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| Product | Description | |
|---|---|---|
| 2-Ketoglutaric acid | 100g Pack Size. Group: Biochemicals, Carbohydrates. Formula: C5H6O5. CAS No. 328-50-7. Prepack ID 12974102-100g. Molecular Weight 146.1. See USA prepack pricing. |  |
| 2-Ketoglutaric Acid-13C | 13C Labeled Compounds. Alternative Names: 2-Oxopentanedioic acid-13C. CAS No. 108395-15-9. Molecular formula: C413CH6O5. Mole weight: 147.09. Catalog: ACM108395159. |  |
| 2-Ketoglutaric Acid (alpha Ketoglutaric Acid) | 2-Ketoglutaric Acid (alpha Ketoglutaric Acid). Group: Biochemicals. Alternative Names: 2-Oxopentanedioic Acid; 2-Oxo-1,5-pentanedioic Acid; 2-Oxoglutaric Acid; 2-Oxopentanedioic Acid; NSC 17391; α-Ketoglutaric Acid; α-Oxoglutaric Acid; α-Oxopentanedioic Acid; α-keto-Glutaric Acid. Grades: Cell Culture Grade. CAS No. 328-50-7. Pack Sizes: 100g, 500g, 1Kg, 5Kg. Molecular Formula: C5H6O5, Molecular Weight: 146.1. US Biological Life Sciences. |  Worldwide |
| 2-Ketoglutaric Acid-d2 Cacium Salt (d3 major) | 2-Ketoglutaric Acid-d2 Cacium Salt is a isotope labelled derivative of glutaric acid and is an intermediate in the krebs cycle catalyzed by glutamate dehydrogenase enzyme on glutamate. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 5mg, 25mg. Molecular Formula: C5H2D2CaO5. US Biological Life Sciences. | Worldwide |
| 2-Ketoglutaric acid-d4 | 2-Ketoglutaric acid-d4 is the deuterium labeled 2-Ketoglutaric acid. 2-Ketoglutaric acid (Alpha-Ketoglutaric acid) is an intermediate in the production of ATP or GTP in the Krebs cycle. Group: Isotope-labeled synthetic intermediates. Alternative Names: Alpha-Ketoglutaric acid-d4. CAS No. 1381759-60-9. Molecular formula: C5H2D4O5. Mole weight: 150.12. Canonical SMILES: OC (C ([2H]) ([2H])C ([2H]) ([2H])C (C (O)=O)=O)=O. Catalog: ACM1381759609. | |
| 2-Ketoglutaric acid-d6 | 2H Labeled Compounds. CAS No. 1173021-86-7. Catalog: ACM1173021867. | |
| 2-Ketoglutaric acid disodium salt dihydrate | 100g Pack Size. Group: Biochemicals, Building Blocks. Formula: C5H4Na2O5 · 2H2O. CAS No. 305-72-6. Prepack ID 36337209-100g. Molecular Weight 226.09. See USA prepack pricing. | |
| 2-Ketoglutaric acid monopotassium salt | 100g Pack Size. Group: Biochemicals, Building Blocks. Formula: C5H5O5K. CAS No. 997-43-3. Prepack ID 37634186-100g. Molecular Weight 184.19. See USA prepack pricing. | |
| 2-Ketoglutaric acid monopotassium salt | 250g Pack Size. Group: Biochemicals, Building Blocks. Formula: C5H5O5K. CAS No. 997-43-3. Prepack ID 37634186-250g. Molecular Weight 184.19. See USA prepack pricing. | |
| 2-Ketoglutaric acid monosodium salt | 100g Pack Size. Group: Biochemicals. Formula: C5H5NaO5. CAS No. 22202-68-2. Prepack ID 68277085-100g. Molecular Weight 168.08. See USA prepack pricing. | |
| 2-Ketoglutaric acid (standard) | 2-Ketoglutaric acid (Standard) is the analytical standard of 2-Ketoglutaric acid. This product is intended for research and analytical applications. 2-Ketoglutaric acid (Alpha-Ketoglutaric acid) is an intermediate in the production of ATP or GTP in the Krebs cycle. 2-Ketoglutaric acid also acts as the major carbon skeleton for nitrogen-assimilatory reactions. 2-Ketoglutaric acid is a reversible inhibitor of tyrosinase ( IC 50 =15 mM) [1]. Uses: Scientific research. Group: Natural products. CAS No. 328-50-7. Pack Sizes: 10 mg; 25 mg; 50 mg. Product ID: HY-W013636R. |  |
| a-Ketoglutaric acid disodium salt | a-Ketoglutaric acid disodium salt. Group: Biochemicals. Grades: Reagent Grade. Pack Sizes: 100g, 250g, 25g, 1Kg, 5Kg. US Biological Life Sciences. | Worldwide |
| a-Ketoglutaric Acid Disodium Salt Dihydrate | a-Ketoglutaric Acid Disodium Salt Dihydrate. Group: Biochemicals. Alternative Names: 2-Oxoglutaric acid disodium salt; Disodium 2-ketoglutarate. Grades: Highly Purified. CAS No. 305-72-6. Pack Sizes: 50g, 100g, 250g, 500g, 1Kg. Molecular Formula: C5H4Na2O5·2H2O, Molecular Weight: 226.09. US Biological Life Sciences. | Worldwide |
| a-Ketoglutaric acid disodium salt dihydrate 99+% | a-Ketoglutaric acid disodium salt dihydrate 99+%. Group: Biochemicals. Grades: Reagent Grade. Pack Sizes: 25g, 100g, 250g, 1Kg, 5Kg. US Biological Life Sciences. | Worldwide |
| a-Ketoglutaric acid potassium salt | a-Ketoglutaric acid potassium salt. Group: Biochemicals. Alternative Names: 2-Oxopentanedioic acid potassium salt; Potassium hydrogen 2-ketoglutarate. Grades: Highly Purified. CAS No. 997-43-3. Pack Sizes: 25g, 50g, 100g. Molecular Formula: C?H?O?K, Molecular Weight: 184.19. US Biological Life Sciences. | Worldwide |
| Alpha-ketoglutaric acid-[3,3,4,4-d4] | Synonyms: alpha-ketoglutaric acid-3,3,4,4-d4; [2H4]-2-Oxoglutaric acid. Grades: 90% by CP; 98% atom D. Molecular formula: C5H2D4O5. Mole weight: 150.12. |  |
| Alpha Ketoglutaric Acid 98% HPLC | Alpha Ketoglutaric Acid 98% HPLC. |  CA, FL & NJ |
