) inhibitor with Ki 2.3 nM. It has good preclinical pharmacokinetic properties. It inhibits the conversion of prednisone to prednisolone in human hepatocytes in vitro and has antidiabetic activity in vivo. It maintains potency in our cellular assay against human 11βHSD1 and is selective against human 11βHSD2 in vitro. It displays only weak affinity for the rodent choline transporter (Ki = 9.6 μM) and the hamster melatonin MT3 receptor (Ki = 9.6 μM) in the Cerep Bioprint screening panel. It has good in vitro pharmacokinetic properties. It has low clearance and high permeability. It has an excellent pharmacokinetic profile characterized by low clearance, long half-life and good oral bioavailability. Uses: Pf-915275 inhibits the conversion of prednisone to prednisolone in human hepatocytes in vitro and has antidiabetic activity in vivo. it has an excellent pharmacokinetic profile characterized by low clearance, long half-life and good oral bioavailability. Synonyms: PF-915275; PF 915275; PF915275; N-(6-Amino-2-pyridinyl)-4'-cyano-[1,1'-biphenyl]-4-sulfonamide;N-(6-aminopyridin-2-yl)-4-(4-cyanophenyl)benzenesulfonamide;[1,1'-Bip;4'-cyanobiphenyl-4-sulfonic acid (6-aminopyridin-2-yl)amide. Grades: >98 %. CAS No. 857290-04-1. Molecular formula: C18H14N4O2S. Mole weight: 350.39. | |
| Recombinant Ketol-acid reductoisomerase from Mycobacterium tuberculosis | Ketol-acid reductoisomerase catalyzes two steps in the biosynthesis of branched-chain amino acids. Group: Enzymes. Synonyms: dihydroxyisovalerate dehydrogenase (isomerizing); acetohydroxy acid isomeroreductase; ketol acid reductoisomerase; alpha-keto-beta-hydroxylacyl reductoisomerase; 2-hydroxy-3-keto acid reductoisomerase; acetohydroxy acid reductoisomerase; acetolactate reductoisomerase; dihydroxyisovalerate (isomerizing) dehydrogenase; isomeroreductase; reductoisomerase; EC 1.1.1.86. Enzyme Commission Number: EC 1.1.1.86. CAS No. 9075-2-9. Purity: > 80 %. Ketol-acid reductoisomerase. Mole weight: 38 kDa. Appearance: Colourless clear liquid. Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C. Source: E. coli. Species: Mycobacterium tuberculosis. dihydroxyisovalerate dehydrogenase (isomerizing); acetohydroxy acid isomeroreductase; ketol acid reductoisomerase; alpha-keto-beta-hydroxylacyl reductoisomerase; 2-hydroxy-3-keto acid reductoisomerase; acetohydroxy acid reductoisomerase; acetolactate reductoisomerase; dihydroxyisovalerate (isomerizing) dehydrogenase; isomeroreductase; reductoisomerase; EC 1.1.1.86. Cat No: NATE-1016. | |
| Sarcosine 99+% | Sarcosine, also known as N-methylglycine, is an intermediate and byproduct in glycine synthesis and degradation. Sarcosine is metabolized to glycine by the enzyme sarcosine dehydrogenase, while glycine-N-methyl transferase generates sarcosine from glycine. Sarcosine is a natural amino acid found in muscles and other body tissues. In the laboratory, it may be synthesized from chloroacetic acid and methylamine. Sarcosine is found naturally as an intermediate in the metabolism of choline to glycine. Sarcosine is sweet to the taste and dissolves in water. It is used in manufacturing biodegradable surfactants and toothpastes as well as in other applications. Group: Biochemicals. Alternative Names: Sar-OH; N-Methylglycine. Grades: Reagent Grade. CAS No. 107-97-1. Pack Sizes: 25g, 100g, 250g, 1Kg, 2.5Kg. US Biological Life Sciences. | Worldwide |
| Sodium Oxamate | Sodium oxamate is an inhibitor of lactate dehydrogenase (LDH), a key regulator of glycolysis, reversibly catalyzing the conversion of pyruvate to lactate. Synonyms: Sodium 2-amino-2-oxoacetate; Oxamic acid sodium salt. Grades: ≥95%. CAS No. 565-73-1. Molecular formula: C2H2NO3·Na. Mole weight: 111. | |
