Creative Enzymes - Products
Enzyme manufacturing for life science research and medicines, food, alcohol, fabric, paper etc. Uses include: drug discovery, cancer and infectious disease research, microbiology and personalized medicine.
| Product | Description | |
|---|---|---|
| Native Clostridium botulinum ADP-ribosyltransferase C3 | ADP-ribosyltransferase C3 from Clostridium botulinum ribosylates rho in eukaryotes in the presence of NAD. The ADP-ribosylating exoenzyme forms a single major 25 kDA (approx.) band with SDS electrophoresis. The enzyme labels 21-24 kDa proteins in tissues such as the human platelet membranes. Applications: Adp-ribosyltransferase c3 from clostridium botulinum may be used to study cellular signaling and g protein expression. Group: Enzymes. Synonyms: ADP-ribosyltransferase C3; 58319-92-9; Botulinum neurotoxin C3; C3 Exoenzyme; C3 Exotoxin; C3 Transferase. CAS No. 58319-92-9. C3 Transferase. Storage: 2-8°C. Source: Clostridium botulinum. ADP-ribosyltransferase C3; 58319-92-9; Botulinum neurotoxin C3; C3 Exoenzyme; C3 Exotoxin; C3 Transferase. Cat No: NATE-0095. |  |
| Native Clostridium histolyticum Clostripain | Clostripain from Clostridium histolyticum is composed of two polypeptide chains, with molecular masses of 41.7 kDa and 15.4 kDa. Clostripain has a highly restricted substRate specificity for Arg-Xaa peptide bonds. Therefore, clostripain has been explored as a potential enzyme for protein sequencing purposes. It has also been studied as a catalyst for condensation of pharmaceutically important peptides containing Arg-Pro bonds. The isoelectric point of the enzyme is 4.8-4.9 (at 8°C), and optimum pH is 7.4~7.8 (against α-benzoyl-arginine ethyl ester). Group: Enzymes. Synonyms: clostridiopeptidase B; clostridium histolyticum proteinase B; α-clostridipain; clostridiopeptidase; Endoproteinase Arg-C; EC 3.4.22.8; 9028-00-6. Enzyme Commission Number: EC 3.4.22.8. CAS No. 9028-00-6. Kallikrein. Activity: > 20 units/mg solid. Storage: 2-8°C. Form: lyophilized powder. Source: Clostridium histolyticum. clostridiopeptidase B; clostridium histolyticum proteinase B; α-clostridipain; clostridiopeptidase; Endoproteinase Arg-C; EC 3.4.22.8; 9028-00-6. Cat No: NATE-0143. | |
| Native Clostridium histolyticum Collagenase | Collagenases are endopeptidases that digest native collagen in the triple helix region. Collagens are the major fibrous component of animal extracellular connective tissue. Bacterial collagenases differ from vertebrate collagenases in that they exhibit broader substrate specificity (Peterkofsky 1982, Birkedal-Hansen 1987). Unlike animal collagenases that split collagen in its native triple-helical conformation (Woolley et al. 1975, Gross et al. 1974), bacterial collagenase is unique because it can degrade both water-insoluble native collagens and water-soluble denatured ones. It can attack almost all collagen types, and is able to make multiple cleavages within triple h...ations needing to avoid introduction of animal derived pathogens into bioprocessing procedures. Group: Enzymes. Synonyms: EC 3.4.24.3; Collagenase; Clostridiopeptidase A; Clostridium histolyticum collagenase; collagenase A; collagenase I; Achromobacter iophagus collagenase; aspergillopeptidase C; nucleolysin; Collagenase, Type 1; Collagenase, Type 2; Collagenase, Type 3; Collagenase, Type 4; Collagenase, Type 5. Enzyme Commission Number: EC 3.4.24.3. CAS No. 9001-12-1. Collagenase. Mole weight: 68 to 130 kDa. Activity: Type 1 > 125 units per mg; Type 2 > 125 units per mg; Type 3 > 100 units per mg; Type 4 > 160 units per mg; Type 5 > 450 units per mg. Stability: This pro | |