| β-Ketoglutaric Acid | β-Ketoglutaric Acid. Group: Biochemicals. Alternative Names: 3-oxo-Glutaric Acid; β-oxo-Glutaric Acid; 1,3-Dicarboxyacetone; 3-Ketoglutaric Acid; 3-Oxoglutaric Acid; 3-Oxopentanedioic Acid; Acetone-1,3-dicarboxylic Acid; s-Acetonedicarboxylic Acid; ; β-Oxoglutaric Acid. Grades: Highly Purified. CAS No. 542-05-2. Pack Sizes: 10g. Molecular Formula: C5H6O5, Molecular Weight: 146.1. US Biological Life Sciences. | Worldwide |
| 4-aminobutyrate-2-oxoglutarate transaminase | Requires pyridoxal phosphate. Some preparations also act on β-alanine, 5-aminopentanoate and (R,S)-3-amino-2-methylpropanoate. Group: Enzymes. Synonyms: β-alanine-oxoglutarate transaminase; aminobutyrate aminotransferase (ambiguous); β-alanine aminotransferase; β-alanine-oxoglutarate aminotransferase; γ-aminobutyrate aminotransaminase (ambiguous); γ-aminobutyrate transaminase (ambiguous); γ-aminobutyrate-α-ketoglutarate aminotransferase; γ-aminobutyrate-α-ketoglutarate transaminase; γ-aminobutyrate:α-oxoglutarate aminotransferase; γ-aminobutyric acid aminotransferase (ambiguous); γ-aminobutyric acid transaminase (ambiguous); γ-aminobutyric acid-α-ketoglutarate transaminase; γ-aminobutyric acid-α-ketoglutaric acid aminotransferase; γ-aminobutyric acid-2-oxoglutarate transaminase; γ-aminobutyric transaminase (ambiguous); 4-aminobutyrate aminotransferase (ambiguous); 4-aminobutyrate-2-ketoglutarate aminotransferase; 4-aminobutyrate-2-oxoglutarate aminotransferase;. Enzyme Commission Number: EC 2.6.1.19. CAS No. 9037-67-6. 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-2859; 4-aminobutyrate-2-oxoglutarate transaminase; EC 2.6.1.19; 9037-67- |  |
| Glutamate dehydrogenase | Glutamate dehydrogenase is an enzyme in both prokaryotes and eukaryotic mitochondria. Glutamate dehydrogenase can be used for the enzymatic determination of ammonia, alpha-ketoglutaric acid, L-glutamate and urease [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9001-46-1. Pack Sizes: 1 KU. Product ID: HY-E70003. | |
| 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. | |
| 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 α-Ketoglutarate Dehydrogenase | The oxoglutarate dehydrogenase complex (OGDC) or α-ketoglutarate dehydrogenase complex is an enzyme complex, most commonly known for its role in the citric acid cycle. Group: Enzymes. Synonyms: 2-ketoglutarate dehydrogenase; 2-oxoglutarate dehydrogenase; 2-oxoglutarate:lipoate oxidoreductase; 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-succinylating); α-k. Enzyme Commission Number: EC 1.2.4.2. CAS No. 9031-2-1. AKGDH. Activity: 0.1-1.0 units/mg protein (Lowry). Storage: -20°C. Form: buffered aqueous glycerol solution. Supplied as a 50% glycerol solution containing ~9 mg per mL bovine serum albumin, 30% sucrose, 1.5 mM EDTA, 1.5 mM EGTA, 1.5 mM 2-mercaptoethanol, 0.3% TRITON(TM) X-100, 0.003% sodium azide, and 15 mM potassium phosphate, pH 6.8. Source: Porcine heart. Species: Porcine. 2-ketoglutarate dehydrogenase; 2-oxoglutarate dehydrogenase; 2-oxoglutarate:lipoate oxidoreductase; 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-succinylating); α-ketoglutarate dehydrogenase; αketoglutaric acid dehydrogenase; α-ketoglutaric dehydrogenase; α-oxoglutarate dehydrogenase; AKGDH; OGDC; ketoglutaric dehydrogenase; oxoglutarate decarboxylase; oxoglutarate dehydrogenase; oxoglutarate dehydrogenase (lipoamide); EC 1.2.4.2; 9031-02-1. Cat No: NATE-0495. | |
| 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. | |
| Nopaline | Nopaline is a reductive conjugate of arginine and α-ketoglutaric acid found in plant tumors and is classified as a opine. Group: Biochemicals. Alternative Names: N-[ (1S) -4-[ (Aminoiminomethyl) amino]-1-carboxybutyl]-D-glutamic Acid. Grades: Highly Purified. CAS No. 22350-70-5. Pack Sizes: 100mg. US Biological Life Sciences. | Worldwide |
| oxoglutarate dehydrogenase (succinyl-transferring) | Contains thiamine diphosphate. It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, dihydrolipoyllysine-residue succinyltransferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61. Group: Enzymes. Synonyms: 2-ketoglutarate dehydrogenase; 2-oxoglutarate dehydrogenase; 2-oxoglutarate: lipoate oxidoreductase; 2-oxoglutarate:lipoamide 2-oxidored. Enzyme Commission Number: EC 1.2.4.2. CAS No. 9031-2-1. AKGDH. 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-1218; oxoglutarate dehydrogenase (succinyl-transferring); EC 1.2.4.2; 9031-02-1; 2-ketoglutarate dehydrogenase; 2-oxoglutarate dehydrogenase; 2-oxoglutarate: lipoate oxidoreductase; 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-succinylating); α-ketoglutarate dehydrogenase; αketoglutaric acid dehydrogenase; α-ketoglutaric dehydrogenase; α-oxoglutarate dehydrogenase; AKGDH; OGDC; ketoglutaric dehydrogenase; oxoglutarate decarboxylase; oxoglutarate dehydrogenase; oxoglutarate dehydrogenase (lipoamide). Cat No: EXWM-1218. | |
