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| Product | Description | |
|---|---|---|
| Oxaloacetic acid | ?97% (HPLC). Group: Fluorescence/luminescence spectroscopy. |  |
| Oxaloacetic acid | Oxaloacetic acid (2-Oxosuccinic acid) is a metabolic intermediate involved in several ways, such as citric acid cycle, gluconeogenesis, the urea cycle, the glyoxylate cycle, amino acid synthesis, and fatty acid synthesis, whereby Oxaloacetic acid facilitates the clearance of reactive oxygen species ( ROS ) and improves mitochondrial function [1] [2] [3]. Uses: Scientific research. Group: Natural products. Alternative Names: 2-Oxosuccinic acid. CAS No. 328-42-7. Pack Sizes: 10 mM * 1 mL; 100 mg; 500 mg. Product ID: HY-W010382. |  |
| Oxaloacetic acid-13C4 | Oxaloacetic acid- 13 C 4 is the 13 C-labeled Oxaloacetic acid. Oxaloacetic acid (2-Oxosuccinic acid) is a metabolic intermediate involved in several ways, such as citric acid cycle, gluconeogenesis, the urea cycle, the glyoxylate cycle, amino acid synthesis, and fatty acid synthesis[1][2][3]. Uses: Scientific research. Group: Isotope-labeled compounds. Alternative Names: 2-Oxosuccinic acid- 13 C4. CAS No. 161096-82-8. Pack Sizes: 1 mg. Product ID: HY-W010382S. | |
| Oxaloacetic Acid-13C4 | Oxaloacetic Acid-13C4 is labelled form of Oxaloacetic Acid (O845030) which is a four carbon dicarboxylic acid that is an intermediate in the citric acid cycle and glucogenesis. It has been shown to inhibit succinate dehydrogenase. Group: Biochemicals. Grades: Highly Purified. CAS No. 161096-82-8. Pack Sizes: 1mg, 2.5mg. Molecular Formula: 13C4H4O5, Molecular Weight: 136.04. US Biological Life Sciences. |  Worldwide |
| 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 |
| 2-Methylcitric Acid | 2-Methylcitric Acid is a metabolite of Citric Acid. It is formed from the condensation of propionoyl-CoA and oxaloacetic acid catalyzed by a citrate synthase enzyme. 2-Methylcitric acid is an endogenous tricarboxylic acid formed by the condensation of propionyl-CoA with oxaloacetic acid by citrate synthase under conditions of propionyl-CoA accumulation. Accumulation of 2-methylcitric acid is associated with cobalamin deficiencies, propionic acidemia, and methylmalonic acidurias. Group: Biochemicals. Alternative Names: 2-Hydroxy-1,2,3-butanetricarboxylic Acid. Grades: Highly Purified. CAS No. 6061-96-7. Pack Sizes: 50mg, 250mg. Molecular Formula: C?H??O?, Molecular Weight: 206.15. US Biological Life Sciences. | Worldwide |
| 2-Methylcitric Acid-d3 | 2-Methylcitric Acid-d3 is the isotope labelled analog of 2-Methylcitric Acid (M265080); a metabolite of Citric Acid (C521000) that can be formed from the condensation of propionoyl-CoA and oxaloacetic acid catalyzed by a citrate synthase enzyme. Group: Biochemicals. Grades: Highly Purified. CAS No. 146764-58-1. Pack Sizes: 2.5mg, 25mg. Molecular Formula: C7H7D3O7, Molecular Weight: 209.17. US Biological Life Sciences. | Worldwide |
| acetylenedicarboxylate decarboxylase | The mechanism appears to involve hydration of the acetylene and decarboxylation of the oxaloacetic acid formed, although free oxaloacetate is not an intermediate. It is thus analogous to EC 4.2.1.27 (acetylenecarboxylate hydratase) in its mechanism. Group: Enzymes. Synonyms: acetylenedicarboxylate hydratase; acetylenedicarboxylate hydrase; acetylenedicarboxylate carboxy-lyase. Enzyme Commission Number: EC 4.1.1.78. CAS No. 72561-10-5. 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-4826; acetylenedicarboxylate decarboxylase; EC 4.1.1.78; 72561-10-5; acetylenedicarboxylate hydratase; acetylenedicarboxylate hydrase; acetylenedicarboxylate carboxy-lyase. Cat No: EXWM-4826. |  |
| Aspartate Aminotransferase from Human, Recombinant | GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.GOT1 Human Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-413 a.a.) and having a molecular mass of 48.4 kDa. The GOT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Aspartate transaminase; AST; aspartate aminotransferase; sgot AspAT; ASAT; AAT; serum glutamic oxaloac. Purity: Greater than 95.0% as determined by SDS-PAGE. AST. Activity: > 50 units/mg. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. Form: Sterile filtered colorless solution. Source: E.coli. Species: Human. Aspartate transaminase; AST; aspartate aminotransferase; sgot AspAT; ASAT; AAT; serum glutamic oxaloacetic transaminase; SGOT; pyridoxal phosphate PLP-dependent transaminase enzyme; EC 2.6.1.1; 9000-97-9; Aspartate aminotransferase 1; Transaminase A; GIG18. Cat No: DIA-128. | |
