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| Product | Description | |
|---|---|---|
| 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. |  |
| oxaloacetate tautomerase | This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting keto- and enol-groups. Group: Enzymes. Synonyms: oxalacetic keto-enol isomerase. Enzyme Commission Number: EC 5.3.2.2. CAS No. 37318-45-9. 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-5482; oxaloacetate tautomerase; EC 5.3.2.2; 37318-45-9; oxalacetic keto-enol isomerase. Cat No: EXWM-5482. | |
| Glutamate oxaloacetate aminotransferase, porcine heart | Glutamate oxaloacetate aminotransferase, porcine heart catalyzes the reversible reaction of L-aspartate and α-ketoglutarate into oxaloacetate and L-glutamate [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9000-97-9. Pack Sizes: 1 KU. Product ID: HY-P3016A. |  |
| glycine-oxaloacetate transaminase | A pyridoxal-phosphate protein. Group: Enzymes. Synonyms: glycine-oxalacetate aminotransferase. Enzyme Commission Number: EC 2.6.1.35. CAS No. 37277-90-0. 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-2875; glycine-oxaloacetate transaminase; EC 2.6.1.35; 37277-90-0; glycine-oxalacetate aminotransferase. Cat No: EXWM-2875. | |
| malate dehydrogenase (oxaloacetate-decarboxylating) | Unlike EC 1.1.1.39, malate dehydrogenase (decarboxylating), this enzyme can also decarboxylate oxaloacetate. cf. EC 1.1.1.40, malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+). Group: Enzymes. Synonyms: malic' enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); NAD+-specific malic enzyme; NAD+-malic enzyme; NAD+-linked malic enzyme. Enzyme Commission Number: EC 1.1.1.38. CAS No. 9080-52-8. MDH. 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-0298; malate dehydrogenase (oxaloacetate-decarboxylating); EC 1.1.1.38; 9080-52-8; malic' enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); NAD+-specific malic enzyme; NAD+-malic enzyme; NAD+-linked malic enzyme. Cat No: EXWM-0298. | |
| malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) | The enzyme catalyses the oxidative decarboxylation of (S)-malate in the presence of NADP+ and divalent metal ions, and the decarboxylation of oxaloacetate. cf. EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), and EC 1.1.1.39, malate dehydrogenase (decarboxylating). Group: Enzymes. Synonyms: malic' enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); malate dehydrogenase (decarboxylating, NADP+); NADP+-linked decarboxylating malic enzyme; NADP+-malic enzyme; NADP+-specific malic enzyme; NADP+-specific malate dehydrogenase; malate dehydrogenase (NADP+, decarboxylating); L-malate:NADP+ oxidoreductase. Enzyme Commission Number: EC 1.1.1.40. CAS No. 9028-47-1. MDH. 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-0321; malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+); EC 1.1.1.40; 9028-47-1; malic' enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); malate dehydrogenase (decarboxylating, NADP+); NADP+-linked decarboxylating malic enzyme; NADP+-malic enzyme; NADP+-specific malic enzyme; NADP+-specific malate dehydrogenase; malate dehydrogenase (NADP+, decarboxylating); L-malate:NADP+ oxidoreductase. Cat No: EXWM-0321. | |
| Native Pseudomonas sp. Oxaloacetate decarboxylase | Oxaloacetate decarboxylase is a carboxy-lyase involved in the conversion of oxaloacetate into pyruvate. It is categorized under EC 4.1.1.3. In some bacteria this enzyme is a trimer, composed of alpha, beta and gamma subunits. The beta and gamma subunits are integral membrane proteins. Native oxaloacetate decarboxylase (ec 4.1.1.3) was purified from pseudomonas sp. Applications: Useful for enzymatic determination of ast. Group: Enzymes. Synonyms: EC 4.1.1.3; Oxaloacetate decarboxylase; Oxalate beta-decarboxylase; Oxaloacetate carboxy-lyase. Enzyme Commission Number: EC 7.2.4.2 (Formerly EC 4.1.1.3). CAS No. 9024-98-0. Oxaloacetate decarboxylase. Activity: > 100 U/mg. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Pseudomonas sp. EC 4.1.1.3; Oxaloacetate decarboxylase; Oxalate beta-decarboxylase; Oxaloacetate carboxy-lyase. Cat No: DIA-161. | |
| pyridoxamine-oxaloacetate transaminase | This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is pyridoxamine:oxaloacetate aminotransferase. This enzyme participates in vitamin B6 metabolism. Group: Enzymes. Enzyme Commission Number: EC 2.6.1.31. CAS No. 37277-88-6. 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-2871; pyridoxamine-oxaloacetate transaminase; EC 2.6.1.31; 37277-88-6. Cat No: EXWM-2871. | |