| Native Clostridium kluyveri Diaphorase | Native Clostridium kluyveri Diaphorase. Applications: Diaphorase from clostridium kluyveri, or lipoyl dehydrogenase, has been used in a study to assess the protein-protein interactions in assembly of lipoic acid on the 2-oxoacid dehydrogenases of aerobic metabolism. lipoyl dehydrogenase has also been used in a study to investigate the redox regulation of tyrosine nitration and 3-nitrotyrosine reduction by antioxidants. Group: Enzymes. Synonyms: dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxidoreductase (NADH); lipoamide reductase; lipo. Enzyme Commission Number: EC 1.8.1.4. CAS No. 9001-18-7. Diaphorase. Activity: 3.0-20.0 units/mg protein (biuret). Storage: Store at -20°C. Form: Lyophilized powder. Source: Clostridium kluyveri. dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxidoreductase (NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate dehydrogenase; lipoic acid dehydrogenase; lipoyl dehydrogenase; dihydrolipoyl dehydrogenase; EC 1.8.1.4; 9001-18-7; Lipoamide Dehydrogenase. Cat No: NATE-0875. | |
| Native Clostridium perfringens (C. welchII) Choloylglycine Hydrolase | Choloylglycine hydrolase (EC 3.5.1.24) is an N-terminal nucleophilic (Ntn) hydrolase that catalyzes the hydrolysis of amide bonds, libeRates the glycine/taurine moiety from the steroid core and eventually yields unconjugated bile acids. Agents that oxidize thiol groups (e.g., p-mercuribenzoate, iodoacetamide, Hg2+, Cu2+, and Cd2+) have been shown to strongly inhibit bile salt hydrolase (BSH) activity in Clostridium perfringens. Applications: The enzyme from creative enzymes has been used in the analysis of bile samples in various studies. Group: Enzymes. Synonyms: EC 3.5.1.24; glycocholase; bile salt hydrolase; choloyltaurine hydrolase; 3α,7α,12α-trihydroxy-5β-cholan-24-oylglycine amidohydrolase; 37289-07-9. Enzyme Commission Number: EC 3.5.1.24. CAS No. 37289-07-9. Choloylglycine Hydrolase. Activity: > 100 units/mg protein. Storage: -20°C. Form: lyophilized powder. Partially purified lyophilized powder containing buffer salts and stabilizer. Source: Clostridium perfringens (C. welchII). EC 3.5.1.24; glycocholase; bile salt hydrolase; choloyltaurine hydrolase; 3α,7α,12α-trihydroxy-5β-cholan-24-oylglycine amidohydrolase; 37289-07-9. Cat No: NATE-0129. | |
| Native Clostridium perfringens (C. welchII) Neuraminidase | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. At least four mammalian sialidase homologs have been descr...ic mesenchymal stem cells in the treatment of f ocal cerebral ischemia. it has also been used in a study to investigate sinonasal terat ocarcinosarcoma with rhabdoid features. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18. Enzyme Commission Number: EC 3.2.1.18. Purity: > 95% (SDS-PAGE). Neuraminidase. Storage: -20°C. Form: buffered aqueous solution; Solution in 100 mM Tris-HCl, 5 mM MgSO4, 250 mM KCl, pH 5.0-5.2. Source: Clostridium perfringens (C. welchII). neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18. Cat No: NATE-0480. | |
| Native Clostridium perfringens (C. welchII) Neuraminidase Agarose | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Neuraminidase enzymes are hydrolase enzymes that promo...cells. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Enzyme Commission Number: EC 3.2.1.18. CAS No. 9001-67-6. Neuraminidase. Activity: Type I, 6-10 units/mg protein (using 4MU-NANA), 2-5 units/mg protein (mucin); Type II, 10-20 units/mg protein (using 4MU-NANA), 3.5-8.0 units/mg protein (mucin); Type III, > 50 units/mg protein (using 4MU-NANA). Storage: -20°C. Form: lyophilized powder. Source: Clostridium perfringens (C. welchII). neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Cat No: NATE-0479. | |