| Tris(hydroxymethyl)aminomethane | Tris(hydroxymethyl)aminomethane. Synonyms: Tris(Hydroxymethyl)Aminomethane. CAS No. 77-86-1. Product ID: CDC10-0247. Molecular formula: C4H11NO3. Category: Buffering Agents. Product Keywords: Cosmetic Ingredients; Buffering Agents; Tris(hydroxymethyl)aminomethane; CDC10-0247; 77-86-1; C4H11NO3; Tris(Hydroxymethyl)Aminomethane; 201-064-4; MFCD00004679; 77-86-1. Grade: AR. Purity: 0.995. Color: White Crystalline. EC Number: 201-064-4. Physical State: Powder. Quality Level: 200. Storage: Store in cool place. Keep container tightly closed in a dry and well-ventilated place. Application: Tris(hydroxymethyl)aminomethane has been used as a buffer solution for lactate dehydrogenase assay, in situ hybridization procedure and protein extraction from cells. Melting Point: 168.0-171.0. Product Description: Tris(hydroxymethyl)aminomethane is used as buffers in biochemistry and molecular biology laboratories. It is used as a primary standard to standardize acid solutions for chemical analysis. It finds application in cell membranes to increase its permeability. As an alternative to sodium bicarbonate, it used in the treatment of metabolic acidosis. |  |
| UDP-4-amino-4-deoxy-L-arabinose formyltransferase | The activity is part of a bifunctional enzyme also performing the reaction of EC 1.1.1.305 [UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)]. Group: Enzymes. Synonyms: UDP-L-Ara4N formyltransferase; ArnAFT. Enzyme Commission Number: EC 2.1.2.13. 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-2003; UDP-4-amino-4-deoxy-L-arabinose formyltransferase; EC 2.1.2.13; UDP-L-Ara4N formyltransferase; ArnAFT. Cat No: EXWM-2003. | |
| UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating) | The activity is part of a bifunctional enzyme also performing the reaction of EC 2.1.2.13 (UDP-4-amino-4-deoxy-L-arabinose formyltransferase). Group: Enzymes. Synonyms: UDP-GlcUA decarboxylase; ArnADH; UDP-glucuronate:NAD+ oxidoreductase (decarboxylating). Enzyme Commission Number: EC 1.1.1.305. 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-0216; UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating); EC 1.1.1.305; UDP-GlcUA decarboxylase; ArnADH; UDP-glucuronate:NAD+ oxidoreductase (decarboxylating). Cat No: EXWM-0216. | |
| UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase | This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the the enzyme catalysing the next step the pathway (EC 2.6.1.98, UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase). The enzyme also possesses an EC 1.1.99.2 (L-2-hydroxyglutarate dehydrogenase) activity, and utilizes the 2-oxoglutarate produced by EC 2.6.1.98 to regenerate the tightly bound NAD+. The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD+ as tightly and do not require 2-oxoglutarate to function. Group: Enzymes. Synonyms: WlbA; WbpB. Enzyme Commission Number: EC 1.1.1.335. 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-0249; UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase; EC 1.1.1.335; WlbA; WbpB. Cat No: EXWM-0249. | |
| uracil/thymine dehydrogenase | Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 3.5.2.1 (barbiturase) and EC 3.5.1.95 (N-malonylurea hydrolase). Mammals, plants and other microorganisms utilize the reductive pathway, comprising EC 1.3.1.1 [dihydrouracil dehydrogenase (NAD+)] or EC 1.3.1.2 [dihydropyrimidine dehydrogenase (NADP+)], EC 3.5.2.2 (dihydropyrimidinase) and EC 3.5.1.6 (β-ureidopropionase), with the ultimate degradation products being an L-amino acid, NH3 and CO2. Group: Enzymes. Synonyms: uracil oxidase; uracil-thymine oxidase; uracil dehydrogenase. Enzyme Commission Number: EC 1.17.99.4. CAS No. 9029-00-9. 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-1104; uracil/thymine dehydrogenase; EC 1.17.99.4; 9029-00-9; uracil oxidase; uracil-thymine oxidase; uracil dehydrogenase. Cat No: EXWM-1104. | |
| AKR1C3 Inhibitor (3- (4- (Trifluoromethyl) phenylamino) benzoic Acid) | A cell-permeable 3-phenyl-aminobenzoate compound that acts as a potent, competitive, reversible, active-site targeting inhibitor of aldo-keto reductase 1C3 (AKR1C3; type 5 17b-hydroxysteroid dehydrogenase) (IC50 = 60nM) with excellent selectivity over other closely related human AKR isoforms (IC50 = 22.7, 15.4, 62.7, >50, and >50uM for and AKR1C1, AKR1C2, AKR1C4, AKR1B1 and AKR1B10, respectively. Exhibits a weak inhibitory effect on cyclooxygenase 1 and 2 (IC50 = 100uM). Shown to efficiently block the AKR1C3-mediated production of testosterone in LNCaP-AKR1C3 cells (~10uM). Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 25mg. US Biological Life Sciences. | Worldwide |
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