| 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 |
| 2-methylcitrate synthase | The enzyme acts on acetyl-CoA, propanoyl-CoA, butanoyl-CoA and pentanoyl-CoA. The relative rate of condensation of acetyl-CoA and oxaloacetate is 140% of that of propanoyl-CoA and oxaloacetate, but the enzyme is distinct from EC 2.3.3.1, citrate (Si)-synthase. Oxaloacetate cannot be replaced by glyoxylate, pyruvate or 2-oxoglutarate. Group: Enzymes. Synonyms: 2-methylcitrate oxaloacetate-lyase; MCS; methylcitrate synthase; methylcitrate synthetase. Enzyme Commission Number: EC 2.3.3.5. CAS No. 57827-78-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2321; 2-methylcitrate synthase; EC 2.3.3.5; 57827-78-8; 2-methylcitrate oxaloacetate-lyase; MCS; methylcitrate synthase; methylcitrate synthetase. Cat No: EXWM-2321. | |
| 4-hydroxy-4-methyl-2-oxoglutarate aldolase | Requires a divalent metal ion. This enzyme participates in the degradation of protocatechuate (via the meta-cleavage pathway), phthalate, syringate and gallate. The enzyme from Pseudomonas ochraceae can also cleave 4-hydroxy-2-oxoglutarate to glyoxylate and pyruvate, and also catalyses the reaction of EC 4.1.1.3 (oxaloacetate decarboxylase). Group: Enzymes. Synonyms: pyruvate aldolase; γ-methyl-γ-hydroxy-α-ketoglutaric aldolase; 4-hydroxy-4-methyl-2-ketoglutarate aldolase; 4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase; HMG aldolase; CHA aldolase; 4-carboxy-4-hydroxy-2-oxoadipate aldolase. Enzyme Commission Number: EC 4.1.3.17. CAS No. 37290-65-6. 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-4902; 4-hydroxy-4-methyl-2-oxoglutarate aldolase; EC 4.1.3.17; 37290-65-6; pyruvate aldolase; γ-methyl-γ-hydroxy-α-ketoglutaric aldolase; 4-hydroxy-4-methyl-2-ketoglutarate aldolase; 4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase; HMG aldolase; CHA aldolase; 4-carboxy-4-hydroxy-2-oxoadipate aldolase. Cat No: EXWM-4902. | |
| 4-hydroxyglutamate transaminase | Oxaloacetate can replace 2-oxoglutarate. This enzyme may be identical with EC 2.6.1.1 aspartate transaminase. Group: Enzymes. Synonyms: 4-hydroxyglutamate aminotransferase. Enzyme Commission Number: EC 2.6.1.23. CAS No. 37277-86-4. 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-2863; 4-hydroxyglutamate transaminase; EC 2.6.1.23; 37277-86-4; 4-hydroxyglutamate aminotransferase. Cat No: EXWM-2863. | |
| 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. | |
| (4S)-4-hydroxy-2-oxoglutarate aldolase | The enzyme from the bacterium Escherichia coli is specific for the (S) enantiomer. That enzyme is trifunctional, and also catalyses the reactions of EC 4.1.1.3, oxaloacetate decarboxylase and EC 4.1.2.14, 2-dehydro-3-deoxy-phosphogluconate aldolase. cf. EC 4.1.3.16, 4-hydroxy-2-oxoglutarate aldolase. Group: Enzymes. Synonyms: 2-oxo-4-hydroxyglutarate aldolase (ambiguous); hydroxyketoglutaric aldolase (ambiguous); 4-hydroxy-2-ketoglutaric aldolase (ambiguous); 2-keto-4-hydroxyglutaric aldolase (ambiguous); 4-hydroxy-2-ketoglutarate aldolase (ambiguous); 2-keto-4-hydroxyglutarate aldolase. Enzyme Commission Number: EC 4.1.3.42. CAS No. 9030-81-3. 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-4919; (4S)-4-hydroxy-2-oxoglutarate aldolase; EC 4.1.3.42; 9030-81-3; 2-oxo-4-hydroxyglutarate aldolase (ambiguous); hydroxyketoglutaric aldolase (ambiguous); 4-hydroxy-2-ketoglutaric aldolase (ambiguous); 2-keto-4-hydroxyglutaric aldolase (ambiguous); 4-hydroxy-2-ketoglutarate aldolase (ambiguous); 2-keto-4-hydroxyglutarate aldolase (ambiguous); 2-oxo-4-hydroxyglutaric aldolase (ambiguous); hydroxyketoglutarate aldolase (ambiguous); 2-keto-4-hydroxybutyrate aldolase (ambiguous); 4-hydroxy-2-oxoglutarate glyoxylate-lyase (ambiguous); eda (gene name). Cat No: EXWM-4919. | |
| 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. | |
| acetylpyruvate hydrolase | Highly specific; does not act on pyruvate, oxaloacetate, maleylpyruvate, fumarylpyruvate or acetylacetone. Group: Enzymes. Enzyme Commission Number: EC 3.7.1.6. CAS No. 56214-30-3. 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-4735; acetylpyruvate hydrolase; EC 3.7.1.6; 56214-30-3. Cat No: EXWM-4735. | |
| 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. | |