| Taurine Dioxygenase from E. coli, Recombinant | Taurine dioxygenase (TauD) is a Fe(II) and α-ketoglutaric aciddependent dioxygenase, which enables E.coli to use taurine as a sulfur source. The oligomeric state of the enzyme from E.coli is reported both as a dimer and tetramer. It contains a 2-His, 1- carboxylate facial triad, which is present in most members of the family of Fe(II)/ α-KG-dependent enzymes. TauD catalyzes the conversion of the amino acid taurine (2-aminoethane-1-sulfonic acid) to sulfite and aminoacetaldehyde. Group: Enzymes. Synonyms: TauD; 2-aminoethanesulfonate dioxygenase; Sulfate starvation-induced protein 3; SSI3; alpha-ketoglutarate-dependent taurine dioxygenase. Enzyme Commission Number: EC 1.14.11.17. Purity: > 90% by SDS-PAGE. Mole weight: 34.3 kDa, His tagged. Activity: >170 mU/mg. Storage: Aliquot and store at -20°C. Avoid repeated freeze-thaw cycles. Form: Liquid. Source: E. coli. TauD; 2-aminoethanesulfonate dioxygenase; Sulfate starvation-induced protein 3; SSI3; alpha-ketoglutarate-dependent taurine dioxygenase; Taurine dioxygenase. Cat No: NATE-1648. | |
| tryptophan transaminase | A pyridoxal-phosphate protein. Also acts on 5-hydroxytryptophan and, to a lesser extent, on the phenyl amino acids. Group: Enzymes. Synonyms: L-phenylalanine-2-oxoglutarate aminotransferase; tryptophan aminotransferase; 5-hydroxytryptophan-ketoglutaric transaminase; hydroxytryptophan aminotransferase; L-tryptophan aminotransferase; L-tryptophan transaminase. Enzyme Commission Number: EC 2.6.1.27. CAS No. 9022-98-4. 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-2866; tryptophan transaminase; EC 2.6.1.27; 9022-98-4; L-phenylalanine-2-oxoglutarate aminotransferase; tryptophan aminotransferase; 5-hydroxytryptophan-ketoglutaric transaminase; hydroxytryptophan aminotransferase; L-tryptophan aminotransferase; L-tryptophan transaminase. Cat No: EXWM-2866. | |
| 2,4-Pyridinedicarboxylic acid monohydrate | 2,4-Pyridinedicarboxylic acid (2,4-PDCA) is a compound that structurally mimics 2-oxoglutarate (2-OG, also known as α-ketoglutarate) and chelates zinc, thus affecting a range of enzymes. Synonyms: pyridine-2,4-dicarboxylic acid;hydrate. Grades: ≥ 98 %. CAS No. 207671-42-9. Molecular formula: C7H5NO4 · H2O. Mole weight: 185.13. | |
| (2S)-Octyl-α-hydroxyglutarate | (2S)-Octyl-α-hydroxyglutarate is a cell permeable derivative of the L-isomer of 2-Hydroxyglutaric Acid (H942575), a potential inhibitor of glutamate carboxypeptidase. Also, being structurally similar to α-ketoglutarate, it competitively inhibits α-ketoglutarate dependent dioxygenases. Group: Biochemicals. Grades: Highly Purified. CAS No. 1391194-64-1. Pack Sizes: 1mg, 5mg. Molecular Formula: C13H24O5. US Biological Life Sciences. | Worldwide |
| alanine transaminase | A pyridoxal-phosphate protein. 2-Aminobutanoate can act slowly instead of alanine. Group: Enzymes. Synonyms: glutamic-pyruvic transaminase; glutamic-alanine transaminase; GPT (ambiguous); β-alanine aminotransferase; alanine aminotransferase; alanine-α-ketoglutarate aminotransferase; alanine-pyruvate aminotransferase; ALT; glutamic acid-pyruvic acid transaminase; glutamic-pyruvic aminotransferase; L-alanine aminotransferase; L-alanine transaminase; L-alanine-α-ketoglutarate aminotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. Enzyme Commission Number: EC 2.6.1.2. CAS No. 9000-86-6. ALT. 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-2860; alanine transaminase; EC 2.6.1.2; 9000-86-6; glutamic-pyruvic transaminase; glutamic-alanine transaminase; GPT (ambiguous); β-alanine aminotransferase; alanine aminotransferase; alanine-α-ketoglutarate aminotransferase; alanine-pyruvate aminotransferase; ALT; glutamic acid-pyruvic acid transaminase; glutamic-pyruvic aminotransferase; L-alanine aminotransferase; L-alanine transaminase; L-alanine-α-ketoglutarate aminotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. Cat No: EXWM-2860. | |
| Alanine-Valine transaminase (Crude Enzyme) | Branched chain aminotransferase is an aminotransferase enzyme which acts upon branched-chain amino acids. It uses largely α-ketoglutarate in forming branched chain α-keto acids and glutamate. The biological function of branched chain aminotransferases (BCAT) is to catalyse the synthesis or degradation of the branched chain amino acids leucine, isoleucine, and valine. In humans, branched chain amino acids are essential and are degraded by BCATs. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Nutrition. Group: Enzymes. Synonyms: Transaminase B; branched-chain amino acid aminotransferase; branched-chain amino acid-glutamate Transaminase; branched-chain aminotransferase; L-branched chain amino acid aminotransferase; glutamate-branched-chain amino acid Transaminase. Enzyme Commission Number: EC 2.6.1.42. CAS No. 9054-65-3. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. Transaminase B; branched-chain amino acid aminotransferase; branched-chain amino acid-glutamate Transaminase; branched-chain aminotransferase; L-branched chain amino acid aminotransferase; glutamate-branched-chain amino acid Transaminase. Pack: 100ml. Cat No: NATE-1821. | |
