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| Product | Description | |
|---|---|---|
| 2,3-Diphospho-D-glyceric acid penta(cyclohexylammonium) salt | D-Glycerate 2,3-diphosphate (DPG), cofactor of both phosphoglyceric acid mutase and hemoglobin, may be used as a reference compound in analysis of blood cell (erythrocyte) glycolysic cycle metabolites. 2,3-diphosphoglycerate (DPG) may be used as a reference in assays that measure DPG levels to indicate the health status of erythrocytes/red blood cells (RBC). Applications: Used as a reference compound in analysis of blood cell (erythrocyte) glycolysic cycle metabolites. Group: Coenzymes. Synonyms: D-Glycerate 2,3-diphosphate pentacyclohexylamine salt. CAS No. 62868-79-5. Purity: ≥95%. Mole weight: 761.91. Appearance: Powder. Form: Solid. D-Glycerate 2,3-diphosphate pentacyclohexylamine salt; 2,3-Diphospho-D-glyceric acid penta(cyclohexylammonium) salt; 62868-79-5. Cat No: COEC-080. |  |
| 5-aminolevulinate synthase | A pyridoxal-phosphate protein. The enzyme in erythrocytes is genetically distinct from that in other tissues. Group: Enzymes. Synonyms: ALAS; ALA synthase; α-aminolevulinic acid synthase; Δ-aminolevulinate synthase; Δ-aminolevulinate synthetase; Δ-aminolevulinic acid synthase; Δ-aminolevulinic acid synthetase; Δ-aminolevulinic synthetase; 5-aminolevulinate synthetase; 5-aminolevulinic acid synthetase; ALA synthetase; aminolevulinate synthase; aminolevulinate synthetase; aminolevulinic acid synthase; aminolevulinic acid synthetase; aminolevulinic synthetase. Enzyme Commission Number: EC 2.3.1.37. CAS No. 9037-14-3. 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-2215; 5-aminolevulinate synthase; EC 2.3.1.37; 9037-14-3; ALAS; ALA synthase; α-aminolevulinic acid synthase; Δ-aminolevulinate synthase; Δ-aminolevulinate synthetase; Δ-aminolevulinic acid synthase; Δ-aminolevulinic acid synthetase; Δ-aminolevulinic synthetase; 5-aminolevulinate synthetase; 5-aminolevulinic acid synthetase; ALA synthetase; aminolevulinate synthase; aminolevulinate synthetase; aminolevulinic acid synthase; aminolevulinic acid synthetase; aminolevulinic synthetase. Cat No: EXWM-2215. | |
| Chemically modified Glucose-6-phosphate Dehydrogenase from Leuconostoc mesenteroides | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Applications: Use glucose-6-phosphate dehydrogenase for the determination of blood glucose or creatine kinase. Group: Enzymes. Synonyms: D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glu. Glucose-6-phosphate dehydrogenase. Mole weight: 110 kD (2 identical subunits 55,000 D). Activity: >30 U/mg lyophilizate. Stability: At +2 to +8°C within specification range for 18 months. Store dry. Appearance: White lyophilizate. Source: E. coli. Species: Leuconostoc mesenteroides. EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase; 9001-40-5. Cat No: DIA-280. | |
| Entacapone | Entacapone is a potent, reversible, peripherally acting and orally active catechol-O-methyltransferase (COMT) inhibitor. Entacapone inhibits COMT from rat brain, erythrocytes and liver with IC 50 values of 10 nM, 20 nM, and 160 nM, respectively. Entacapone is selective for COMT over other catecholamine metabolizing enzymes, including MAO-A, MAO-B, phenolsulphotransferase M (PST-M) and PST-P (IC 50 s>50 μM). Entacapone can be used for the research of Parkinson's disease [1]. Entacapone serves as a inhibitor of FTO demethylation with an IC 50 of 3.5 μM, can be used for the research of metabolic disorders [2]. Uses: Scientific research. Group: Signaling pathways. CAS No. 130929-57-6. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 50 mg; 100 mg. Product ID: HY-14280. |  |
| globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase | Globoside is a neutral glycosphingolipid in human erythrocytes and has blood-group-P-antigen activity. The enzyme requires a divalent cation for activity, with Mn2+ required for maximal activity. UDP-GalNAc is the only sugar donor that is used efficiently by the enzyme: UDP-Gal and UDP-GlcNAc result in very low enzyme activity. Lactosylceramide, globoside and gangliosides GM3 and GD3 are not substrates. For explanation of the superscripted '3' in the systematic name, see GL-5.3.4. Group: Enzymes. Synonyms: uridine diphosphoacetylgalactosamine-galactosylgalactosylglucosylceramide acetylgalactosaminyltransferase; globoside synthetase; UDP-N-acetylgalactosamine: globotriaosylceramide β-3-N-acetylgalactosaminyltransferase; galactosylgalactosylglucosylceramide β-D-acetylgalactosaminyltransferase; UDP-N-acetylgalactosamine: globotriaosylceramide β1,3-N-acetylgalactosaminyltrans. Enzyme Commission Number: EC 2.4.1.79. CAS No. 62213-46-1. 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-2619; globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase; EC 2.4.1.79; 62213-46-1; uridine diphosphoacetylgalactosamine-galactosylgalactosylglucosylceramide acetylgalactosaminyltransferase; globoside synthetase; UDP-N-acetylgala | |
| Glucose-6-phosphate Dehydrogenase from E. coli, Recombinant | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Group: Enzymes. Synonyms: EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate . Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Mole weight: ~ 56,770. Activity: 172 U/mg. Stability: > 2 years. Storage: 4°C. Form: In 3.2 M ammonium sulphate. Source: E. coli. Species: E. coli. EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase; 9001-40-5. Cat No: DIA-407. | |
| Leuconostoc mesenteroides Glucose-6-phosphate Dehydrogenase, Recombinant | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Glucose 6-phosphate dehydrogenase (g-6-p-dh) is a key regulatory enzyme in the first step of the pentose phosphate pathway. g-6-p-dh is a glycoprotein with a molecular mass of 128 kda (gel filtration). Applications: Glucose-6-phosphate...its/mg protein (biuret). Storage: 2-8°C. Form: Type I, Lyophilized powder containing Ficoll and Tris buffer salts; Type II, ammonium sulfate suspension, Supplied in 3.2M ammonium sulfate containing 50mM Tris and 1mM magnesium chloride, pH 7.5. Source: E. coli. Species: Leuconostoc mesenteroides. EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase; 9001-40-5. Cat No: DIA-323. | |
| Native Bacillus sp. Glucose-6-phosphate dehydrogenase | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Native glucose-6-phosphate dehydrogenase (ec 1.1.1.49) was purified from bacillus sp. Applications: Useful for enzymatic determination of glucose or atp when coupled with hexokinase. Group: Enzymes. Synonyms: Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosph. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Mole weight: 104 kDa dalton (two subunits of approx. 55 kDa). Activity: > 200 U/mg. Appearance: White/off white powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus sp. Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; GPD. Cat No: DIA-143. | |
| Native baker's yeast (S. cerevisiae) Glucose-6-phosphate Dehydrogenase | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Applications: Glucose-6-phosphate dehydrogenase is used to test ketose reductase activity in developing maize endosperm. Group: Enzymes. Synonyms: Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; GPD. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Storage: -20°C. Form: lyophilized powder. Source: Baker's yeast (S. cerevisiae). Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; GPD. Cat No: DIA-219. | |