| Aspartate aminotransferase, Genetically engineered bacteria | Aspartate aminotransferase, Genetically engineered bacteria (EC 2.6.1.1) (AST) is a transaminase enzyme, is often used in biochemical studies. Aspartate aminotransferase catalyzes aspartate and alpha-ketoglutarate converts to oxaloacetate and glutamate. Aspartate aminotransferase can be found in cerebrospinal fluid, exudates, and transudates [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: EC 2.6.1.1; GOT; AST. CAS No. 9000-97-9. Pack Sizes: 200 U; 1 KU. Product ID: HY-P3016. | |
| 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. | |
| ATP citrate synthase | The enzyme can be dissociated into components, two of which are identical with EC 4.1.3.34 (citryl-CoA lyase) and EC 6.2.1.18 (citrate-CoA ligase). Group: Enzymes. Synonyms: 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. Enzyme Commission Number: EC 2.3.3.8. CAS No. 9027-95-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2324; ATP citrate synthase; EC 2.3.3.8; 9027-95-6; 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: EXWM-2324. | |
| carboxybiotin decarboxylase | The integral membrane protein MadBfrom the anaerobic bacterium Malonomonas rubra is a component of the multienzyme complex EC 4.1.1.89, biotin-dependent malonate decarboxylase. The free energy of the decarboxylation reaction is used to pump Na+ out of the cell. The enzyme is a member of the Na+-translocating decarboxylase family, other members of which include EC 4.1.1.3 (oxaloacetate decarboxylase) and EC 4.1.1.41 (methylmalonyl-CoA decarboxylase). Group: Enzymes. Synonyms: MadB; carboxybiotin protein decarboxylase. Enzyme Commission Number: EC 7.2.4.1 (Formerly EC 4.3.99.2). 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-5309; carboxybiotin decarboxylase; EC 4.3.99.2; MadB; carboxybiotin protein decarboxylase. Cat No: EXWM-5309. | |
| citrate (pro-3S)-lyase | The enzyme can be dissociated into components, two of which are identical with EC 2.8.3.10 (citrate CoA-transferase) and EC 4.1.3.34 (citryl-CoA lyase). EC 3.1.2.16, citrate lyase deacetylase, deacetylates and inactivates the enzyme. Group: Enzymes. Synonyms: citrase; citratase; citritase; citridesmolase; citrate aldolase; citric aldolase; citrate lyase; citrate oxaloacetate-lyase; citrate oxaloacetate-lyase [(pro-3S)-CH2COO-?acetate]. Enzyme Commission Number: EC 4.1.3.6. CAS No. 9012-83-3. Citrase. 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-4924; citrate (pro-3S)-lyase; EC 4.1.3.6; 9012-83-3; citrase; citratase; citritase; citridesmolase; citrate aldolase; citric aldolase; citrate lyase; citrate oxaloacetate-lyase; citrate oxaloacetate-lyase [(pro-3S)-CH2COO-?acetate]. Cat No: EXWM-4924. | |
| citrate (Re)-synthase | This enzyme is inactivated by oxygen and is found in some anaerobes. Its stereospecificity is opposite to that of EC 2.3.3.1, citrate (Si)-synthase. Group: Enzymes. Synonyms: (R)-citrate synthase; Re-citrate-synthase; citrate oxaloacetate-lyase [(pro-3R)-CH2COO-?acetyl-CoA]. Enzyme Commission Number: EC 2.3.3.3. CAS No. 9077-70-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2319; citrate (Re)-synthase; EC 2.3.3.3; 9077-70-7; (R)-citrate synthase; Re-citrate-synthase; citrate oxaloacetate-lyase [(pro-3R)-CH2COO-?acetyl-CoA]. Cat No: EXWM-2319. | |
| citrate (Si)-synthase | The stereospecificity of this enzyme is opposite to that of EC 2.3.3.3, citrate (Re)-synthase, which is found in some anaerobes. Citrate synthase for which the stereospecificity with respect to C2 of oxaloacetate has not been established are included in EC 2.3.3.16, citrate synthase. Group: Enzymes. Synonyms: (R)-citric synthase; citrate oxaloacetate-lyase [(pro-3S)-CH2COO-?acetyl-CoA]. Enzyme Commission Number: EC 2.3.3.1. CAS No. 9027-96-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2310; citrate (Si)-synthase; EC 2.3.3.1; 9027-96-7; (R)-citric synthase; citrate oxaloacetate-lyase [(pro-3S)-CH2COO-?acetyl-CoA]. Cat No: EXWM-2310. | |
| 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. | |
| citrate synthase (unknown stereospecificity) | This entry has been included to accommodate those citrate synthases for which the stereospecificity with respect to C2 of oxaloacetate has not been established [cf. EC 2.3.3.1, citrate (Si)-synthase and EC 2.3.3.3, citrate (Re)-synthase]. Group: Enzymes. Synonyms: citrate condensing enzyme; CoA-acetylating citrate oxaloacetate-lyase; citrate synthetase; citric synthase; citric-condensing enzyme; citrogenase; condensing enzyme (ambiguous); oxaloacetate transacetase; oxalacetic transacetase. Enzyme Commission Number: EC 2.3.3.16. 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-2317; citrate synthase (unknown stereospecificity); EC 2.3.3.16; citrate condensing enzyme; CoA-acetylating citrate oxaloacetate-lyase; citrate synthetase; citric synthase; citric-condensing enzyme; citrogenase; condensing enzyme (ambiguous); oxaloacetate transacetase; oxalacetic transacetase. Cat No: EXWM-2317. | |
