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| Product | Description | |
|---|---|---|
| 1,6-Dichloro-1,6-dideoxy-D-fructose | 1,6-Dichloro-1,6-dideoxy-D-fructose, a chemical compound extensively utilized in the biomedical sphere, manifests enzymatic inhibitory properties against fructose-1,6-bisphosphatase, a vital enzyme involved in gluconeogenesis. Epidemiological evidence suggests its potential effectiveness as a therapeutic agent to combat debilitating ailments such as Type 2 diabetes and other closely related metabolic dysfunctions. |  |
| 1-Methylhistamine | 1-Methylhistamine (CAS# 501-75-7) is used in high fiber diets, promoting gluconeogenesis and inhibit glycolysis in muscle. Uses: Enzyme inhibitors. Synonyms: 2-(1-methyl-4-imidazolyl)ethanamine; 2-(1-methylimidazol-4-yl)ethanamine. Grades: > 95 %. CAS No. 501-75-7. Molecular formula: C6H11N3. Mole weight: 125.17. | |
| aldehyde dehydrogenase [NAD(P)+] | This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is aldehyde:NAD(P)+ oxidoreductase. Other names in common use include aldehyde dehydrogenase [NAD(P)+], and ALDH. This enzyme participates in 5 metabolic pathways: glycolysis / gluconeogenesis, histidine metabolism, tyrosine metabolism, phenylalanine metabolism, and metabolism of xenobiotics by cytochrome p450. Group: Enzymes. Synonyms: ALDH. Enzyme Commission Number: EC 1.2.1.5. CAS No. 9028-88-0. ALDH. 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-1153; aldehyde dehydrogenase [NAD(P)+]; EC 1.2.1.5; 9028-88-0; ALDH. Cat No: EXWM-1153. |  |
| D-(+)-2-Phosphoglyceric Acid Sodium Hydrate | Enantiomerically pure metabolite of glycolysis / gluconeogenesis and also substrate for a number of important enzymes in central metabolism like enolase and phosphoglycerate mutase. Group: Biochemicals. Alternative Names: (R) -3-Hydroxy-2- (phosphonooxy) propanoic Acid Trisodium Salt. Grades: Highly Purified. CAS No. 70195-25-4. Pack Sizes: 5mg, 10mg. Molecular Formula: C?H?Na?O?P, Molecular Weight: 252. US Biological Life Sciences. |  Worldwide |
| D-Fructose-1,6-diphosphate magnesium salt | D-Fructose-1,6-diphosphate magnesium salt is a crucial compound known to regulate glycolysand gluconeogenesis processes, aiding in the research of various metabolic disorders. It also acts as a coenzyme, supporting enzymes involved in energy metabolism. Uses: Neuroprotective agents. Synonyms: beta-D-Fructose 1,6-bisphosphate; 1,6-di-O-phosphono-beta-D-fructofuranose; beta-D-fructofuranose 1,6-bisphosphate; fructose-1,6-diphosphate; Beta-Fructose-1,6-Diphosphate; Fructose 1,6-diphosphate; fructose-1,6-bisphosphate; D-fructose-1,6-diphosphate; Esafosfan; beta-D-fructofuranose 1,6-bis(dihydrogen phosphate); Diphosphofructose; [(2R,3S,4S,5R)-2,3,4-trihydroxy-5-(phosphonooxymethyl)oxolan-2-yl]methyl dihydrogen phosphate; D-Fructose 1,6-biphosphate; beta-D-fructofuranose 1,6-bisphosphate (RSSR closed ring). CAS No. 34693-15-7. Molecular formula: C6H12O12P2 Mg. Mole weight: 362.40. | |
| D-Fructose-2,6-diphosphate sodium salt | D-Fructose-2,6-diphosphate sodium salt is a vital compound in biomedicine used as a metabolic regulator. It plays a crucial role in the regulation of glycolysis and gluconeogenesis. D-Fructose-2,6-diphosphate sodium salt is employed in researching enzyme mechanisms, drug development targeting metabolic disorders, and in studying the treatment of diseases like diabetes and cancer. Synonyms: D-Fructose-2,6-bisphosphate sodium salt. CAS No. 84364-89-6. Molecular formula: C6H13NaO12P2. Mole weight: 362.1. | |
| D-Glucan | D-Glucan is an orally effective Dectin-1 receptor immune activator with antioxidant properties (reducing TNF-α ). D-Glucan activates macrophages and neutrophils to scavenge free radicals, inhibit oxidative stress and inflammatory responses, and improve insulin sensitivity. D-Glucan promotes glycolysis by enhancing the activity of the antioxidant enzyme glutathione, inhibiting gluconeogenesis and activating GK. D-Glucan can be used in the research of liver damage protection (antagonizing Acetaminophen (HY-66005) toxicity), radiation protection (synergistic with vitamin E) and diabetes (improving glucose metabolism) [1] [2] [3] [4]. Uses: Scientific research. Group: Biochemical assay reagents. CAS No. 9012-72-0. Pack Sizes: 100 mg; 500 mg. Product ID: HY-134816. |  |