| 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 | |
| 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 | |
| Oxalacetic Acid | Oxalacetic Acid. Categories: oxalacetic acid; oxaloacetic acid. |  CA, FL & NJ |
| 1-Hydroxycyclopropane carboxylic Acid Phosphate, Biscyclohexylamine Salt | A potent reversible inhibitor of enzymes utilizing phosphoenolpyruvate (PEP), such as phosphoenolpyruvate carboxylase which catalyzes the carboxylation of PEP to give oxaloacetate. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 10mg. US Biological Life Sciences. | Worldwide |
| 4-phosphoerythronate dehydrogenase | This enzyme catalyses a step in a bacterial pathway for the biosynthesis of pyridoxal 5'-phosphate. The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD+. In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyses the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)-hydroxy acid. cf. EC 1.1.1.399, 2-oxoglutarate reductase. Group: Enzymes. Synonyms: PdxB; PdxB 4PE dehydrogenase; 4-O-phosphoerythronate dehydrogenase; 4PE dehydrogenase; erythronate-4-phosphate dehydrogenase. Enzyme Commission Number: EC 1.1.1.290. CAS No. 125858-75-5. 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-0199; 4-phosphoerythronate dehydrogenase; EC 1.1.1.290; 125858-75-5; PdxB; PdxB 4PE dehydrogenase; 4-O-phosphoerythronate dehydrogenase; 4PE dehydrogenase; erythronate-4-phosphate dehydrogenase. Cat No: EXWM-0199. | |
| aromatic-amino-acid transaminase | A pyridoxal-phosphate protein. L-Methionine can also act as donor, but more slowly; oxaloacetate can act as acceptor. Controlled proteolysis converts the enzyme into EC 2.6.1.1 aspartate transaminase. Group: Enzymes. Synonyms: aromatic amino acid aminotransferase; aromatic aminotransferase; ArAT. Enzyme Commission Number: EC 2.6.1.57. CAS No. 37332-38-0. 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-2898; aromatic-amino-acid transaminase; EC 2.6.1.57; 37332-38-0; aromatic amino acid aminotransferase; aromatic aminotransferase; ArAT. Cat No: EXWM-2898. | |
| ATP Citrate Lyase Active from Human, Recombinant | ATP Citrate lyase is an enzyme involved in fatty acid synthesis that generates cytosolic acetyl-CoA and oxaloacetate from Citrate and CoA. ATP Citrate lyase is often upregulated in cancer. Applications: Active human atp citrate lyase is useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling. active human atp citrate lyase has been used in a study to ascertain the nature of the catalytic phosphorylation that initiates the acl reaction, and to identity the active site residues involved. active human atp citrate lyase has also been used in a study to analyze tumor metabolism to reveal mitochondrial glucose oxidation in genetically diverse human glioblastomas. Group: Enzymes. S. Purity: > 90% (SDS-PAGE). ACLY. Mole weight: 147 kDa. Storage: Store at -70°C. Avoid multiple freeze-thaw cycles. Form: Aqueous solution, Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20 and 10% glycerol. Source: Baculovirus. Species: Human. ACLY; ATP-Citrate synthase; ATPCL; CLATP; ATP-citric lyase; ATP:Citrate oxaloacetate-lyase [(pro-S)-CH2COO-->acetyl-CoA] (ATP-dephosphorylating); acetyl-CoA:oxaloacetate acetyltransferase (isomerizing; ADP-phosphorylating); adenosine triphosphate Citrate lyase; Citrate cleavage enzyme; Citrate-ATP lyase; citric cleavage enzyme; ATP Citrate (pro-S)-lyase. Cat No: NATE-0944. | |
| Citrate synthase | Citrate synthase is responsible for catalyzing the first reaction of the citric acid cycle: the condensation of acetyl-CoA and oxaloacetate to form citrate. Citrate synthase is localized within eukaryotic cells in the mitochondrial matrix [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9027-96-7. Pack Sizes: 250 U; 500 U; 1000 U. Product ID: HY-P2739. | |
| Malate dehydrogenase from Bacteria, Recombinant | Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner mit...EC 1.1.1.37; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Mole weight: 40 kD (SDS-PAGE). Activity: > 550 units / mg. Storage: Below -20°C. Form: Lyophilized powder. Source: E. coli. Species: Bacteria. 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: NATE-1038. | |