| citryl-CoA lyase | The enzyme is a component of EC 4.1.3.6 {[citrate (pro-3S)-lyase]}and EC 2.3.3.8 [ATP citrate synthase]. Also acts on (3S)-citryl thioacyl-carrier protein. Group: Enzymes. Synonyms: (3S)-citryl-CoA oxaloacetate-lyase. Enzyme Commission Number: EC 4.1.3.34. CAS No. 131095-35-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4911; citryl-CoA lyase; EC 4.1.3.34; 131095-35-7; (3S)-citryl-CoA oxaloacetate-lyase. Cat No: EXWM-4911. | |
| decylcitrate synthase | This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. Group: Enzymes. Synonyms: 2-decylcitrate synthase; (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate oxaloacetate-lyase (CoA-acylating). Enzyme Commission Number: EC 2.3.3.2. CAS No. 9068-72-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2318; decylcitrate synthase; EC 2.3.3.2; 9068-72-8; 2-decylcitrate synthase; (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate oxaloacetate-lyase (CoA-acylating). Cat No: EXWM-2318. | |
| decylhomocitrate synthase | Decanoyl-CoA can act instead of dodecanoyl-CoA, but 2-oxoglutarate cannot be replaced by oxaloacetate or pyruvate. Group: Enzymes. Synonyms: 2-decylhomocitrate synthase; 3-hydroxytetradecane-1,3,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acylating). Enzyme Commission Number: EC 2.3.3.4. CAS No. 51845-40-0. 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-2320; decylhomocitrate synthase; EC 2.3.3.4; 51845-40-0; 2-decylhomocitrate synthase; 3-hydroxytetradecane-1,3,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acylating). Cat No: EXWM-2320. | |
| D-methionine-pyruvate transaminase | Oxaloacetate can replace pyruvate. Group: Enzymes. Synonyms: D-methionine transaminase; D-methionine aminotransferase. Enzyme Commission Number: EC 2.6.1.41. CAS No. 37277-93-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2882; D-methionine-pyruvate transaminase; EC 2.6.1.41; 37277-93-3; D-methionine transaminase; D-methionine aminotransferase. Cat No: EXWM-2882. | |
| FMN Reductase from Escherichia coli (Fre), Recombinant | E.coli. Applications: Bacterial (e. coli) nad(p)h-dependent fmn-oxidoreductase is a recombinant protein of ca. 26kda overexpressed in e.coli. the sequence of cloned fre (swissprot accession number p0aen1) was confirmed by dna sequencing (100% identity). Group: Enzymes. Synonyms: NAD(P)H:flavin oxidoreduct. Enzyme Commission Number: EC 1.5.1.29. Mole weight: 26kDa. Activity: >2U/mg. Appearance: Coupling of bacterial luciferase to FMN-NAD(P)H oxidoreductase has been used to provide ultrasensitive analytical tools for thequantification of NADH and the substrates of NADH-, NADPH- dependent enzymes (e.g. glucose, lactate, malate, ethanol, sorbitol,oxaloacetate). Although FMN-reductase often present in luciferase enzyme preparations may be sufficient for producing light in the presence of NAD(P)H, highly purified and characterized Fre enzyme can offer some advantages such as an increased sensitivity,better control of the signal intensity and duration, and saving of the luciferase enzyme. Species: FMN Reductase. NAD(P)H:flavin oxidoreductase; NAD(P)H:flavin mono-nucleotide oxidoreductase; NAD(P)H(2):FMN oxidoreductase; NAD(P)H-FMN reductase; NAD(P)H-dependent FMN reductase; NAD(P)H:FMN oxidoreductase; riboflavin mononucleotide reductase; flavin mononucleotide reductase; EC 1.5.1.29. Pack: stable lyophilized form. Cat No: NATE-1744. | |
| homocitrate synthase | Belongs in the α-aminoadipate pathway of lysine synthesis, along with EC 4.2.1.36, homoaconitate hydratase. The enzyme also acts with oxaloacetate as substrate, but more slowly. Group: Enzymes. Synonyms: 2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acetylating); acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase; homocitrate synthetase; HCS. Enzyme Commission Number: EC 2.3.3.14. CAS No. 9075-60-9. 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-2315; homocitrate synthase; EC 2.3.3.14; 9075-60-9; 2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acetylating); acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase; homocitrate synthetase; HCS. Cat No: EXWM-2315. | |