| Native Bovine Carbonic Anhydrase | The carbonic anhydrases (or carbonate dehydratases) form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons (or vice versa), a reversible reaction that occurs relatively slowly in the absence of a catalyst. The active site of most carbonic anhydrases contains a zinc ion; they are therefore classified as metalloenzymes. It was from bovine erythrocytes. a dialyzed, lyophilized powder. Applications: Co2 determination in blood; elimination of co2 in reagents for acidity testing; carboxy group transfers; reduction reactions. Group: Enzymes. Synonyms: carbonic anhydrases; carbonate dehydratases; EC 4.2.1.1; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase. Enzyme Commission Number: EC 4.2.1.1. CAS No. 9001-03-0. Carbonic Anhydrase. Mole weight: 29.0 kDa (Theoretical) 30 kDa (Lindskog et al. 1971). Activity: > 3,000 units per mg dry weight. Storage: 2-8°C. Form: lyophilized powder. Source: Bovine Erythrocytes. Species: Bovine. carbonic anhydrases; carbonate dehydratases; EC 4.2.1.1; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase. Cat No: NATE-0101. | |
| Native Bovine Superoxide Dismutase | Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice by preventing the conversion of NO to peroxynitrate, an inducer of apoptosis. Group: Enzymes. Synonyms: Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide di. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Mole weight: mol wt 32.5 kDa. Activity: Type I, > 3 ,000 units/mg protein; Type II, > 4,500 units/mg protein; Type III, 2,500-7 ,000 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Bovine erythrocytes. Species: Bovine. Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuperoxide dismutase; superoxide dismutase I; superoxide dismutase II; SOD; Cu,Zn-SOD; Mn-SOD; Fe-SOD; SODF; SODS; SOD-1; SOD-2; SOD-3; SOD-4; hemocuprein; erythrocuprein; cytocuprein; cuprein ; hepatocuprein; 9054-89-1. Cat No: NATE-0675. | |
| Native Canine Superoxide Dismutase | Superoxide dismutases (SOD) are enzymes that alternately catalyze the dismutation (or partitioning) of the superoxide (O2-) radical into either ordinary molecular oxygen (O2) or hydrogen peroxide (H2O2). Superoxide is produced as a by-product of oxygen metabolism and, if not regulated, causes many types of cell damage. Hydrogen peroxide is also damaging, but less so, and is degraded by other enzymes such as catalase. Thus, SOD is an important antioxidant defense in nearly all living cells exposed to oxygen. One exception is Lactobacillus plantarum and related lactobacilli, which use a different mechanism to prevent damage from reactive (O2-). Group: Enzymes. Synonyms: EC 1.15.1.1; 9054-89-1; SOD; Superoxide:superoxide oxidoreductase; Superoxide Dismutase. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Mole weight: mol wt ~31.2 kDa (two identical subunits). Activity: 2,000-6,000 units/mg protein. Stability: -20°C. Form: lyophilized powder. Source: canine erythrocytes. Species: Canine. EC 1.15.1.1; 9054-89-1; SOD; Superoxide:superoxide oxidoreductase; Superoxide Dismutase. Cat No: NATE-0677. | |
| Native Human Carbonic Anhydrase | Carbonic anhydrase (carbonate dehydratase) catalyzes the following reaction: CO2 + H2O ------> H2CO3 The enzyme is widespread in nature. In animals it plays an important role in respiration by facilitating the transport of carbon dioxide. In plants, carbonic anhydrases are involved in the photosynthetic fixation of CO2.Mammalian erythrocytes contain two distinct forms of carbonic anhydrase distinguished by differences in their catalytic activities. The enzyme requires zinc for its activity and it has a molecular weight of 30,000. Group: Enzymes. Synonyms: carbonic anhydrases; carbonate dehydratases; EC 4.2.1.1; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase. Enzyme Commission Number: EC 4.2.1.1. CAS No. 9001-03-0. Carbonic Anhydrase. Activity: 2000 U/mg protein. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Human Liver. Species: Human. carbonic anhydrases; carbonate dehydratases; EC 4.2.1.1; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase. Cat No: NATE-1678. | |