| Fructose 1,6-bisphosphatase from Human, Recombinant | Fructose 1,6-bisphosphatase (FBPase; EC 3.1.3.11) is an enzyme in the liver that converts fructose-1,6-bisphosphate to fructose 6-phosphate in gluconeogenesis. Fructose bisphosphatase catalyses the reverse of the reaction which is catalysed by phosphofructokinase, which is involved in the process of glycolysis. These enzymes only catalyse the reaction in one direction each, and are regulated by metabolites such as fructose 2,6-bisphosphate so that high activity of one of the two enzymes is accompanied by low activity of the other. It is involved in many different metabolic pathways and found in most organisms. FBPase requires metal ions for catalysis (Mg2+ and Mn2+ being preferred) and the enzyme is potently inhibited by Li+. Group: Enzymes. Synonyms: Fructose-bisphosphatase; EC 3.1.3.11; FBPase; Hexose diphosphatase. Enzyme Commission Number: EC 3.1.3.11. Purity: > 90% (densitometry). FBPase. Mole weight: 36.8 kDa. Activity: 1525 pmol/min/ug. Storage: Stable for > 6 months at -80°C. Form: Liquid. Storage Buffer: 50 mM potassium phosphate pH-7.4, 50 mM sodium chloride, 0.5 mM ethylenediaminetetraaceticacid, and 2.5% glycerol. Source: E. coli. Species: Human. Fructose-bisphosphatase; EC 3.1.3.11; FBPase; Hexose diphosphatase. Cat No: NATE-1576. | |
| glucose-1-phosphate phosphodismutase | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is D-glucose-1-phosphate:D-glucose-1-phosphate 6-phosphotransferase. This enzyme participates in glycolysis / gluconeogenesis and starch and sucrose metabolism. Group: Enzymes. Enzyme Commission Number: EC 2.7.1.41. CAS No. 9026-25-9. 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-3071; glucose-1-phosphate phosphodismutase; EC 2.7.1.41; 9026-25-9. Cat No: EXWM-3071. | |
| Glucose-6-Phosphate Isomerase from Human, Recombinant | Glucose-6-phosphate isomerase (GPI) is a part of the GPI family whose members encode multifunctional phosphoglucose isomerase proteins involved in energy pathways. GPI is a dimeric enzyme which catalyzes the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. Mammalian GPI also functions as a tumor-secreted cytokine and an angiogenic factor (AMF) which stimulates endothelial cell motility. In addition, GPI is a neurotrophic factor (Neuroleukin) for spinal and sensory neurons. GPI performs in different capacities inside and outside the cell. In the cytoplasm, GPI is involved in glycolysis and gluconeogenesis, while outside the cell it acts as a...somerase; Autocrine motility factor; Neuroleukin; Sperm antigen 36; GPI; PGI; PHI; AMF; NLK; SA-36; GNPI. Purity: Greater than 95.0% as determined by SDS-PAGE. PGI. Mole weight: 65.3 kDa. Stability: GPI although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. Appearance: Sterile Filtered colorless solution. Source: E. coli. Species: Human. Glucose-6-phosphate isomerase; Phosphoglucose isomerase; Phosphohexose isomerase; Autocrine motility factor; Neuroleukin; Sperm antigen 36; GPI; PGI; PHI; AMF; NLK; SA-36; GNPI. Cat No: NATE-0841. | |
| LY3522348 | KHK-IN-3 (Example 1) is a ketohexokinase ( KHK ) inhibitor. KHK-IN-3 can be used in the study of kidney disease, nonalcoholic steatohepatitis (NASH), diabetes and heart failure. KHK is a rate-limiting enzyme and fructokinase involved in fructose metabolism. KHK catalyzes the phosphorylation of fructose to fructose-1-phosphate (FIP) at the expense of ATP. The lack of feedback inhibition of fructose metabolism triggers the accumulation of downstream intermediates such as lipogenesis, gluconeogenesis, and oxidative phosphorylation [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: KHK-IN-3. CAS No. 2568608-48-8. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-149987. | |