| iGOT1-01 | iGOT1-01 is an inhibitor of aspartate aminotransferase 1 (glutamate oxaloacetate transaminase 1, GOT1). Group: Inhibitors. Alternative Names: iGOT101; iGOT1 01; iGOT1-01; iGOT 101; iGOT-101. CAS No. 882256-55-5. Molecular formula: C19H20N4O. Mole weight: 320.4. Appearance: Solid powder. Purity: >98%. IUPACName: 4-(1H-Indol-4-yl)-N-phenylpiperazine-1-carboxamide. Canonical SMILES: O=C (N1CCN (C2=CC=CC3=C2C=CN3)CC1)NC4=CC=CC=C4. Catalog: ACM882256555. |  |
| L-2-hydroxycarboxylate dehydrogenase [NAD(P)+] | The enzyme from the archaeon Methanocaldococcus jannaschii catalyses the reversible oxidation of (2R)-3-sulfolactate and (S)-malate to 3-sulfopyruvate and oxaloacetate, respectively (note that (2R)-3-sulfolactate has the same stereochemical configuration as (2S)-2-hydroxycarboxylates). The enzyme can use both NADH and NADPH, although activity is higher with NADPH. The oxidation of (2R)-3-sulfolactate was observed only in the presence of NADP+. The same organism also possesses an NAD+-specific enzyme with similar activity, cf. EC 1.1.1.337, L-2-hydroxycarboxylate dehydrogenase (NAD+). Group: Enzymes. Synonyms: MdhII; lactate/malate dehydrogenase. Enzyme Commission Number: EC 1.1.1.375. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0293; L-2-hydroxycarboxylate dehydrogenase [NAD(P)+]; EC 1.1.1.375; MdhII; lactate/malate dehydrogenase. Cat No: EXWM-0293. | |
| L-aspartate oxidase | A flavoprotein (FAD). L-Aspartate oxidase catalyses the first step in the de novo biosynthesis of NAD+ in some bacteria. O2 can be replaced by fumarate as electron acceptor, yielding succinate. The ability of the enzyme to use both O2 and fumarate in cofactor reoxidation enables it to function under both aerobic and anaerobic conditions. Iminosuccinate can either be hydrolysed to form oxaloacetate and NH3 or can be used by EC 2.5.1.72, quinolinate synthase, in the production of quinolinate. The enzyme is a member of the succinate dehydrogenase/fumarate-reductase family of enzymes. Group: Enzymes. Synonyms: NadB; Laspo; AO. Enzyme Commission Number: EC 1.4.3.16. CAS No. 69106-47-4. 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-1472; L-aspartate oxidase; EC 1.4.3.16; 69106-47-4; NadB; Laspo; AO. Cat No: EXWM-1472. | |
| L-Aspartic acid | Aspartic acid (abbreviated as Asp or D; encoded by the codons [GAU and GAC]), also known as aspartate, is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated -NH+ 3 form under biological conditions), an α-carboxylic acid group (which is in the deprotonated -COO- form under biological conditions), and a side chain CH2COOH. Under physiological conditions in proteins the sidechain usually occurs as the negatively charged aspartate form, -COO-. It is semi-essential in humans, meaning the body can synthesize it from oxaloacetate.In proteins aspartate sidechains are often hydrogen bonded, often as asx turns or asx motifs, which often occur at the N-termini of alpha helices.Asps L-isomer is one of the 23 proteinogenic amino acids, i.e., the building blocks of proteins. Asp (and glutamic acid) is classified as acidic, with a pKa of 3.9, however in a peptide this is highly dependent on the local environment (as with all amino acids), and could be as high as 14. Asp is pervasive in biosynthesis.L-aspartic acid is one of the two main ingredients of the artificial sweetener aspartame, along with L-phenylalanine. Group: Heterocyclic organic compound. Alternative Names: (S)-Butanedioicaci. CAS No. 56-84-8. Molecular formula: C4H7NO4. Mole weight: 133.1. Appearance: White powder. Purity: 0.98. IUPACName: (2S)-2-Aminobutanedioic acid. Canonical SMILES: C | |
| LL-diaminopimelate aminotransferase | A pyridoxal-phosphate enzyme. In vivo, the reaction occurs in the opposite direction to that shown above. This is one of the final steps in the lysine-biosynthesis pathway of plants (ranging from mosses to flowering plants). meso-Diaminoheptanedioate, an isomer of LL-2,6-diaminoheptanedioate, and the structurally related compounds lysine and ornithine are not substrates. 2-Oxoglutarate cannot be replaced by oxaloacetate or pyruvate. It is not yet known if the substrate of the biosynthetic reaction is the cyclic or acyclic form of tetrahydropyridine-2,6-dicarboxylate. Group: Enzymes. Synonyms: LL-diaminopimelate transaminase; LL-DAP aminotransferase; LL-DAP-AT. Enzyme Commission Number: EC 2.6.1.83. CAS No. 949001-34-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2924; LL-diaminopimelate aminotransferase; EC 2.6.1.83; 949001-34-7; LL-diaminopimelate transaminase; LL-DAP aminotransferase; LL-DAP-AT. Cat No: EXWM-2924. | |