| Native Human Carbonic Anhydrase I | Carbonic anhydrase is a zinc metalloenzyme that has a molecular weight of approximately 30 kDa Da. The enzyme catalyzes the hydRation of carbon dioxide to carbonic acid. It is involved in vital processes such as pH and CO2 homeostasis, transport of bicarbonate and CO2, biosynthetic reactions, bone resorption, calcification, and tumorigenicity. Therefore, this enzyme is an important target for inhibitors with clinical applications in various pathologies such as glaucoma, epilepsy and Parkinsons disease. Applications: Carbonic anhydrase from human erythrocytes (hca) has been used to study the molten-globule state of carbonic anhydrase (ca). chaperone-like α-crystallin bi...on-small cell lung cancer. Group: Enzymes. Synonyms: Carbonic Anhydrase I; carbonate dehydRatase; carbonic anhydrase; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase; EC 4.2.1.1; 9001-03-0; CA-I; CA1. Enzyme Commission Number: EC 4.2.1.1. CAS No. 9001-03-0. Carbonic Anhydrase. Activity: 100-500 W-A units/mg protein. Form: powder. Source: Human erythrocytes. Species: Human. Carbonic Anhydrase I; carbonate dehydRatase; carbonic anhydrase; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase; EC 4.2.1.1; 9001-03-0; CA-I; CA1. Cat No: NATE-0097. | |
| Native Human Catalase | Catalase activates the decomposition of hydrogen peroxide, a reactive oxygen species, into water and oxygen. It functions as a natural antioxidant, protecting cells against oxidative damage to proteins, lipids and nucleic acids. Catalase has also been used to study the role reactive oxygen species play in gene expression and apoptosis. Protein determined by biuret. Group: Enzymes. Synonyms: EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase; 9001-05-2. Enzyme Commission Number: EC 1.11.1.6. CAS No. 9001-5-2. Purity: > 90% (SDS-PAGE). CAT. Mole weight: tetramer mol wt ~250 kDa. Activity: > 30,000 units/mg protein. Storage: -20°C. Form: buffered aqueous solution. Solution in 50 mM Tris, pH 8.0. Source: Human erythrocytes. Species: Human. EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase; 9001-05-2. Cat No: NATE-0108. | |
| Native Human erythrocytes Acetylcholinesterase | Acetylcholinesterase, also known as AChE or acetylhydrolase, is a hydrolase that hydrolyzes the neurotransmitter acetylcholine. AChE is found at mainly neuromuscular junctions and cholinergic brain synapses, where its activity serves to terminate synaptic transmission. It belongs to carboxylesterase family of enzymes. It is the primary target of inhibition by organophosphorus compounds such as nerve agents and pesticides. The activity obtained using acetylcholine as substrate is 30-100 times that obtained with butyrylcholine, using acetylcholinesterase from electric eel. Applications: Acetylcholinesterase (ache) from creative enzymes has been used in the structure-activity study of phosphoramido acid esters as inhibitors of ache. Group: Enzymes. Synonyms: true cholinesterase; choline esterase I; cholines. Enzyme Commission Number: EC 3.1.1.7. CAS No. 9000-81-1. Acetylcholinesterase. Mole weight: ~80 kDa. Activity: > 500 units/mg protein (BCA). Storage: 2-8°C. Form: buffered aqueous solution. Solution in 20 mM HEPES, pH 8.0, containing 0.1% TRITON X-100. Source: Human erythrocytes. Species: Human. true cholinesterase; choline esterase I; cholinesterase; acetylthiocholinesterase; acetylcholine hydrolase; acetyl; β-methylcholinesterase; AcCholE; EC 3.1.1.7; 9000-81-1; Acetylcholinesterase; AChE; acetylhydrolase. Cat No: NATE-0019. | |
| Native Human Glyceraldehyde-3-phosphate Dehydrogenase | Glyceraldehyde-3-phosphate dehydrogenase catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as part of glycolysis. It has also been shown to have roles in initiation of apoptosis, transcription activation and the shuttling of ER to Golgi vesicles. Group: Enzymes. Synonyms: EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceralde. Enzyme Commission Number: EC 1.2.1.12. CAS No. 9001-50-7. Glyceraldehyde-3-phosphate Dehydrogenase. Activity: 50-150 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing sodium Citrate buffer salts. Source: Human erythrocytes. Species: Human. EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phosphate dehydrogenase (NAD+); glyceraldehyde-3-phosphate dehydrogenase (NAD+); NADH-glyceraldehyde phosphate dehydrogenase; glyceraldehyde-3-P-dehydrogenase; 9001-50-7. Cat No: NATE-0280. | |