| 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. | |
| MB06322 | MB06322 (CS-917) is a novel inhibitor of fructose 1,6-bisphphosphatase (FBPase) which is one of the rate-limiting enzymes of gluconeogenesis. CS-917 suppressed plasma glucose elevation after meal loading in a dose-dependent manner at doses ranging from 10 to 40 mg/kg. Research findings suggest that enhanced gluconeogenesis contributes to hyperglycemia in postprandial conditions as well as in fasting conditions, and that CS-917 as an FBPase inhibitor corrects postprandial hyperglycemia as well as fasting hyperglycemia. Synonyms: Managlinat dialanetil; MB 06322; MB-06322; CS-917; CS917; CS 917; diethyl 2, 2'-(((5-(2-amino-5-isobutylthiazol-4-yl)furan-2-yl)phosphanediyl)bis(azanediyl))(2S, 2'S)-dipropionate. CAS No. 280782-97-0. Molecular formula: C21H33N4O5PS. Mole weight: 484.55. | |
| Native Baker's yeast (S. cerevisiae) 3-Phosphoglyceric Phosphokinase | PhosphoglyceRate kinase (EC 2.7.2.3) (PGK) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglyceRate (1,3-BPG) to ADP producing 3-phosphoglyceRate (3-PG) and ATP. Like all kinases it is a transferase. PGK is a major enzyme used in glycolysis, in the first ATP-geneRating step of the glycolytic pathway. In gluconeogenesis, the reaction catalyzed by PGK proceeds in the opposite direction, geneRating ADP and 1,3-BPG. Applications: 3-phosphoglyceric phosphokinase generates atp by catalyzing the transfer of a phosphate group from 1,3-diphosphoglycerate to adp. 3-phosphoglycerate phosphokinase is used to study glycolysis ...phoglyceric kinase; phosphoglycerokinase; EC 2.7.2.3. Enzyme Commission Number: EC 2.7.2.3. CAS No. 9001-83-6. 3-PGK. Activity: > 1000 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Source: Baker's yeast (S. cerevisiae). PGK; 3-PGK; ATP-3-phospho-D-glyceRate-1-phosphotransferase; ATP:D-3-phosphoglyceRate 1-phosphotransferase; 3-phosphoglyceRate kinase; 3-phosphoglyceRate phosphokinase; 3-phosphoglyceric acid kinase; 3-phosphoglyceric acid phosphokinase; 3-phosphoglyceric kinase; glyceRate 3-phosphate kinase; glycerophosphate kinase; phosphoglyceric acid kinase; phosphoglyceric kinase; phosphoglycerokinase; EC 2.7.2.3. Cat No: NATE-0006. | |
| Native Baker's yeast (S. cerevisiae) Enolase | Enolase is a metalloenzyme that catalyzes the interconversion of 2-phosphoglycerate to phosphoenolpyruvate. Enolase is essential for both glycolysis and gluconeogenesis. Enolase from bakers yeast is a homodimer containing two bound Mg2+ ions. The molecular weight is 93.069 kDa.The peptide consists of 436 amino acids and contains a single cysteine residue. Two of the active site components include His191 and Arg414. The phosphorylated tyrosine residue present in yeast enolase forms a substrate for phosphorylation by tyrosine protein kinase. Apart from Mg2+, the enzyme can be activated by Zn2+, Mn2+, and Cd2+. Applications: Enolase from baker?s yeast has been used in a st...d spectroscopy. it has also been used along with other proteins to study gradient chromatof ocusing-mass spectrometry; a new technique for protein analysis. Group: Enzymes. Synonyms: EC 4.2.1.11; enolase; 2-phosphoglyceRate dehydRatase; 14-3-2-protein; nervous-system specific enolase; phosphoenolpyruvate hydRatase; 2-phosphoglyceRate dehydRatase; 2-phosphoglyceric dehydRatase; 2-phosphoglyceRate enolase; γ-enolase; 2-phospho-D-glyceRate hydro-lyase; 9014-08-8. Enzyme Commission Number: EC 4.2.1.11. CAS No. 9014-8-8. Enolase. Activity: > 50 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Baker's yeast (S. cerevisiae) | |