| malate dehydrogenase (decarboxylating) | Does not decarboxylate added oxaloacetate. Group: Enzymes. Synonyms: malic' enzyme; pyruvic-malic carboxylase; NAD-specific malic enzyme; NAD-malic enzyme. Enzyme Commission Number: EC 1.1.1.39. CAS No. 9028-46-0. 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-0309; malate dehydrogenase (decarboxylating); EC 1.1.1.39; 9028-46-0; malic' enzyme; pyruvic-malic carboxylase; NAD-specific malic enzyme; NAD-malic enzyme. Cat No: EXWM-0309. | |
| 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. | |
| malate dehydrogenase [NAD(P)+] | This enzyme, which was characterized from the methanogenic archaeon Methanobacterium thermoautotrophicum, catalyses only the reduction of oxaloacetate, and can use NAD+ and NADP+ with similar specific activity.Different from EC 1.1.1.37 (malate dehydrogenase (NAD+)), EC 1.1.1.82 (malate dehydrogenase (NADP+)) and EC 1.1.5.4 (malate dehydrogenase (quinone)). Group: Enzymes. Synonyms: MdH II, NAD(P)+-dependent malate dehyrogenase. Enzyme Commission Number: EC 1.1.1.299. 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-0208; malate dehydrogenase [NAD(P)+]; EC 1.1.1.299; MdH II, NAD(P)+-dependent malate dehyrogenase. Cat No: EXWM-0208. | |
| Malic dehydrogenase, microorganism | Malate dehydrogenase (EC 1.1.1.37) (MDH) catalyzes the mutual conversion of oxaloacetate and malate, and is associated with the oxidation/reduction of dinucleotide coenzymes [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: MDH; EC 1.1.1.37. CAS No. 9001-64-3. Pack Sizes: 1 KU; 10 KU. Product ID: HY-P2809. | |
| 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 Bovine Pyruvate Carboxylase | Pyruvate carboxylase catalyzes the carboxylation of pyruvate to oxaloacetate. Pyruvate carboxylase is a mitochondrial protein that has a biotin prosthetic group that requiries magnesium or manganese and acetyl CoA. Applications: Pyruvate is critical for gluconeogenesis, lipogenesis, glyceroneogenesis, neurotransmitter biosynthesis and glucose-induced insulin, and is used to study these pr ocesses. the enzyme from creative enzymes has been used as a positive control during the assay of pyruvate carboxylase activity in cell-free extracts of corynebacterium glutamicum. Group: Enzymes. Synonyms: Pyruvate carboxylase; PC; EC 6.4.1.1; 9014-19-1; pyruvic carboxylase. Enzyme Commission Number: EC 6.4.1.1. CAS No. 9014-19-1. PC. Activity: 5-25 units/mg protein (BCA). Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 0.05 M Tris-HCl, pH 7.4, 2 mM magnesium acetate and 1 mM EDTA. Source: Bovine liver. Species: Bovine. Pyruvate carboxylase; PC; EC 6.4.1.1; 9014-19-1; pyruvic carboxylase. Cat No: NATE-0508. | |
| Native Chicken Malic Dehydrogenase (oxalacetate-decarboxylating) | 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 (mdh) exists as two isoforms within eukaryotic cells, one that is expressed in the mit ochondria and functions in the tca cycle and one in the cytoplasm that converts malate from the mit ochondria back into oxaloacetate. Applications: Malic dehydrogenase has been used in a study to assess the dietary manganese requirement of juvenile yellow catfish (pelteobagrus fulvidraco) and effects on whole body minera...ctivity: 10-30 units/mg protein (modified Warburg-Christian). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 2.9 M (NH4)2SO4 solution containing 10 mM potassium phosphate, 0.5 mM 2-mercaptoethanol, 10 mM manganese chloride, and 3 mM Na4EDTA, pH 6.0. Source: Chicken liver. Species: Chicken. malic enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); malate dehydrogenase (decarboxylating, NADP+); NADP+-linked decarboxylating malic enzyme; NADP+-malic enzyme; NADP+-specific malic enzyme; NADP-specific malate dehydrogenase; malate dehydrogenase (NADP+, decarboxylating); L-malate:NADP+oxidoreductase; EC 1.1.1.40; 9028-47-1. Cat No: NATE-0446. | |
| Native Corn Phospho (enol)pyruvate Carboxylase | Phospho (enol)pyruvate carboxylase is a ubiquitous, highly regulated oligomeric, cytosolic enzyme in plants. Phospho (enol)pyruvate Carboxylase from corn was found to be highly susceptible to trypsin digestion. Phospho (enol)pyruvate carboxylase is a ubiquitous, highly regulated oligomeric, cytosolic enzyme in plants. Applications: Phospho (enol)pyruvate carboxylase has been used in a study to assess activity of carbon metabolism enzymes in wheat plants treated with kartolin-4 and exposed to water stress. it has also been used in a study to investigate the specific density of leaf as a characteristic of the photosynthetic apparatus. Group: Enzymes. Synonyms: phosphopyruvate (phosphate) carboxylase; PEP carboxylase; phosphoenolpyruvic carboxylase; PEPC; PEPCase; phosphate:oxaloacetate carboxy-lyase (phosphorylating); EC 4.. Enzyme Commission Number: EC 4.1.1.31. CAS No. 9067-77-0. PEPC. Activity: > 1 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 2.4 M (NH4)2SO4 solution containing 10 mM phosphate buffer, pH 7.0, 1 mM biotin, 5 mM dithiothreitol and 1 mM phenylmethylsulfonyl fluoride. Source: Corn. phosphopyruvate (phosphate) carboxylase; PEP carboxylase; phosphoenolpyruvic carboxylase; PEPC; PEPCase; phosphate:oxaloacetate carboxy-lyase (phosphorylating); EC 4.1.1.31; 9067-77-0. Cat No: NATE-0543. | |