| Native Human Superoxide Dismutase | Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice by preventing the conversion of NO to peroxynitrate, an inducer of apoptosis. Applications: Superoxide dismutase from human erythr ocytes has been used in a study to identify in vitro glycated sites of hu...-3; SOD-4; hemocuprein; erythrocuprein; cytocuprein; cuprein ; hepatocuprein; 9054-89-1. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Activity: > 2,500 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Human erythrocytes. Species: Human. Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuperoxide dismutase; superoxide dismutase I; superoxide dismutase II; SOD; Cu,Zn-SOD; Mn-SOD; Fe-SOD; SODF; SODS; SOD-1; SOD-2; SOD-3; SOD-4; hemocuprein; erythrocuprein; cytocuprein; cuprein ; hepatocuprein; 9054-89-1. Cat No: NATE-0680. | |
| Native Leuconostoc mesenteroides Glucose-6-phosphate Dehydrogenase | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ ? 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Applications: Glucose-6-phosphate dehydrogenase was used as a model to test the effect of seed protein fractions on enzyme protection during dehydration. g-6-pdh has been utilized in assays for nicotinamide adenine dinucleotide and tissue pyridine nucleotides. Group: Enzymes. Synonyms: EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-p. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Activity: 20U/mg-solid or more. Storage: 2-8°C. Form: Freeze dried powder. Source: Leuconostoc mesenteroides. EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase; 9001-40-5. Cat No: DIA-321. | |
| Native Microorganism Glucose-6-phosphate Dehydrogenase | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ ? 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Applications: The enzyme is useful for enzymatic determination of nad+(nadp+) and g-6-p, and activities of phosphoglucose isomerase, phosphoglucomutase and hexokinase. the enzyme is also used for enzymatic determination of glucose and creatine phosphokinase activity when coupled with hexokinase. Group: Enzymes. Synonyms: Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-ph. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Mole weight: approx. 140 kDa (by gel filtration). Activity: 200U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; GPD. Cat No: DIA-145. | |
| Native Porcine Calpain 1 | Caplain 1 is a neutral calcium-dependent cysteine protease containing the EF-hand motif. The protease consists of two subunits; the larger subunit has four domains that are homologous with papain and calmodulin. The smaller subunit has one domain that shares homology with calmodulin. It is activated by micromolar levels of calcium and hence, it is also called as micro-calpain. Its activation leads to cellular protein degradation, neuronal cell degeneRation, and autoimmune demyelinating diseases such as multiple sclerosis. Group: Enzymes. Synonyms: μ-calpain; calcium-activated neutral protease I; EC 3.4.22.52. Purity: > = 95% by SDS-PAGE. Calpain 1. Mole weight: 110000. Stability: > 1 year. Storage: -70°C or lower; avoid freeze/thaw cycles. Form: Frozen. Source: Porcine Erythrocytes. Species: Porcine. calpain 1, μ-calpain; calcium-activated neutral protease I; EC 3.4.22.52. Cat No: NATE-1625. | |
| Native Rabbit S-(5'-Adenosyl)-L-homocysteine Hydrolase | Enzyme in vertebrates which catabolizes S-adenosyl-L-homocysteine. Group: Enzymes. Synonyms: Adenosylhomocysteinase; EC 3.3.1.1; S-adenosylhomocysteine synthase; S-adenosylhomocysteine hydrolase; adenosylhomocysteine hydrolase (ambiguous); S-adenosylhomocysteinase; SAHase; AdoHcyase; 9025-54-1. Enzyme Commission Number: EC 3.3.1.1. CAS No. 9025-54-1. AHCY. Activity: > 10 units/mg protein (Lowry). Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 25 mM Tris, pH 7.4, containing 1 mM dithiothreitol, 1 mM EDTA, and 20% glycerol. Source: Rabbit erythrocytes. Species: Rabbit. Adenosylhomocysteinase; EC 3.3.1.1; S-adenosylhomocysteine synthase; S-adenosylhomocysteine hydrolase; adenosylhomocysteine hydrolase (ambiguous); S-adenosylhomocysteinase; SAHase; AdoHcyase; 9025-54-1. Cat No: NATE-0662. | |