| Native Bovine Malic Dehydrogenase | Malic dehydrogenase (MDH) exists as two isoforms within eukaryotic cells, one that is expressed in the mitochondria and functions in the TCA cycle and one in the cytoplasm that converts malate from the mitochondria back into oxaloacetate. Malic dehydrogenase from bovine heart contains a histidine residue at the nad-binding active site which is critical for activity. when this histidine is mutated a loss in activity is observed. Applications: Malic dehydrogenase has been used in a study to assess a flow injection system for on-line monitoring of fumaric acid in biological pr ocesses. 1 it has also been used in a study to investigate a root-knot nematode parasitizing peanut in...001-64-3. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Activity: 2000-4000 units/mg protein (modified Warburg-Christian). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3 M (NH4)2SO4-0.01 M KH2PO4 solution, pH 7.3. Source: Bovine heart. Species: Bovine. 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-specific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; EC 1.1.1.37; 9001-64-3. Cat No: NATE-0445. | |
| Native Malate dehydrogenase (Decarboxylating) from Thermophillic bacteria | Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses ...; 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 1.1.1.38; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.38. CAS No. 9080-52-8. MDH. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. 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- | |
| Native Malate dehydrogenase from Thermophillic bacteria | Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner...e 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. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. 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+ oxidored | |
| Native Microorganism Malate Dehydrogenase | Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner mitoch...-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; S-malate: NAD+ oxidoreductase; EC 1.1.1.37; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. Activity: 40U/mg-solid or more. Appearance: Slightly yellowish amorphous powder, lyophilized. Storage: Stable at-20°C for at least one year. Form: Freeze dried powder. Source: Microorganism. 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 m | |
| Native Microorganism Phosphoenolpyruvate carboxylase | Phosphoenolpyruvate carboxylase is an enzyme in the family of carboxy-lyases found in plants and some bacteria that catalyzes the addition of bicarbonate (HCO3-) to phosphoenolpyruvate (PEP) to form the four-carbon compound oxaloacetate and inorganic phosphate: PEP + HCO3-? oxaloacetate + Pi. This reaction is used for carbon fixation in CAM (crassulacean acid metabolism) and C4 organisms, as well as to regulate flux through the citric acid cycle (also known as Krebs or TCA cycle) in bacteria and plants. The enzyme structure and its two step catalytic, irreversible mechanism have been well studied. PEP carboxylase is highly regulated, both by phosphorylation and allostery. Applications: This enzyme is useful for enzymatic determination of carbon dioxide when coupled with malate dehydrogenase in clinical analysis. Group: Enzymes. Synonyms: PEP carboxylase; PEPCase; PEPC; EC 4.1.1.31; Phosphoenolpyruvate carboxylase; PDB ID: 3ZGE. Enzyme Commission Number: EC 4.1.1.31. CAS No. 9067-77-0. PEPC. Mole weight: approx. 390 kDa (by gel filtration). Activity: Grade? 5.0U/mg-solid or more. Stability: Stable at-20°C for at least one year. Appearance: White amorphous powder, lyophilized. Source: Microorganism. PEP carboxylase; PEPCase; PEPC; EC 4.1.1.31; Phosphoenolpyruvate carboxylase; PDB ID: 3ZGE. Cat No: DIA-212. | |
| 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 Porcine Malic Dehydrogenase | Malic dehydrogenase (MDH) exists as two isoforms within eukaryotic cells, one that is expressed in the mitochondria and functions in the TCA cycle and one in the cytoplasm that converts malate from the mitochondria back into oxaloacetate. Group: Enzymes. Synonyms: malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid deh. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Activity: Type I, ~1,000 units/mg protein (biuret); Type II, > 400 units/mg protein (biuret); Type III, > 600 units/mg protein (biuret); Type IV, 600-1000 units/mg protein (biuret). Storage: 2-8°C. Form: Type I, Type III, ammonium sulfate suspension; Suspension in 2.8 M (NH4)2SO4 solution, pH 6.0; Type II, ammonium sulfate suspension, Suspension in 3.2 M (NH4)2SO4, 0.1 M KH2PO4, pH 7.0; Type IV, buffered aqueous glycerol solution, Solution in 50% glycerol containing 0.05 M potassium phosphate buffer, pH 7.5. Source: Porcine heart. Species: Porcine. 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-specific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; EC 1.1.1.37; 9001-64-3. Cat No: NATE-0447. | |