| 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 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 Fructose-bisphosphate aldolase from Thermophillic bacteria | Fructose-bisphosphate aldolase (EC 4.1.2.13), often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate. Gluconeogenesis and the Calvin cycle, which are anabolic pathways, use the reverse reaction. Glycolysis, a catabolic pathway, uses the forward reaction. Aldolase is divided into two classes by mechanism. Applications: Carbon bond formation between dihydroxyacetone phosphate and linear aldehydes. Group: Enzymes. Synonyms: aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Enzyme Commission Number: EC 4.1.2.13. CAS No. 9024-52-6. Aldolase. Storage: Store at -20°C. Form: Frozen liquid. Source: Thermophillic bacteria. aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Cat No: NATE-1152. | |
| 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 Mutarotase | In enzymology, an aldose 1-epimerase (EC 5.1.3.3) is an enzyme that catalyzes the chemical reaction:alpha-D-glucose<-> beta-D-glucose. Hence, this enzyme has one substrate, alpha-D-glucose, and one product, beta-D-glucose. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. This enzyme participates in glycolysis and gluconeogenesis. Applications: This enzyme is useful for enzymatic determination of glucose. Group: Enzymes. Synonyms: mutarotase; aldose mutarotase; galactose mutarotase; galactose 1-epimerase; D-galactose 1-epimerase; aldose 1-epimerase; EC 5.1.3.3. Enzyme Commission Number: EC 5.1.3.3. CAS No. 9031-76-9. Mutarotase. Mole weight: ca. 39,500. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Microorganism. mutarotase; aldose mutarotase; galactose mutarotase; galactose 1-epimerase; D-galactose 1-epimerase; aldose 1-epimerase; EC 5.1.3.3. Cat No: NATE-1907. | |
| Native Porcine Mutarotase | In enzymology, an aldose 1-epimerase (EC 5.1.3.3) is an enzyme that catalyzes the chemical reaction:alpha-D-glucose<-> beta-D-glucose. Hence, this enzyme has one substrate, alpha-D-glucose, and one product, beta-D-glucose. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. This enzyme participates in glycolysis and gluconeogenesis. Applications: Clinical chemistry. Group: Enzymes. Synonyms: mutarotase; aldose mutarotase; galactose mutarotase; galactose 1-epimerase; D-galactose 1-epimerase; aldose 1-epimerase; EC 5.1.3.3. Enzyme Commission Number: EC 5.1.3.3. CAS No. 9031-76-9. Mutarotase. Storage: Store desiccated at-15°C or below. Allow to come to room temperature before opening. Before returning to storage, redesiccate under vacuum over silica gel for a minimum of four hours. Re-seal before returning to-15°C or below. Form: A freeze-dried material. Source: Porcine kidney. Species: Porcine. mutarotase; aldose mutarotase; galactose mutarotase; galactose 1-epimerase; D-galactose 1-epimerase; aldose 1-epimerase; EC 5.1.3.3. Cat No: NATE-0465. | |
| Native Rabbit Aldolase | Fructose-bisphosphate aldolase (EC 4.1.2.13), often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate. Gluconeogenesis and the Calvin cycle, which are anabolic pathways, use the reverse reaction. Glycolysis, a catabolic pathway, uses the forward reaction. Aldolase is divided into two classes by mechanism. Applications: Aldolase is used to convert fructose 1,6-diphosphate to dihydroxyacetone p...aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Enzyme Commission Number: EC 4.1.2.13. CAS No. 9024-52-6. Aldolase. Activity: Type I, lyophilized powder, > 8.0 units/mg protein; Type II, ammonium sulfate suspension, 10-20 units/mg protein. Storage: -20°C. Form: lyophilized powder. Essentially sulfate-free containing Citrate buffer salts. Source: Rabbit muscle. Species: Rabbit. aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Cat No: NATE-0048. | |