| Native Clostridium perfringens (C. welchII) Phospholipase C | Phospholipase C is induced by thrombin and platelet-activating factor, forming 1,2-diacylglycerol and phosphatidic acid. PLC hydrolyzes the phosphate bond on phosphatidylcholine and other glycerophospholipids yielding diacylglycerol; this enzyme will also hydrolyze the phosphate bonds of sphingomyelin, cardiolipin, choline plasmalogen and ceramide phospholipids. Group: Enzymes. Synonyms: Phospholipase C; PLC; 9001-86-9; lipophosphodiesterase I; lecithinase C; Clostridium welchii α-toxin; Clostridium oede. Enzyme Commission Number: EC 3.1.4.3. CAS No. 9001-86-9. Phospholipase C. Activity: Type I, > 150 units/mg protein; Type II, 10-50 units/mg protein; Type III, Type IV, > 1,000 units/mg protein (Lowry). Storage: -20°C. Form: Type I, Lyophilized powder in buffered salts; Type II, lyophilized powder; Type III, buffered aqueous glycerol solution; Solution in 60% (v/v) glycerol containing 10 mM Tris-HCl, pH 8.0 and 10 mM EDTA; Type IV, lyophilized powder, Contains phosphate buffer salts, EDTA and stabilizer. Source: Clostridium perfringens (C. welchII). Phospholipase C; PLC; 9001-86-9; lipophosphodiesterase I; lecithinase C; Clostridium welchii α-toxin; Clostridium oedematiens β-and γ-toxins; lipophosphodiesterase C; phosphatidase C; heat-labile hemolysin; α-toxin; EC 3.1.4.3. Cat No: NATE-0593. | |
| Native Clostridium sp. Diaphorase | Native Clostridium sp. Diaphorase. Applications: This enzyme is useful for colorimetric determination of nad(p)h and many dehydrogenases when coupled with various dyes which act as hydrogen acceptors from nad(p)h. Group: Enzymes. Synonyms: Diaphorase; EC 1.6.99.-. Enzyme Commission Number: EC 1.6.99.-. Diaphorase. Mole weight: 24 kDa. Activity: Grade? 30U/mg-solid or more (containing approx. 15% of stabilizers). Stability: Stable at-20°C for at least one year. Appearance: Yellowish amorphous powder, lyophilized. Form: Freeze dried powder. Source: Clostridium sp. Diaphorase; EC 1.6.99.-. Cat No: DIA-187. | |
| Native Clostridium tetani Tetanolysin | Tetanolysin is a toxin produced by Clostridium tetani bacteria. Its function is unknown but it is believed to contribute to the pathogenesis of tetanus. The other C. tetani toxin, tetanospasmin, is more definitively linked to tetanus. Tetanolysin belongs to a family of protein toxins known as cytolysins which bind to cholesterol. Cytolysins form pores in the cytoplasmic membrane that allows for the passage of ions and other molecules into the cell. The molecular weight of tetanolysin is approximately 55 kDa daltons. Hemolytic activity of tetanolysin is determined using 2.5% rabbit red blood cells at 37°c for 40 min. Applications: Tetanolysin has been used to analyze the formation of lytic pores in red blood cells (rbcs). it has also been used to permeabilize infected rbcs. Group: Others. Synonyms: Tetanolysin. Mole weight: 55 kDa. Storage: 2-8°C. Form: lyophilized powder containing sodium chloride and sodium acetate. Source: Clostridium tetani. Tetanolysin. Cat No: NATE-0693. | |
| Native Corallina officinalis Bromoperoxidase | Bromoperoxidase from Corallina officinalis is a phenoxazine dye. The brilliant cresyl blue (BCB) test determines the activity of glucose-6-phosphate dehydrogenase (G6PDH). The activity of this enzyme is greatest in growing oocytes and declines as oocytes mature. It stains reticulocytes and trichomonads. Bromoperoxidase contains a significant amount of nonheme iron. It is activated by vanadate ions. Maximal activity is achieved with stoichiometric vanadium incorporation. Applications: Bromoperoxidase from corallina officinalis may be used for staining brain tissue, nuclei, plant chromosomes, reticulocytes, platelets and reticulated red cells. it may be used for the detection of biochemical molecules and the bcb enzyme assay. the bcb assay is also used industrially in optical data storage. Group: Enzymes. Synonyms: BCB; Bromide Peroxidase; Bromoperoxidase; 69279-19-2. CAS No. 69279-19-2. BCB. Activity: > 100 units/mg protein (Lowry). Storage: -20°C. Form: Partially purified, lyophilized powder containing MES buffer salts. Source: Corallina officinalis. BCB; Bromide Peroxidase; Bromoperoxidase; 69279-19-2. Cat No: NATE-0091. | |
