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| Product | Description | |
|---|---|---|
| Isocitrate Dehydrogenase 1 (NADP+) human | recombinant, expressed in Sf9 cells, ?90% (SDS-PAGE). Group: Fluorescence/luminescence spectroscopy. |  |
| isocitrate dehydrogenase (NAD+) | Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.42, isocitrate dehydrogenase (NADP+), oxalosuccinate cannot be used as a substrate. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD+-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP+-linked enzyme that is found in both mitochondria and cytoplasm. The enzyme from some species can also use NADP+ but much more slowly. Group: Enzymes. Synonyms: isocitric dehydrogenase; β-ketoglutaric-isocitric carboxylase; isocitric acid dehydrogenase; NAD dependent isocitrate dehydrogenase; NAD isocitrate dehydrogenase; NAD-linked isocitrate dehydrogenase; NAD-specific isocitrate dehydr. Enzyme Commission Number: EC 1.1.1.41. CAS No. 9001-58-5. IDH. 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-0326; isocitrate dehydrogenase (NAD+); EC 1.1.1.41; 9001-58-5; isocitric dehydrogenase; β-ketoglutaric-isocitric carboxylase; isocitric acid dehydrogenase; NAD dependent isocitrate dehydrogenase; NAD isocitrate dehydrogenase; NAD-linked isocitrate dehydrogenase; NAD-specific isocitrate dehydrogenase; NAD isocitric dehydrogenase; isocitrate dehydrogenase (NAD); IDH (ambiguous); nicotinamide adenine dinucleotide isocitrate dehydrogenase. Cat No: EXWM-0326. |  |
| 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+) | Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+), oxalosuccinate can be used as a substrate. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD+-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP+-linked enzyme that is found in both mitochondria and cytoplasm. The enzyme from some species can also use NAD+ but much more slowly. Group: Enzymes. Synonyms: ox. Enzyme Commission Number: EC 1.1.1.42. CAS No. 9028-48-2. IDH. 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-0327; isocitrate dehydrogenase (NADP+); EC 1.1.1.42; 9028-48-2; oxalosuccinate decarboxylase; oxalsuccinic decarboxylase; isocitrate (NADP) dehydrogenase; isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; NADP-specific isocitrate dehydrogenase; NADP-linked isocitrate dehydrogenase; NADP-dependent isocitrate dehydrogenase; NADP isocitric dehydrogenase; isocitrate dehydrogenase (NADP-dependent); NADP-dependent isocitric dehydrogenase; triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase; NADP+-linked isocitrate dehydrogenase; IDH (ambiguous); dual-cofactor-specific isocitrate dehydrogenase; NADP+-ICDH; NADP+-IDH; IDP; IDP1; IDP2; IDP3. | |
| 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 | |
| [isocitrate dehydrogenase (NADP+)] kinase | The enzyme has no activating compound but is specific for its substrate. Phosphorylates and inactivates EC 1.1.1.42, isocitrate dehydrogenase (NADP+). Group: Enzymes. Synonyms: [isocitrate dehydrogenase (NADP)] kinase; ICDH kinase/phosphatase; IDH kinase; IDH kinase/phosphatase; IDH-K/P; IDHK/P; isocitrate dehydrogenase kinase (phosphorylating); isocitrate dehydrogenase kinase/phosphatase; STK3. Enzyme Commission Number: EC 2.7.11.5. CAS No. 83682-93-3. 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-3156; [isocitrate dehydrogenase (NADP+)] kinase; EC 2.7.11.5; 83682-93-3; [isocitrate dehydrogenase (NADP)] kinase; ICDH kinase/phosphatase; IDH kinase; IDH kinase/phosphatase; IDH-K/P; IDHK/P; isocitrate dehydrogenase kinase (phosphorylating); isocitrate dehydrogenase kinase/phosphatase; STK3. Cat No: EXWM-3156. | |
| 2-oxoglutarate carboxylase | A biotin-containing enzyme that requires Mg2+ for activity. It was originally thought that this enzyme was a promoting factor for the carboxylation of 2-oxoglutarate by EC 1.1.1.41, isocitrate dehydrogenase (NAD+), but this has since been disproved. The product of the reaction is unstable and is quickly converted into isocitrate by the action of EC 1.1.1.41. Group: Enzymes. Synonyms: oxalosuccinate synthetase; carboxylating factor for ICDH (incorrect); CFI; OGC. Enzyme Commission Number: EC 6.4.1.7. CAS No. 60382-75-4. 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-5818; 2-oxoglutarate carboxylase; EC 6.4.1.7; 60382-75-4; oxalosuccinate synthetase; carboxylating factor for ICDH (incorrect); CFI; OGC. Cat No: EXWM-5818. | |