| Native Torula yeast Glucose-6-phosphate dehydrogenase | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Group: Enzymes. Synonyms: EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Activity: 300-600 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 2.6 M (NH4)2SO4 solution, pH 7.5. Source: Torula yeast. EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase; 9001-40-5. Cat No: DIA-322. | |
| Native Zymomonas mobilis Glucose-6-Phosphate Dehydrogenase | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Applications: The enzyme is useful for diagnostic reagent, for example, glucose determination or ck determination, and for the specificdetermination of glucose. Group: Enzymes. Synonyms: Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; GPD. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Mole weight: ca. 208000; Subunit molecular weight: ca. 52,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Zymomonas mobilis. Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; GPD. Cat No: NATE-1898. | |
| acylaminoacyl-peptidase | Active at neutral pH. Several variants of this enzyme exist; the human erythrocyte enzyme is relatively specific for removal of N-acetylalanine from peptides. Displays dipeptidyl-peptidase activity on glycyl-peptides, perhaps as a result of mis-recognition of the glycyl residue as an uncharged N-acyl group. Inhibited by diisopropyl fluorophosphate. In peptidase family S9 (prolyl oligopeptidase family). Group: Enzymes. Synonyms: acylamino-acid-releasing enzyme; N-acylpeptide hydrolase; N-formylmethionine (fMet) aminopeptidase; α-N-acylpeptide hydrolase. Enzyme Commission Number: EC 3.4.19.1. CAS No. 73562-30-8. 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-4082; acylaminoacyl-peptidase; EC 3.4.19.1; 73562-30-8; acylamino-acid-releasing enzyme; N-acylpeptide hydrolase; N-formylmethionine (fMet) aminopeptidase; α-N-acylpeptide hydrolase. Cat No: EXWM-4082. | |
| cathepsin E | Found in stomach, spleen, erythrocyte membrane; not lysosomal. Pro-cathepsin E is an 86 kDa disulfide-linked dimer; activation or reduction produces monomer. In peptidase family A1 (pepsin A family). Group: Enzymes. Synonyms: slow-moving proteinase; erythrocyte membrane aspartic proteinase; SMP; erythrocyte membrane aspartic proteinase; EMAP; non-pepsin proteinase; cathepsin D-like acid proteinase; cathepsin E-like acid proteinase; cathepsin D-type proteinase. Enzyme Commission Number: EC 3.4.23.34. CAS No. 110910-42-4. 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-4271; cathepsin E; EC 3.4.23.34; 110910-42-4; slow-moving proteinase; erythrocyte membrane aspartic proteinase; SMP; erythrocyte membrane aspartic proteinase; EMAP; non-pepsin proteinase; cathepsin D-like acid proteinase; cathepsin E-like acid proteinase; cathepsin D-type proteinase. Cat No: EXWM-4271. | |
| Conquinine | Conquinine is a Cytochrome P450 2D6 inhibitor. It is a dextrorotatory stereoisomer of quinine extracted from the bark of the Cinchona tree and similar plant species. It is an alkaloid with class 1A antiarrhythmic and antimalarial effects. It also blocks muscarinic and alpha-adrenergic neurotransmission. It stabilizes the neuronal membrane by binding to and inhibiting voltage-gated sodium channels, thus inhibiting the sodium influx required for the initiation and conduction of impulses resulting in an increase of the threshold for excitation and decreased depolarization during phase 0 of the action potential. It acts primarily as an intra-erythrocytic schizonticide through association with the heme polymer (hemazoin) in the acidic food vacuole of the parasite thereby preventing further polymerization by heme polymerase enzyme. Uses: Conquinine is an alkaloid with class 1a antiarrhythmic and antimalarial effects. it also blocks muscarinic and alpha-adrenergic neurotransmission. Synonyms: Quinidine;Chinidin;Pitayine;(+)-Quinidine;Quinidex;Chinidin;(S)-[(2R,4S,5R)-5-ethenyl-1-azabicyclo[2.2.2]octan-2-yl]-(6-methoxyquinolin-4-yl)methanol. Grades: 98%. CAS No. 56-54-2. Molecular formula: C20H24N2O2. Mole weight: 324.42. |  |
