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| Product | Description | |
|---|---|---|
| Potassium pyruvate | Potassium pyruvate. Uses: Designed for use in research and industrial production. Additional or Alternative Names: 2-Oxopropionic acid potassium salt. Appearance: White to off-white solid. CAS No. 4151-33-1. Molecular formula: C3H3KO3. Mole weight: 126.15. Purity: 0.98. IUPACName: Potassium;2-oxopropanoate. Canonical SMILES: CC(=O)C(=O)[O-].[K+]. ECNumber: 223-978-2. Product ID: ACM4151331. Alfa Chemistry ISO 9001:2015 Certified. |  |
| Potassium Pyruvate | Pyruvic Acid Potassium Salt is an intermdiate in sugar metabolism and enzymatic carbohydrate degredation. It is converted by carboxylase into acetaldehyde and CO2. In muscle, it is reduced to lactic acid during exertion, then reoxidized and partly retransformed to glycogen upon resting. When present in culture medium, it improves coliform recovery. It has been shown to be involved in a mitochondrial oxidant-activated metabolic regulatory pathway. It has also been shown to be involved in plant respiratory regulation. Group: Biochemicals. Alternative Names: Pyruvic Acid Potassium Salt. Grades: Highly Purified. CAS No. 4151-33-1. Pack Sizes: 50g, 100g, 250g, 500g. Molecular Formula: C3H3KO3, Molecular Weight: 126.15. US Biological Life Sciences. |  Worldwide |
| Azemiglitazone potassium | Azemiglitazone potassium (MSDC-0602K), a PPARγ -sparing thiazolidinedione (Ps-TZD), binds to PPARγ with the IC 50 of 18.25 μM [1]. Azemiglitazone potassium modulates the mitochondrial pyruvate carrier (MPC). Azemiglitazone potassium can be used for the research of fatty liver including dysfunctional lipid metabolism, inflammation, and insulin resistance [2]. Azemiglitazone potassium, an insulin sensitizer, improves insulinemia and fatty liver disease in mice, alone and in combination with Liraglutide [3]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: MSDC-0602K. CAS No. 1314533-27-1. Pack Sizes: 5 mg; 10 mg; 25 mg; 50 mg. Product ID: HY-108022A. |  |
| diaminobutyrate-2-oxoglutarate transaminase | A pyridoxal-phosphate protein that requires potassium for activity.In the proteobacterium Acinetobacter baumannii, this enzyme is cotranscribed with the neighbouring ddc gene that also encodes EC 4.1.1.86, diaminobutyrate decarboxylase. Differs from EC 2.6.1.46, diaminobutyrate-pyruvate transaminase, which has pyruvate as the amino-group acceptor. This is the first enzyme in the ectoine-biosynthesis pathway, the other enzymes involved being EC 2.3.1.178, diaminobutyrate acetyltransferase and EC 4.2.1.108, ectoine synthase. Group: Enzymes. Synonyms: L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase; 2,4-diaminobutyrate 4-aminotransferase; diaminobutyrate aminotransferase; DABA aminotransferase; DAB aminotransferase; EctB; diaminibutyric acid aminotransferase; L-2,4-diamin. Enzyme Commission Number: EC 2.6.1.76. CAS No. 196622-96-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2916; diaminobutyrate-2-oxoglutarate transaminase; EC 2.6.1.76; 196622-96-5; L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase; 2,4-diaminobutyrate 4-aminotransferase; diaminobutyrate aminotransferase; DABA aminotransferase; DAB aminotransferase; EctB; diaminibutyric acid aminotransferase; L-2,4-diaminobutyrate:2-oxoglutarate 4-aminotransferase. Cat No: EXWM-2916. |  |
| Galloflavin Potassium salt | Galloflavin Potassium salt is an inhibitor of human lactate dehydrogenase (LDH) (Ki = 5.46 and 15.1 μM for LDH-A and LDH-B, respectively, in competition with pyruvate) with anticancer activity. Galloflavin inhibits lactate production and decreases ATP synthesis in PLD/PRF/5 cells. Synonyms: NSC-107022 potassium; NSC 107022 potassium; NSC107022 potassium; 3,8,9,10-Tetrahydroxypyrano[3,2-c][2]benzopyran-2,6-dione potassium salt. Grades: ≥95% by HPLC. CAS No. 1780260-20-9. Molecular formula: C12H5O8K. Mole weight: 316.26. |  |
| Moniliformin potassium salt | It is a potent, water-soluble mycotoxin produced by several species of fusarium. It selectively inhibits mitochondrial oxidization of pyruvate and α-ketoglutarate. Synonyms: Semisquaric acid potassium salt; 3-Cyclobutene-1,2-dione, 3-hydroxy-, potassium salt; 1-Hydroxycyclobut-1-ene-3,4-dione potassium salt. Grades: >99% by HPLC. CAS No. 52591-22-7. Molecular formula: C4HKO3. Mole weight: 136.15. | |