| D-2-Hydroxyglutarate Dehydrogenase from Acidaminococcus fermentans, Recombinant | D-2-hydroxyglutarate (D2HG) level is significantly increased in metabolic diseases and various cancers such as acute myeloid leukemia. Studies suggest that the detection of D2HG serves as a biomarker assay related to IDH (isocitrate dehydrogenase) mutations. D2HGDH is a special NAD-dependent enzyme which reacts with D2HG specifically and converts D2HG to α-ketoglutarate. D2HGDH is a key enzyme to distinguish between two metabolites, D2HG and L-2-hydroxyglutarate (L2HG), during biomarker assays. Group: Enzymes. Synonyms: D-2-hydroxyglutarate dehydrogenase; D2HGDH; D2HGD. Enzyme Commission Number: EC 1.1.99.39. Purity: > 99% by SDS - PAGE. Mole weight: 39 kDa. Activity: > 90,000 mU/mg. Storage: Can be stored at 4°C up to 2 weeks. For long term storage, aliquot and store at -20°C. Avoid repeated freezing and thawing cycles. Form: Lyophilized in 50mM Tris, pH 8 without any additives. Source: E. coli. Species: Acidaminococcus fermentans. D-2-hydroxyglutarate dehydrogenase; D2HGDH; D2HGD. Cat No: NATE-1660. | |
| Isocitrate dehydrogenase, Porcine heart | Isocitrate dehydrogenase, Porcine heart (ICDH) is a citric acid or tricarboxylic acid cycle enzyme, is often used in biochemical studies. Isocitrate dehydrogenase catalyzes the oxidative decarboxylation of isocitrate to α-ketoglutarate and reduces NAD(P) + to NAD(P)H, it plays important roles in cellular metabolism [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: ICDH; IDH. CAS No. 9028-48-2. Pack Sizes: 5 mg; 10 mg. Product ID: HY-P2993. |  |
| isocitrate-homoisocitrate dehydrogenase | Requires Mn2+ and K+ or NH4+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+) and EC 1.1.1.87, homoisocitrate dehydrogenase, this enzyme, from Pyrococcus horikoshii, can use both isocitrate and homoisocitrate as substrates. The enzyme may play a role in both the lysine and glutamate biosynthesis pathways. Group: Enzymes. Synonyms: homoisocitrate-isocitrate dehydrogenase; PH1722. Enzyme Commission Number: EC 1.1.1.286. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0194; isocitrate-homoisocitrate dehydrogenase; EC 1.1.1.286; homoisocitrate-isocitrate dehydrogenase; PH1722. Cat No: EXWM-0194. | |
| 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 Porcine Isocitric Dehydrogenase (NADP) | 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 of NAD+. They localize to the cytosol as well as the mitochondrion and peroxisome. Group: Enzymes. Synonyms: oxalosuccinate decarboxylase; Isocitrate dehyd. Enzyme Commission Number: EC 1.1.1.42. CAS No. 9028-48-2. IDH. Activity: Type I, 0.5-3.0 unit/mg solid; Type II, 3-20 units/mg protein. Storage: -20°C. Form: Type II, buffered aqueous glycerol solution, Solution in 50% glycerol in EDTA buffer salts, pH 6.0. Source: Porcine heart. Species: Porcine. oxalosuccinate decarboxylase; Isocitrate dehydrogenase (NADP); oxalsuccinic decarboxylase; Isocitrate (NADP) dehydrogenase; Isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; NADP-specific Isocitrate dehydrog | |
| Oxalomalic acid sodium salt | Oxalomalic acid is an inhibitor of both aconitase and NADP-dependent isocitrate dehydrogenase, At 5 mM, oxalomalic acid inhibition of aconitase leads to a decrease in the binding activity of IRP1 and a decrease in glutamate secretion in cultured lens epithelial cells, retinal pigment epithelial cells, and neurons. Synonyms: Oxalomalic acid trisodium salt. Grades: ≥95%. CAS No. 89304-26-7. Molecular formula: C6H6O8·3Na. Mole weight: 275. |  |
| Oxalomalic acid trisodium | Oxalomalic acid (Oxalomalate) trisodium is a aconitase and NADP-dependent isocitrate dehydrogenase inhibitor. Oxalomalic acid trisodium inhibits nitrite production and iNOS protein expression in lipopolysaccharide (HY-D1056)-activated J774 macrophages [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Oxalomalate trisodium. CAS No. 89304-26-7. Pack Sizes: 5 mg. Product ID: HY-131521. | |
| Isocitric Dehydrogenase (NADP) from porcine heart | Type I, 0.5-3.0 unit/mg solid (plus numerous enzyme activities associated with porcine heart). Group: Fluorescence/luminescence spectroscopy. | |
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