| α-Hydroxyglutaric acid | α-Hydroxyglutaric acid (2-Hydroxyglutarate) is an α-hydroxy acid form of glutaric acid. α-Hydroxyglutaric acid is a competitive inhibitor of multiple α-ketoglutarate-dependent dioxygenases, including histone demethylases and the TET family of 5-methlycytosine (5mC) hydroxylases [1]. Uses: Scientific research. Group: Natural products. Alternative Names: 2-Hydroxyglutarate; 2-Hydroxyglutaric acid; 2-Hydroxypentanedioic acid. CAS No. 2889-31-8. Pack Sizes: 5 mg (67.52 mM * 0.5mL in Ethanol); 10 mg (67.52 mM * 1mL in Ethanol); 25 mg (67.52 mM * 2.5mL in Ethanol). Product ID: HY-113038B. | |
| α-Hydroxyglutaric acid-13C5 disodium | α-Hydroxyglutaric acid- 13 C 5 (sodium) is the 13 C labeled α-Hydroxyglutaric acid sodium[1]. α-Hydroxyglutaric acid (2-Hydroxyglutarate) sodium is an α-hydroxy acid form of glutaric acid. α-Hydroxyglutaric acid sodium is a competitive inhibitor of multiple α-ketoglutarate-dependent dioxygenases, including histone demethylases and the TET family of 5-methlycytosine (5mC) hydroxylases[2]. Uses: Scientific research. Group: Isotope-labeled compounds. Alternative Names: 2-Hydroxyglutarate- 13 C5 disodium; 2-Hydroxyglutaric acid- 13 C5 sodium; 2-Hydroxypentanedioic acid- 13 C5 disodium. CAS No. 2482467-23-0. Pack Sizes: 1 mg. Product ID: HY-113038AS. | |
| α-Hydroxyglutaric acid disodium | α-Hydroxyglutaric acid (2-Hydroxyglutarate) disodium is an α-hydroxy acid form of glutaric acid. α-Hydroxyglutaric acid disodium is a competitive inhibitor of multiple α-ketoglutarate-dependent dioxygenases, including histone demethylases and the TET family of 5-methlycytosine (5mC) hydroxylases [1]. Uses: Scientific research. Group: Natural products. Alternative Names: 2-Hydroxyglutarate disodium; 2-Hydroxyglutaric acid disodium; 2-Hydroxypentanedioic acid disodium. CAS No. 40951-21-1. Pack Sizes: 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-113038A. | |
| aspartate transaminase | A pyridoxal-phosphate protein. Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. Aspartate transaminase activity can be formed from the aromatic-amino-acid transaminase (EC 2.6.1.57) of Escherichia coli by controlled proteolysis, some EC 2.6.1.57 activity can be found in this enzyme from other sources; indeed the enzymes are identical in Trichomonas vaginalis. Group: Enzymes. Synonyms: glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutarate-glutamate aminotransferase; aspartate α-ketoglutarate transaminase; aspartate aminotransferase; aspartate-2-oxoglutarate transaminase; aspartic acid aminotransferase; aspartic aminot. Enzyme Commission Number: EC 2.6.1.1. CAS No. 9000-97-9. AST. 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-2839; aspartate transaminase; EC 2.6.1.1; 9000-97-9; glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutarate-glutamate aminotransferase; aspartate α-ketoglutarate transaminase; aspartate aminotransferase; aspartate-2-oxoglutarate transaminase; aspartic acid aminotransferase; aspartic aminotransferase; aspartyl aminotransferase; AST; glutamate-oxalacetate aminotransferase; glutamate-oxalate transaminase; glutamic-aspartic a | |
| Aspartate Transaminase (Crude Enzyme) | (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or serum glutamic oxaloacetic transaminase(SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme (EC 2. 6. 1. 1) that was first described by Arthur Karmen and colleagues in 1954. AST catalyzes the reversible transfer of an α-amino group between aspartate and glutamate and, as such, is an important enzyme in amino acid metabolism. AST is found in the liver, heart, skeletal muscle, kidneys, brain, and red blood cells. Serum AST level, serum ALT (alanine transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; medicine; biotechnology. Group: Enzymes. Synonyms: glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutarate-glutamate aminotransferase; aspartate α-ketoglutarate transaminase; aspartate aminotransferase; aspartate-2-oxoglutarate transaminase; aspartic a. Enzyme Commission Number: EC 2.6.1.1. CAS No. 9000-97-9. AST. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. glutamic-oxaloacetic transamina | |
| 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. | |