| 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 Klebsiella pneumoniae Citrate Lyase | Citrate lyase is found in several microorganisms and catalyzes the first step of Citrate degradation, forming acetate and oxaloacetate. The enzyme contains 3 polypeptide subunits, α-subunit (a transferase), β-subunit (acyl lyase) and γ-subunit (acyl-carrier protein). Group: Enzymes. Synonyms: EC 4.1.3.6, citrase; citRatase; citritase; citridesmolase; Citrate aldolase; citric aldolase; Citrate lyase; Citrate oxaloacetate-lyase; Citrate oxaloacetate-lyase [(pro-3S)-CH2COO-?acetate]; 9012-83-3. Enzyme Commission Number: EC 4.1.3.6. CAS No. 9012-83-3. Citrase. Activity: > 0.20 unit/mg solid. Storage: 2-8°C. Form: Lyophilized powder containing bovine serum albumin, sucrose, MgSO4 and EDTA. Source: Klebsiella pneumoniae. EC 4.1.3.6, citrase; citRatase; citritase; citridesmolase; Citrate aldolase; citric aldolase; Citrate lyase; Citrate oxaloacetate-lyase; Citrate oxaloacetate-lyase [(pro-3S)-CH2COO-?acetate]; 9012-83-3. Cat No: NATE-0135. | |
| 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 Photobacterium phosphoreum (Lux) Bacterial Luciferase | P. phosphoreum. Applications: Bacterial luciferase is purified from a photobacterium phosphoreum strain isolated from squid by our team and selected for its brightest luminescence. the luxab gene was amplified by pcr and cloned. the sequences of cloned α and β subunits have shown 94% and 92% identity to p24113 and p12744 proteins of photobacterium phosphoreum (swissprot entry). Group: Enzymes. Synonyms: aldehyde monooxygenase; luciferase; Vibrio fischeri luciferase; alkanal,reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing); alkanal,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing); alkanal monooxygenase (FMN); aldehyde,FMNH2:ox... presence of limiting concentrations of NADH substrate, light intensity is proportional to NAD(P)H concentration. The coupling of bacterial luciferase to FMN-NAD(P)H oxidoreductase has been used to provide ultrasensitive analytical tools for the quantification of NAD(P)H and the substrates of NADH-, NADPH- dependent enzymes (e.g. glucose, lactate, malate, ethanol, sorbitol, oxaloacetate).Bacterial Luciferase can be used for NAD(P)H quantification or in dehydrogenase-coupled assays.The enzyme is provided lyophilized, alone or with lyophilized FMN-reductase. Species: Luciferase. aldehyde monooxygenase; luciferase; Vibrio fischeri luciferase; alkanal,reduced-FMN:ox | |
| Native Pigeon Citrate Synthase | Citrate synthase catalyses the conversion of Citrate to acetyl-CoA in the presence of coenzyme-A with the release of H2O and oxaloacetate. The enzyme has a molecular weight of 85 kDa and a pI of 6.1-6.6. It is inhibited by fluoroacetyl-CoA, palmitoyl-CoA, and citroyl-CoA. It is also inhibited when it is acetylated by acetic anhydride or iodinated by iodine. Group: Enzymes. Synonyms: CS; EC 4.1.3.7; EC 2.3.3.1; 9027-96-7; Citrate (Si)-synthase; (R)-citric synthase; Citrate oxaloacetate-lyase [(pro-3S)-CH2COO-->acetyl-CoA]. Enzyme Commission Number: EC 4.1.3.7. CAS No. 9027-96-7. CS. Activity: 80-150 units/mg protein (modified Warburg-Christian). Storage: 2-8°C. Form: ammonium sulfate suspension. Crystalline suspension in 2.2 M (NH4)2SO4 solution, pH 7.0, containing 6 mM phosphate and 0.5 mM Citrate. Source: Pigeon breast muscle. Species: Pigeon. CS; EC 4.1.3.7; EC 2.3.3.1; 9027-96-7; Citrate (Si)-synthase; (R)-citric synthase; Citrate oxaloacetate-lyase [(pro-3S)-CH2COO-->acetyl-CoA]. Cat No: NATE-0165. | |