| Native Bacillus stearothermophilus Phosphotransacetylase | Phosphotransacetylase converts CoA to acetyl CoA. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. This enzyme participates in 3 metabolic pathways:taurine and hypotaurine metabolism, pyruvate metabolism, and propanoate metabolism. Applications: Phosphotransacetylase, from bacillus stearothermophilus, is used to convert coa to acetyl coa. phosphotransacetylase (pta) is used to study transport systems for acetate. it is used to study metabolic pathways in various bacterium. Group: Enzymes. Synonyms: phosphate acetyltransferase; phosphotransacetylase; phosphoacylase; PTA; EC 2.3.1.8; 9029-91-8. Enzyme Commission Number: EC 2.3.1.8. CAS No. 9029-91-8. PTA. Activity: > 3,000 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized powder containing potassium phosphate. Source: Bacillus stearothermophilus. phosphate acetyltransferase; phosphotransacetylase; phosphoacylase; PTA; EC 2.3.1.8; 9029-91-8. Cat No: NATE-0641. | |
| Native Bacillus subtilis L-Alanine Dehydrogenase | L-Alanine dehydrogenase is an A-stereospecific dehydrogenase that catalyzes the reversible deamination of L-alanine to pyruvate and ammonium. It is important for the geneRation of pyruvate during sporulation. L-Alanine dehydrogenase from Bacillus subtilis has a predominately ordered kinetic mechanism in which NAD binds before L-alanine. Subsequently, ammonia, pyruvate, and NADH are released in that specific order. Optimal pH for the amination reaction is 8.8-9.0, whereas it is 10-10.5 for the deamination reaction. The enzyme is inactivated by divalent metal ions and p-chloromercuribenzoate, mercuric ion being most effective. The inactivation may be reversed by L-or D-...genase. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. Activity: Type I, ~30 units/mg protein (Lowry); Type II, > 20 units/mg protein (Lowry). Storage: -20°C. Form: Type I, buffered aqueous glycerol solution, Solution in 50% glycerol containing 10 mM potassium phosphate buffer, pH 7.7; Type II, ammonium sulfate suspension, Suspension in 2.4 M (NH4)2SO4 solution, pH 7.0. Source: Bacillus subtilis. L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Cat No: NATE-0043. | |
| Native Baker's yeast (S. cerevisiae) Pyruvate Decarboxylase | Pyruvate decarboxylase (PDC) is a homotetrameric enzyme that catalyses the decarboxylation of pyruvic acid to acetaldehyde and carbon dioxide in the cytoplasm. Pyruvate decarboxylase depends on cofactors thiamine pyrophosphate (TPP) and magnesium. PDC contains a β-α-β structure, yielding parallel β-sheets. Applications: Pyruvate decarboxylase (pdc) is used to study residues involved in thiamine pyrophosphate (tpp) binding. it is used to study the regulation of fermentation pathways in plant species. Group: Enzymes. Synonyms: Pyruvate decarboxylase; EC 4.1.1.1; α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase; 9001-04-1; 2-Oxo-acid carboxy-lyase; PDC. Enzyme Commission Number: EC 4.1.1.1. CAS No. 9001-4-1. PDC. Activity: 5.0-20.0 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.2 M (NH4)2SO4 pH 6.5, stabilized with 5% glycerol, 5 mM potassium phosphate, 1 mM magnesium acetate, 0.5 mM EDTA, and 25 μM c ocarboxylase. Source: Baker's yeast (S. cerevisiae). Pyruvate decarboxylase; EC 4.1.1.1; α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase; 9001-04-1; 2-Oxo-acid carboxy-lyase; PDC. Cat No: NATE-0510. | |
| Native Baker's yeast (S. cerevisiae) S-Acetyl-coenzyme A synthetase | Acetyl-coenzyme A synthetase catalyzes the production of acetyl-CoA. It is involved in histone acetylation in the nucleus. It may be involved in the growth of nonfermentable carbon sources such as glycerol. Acetyl-coenzyme A synthetase is induced by acetate, acetaldehyde and ethanol. Applications: S-acetyl-coenzyme a synthetase may be used to study various metabolic pathways, such as glycolysis, gluconeogenesis, pyruvate metabolism and co fixation. it may also be used in gene expression studies. Group: Enzymes. Synonyms: acetyl-CoA synthetase; acetyl activating enzyme; acetate thiokinase; acyl-activating enzyme; acetyl coenzyme A synthetase; acetic thiokinase; acetyl CoA ligase; acetyl C. Enzyme Commission Number: EC 6.2.1.1. CAS No. 9012-31-1. ACS. Activity: > 3 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing stabilizers as potassium phosphate, sucrose, and reduced glutathione. Source: Baker's yeast (S. cerevisiae). acetyl-CoA synthetase; acetyl activating enzyme; acetate thiokinase; acyl-activating enzyme; acetyl coenzyme A synthetase; acetic thiokinase; acetyl CoA ligase; acetyl CoA synthase; acetyl-coenzyme A synthase; short chain fatty acyl-CoA synthetase; short-chain acyl-coenzyme A synthetase; ACS; EC 6.2.1.1; 9012-31-1. Pack: Package size based on protein content. Cat No: NATE-0026. | |