| diaminobutyrate-2-oxoglutarate transaminase | A pyridoxal-phosphate protein that requires potassium for activity.In the proteobacterium Acinetobacter baumannii, this enzyme is cotranscribed with the neighbouring ddc gene that also encodes EC 4.1.1.86, diaminobutyrate decarboxylase. Differs from EC 2.6.1.46, diaminobutyrate-pyruvate transaminase, which has pyruvate as the amino-group acceptor. This is the first enzyme in the ectoine-biosynthesis pathway, the other enzymes involved being EC 2.3.1.178, diaminobutyrate acetyltransferase and EC 4.2.1.108, ectoine synthase. Group: Enzymes. Synonyms: L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase; 2,4-diaminobutyrate 4-aminotransferase; diaminobutyrate aminotransferase; DABA aminotransferase; DAB aminotransferase; EctB; diaminibutyric acid aminotransferase; L-2,4-diamin. Enzyme Commission Number: EC 2.6.1.76. CAS No. 196622-96-5. 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-2916; diaminobutyrate-2-oxoglutarate transaminase; EC 2.6.1.76; 196622-96-5; L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase; 2,4-diaminobutyrate 4-aminotransferase; diaminobutyrate aminotransferase; DABA aminotransferase; DAB aminotransferase; EctB; diaminibutyric acid aminotransferase; L-2,4-diaminobutyrate:2-oxoglutarate 4-aminotransferase. Cat No: EXWM-2916. | |
| Diethyl 1,3-acetonedicarboxylate | Heterocyclic Organic Compound. Alternative Names: DIETHYL 1,3-ACETONEDICARBOXYLATE;DIETHYL 3-OXOGLUTARATE;DIETHYL 3-KETOGLUTARATE;DIETHYL ACETONE-1,3-DICARBOXYLATE;DIETHYL ACETONEDICARBOXYLATE;ETHYL ACETONEDICARBOXYLATE;1,3-ACETONEDICARBOXYLIC ACID DIETHYL ESTER;ACETONEDICARBOXYLIC ACID DIETHYL ESTER. CAS No. 105-50-0. Molecular formula: C9H14O5. Mole weight: 202.2. Density: 1.113g/mL at 25°C(lit.). Catalog: ACM105500. | |
| Dimethyl-1,3-acetonedicarboxylate | Dimethyl-1,3-acetonedicarboxylate is used in the preparation of optically active lycorane. It has also been substituted into bispidone derivatives for their use as ligands in PET imaging. Group: Biochemicals. Alternative Names: 3-Oxo-pentanedioic Acid 1,5-Dimethyl Ester; 3-Oxo-glutaric Acid Dimethyl Ester; 3-Oxo-pentanedioic Acid Dimethyl Ester; 1,3-Acetonedicarboxylic Acid Dimethyl Ester; 3-Oxopentanedioic Acid Dimethyl Ester; Acetone Dicarboxylic Acid Dimethyl Ester; Dimethyl 1,3-Acetonedicarboxylate; Dimethyl 2-Oxopropane-1,3-dicarboxylate; Dimethyl 3-Ketoglutarate; Dimethyl 3-Oxo-1,5-pentanedioate; Dimethyl 3-Oxoglutarate; Dimethyl 3-Oxopentanedioate; Dimethyl Acetonedicarboxylate; Dimethyl β-Ketoglutarate; Dimethyl β-Oxoglutarate; NSC 4677; β-Oxoglutaric Acid Dimethyl Ester. Grades: Highly Purified. CAS No. 1830-54-2. Pack Sizes: 10g. US Biological Life Sciences. | Worldwide |
| Disodium (R)-2-Hydroxyglutarate | Disodium (R)-2-Hydroxyglutarate is a competitive inhibitor of α-ketoglutarate-dependent dioxygenases with Ki of 0.628 mM. In U-87MG cells, (R)-2-Hydroxyglutarate acts as a weak antagonist of α-KG to inhibit α-KG-dependent histone demethylases and increase dimethylation on both H3K9 and H3K79. Synonyms: MDK4906; MDK 4906; MDK-4906; d-α-hydroxyglutaric acid disodium salt; (2R)-2-Hydroxyglutaric Acid Disodium Salt; D-alpha-Hydroxyglutaric acid (disodium salt). Grades: 98%. CAS No. 103404-90-6. Molecular formula: C5H6Na2O5. Mole weight: 192.08. | |
| Dl-4-hydroxy-2-ketoglutarate | Heterocyclic Organic Compound. Alternative Names: 2-Hydroxy-4-oxopentanedioic Acid. CAS No. 1187-99-1. Molecular formula: C5H6O6. Mole weight: 162.1. Appearance: Yellow solid. Catalog: ACM1187991. | |
| DL-4-Hydroxy-2-ketoglutarate dilithium salt | DL-4-Hydroxy-2-ketoglutarate dilithium salt. Group: Biochemicals. Alternative Names: 2-Hydroxy-4-oxopentanedioic acid. Grades: Highly Purified. CAS No. 1187-99-1. Pack Sizes: 5mg, 10mg, 25mg, 50mg, 100mg. Molecular Formula: C5H4O6Li2. US Biological Life Sciences. | Worldwide |
| D,L-Gabaculine, Hydrochloride (3-Amino-2,3-dihydrobenzoic Acid) | An irreversible inhibitor of mouse brain alpha-aminobutyric acid (GABA)-alpha-ketoglutarate transaminase. Group: Biochemicals. Alternative Names: 3-Amino-2,3-dihydrobenzoic Acid. Grades: Highly Purified. Pack Sizes: 10mg. US Biological Life Sciences. | Worldwide |
| glutamate dehydrogenase | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. Group: Enzymes. Synonyms: glutamic dehydrogenase; glutamate dehydrogenase (NAD); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD-dependent glutamate dehydrogenase; NAD-dependent glutamic dehydrogenase; NAD-glutamate dehydrogenase; NAD-linked glutamate dehydrogenase; NAD-linked glutamic dehydrogenase; NAD-specific glutamic dehydrogenase; NAD-specific glutamate dehydrogenase; N. Enzyme Commission Number: EC 1.4.1.2. CAS No. 9001-46-1. GLDH. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1453; glutamate dehydrogenase; EC 1.4.1.2; 9001-46-1; glutamic dehydrogenase; glutamate dehydrogenase (NAD); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD-dependent glutamate dehydrogenase; NAD-dependent glutamic dehydrogenase; NAD-glutamate dehydrogenase; NAD-linked glutamate dehydrogenase; NAD-linked glutamic dehydrogenase; NAD-specific glutamic dehydrogenase; NAD-specific glutamate dehydrogenase; NAD:glutamate oxidoreductase; NADH-linked glutamate dehydrogenase. Cat No: EXWM-1453. | |