| Native Porcine Citrate Synthase | Citrate synthase catalyses the conversion of Citrate to acetyl-CoA in the presence of coenzyme-A with the release of H2O and oxaloacetate. The enzyme has a molecular weight of 85 kDa and a pI of 6.1-6.6. It is inhibited by fluoroacetyl-CoA, palmitoyl-CoA, and citroyl-CoA. It is also inhibited when it is acetylated by acetic anhydride or iodinated by iodine. Group: Enzymes. Synonyms: CS; EC 4.1.3.7; EC 2.3.3.1; 9027-96-7; Citrate (Si)-synthase; (R)-citric synthase; Citrate oxaloacetate-lyase [(pro-3S)-CH2COO-->acetyl-CoA]. Enzyme Commission Number: EC 4.1.3.7. CAS No. 9027-96-7. CS. Activity: > 100 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.2 M (NH4)2SO4 solution, pH 7.0. Source: Porcine heart. Species: Porcine. CS; EC 4.1.3.7; EC 2.3.3.1; 9027-96-7; Citrate (Si)-synthase; (R)-citric synthase; Citrate oxaloacetate-lyase [(pro-3S)-CH2COO-->acetyl-CoA]. Cat No: NATE-0166. | |
| 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. | |
| 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 |
| phosphoenolpyruvate carboxykinase (ATP) | Phosphoenolpyruvate carboxykinase (ATP) is an enzyme with systematic name ATP:oxaloacetate carboxy-lyase (transphosphorylating; phosphoenolpyruvate-forming). Group: Enzymes. Synonyms: phosphopyruvate carboxylase (ATP); phosphoenolpyruvate carboxylase (ambiguous); phosphoenolpyruvate carboxykinase (ambiguous); phosphopyruvate carboxykinase (adenosine triphosphate); PEP carboxylase (ambiguous); PEP carboxykinase (ambiguous); PEPCK (ATP); PEPK; PEPCK; phosphoenolpyruvic carboxylase (ambiguous); phosphoenolpyruvic carboxykinase (ambiguous); phosphoenolpyruvate carboxylase (ATP); . Enzyme Commission Number: EC 4.1.1.49. CAS No. 9073-94-3. 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-4794; phosphoenolpyruvate carboxykinase (ATP); EC 4.1.1.49; 9073-94-3; phosphopyruvate carboxylase (ATP); phosphoenolpyruvate carboxylase (ambiguous); phosphoenolpyruvate carboxykinase (ambiguous); phosphopyruvate carboxykinase (adenosine triphosphate); PEP carboxylase (ambiguous); PEP carboxykinase (ambiguous); PEPCK (ATP); PEPK; PEPCK; phosphoenolpyruvic carboxylase (ambiguous); phosphoenolpyruvic carboxykinase (ambiguous); phosphoenolpyruvate carboxylase (ATP); phosphopyruvate carboxykinase (ambiguous); ATP:oxaloacetate carboxy-lyase (transphosphorylating). Cat No: EXWM-4794. | |
| phosphoenolpyruvate carboxykinase (GTP) | ITP can act as phosphate donor. Group: Enzymes. Synonyms: phosphoenolpyruvate carboxylase; phosphopyruvate carboxylase; phosphopyruvate (guanosine triphosphate) carboxykinase; phosphoenolpyruvic carboxykinase (GTP); phosphopyruvate carboxylase (GTP); phosphoenolpyruvic carboxylase (GTP); phosphoenolpyruvic carboxykinase; phosphoenolpyruvate carboxykinase; PEP carboxylase; GTP:oxaloacetate carboxy-lyase (transphosphorylating). Enzyme Commission Number: EC 4.1.1.32. CAS No. 9013-8-5. 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-4776; phosphoenolpyruvate carboxykinase (GTP); EC 4.1.1.32; 9013-08-5; phosphoenolpyruvate carboxylase; phosphopyruvate carboxylase; phosphopyruvate (guanosine triphosphate) carboxykinase; phosphoenolpyruvic carboxykinase (GTP); phosphopyruvate carboxylase (GTP); phosphoenolpyruvic carboxylase (GTP); phosphoenolpyruvic carboxykinase; phosphoenolpyruvate carboxykinase; PEP carboxylase; GTP:oxaloacetate carboxy-lyase (transphosphorylating). Cat No: EXWM-4776. | |
| 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. | |
| thyroid-hormone transaminase | A pyridoxal-phosphate protein. Acts on monoiodotyrosine, diiodotyrosine, triiodothyronine, thyroxine and dinitrotyrosine (unlike EC 2.6.1.24 diiodotyrosine transaminase, which does not act on dinitrotyrosine). Pyruvate or oxaloacetate can act as acceptors. Group: Enzymes. Synonyms: 3,5-dinitrotyrosine transaminase; thyroid hormone aminotransferase. Enzyme Commission Number: EC 2.6.1.26. CAS No. 51004-29-6. 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-2865; thyroid-hormone transaminase; EC 2.6.1.26; 51004-29-6; 3,5-dinitrotyrosine transaminase; thyroid hormone aminotransferase. Cat No: EXWM-2865. | |
| VUN73874 | VUN73874, also known as GOT1 inhibitor 2c, is a glutamate-oxaloacetate transaminase 1 (GOT1)? inhibitor. This compound was first reported in Bioorg Med Chem Lett. 2018 Sep 1;28(16):2675-2678. Group: Inhibitors. Alternative Names: GOT1 inhibitor 2c; VUN73874; VUN-73874; VUN 73874. CAS No. 732973-87-4. Molecular formula: C19H19ClN4O. Mole weight: 354.84. Appearance: Solid powder. Purity: >98%. IUPACName: N-(4-Chlorophenyl)-4-(1H-indol-4-yl)piperazine-1-carboxamide. Canonical SMILES: O=C (N1CCN (C2=CC=CC3=C2C=CN3)CC1)NC4=CC=C (Cl)C=C4. Catalog: ACM732973874. | |
| 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 |
| 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. | |
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