| Glutathione Reductase from Human, Recombinant | Glutathione reductase enzyme is a homodimeric enzyme containing 1 FAD molecule and 1 NADPH binding domain per subunit., Both human GR (hGR) and Plasmodium falciparum GR (PfGR) are essential for the survival of the malaria parasite within the human erythrocyte. Thus, this enzyme may be used for studies of candidate anti-malaria reagents. Group: Enzymes. Synonyms: glutathione-disulfide reductase; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase; EC 1.8.1.7; 9001-48-3; GR. Enzyme Commission Number: EC 1.8.1.7. CAS No. 9001-48-3. GR. Activity: > 10 units/mg protein. Storage: -20°C. Form: buffered aqueous solution; Solution containing 25 mM Tris-HCl, pH 7.4, 1 mM EDTA, and 50% (v/v) glycerol. Source: E. coli. Species: Human. glutathione-disulfide reductase; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase; EC 1.8.1.7; 9001-48-3; GR. Cat No: NATE-0320. | |
| Lewisx | Lewisa blood group trisaccharide antigen found on erythrocyte surfaces and epithelial and glandular cells, enzyme substrate standard. CAS No. 71208-06-5. Product ID: 3-00427. Molecular formula: C20H35NO15. Mole weight: 529.5. Reference: AMPIS, 104, 784, 1996; Science, 260, 906, 1993; Cancer Res., 48, 181, 1988. |  |
| Native Bovine Hemoglobin | Hemoglobin is found in the erythrocytes of all vertebrates. It is a conjugated protein with the prosthetic group heme which contains iron. The heme group is involved with the transport of oxygen from the lungs to tissues, while the globin portion of hemoglobin plays a major role in transporting carbon dioxide from the tissues to the lungs. The iron in heme is in the ferrous state. In oxyhemoglobin, it is apparently still in the ferrous state, but the oxygen is loosely bound to it. The structure of the hemoglobin molecule has been extensively studied. Most of the mammalian hemoglobins are composed of four subunits, consisting of four peptide chains to each of which is attached a heme group. But, among the mammalian hemoglobins, there are structural differences in terms of the amino acid residues and their sequences in the polypeptide chains. The molecular weight of hemoglobin is about 66,000 and the iron content is about 0.34%. The principal applications for hemoglobin are as a substrate for proteases, in anemia diagnosis and as a marker during molecular weight determination. Group: Others. Synonyms: Hemoglobin; Bovine Hemoglobin. Purity: Approx. 100%. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Bovine Erythrocytes. Species: Bovine. Hemoglobin; Bovine Hemoglobin. Cat No: NATE-1878. | |
| Native Human Oxyhemoglobin | Hemoglobin is found in the erythrocytes of all vertebrates. It is a conjugated protein with the prosthetic group heme which contains iron. The heme group is involved with the transport of oxygen from the lungs to tissues, while the globin portion of hemoglobin plays a major role in transporting carbon dioxide from the tissues to the lungs. The iron in heme is in the ferrous state. In oxyhemoglobin, it is apparently still in the ferrous state, but the oxygen is loosely bound to it. Group: Others. Synonyms: Oxyhemoglobin; hemoglobin; Human Oxyhemoglobin. Purity: 90% (biuret). Activity: At least 50 U/mg protein. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Human Erythrocytes. Species: Human. Oxyhemoglobin; hemoglobin; Human Oxyhemoglobin. Cat No: NATE-1881. | |
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