| Glutamate Dehydrogenase from Thermophilic Bacterium, recombinant | GDH is an oxidoreductase enzyme which relates carbon and nitrogen metabolism. It catalyzes the reduction of α-ketoglutarate and ammonia to L-glutamate and vice versa. This enzyme is a robust and ideal candidate for research use, and industrial applications in the diagnostics and food industries. Group: Enzymes. Synonyms: glutamate dehydrogenase; glutamic dehydrogenase; glutamate dehydrogenase (NAD+); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD+-dependent glutamate dehydrogenase; NAD+-dependent glutamic dehyd. Enzyme Commission Number: EC 1.4.1.2. CAS No. 9001-46-1. GLDH. Mole weight: 270 kDa; Homohexameric ( 45 kDa per subunit). Activity: > 90 U/mg protein. Storage: at -20 °C. Form: Lyophilized powder. Source: E. coli. Species: Thermophilic Bacterium. glutamate dehydrogenase; glutamic dehydrogenase; glutamate dehydrogenase (NAD+); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD+-dependent glutamate dehydrogenase; NAD+-dependent glutamic dehydrogenase; NAD+-glutamate dehydrogenase; NAD+-linked glutamate dehydrogenase; NAD+-linked glutamic dehydrogenase; NAD+-specific glutamic dehydrogenase; NAD+-specific glutamate dehydrogenase; NAD+:glutamate oxidoreductase; NADH-linked glutamate dehydrogenase; GLDH; EC 1.4.1.2. Cat No: NATE-1701. | |
| glutamate dehydrogenase (NADP+) | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. Group: Enzymes. Synonyms: glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP). Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1459; glutamate dehydrogenase (NADP+); EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP). Cat No: EXWM-1459. | |
| Glutamate Dehydrogenase (NAD(P)) from E.coli, Recombinant | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Applications: Use recombinant glutamate dehydrogenase in diagnostic tests for the determination of ammonia, urea, l-glutamate, glutamate pyruvate transaminase and leucine aminopeptidase. Group: Enzymes. Synonyms: glu. CAS No. 9029-12-3. GLDH. Mole weight: ~2 200 kD for the associated enzyme with 8 subunits; 280 kD for one subunit. Activity: >80 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White lyophilizate. Source: E.coli. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: NATE-0981. | |
| Glutamate 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 | |
| Histone Lysine Demethylase Inhibitor VII, GSK-J1 (3-(6-(4,5-Dihydro-1H-benzo[d]azepin-3(2H)-yl)-2-(pyridin-2-yl)pyrimidin-4-ylamino)propanoic Acid, JHDM Inhibitor II) | A pyridinyl -pyrimidinyl aminopropanoic acid that effectively inhibits KDM6 family H3K27m3 demethylases JMJD3 and UTX (IC50 = 18 and 56uM, respectively, by MALDI Mass detection) in an alpha-ketoglutarate-competitive, peptide substrate-non-competitive manner, displaying much reduced potency against JARID1C, JMJD1a, JMJD2a, JMJD2c, JMJD2d, JMJD2e, as well as112 kinases and 60 non-kinase enzymes. Recommended for cell-free assays only. For culture treatment, use the cell-permeable pro-drug GSK-J4. Group: Biochemicals. Grades: Highly Purified. CAS No. 1373422-53-7. Pack Sizes: 10mg. US Biological Life Sciences. | Worldwide |
| 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, 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. | |
| JMJD Histone Demethylase Inhibitor III ( (E) -4- (Hydroxy (4- (4- ( (naphthalen-1-ylcarbamoyloxy) methyl) benzylamino) butyl) amino) -4-oxobut-2-enoic Acid) | A substrate (methyl lysine) and cofactor (a-ketoglutarate) mimicking bivalent benzylamino-butylamino-N-hydroxybutenoic acid compound that acts as a selective in vitro inhibitor of Jumonji domain-containing histone demethylases (JHDMs; IC50=4.3, 3.4, 5.9, 10 and 43uM for JMJD2A, JMJD2C, JMJD2E, PHF8 and JMJD3, respectively) over LSD1, asparaginyl and prolyl hydroxylases, and histone deacetylases (IC50=54, 83, 31, 22, 620, 680 and >800uM for PHD1, PHD2, PHD3, FIH, LSD1 and HDACs, respectively). The cellular active JHDM Inhibitor, Methylstat is also available. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 5mg. US Biological Life Sciences. | Worldwide |
| L-Arginine α-ketoglutarate | L-Arginine α-ketoglutarate is a salt form of arginine, which is the nitrogen donor for synthesis of nitric oxide, a potent vasodilator that is deficient during times of sickle cell crisis. Protein supplement in health care products. Uses: Ingredient of health care products. Synonyms: Arginine oxoglurate; L-Arginine alpha-Ketoglutarate(1:1); (S)-2-Amino-5-guanidinopentanoic acid 2-oxopentanedioic acid (1:1); L-Arginine alpha-ketoglutarate. Grades: 95%. CAS No. 16856-18-1. Molecular formula: C11H20N4O7. Mole weight: 320.302. | |