| Native Rabbit Glucose-6-Phosphatase | Glucose 6-phosphatase (EC 3.1.3.9, G6Pase) is an enzyme that hydrolyzes glucose-6-phosphate, resulting in the creation of a phosphate group and free glucose. Glucose is then exported from the cell via glucose transporter membrane proteins. This catalysis completes the final step in gluconeogenesis and glycogenolysis and therefore plays a key role in the homeostatic regulation of blood glucose levels. Applications: Glucose-6-phosphatase was used to study the effects of clausena anisata (wild hook leaf) extracts on selected diabetes-related metabolizing enzymes. Group: Enzymes. Synonyms: EC 3.1.3.9; glucose 6-phosphate phosphatase; G6Pase; 9001-39-2; glucose-6-phosphatase. Enzyme Commission Number: EC 3.1.3.9. CAS No. 9001-39-2. Purity: Protein ~30 % (balance mostly sucrose). G6Pase. Activity: > 0.05 units/mg protein. Storage: -20°C. Form: powder with sucrose. Source: Rabbit liver. Species: Rabbit. EC 3.1.3.9; glucose 6-phosphate phosphatase; G6Pase; 9001-39-2; glucose-6-phosphatase. Cat No: NATE-0269. | |
| Native Spinach Aldolase | Fructose-bisphosphate aldolase (EC 4.1.2.13), often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate. Gluconeogenesis and the Calvin cycle, which are anabolic pathways, use the reverse reaction. Glycolysis, a catabolic pathway, uses the forward reaction. Aldolase is divided into two classes by mechanism. Protein determined by lowry. Group: Enzymes. Synonyms: aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Enzyme Commission Number: EC 4.1.2.13. CAS No. 9024-52-6. Aldolase. Activity: 0.3-1.0 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Spinach. aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Cat No: NATE-0049. | |
| Native Yeast Aldehyde Dehydrogenase | In enzymology, an aldehyde dehydrogenase [NAD(P)+] (EC 1.2.1.5) is an enzyme that catalyzes the chemical reaction: an aldehyde + NAD(P)+ + H2O <-> an acid + NAD(P)H + H+. The 4 substrates of this enzyme are aldehyde, NAD+, NADP+, and H2O, whereas its 4 products are acid, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in 5 metabolic pathways: glycolysis / gluconeogenesis, histidine metabolism, tyrosine metabolism, phenylalanine metabolism, and metabolism of xenobiotics by cytochrome p450. Applications: Component of nadh and nadph recycling systems. Group: Enzymes. Synonyms: aldehyde:NAD(P)+ oxidoreductase; aldehyde dehydrogenase [NAD(P)+]; ALDH; Aldehyde Dehydrogenase; EC 1.2.1.5. Enzyme Commission Number: EC 1.2.1.5. CAS No. 9028-88-0. ALDH. Activity: ~20 units/mg protein (At 25 °C with acetaldehyde as the substrate.). Form: Lyophilized. Source: Yeast. aldehyde:NAD(P)+ oxidoreductase; aldehyde dehydrogenase [NAD(P)+]; ALDH; Aldehyde Dehydrogenase; EC 1.2.1.5. Cat No: NATE-0902. | |
| 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. | |
| 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 |
| Phosphoglucomutase, Rabbit muscle | Phosphoglucomutase, Rabbit muscle is often used in biochemical studies. Phosphoglucomutase is an enzyme that can transfer the phosphate group on the α-D-glucose monomer forward from the 1-position to the 6-position or reversely transfer from the 6-position to the 1-position, and promote the glucose-1-phosphate and glucose-6-phosphate Transform each other. Phosphoglucomutase is a key enzyme in glycolysis and gluconeogenesis, and plays an important role in the metabolism of proteins, lipids and nucleic acids [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9001-81-4. Pack Sizes: 500 U; 1 KU. Product ID: HY-P2820. | |
| phosphoglycerate kinase | Phosphoglycerate kinase (EC 2.7.2.3) (PGK) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglycerate (1,3-BPG) to ADP producing 3-phosphoglycerate (3-PG) and ATP. Like all kinases it is a transferase. PGK is a major enzyme used in glycolysis, in the first ATP-generating step of the glycolytic pathway. In gluconeogenesis, the reaction catalyzed by PGK proceeds in the opposite direction, generating ADP and 1,3-BPG. Group: Enzymes. Synonyms: PGK; 3-PGK; ATP-3-phospho-D-glycerate-1-phosphotransferase; ATP:D-3-phosphoglycerate 1-phosphotransferase; 3-phosphoglycerate kinase; 3-phosphoglycerate phosphokinase; 3-phosphoglyceric acid kinase; 3-phosphoglyceric acid pho. Enzyme Commission Number: EC 2.7.2.3. CAS No. 9001-83-6. 3-PGK. 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-3175; phosphoglycerate kinase; EC 2.7.2.3; 9001-83-6; PGK; 3-PGK; ATP-3-phospho-D-glycerate-1-phosphotransferase; ATP:D-3-phosphoglycerate 1-phosphotransferase; 3-phosphoglycerate kinase; 3-phosphoglycerate phosphokinase; 3-phosphoglyceric acid kinase; 3-phosphoglyceric acid phosphokinase; 3-phosphoglyceric kinase; glycerate 3-phosphate kinase; glycerophosphate kinase; phosphoglyceric acid kinase; phosphoglyceric kinase; phosphoglycerokinase. Cat No: EXWM-3175. | |