| Native Thermus flavus Malic Dehydrogenase | Malic dehydrogenase (MDH) exists as two isoforms within eukaryotic cells, one that is expressed in the mitochondria and functions in the TCA cycle and one in the cytoplasm that converts malate from the mitochondria back into oxaloacetate. Malic dehydrogenase from thermus flavus is stable and active at 90 oc. Applications: Malic dehydrogenase has been used in a study to assess electron transport chain activity in mit ochondria from human skeletal muscle. it has also been used in a study to investigate activities of enzymes and ammonia in serum of rats with fluoride hyperglycemia. Group: Enzymes. Synonyms: malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic deh. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Activity: > 50 units/mg solid. Storage: -20°C. Form: lyophilized powder; Contains dextran. Source: Thermus flavus. 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-specific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; EC 1.1.1.37; 9001-64-3. Cat No: NATE-0448. | |
| Native Yeast Malate Dehydrogenase | Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner mitochondr...te: NAD+ oxidoreductase; EC 1.1.1.37; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Activity: > 1,000 units/mg protein (at 25°C and pH 7.5). Storage: 1 -10°C. Form: Ammonium sulfate suspension. Source: Yeast. 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: NATE-1030. | |
| 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. | |
| oxaloacetate decarboxylase | The enzyme from Klebsiella aerogenes is a biotinyl protein and also decarboxylates glutaconyl-CoA and methylmalonyl-CoA. The process is accompanied by the extrusion of two sodium ions from cells. Some animal enzymes require Mn2+. Group: Enzymes. Synonyms: oxaloacetate β-decarboxylase; oxalacetic acid decarboxylase; oxalate β-decarboxylase; oxaloacetate carboxy-lyase. Enzyme Commission Number: EC 4.1.1.3. CAS No. 9024-98-0. Oxaloacetate decarboxylase. 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-4773; oxaloacetate decarboxylase; EC 4.1.1.3; 9024-98-0; oxaloacetate β-decarboxylase; oxalacetic acid decarboxylase; oxalate β-decarboxylase; oxaloacetate carboxy-lyase. Cat No: EXWM-4773. | |
| phosphoenolpyruvate carboxylase | This enzyme replenishes oxaloacetate in the tricarboxylic acid cycle when operating in the reverse direction. The reaction proceeds in two steps: formation of carboxyphosphate and the enolate form of pyruvate, followed by carboxylation of the enolate and release of phosphate. Group: Enzymes. Synonyms: phosphopyruvate (phosphate) carboxylase; PEP carboxylase; phosphoenolpyruvic carboxylase; PEPC; PEPCase; phosphate:oxaloacetate carboxy-lyase (phosphorylating). Enzyme Commission Number: EC 4.1.1.31. CAS No. 9067-77-0. PEPC. 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-4775; phosphoenolpyruvate carboxylase; EC 4.1.1.31; 9067-77-0; phosphopyruvate (phosphate) carboxylase; PEP carboxylase; phosphoenolpyruvic carboxylase; PEPC; PEPCase; phosphate:oxaloacetate carboxy-lyase (phosphorylating). Cat No: EXWM-4775. | |
| Phosphoenolpyruvate carboxylase, Microorganism | Phosphoenolpyruvate carboxylase, Microorganism (PEPC) is a carbon dioxide fixing enzyme that in an irreversible manner and in the presence of Mg 2+ , converts phosphoenolpyruvate and bicarbonate into oxaloacetate and inorganic phosphorus. Phosphoenolpyruvate carboxylase catalyses the primary assimilation of CO(2) in Crassulacean acid metabolism plants. Phosphoenolpyruvate carboxylase plays a major role in setting the day-night pattern of metabolism in plants [1] [2]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: PEPC. CAS No. 9067-77-0. Pack Sizes: 100 U; 500 U. Product ID: HY-E70015. | |
| Recombinant Aspartate transaminase from Mycobacterium tuberculosis | Aspartate transaminase catalyzes the reversible transfer of an α-amino group between aspartate and glutamate and, as such, is an important enzyme in amino acid metabolism. Group: Enzymes. Synonyms: EC 2.6.1.1; AAT; AspT; AST; GOT (enzyme); oxaloacetate transferase; aspartate:2-oxoglutaRate aminotransferase; glutamate oxaloacetate transaminase; 9000-97-9. Enzyme Commission Number: EC 2.6.1.1. CAS No. 9000-97-9. Purity: > 80 %. AST. Mole weight: 47 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. EC 2.6.1.1; AAT; AspT; AST; GOT (enzyme); oxaloacetate transferase; aspartate:2-oxoglutaRate aminotransferase; glutamate oxaloacetate transaminase; 9000-97-9. Cat No: NATE-1017. | |
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