| leucine transaminase | A pyridoxal-phosphate protein. This enzyme differs from EC 2.6.1.42, branched-chain-amino-acid transaminase, in that it does not act on L-valine or L-isoleucine, although it does act on L-methionine. The mitochondrial form from rat liver differs in physical characteristics from the cytoplasmic form. Group: Enzymes. Synonyms: L-leucine aminotransferase; leucine 2-oxoglutarate transaminase; leucine aminotransferase; leucine-α-ketoglutarate transaminase. Enzyme Commission Number: EC 2.6.1.6. CAS No. 9030-37-9. 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-2901; leucine transaminase; EC 2.6.1.6; 9030-37-9; L-leucine aminotransferase; leucine 2-oxoglutarate transaminase; leucine aminotransferase; leucine-α-ketoglutarate transaminase. Cat No: EXWM-2901. | |
| 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 | |
| Malonyl coenzyme A lithium salt | Malonyl coenzyme A lithium salt is a coenzyme A derivative of malonic acid. Malonyl CoA is involved in chain elongation during fatty acid and polyketide synthesis. Malonyl CoA is also used in transporting alpha-ketoglutarate across the mitochondrial membrane into the mitochondrial matrix. Applications: A coenzyme a derivative involved in fatty acid regulation and biosynthesis. Group: Coenzymes. CAS No. 108347-84-8. Purity: ≥90%. Mole weight: 853.58. Appearance: Powder. Form: Solid. Malonyl coenzyme A lithium salt; 108347-84-8. Cat No: COEC-009. | |
| Moniliformin potassium salt | It is a potent, water-soluble mycotoxin produced by several species of fusarium. It selectively inhibits mitochondrial oxidization of pyruvate and α-ketoglutarate. Synonyms: Semisquaric acid potassium salt; 3-Cyclobutene-1,2-dione, 3-hydroxy-, potassium salt; 1-Hydroxycyclobut-1-ene-3,4-dione potassium salt. Grades: >99% by HPLC. CAS No. 52591-22-7. Molecular formula: C4HKO3. Mole weight: 136.15. | |
| Native Bovine L-Glutamic Dehydrogenase | L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate. Mammalian forms of this enzyme, including this bovine form, can use either NADP (H) or NAD (H) as coenzymes. L-glutamic dehydrogenase plays a unique role in mammalian metabolism. The reverse reaction catalyzed by this enzyme is the only pathway by which ammonia can become bound to the α-carbon atom of an α-carboxylic acid and thus, is the only source of de novo amino acid synthesis in mammalian species. Group: Enzymes. Synonyms: glutamic dehydrogenase; glutamate dehydrogenase [NAD (P)]; 9029-12-3; glutamate dehydrogenase [NAD (P)+]; EC 1.4.1.3; L-GLDH; L-Glutamate:NAD[P]+ Oxidoreductase (deaminating). Enzyme Commission Number: EC 1.4.1.3. CAS No. 9029-12-3. GLDH. Activity: Type I, > 40 units/mg protein; Type II, > 20 units/mg protein; Type III, > 35 units/mg protein. Storage: 2-8°C. Form: Type I, ammonium sulfate suspension, Suspension in 2.0 M (NH4)2SO4 solution; Type II, lyophilized powder, Contains primarily Citrate buffer salt; Type III, aqueous glycerol solution, Solution in 50% glycerol, pH 7.3. Source: Bovine liver. Species: Bovine. glutamic dehydrogenase; glutamate dehydrogenase [NAD (P)]; 9029-12-3; glutamate dehydrogenase [NAD (P)+]; EC 1.4.1.3; L-GLDH; L-Glutamate:NAD[P]+ Oxidoreductase (deaminating). Cat No: NATE-0392. | |
| Native Candida utilis L-Glutamic Dehydrogenase (NADP) | L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate. Group: Enzymes. Synonyms: L-Glutamic Dehydrogenase; EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD (P)-glutamate dehydrogenase; NAD (P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP). Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. Activity: 50-200 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salt. Source: Candida utilis. L-Glutamic Dehydrogenase; EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD (P)-glutamate dehydrogenase; NAD (P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP). Cat No: NATE-0394. | |
| Native E. coli Alanine Aminotransferase | Alanine transaminase (ALT) is a transaminase enzyme (EC 2.6.1.2). It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate-pyruvate transaminase (SGPT) or serum glutamic-pyruvic transaminase (SGPT). ALT is found in plasma and in various body tissues, but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Group: Enzymes. Synonyms: Alanine transami. Enzyme Commission Number: EC 2.6.1.2. CAS No. 9000-86-6. Purity: > 95% (SDS-PAGE). ALT. Mole weight: 54,479 of subunit deduced from gene sequence. Activity: > 1,000 U/mL. Storage: -20°C. Form: Liquid. Source: E. coli. Alanine transaminase; ALT; EC 2.6.1.2; alanine aminotransferase; ALAT; glutamic-pyruvic transaminase; glutamic-alanine transaminase; GPT; β-alanine aminotransferase; alanine-α-ketoglutarate aminotransferase; alanine-pyruvate aminotransferase; glutamic acid-pyruvic acid transaminase; glutamic-pyruvic aminotransferase; L-alanine aminotransferase; L-alanine transaminase; L-alanine-α-ketoglutarate aminotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. Cat No: NATE-0064. | |
| Native Glutamate dehydrogenase (NADP+) from Yeast | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Group: Enzymes. Synonyms: glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate d. Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. Activity: > 10 U/mg protein. Storage: Below -20°C. Form: Lyophilized Powder. Source: Yeast. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: NATE-1037. | |