| Phosphoglycerate kinase, yeast | Phosphoglycerate kinase, yeast (PGK), namely phosphoglycerate kinase, is a glycolytic enzyme commonly used in biochemical research. Phosphoglycerate kinase can catalyze the reversible transfer of phosphate groups from 1,3-bisphosphoglycerate (1,3-BPG) to ADP to generate 3-phosphoglycerate (3-PG) and ATP. At the same time, it can also participate in gluconeogenesis, catalyzing the opposite reaction to produce 1,3BPGA and ADP. Phosphoglycerate kinase is involved in energy metabolism, interaction with nucleic acid, tumor progression, cell death and virus replication and other related processes [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: PGK. CAS No. 9001-83-6. Pack Sizes: 500 U; 1 KU. Product ID: HY-P2822. | |
| pyruvate, phosphate dikinase | It is a key enzyme in gluconeogenesis and photosynthesis that is responsible for reversing the reaction performed by pyruvate kinase in Embden-Meyerhof-Parnas glycolysis. Group: Enzymes. Synonyms: pyruvate, orthophosphate dikinase; pyruvate-phosphate dikinase (phosphorylating); pyruvate, phosphate dikinase; pyruvate-inorganic phosphate dikinase; pyruvate-phosphate dikinase; pyruvate-phosphate ligase; pyruvic-phosphate dikinase; pyruvic-phosphate ligase; pyruvate, Pi dikinase; PPDK. Enzyme Commission Number: EC 2.7.9.1. CAS No. 9027-40-1. 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-3348; pyruvate, phosphate dikinase; EC 2.7.9.1; 9027-40-1; pyruvate, orthophosphate dikinase; pyruvate-phosphate dikinase (phosphorylating); pyruvate, phosphate dikinase; pyruvate-inorganic phosphate dikinase; pyruvate-phosphate dikinase; pyruvate-phosphate ligase; pyruvic-phosphate dikinase; pyruvic-phosphate ligase; pyruvate, Pi dikinase; PPDK. Cat No: EXWM-3348. | |
| Triosephosphate isomerase 1 (23-37) | Triosephosphate isomerase 1 (23-37) is a fragment of TPI1. Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis. Synonyms: Triose-phosphate isomerase (23-37); Methylglyoxal synthase (23-37). | |
| L-Arginine, reagent grade, ≥98% | L-Arginine, reagent grade, ≥98%. Uses: L-arginine has been used to study non-enzymatic gluconeogenesis.it has also been used to study the effects of l-arginine supplementation on kidney and liver injury in rats with myocardial infarction. Additional or Alternative Names: (S)-2-Amino-5-guanidinopentanoic acid. Product Category: Amino Acids. CAS No. 74-79-3. Molecular formula: H2NC(=NH)NH(CH2)3CH(NH2)CO2H. Mole weight: 174.2. Canonical SMILES: N[C@@H](CCCNC(N)=N)C(O)=O. ECNumber: 200-811-1. Product ID: ACM74793-3. Alfa Chemistry ISO 9001:2015 Certified. |  |
| L-Glutamine | L-Glutamine is a multifunctional amino acid that plays an important role in various metabolic processes in the human body. This non-essential amino acid is naturally abundant and contributes significantly to a variety of important functions. Uses: L-glutamine has been used to study the effects of amino acids in promoting food consumption in drosophila melanogaster.it has also been used to study non-enzymatic gluconeogenesis. Additional or Alternative Names: (S)-2,5-Diamino-5-oxopentanoic acid, L-Glutamic acid 5-amide, Levoglutamide. Product Category: Amino Acids. Appearance: Solid. CAS No. 56-85-9. Molecular formula: H2NCOCH2CH2CH(NH2)CO2H. Mole weight: 146.14. Purity: 0.99. IUPACName: (2S)-2,5-Diamino-5-oxopentanoic acid. Canonical SMILES: N[C@@H](CCC(N)=O)C(O)=O. Density: 1.47 g/cm³ at 20 °C. ECNumber: 200-292-1. Product ID: ACM56859-2. Alfa Chemistry ISO 9001:2015 Certified. | |
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