| Native Bovine L-Lactic Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: For use in enzymatic determination of lactate or pyruvate. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nL. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 2-8°C. Form: Type I, Suspension in 2.2 M ammonium sulfate; Type II, buffered aqueous glycerol solution, Solution in 50% glycerol containing 0.025 M potassium phosphate buffer, pH 7.5; Type III, ammonium sulfate suspension, Crystalline suspension in 2.1 M (NH4)2SO4 solution, pH 6.0; Type IV, buffered aqueous glycerol solution, Solution in 50% glycerol containing 0.025 M potassium phosphate buffer, pH 7.5. Source: Bovine heart. Species: Bovine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0409. | |
| Native Escherichia coli N-Acetylneuraminic Acid Aldolase | In enzymology, a N-acetylneuraminate lyase (EC 4.1.3.3) is an enzyme that catalyzes the chemical reaction:N-acetylneuraminate<-> N-acetyl-D-mannosamine + pyruvate. Hence, this enzyme has one substrate, N-acetylneuraminate, and two products, N-acetyl-D-mannosamine and pyruvate. This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. This enzyme participates in aminosugars metabolism. Applications: This enzyme is useful for enzymatic determination of n-acetylneuraminic acid and sialic acid when coupled with the related enzymes in clinical analysis. for industrial use, this enzyme is useful for enzymatic synthe...o. 9027-60-5. NALase. Mole weight: mol wt ~98 kDa. Activity: > 20 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salt. Source: Escherichia coli. N-acetylneuraminic acid aldolase; acetylneuraminate lyase; sialic aldolase; sialic acid aldolase; sialate lyase; N-acetylneuraminic aldolase; neuraminic aldolase; N-acetylneuraminate aldolase; neuraminic acid aldolase; N-acetylneuraminic acid aldolase; neuraminate aldolase; N-acetylneuraminic lyase; N-acetylneuraminic acid lyase; NPL; NALase; NANA lyase; acetylneuraminate pyruvate-lyase; N-acetylneuraminate pyruvate-lyase; 9027-60-5; EC 4.1.3.3. Cat No: NATE-0490. | |
| Native Lactobacillus leichmanii D-Lactic Dehydrogenase | D-lactic dehydrogenase catalyzes the conversion of D-lactate into D-pyruvate while reducing NAD+ to NADH and H+. Applications: In the food industry, the primary catalysis is coupled to conversion of nadh and h+ to nad+ with diaphorase coupled with converting the non-fluorescent resazurin to the highly fluorescent substance resorufin to measure the content of d-lactate in food products. Group: Enzymes. Synonyms: EC 1.1.1.28, D-Lactic Dehydrogenase; 9028-36-8; lactic acid dehydrogenase; D-specific lactic dehydrogenase; D-(-)-lactate dehydrogenase (NAD); D-lactic acid dehydrogenase; D-lactic dehydrogenase; (R)-Lactate:NAD+ oxidoreductase; D-LDH. Enzyme Commission Number: EC 1.1.1.28. CAS No. 9028-36-8. D-LDH. Activity: > 30 units/mg protein; ~1000 U/mL; 250-500 units/mg protein (biuret); 150-300 units/mg protein; 1,000-3,000 units/mg protein (biuret). Storage: 2-8°C. Form: Suspension in 3.2 M (NH4)2SO4, 0.1 M potassium phosphate, pH 7.0. Source: Lactobacillus leichmanii. EC 1.1.1.28, D-Lactic Dehydrogenase; 9028-36-8; lactic acid dehydrogenase; D-specific lactic dehydrogenase; D-(-)-lactate dehydrogenase (NAD); D-lactic acid dehydrogenase; D-lactic dehydrogenase; (R)-Lactate:NAD+ oxidoreductase; D-LDH. Cat No: NATE-0195. | |
| Native Porcine L-Lactic Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in ammonium sulfate and 0.1 M potassium phosphate, pH 7.0. Source: Porcine heart. Species: Porcine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0412. | |
| Phospho(enol)pyruvic acid monopotassium salt | Phospho(enol)pyruvic acid monopotassium salt. Uses: Designed for use in research and industrial production. Additional or Alternative Names: 2-(Phosphonooxy)-2-propenoic acid monopotassium sal; mono-Potassium phosphoenolpyruvate; Potassium 1-carboxyvinyl hydrogenphosphate; potassium,1-carboxyethenyl hydrogen phosphate; PEP monopotassium salt,PEP-K,Phospho(enol)pyruvate potassium salt; PHOSPHOENOLPYRUVIC ACID MONOPOTASSIUM SALT. Appearance: White to off-white powder. CAS No. 4265-07-0. Molecular formula: C3H4KO6P. Mole weight: 206.13. Purity: 97%+. IUPACName: potassium;1-carboxyethenylhydrogenphosphate. Canonical SMILES: C=C(C(=O)O)OP(=O)(O)[O-].[K+]. ECNumber: 224-247-0. Product ID: ACM4265070. Alfa Chemistry ISO 9001:2015 Certified. Categories: Potassium hydrogen 2-(phosphonatooxy)acrylate. | |
| 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. | |
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