| Native Human Alanine Aminotransferase | Alanine transaminase (ALT) is a transaminase enzyme (EC 2.6.1.2). It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate-pyruvate transaminase (SGPT) or serum glutamic-pyruvic transaminase (SGPT). ALT is found in plasma and in various body tissues, but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Alanine transaminase, also commonly known as serum glutamate pyruvate transaminase is an enzyme involved in the synthesis o...oup: Enzymes. Synonyms: Alanine transaminase; ALT; EC 2.6.1.2; alanine aminotransferase; ALAT; glutamic-pyruvic transaminase; glutamic-alanine transaminase; GPT; β-alanine aminotransferase; alanine-α-ketoglutarate aminotransferase; alanine-pyruvate aminotransferase; glutamic acid-pyruvic acid transaminase; glutamic-pyruvic aminotransferase; L-alanine aminotransferase; L-alanine transaminase; L-alanine-α-ketoglutarate aminotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. Enzyme Commission Number: EC 2.6.1.2. CAS No. 9000-86-6. ALT. Activity: >5 U /mg. Storage: -20°C. Source: Human Liver. Species: Human. | |
| Native Human Aspartate Aminotransferase | Aspartate Aminotransferase (AST), also known as Glutamate Oxaloacetate Transaminase (GOT), is a pyridoxal phosphate-dependant enzyme which exists in two isoenzymes; mitochondrial and cytosolic forms. The AST enzyme plays an important role in amino acid metabolism and in the urea and tricarboxylic acid cycles. In liver about 80% of the enzyme activity is mitochondrial in origin, whereas in serum the enzyme activity is largely cytosolic. In hepatic disease, serum levels are used to assess liver necrosis and for determining prognosis. In patients with acute Myocardial infarction, measurement of AST isoenzymes provides diagnostic information that differs from that obtained by determination of other marker proteins. Creative Enzymes products are not intended for use in pharmaceutical applications. Applications: Research life science elisa assay clinical chemistry. Group: Enzymes. Synonyms: EC 2.6.1.1; glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutaRate-glutamate aminotransferase; aspartate α-ketoglutaRate transaminase; aspartate aminotransferase; aspartate-2-oxoglutaRate transaminase; aspartic acid aminotransferas. Enzyme Commission Number: EC 2.6.1.1. CAS No. 9000-97-9. AST. Activity: >50U/ml. Storage: -20°C. Source: Human Cardiac Tissue. Species: Human. EC 2.6.1.1; glutamic-oxaloa | |
| Native Porcine Glutamic-Oxalacetic Transaminase | Aspartate transaminase (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or serum glutamic oxaloacetic transaminase (SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme (EC 2.6.1.1). AST catalyzes the reversible transfer of an α-amino group between aspartate and glutamate and, as such, is an important enzyme in amino acid metabolism. AST is found in the liver, heart, skeletal muscle, kidneys, brain, and red blood cells. Serum AST level, serum ALT (alanine transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Group: Enzymes. Synonyms: EC 2.6.1.1; glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutaRate-glutamate aminotransferase; aspartate α-ketoglutaRate transaminase; aspartate aminotransferase; aspartate-2-oxoglutaRate transaminase; aspartic acid aminotr. Enzyme Commission Number: EC 2.6.1.1. CAS No. 9000-97-9. Activity: > 100 U/mg. Storage: 2-8°C. Source: Porcine heart. Species: Porcine. EC 2.6.1.1; glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutaRate-glutamate aminotransferase; aspartate α-ketoglutaRate transaminase; aspartate aminotransferase; aspartate-2-oxoglutaRate transa | |
| Native Porcine Glutamic-Pyruvic Transaminase | Alanine transaminase (ALT) is a transaminase enzyme (EC 2.6.1.2). It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate-pyruvate transaminase (SGPT) or serum glutamic-pyruvic transaminase (SGPT). ALT is found in plasma and in various body tissues, but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Group: Enzymes. Synonyms: Alanine transaminase; ALT; EC 2.6.1.2; alanine aminotransferase; ALA. Enzyme Commission Number: EC 2.6.1.2. CAS No. 9000-86-6. Activity: 100 U/mg. Storage: -20°C. Form: Freeze dried powder. Source: Porcine heart. Species: Porcine. Alanine transaminase; ALT; EC 2.6.1.2; alanine aminotransferase; ALAT; glutamic-pyruvic transaminase; glutamic-alanine transaminase; GPT; β-alanine aminotransferase; alanine-α-ketoglutarate aminotransferase; alanine-pyruvate aminotransferase; glutamic acid-pyruvic acid transaminase; glutamic-pyruvic aminotransferase; L-alanine aminotransferase; L-alanine transaminase; L-alanine-α-ketoglutarate aminotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. Cat No: NATE-0068. | |
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