| Native Coriolus versicolor Laccase | Laccases are copper-containing oxidase enzymes that are found in many plants, fungi, and microorganisms. The copper is bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. Type 1 copper is available to action of solvents, such as water. It can be displaced by mercury, substituted by cobalt or removed via a copper complexone. Removal of type 1 copper causes a decrease in laccase activity. Cyanide can remove all copper from the enzyme however re-embedding with type 1 and type 2 copper has been shown to be impossible. Type 3 copper however can be embed back into the enzyme. Laccases act on phenols and simila...ganisms. the copper is bound in several sites; type 1, type 2, and/or type 3. the ensemble of types 2 and 3 copper is called a trinuclear cluster. type 1 copper is available to action of solvents, such as water. it can be displaced by mercury, substituted by cobalt or removed via a copper complexone. removal of type 1 copper causes a decrease in laccase activity. cyanide can remove all copper from the enzyme however re-embedding with type 1 and type 2 copper has been shown to be impossible. type 3 copper however can be embed back into the enzyme. laccases act on phenols and similar molecules, performing a one-electron oxidations, which remain poorly defined. it is proposed t | |
| Native corn Nitrate Reductase | Nitrate reductase (NADH) is an enzyme with system name nitrite:NAD+ oxidoreductase. This enzyme catalises the following chemical reaction:nitrite + NAD+ + H2O<-> nitrate + NADH + H+. Nitrate reductase us an iron-sulfur molybdenum flavoprotein. Applications: Catalyzes the nadh-dependent reduction of nitrate to nitrite. Group: Enzymes. Synonyms: EC 1.7.1.1; 9013-03-0; Nitrate reductase; NADH; nitrate reductase; NADH-nitrate reductase; NADH-dependent nitrate reductase; assimilatory NADH:nitrate reductase; nitrate reductase (NADH2); NADH2:nitrate oxidoreductase; assimilatory nitrate reductase. Enzyme Commission Number: EC 1.7.1.1. CAS No. 9013-03-0. Nitrate reductase. Activity: > 4 units/mL. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: Corn. EC 1.7.1.1; 9013-03-0; Nitrate reductase; NADH; nitrate reductase; NADH-nitrate reductase; NADH-dependent nitrate reductase; assimilatory NADH:nitrate reductase; nitrate reductase (NADH2); NADH2:nitrate oxidoreductase; assimilatory nitrate reductase. Cat No: NATE-0474. | |
| Native Corn Phospho (enol)pyruvate Carboxylase | Phospho (enol)pyruvate carboxylase is a ubiquitous, highly regulated oligomeric, cytosolic enzyme in plants. Phospho (enol)pyruvate Carboxylase from corn was found to be highly susceptible to trypsin digestion. Phospho (enol)pyruvate carboxylase is a ubiquitous, highly regulated oligomeric, cytosolic enzyme in plants. Applications: Phospho (enol)pyruvate carboxylase has been used in a study to assess activity of carbon metabolism enzymes in wheat plants treated with kartolin-4 and exposed to water stress. it has also been used in a study to investigate the specific density of leaf as a characteristic of the photosynthetic apparatus. Group: Enzymes. Synonyms: phosphopyruvate (phosphate) carboxylase; PEP carboxylase; phosphoenolpyruvic carboxylase; PEPC; PEPCase; phosphate:oxaloacetate carboxy-lyase (phosphorylating); EC 4.. Enzyme Commission Number: EC 4.1.1.31. CAS No. 9067-77-0. PEPC. Activity: > 1 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 2.4 M (NH4)2SO4 solution containing 10 mM phosphate buffer, pH 7.0, 1 mM biotin, 5 mM dithiothreitol and 1 mM phenylmethylsulfonyl fluoride. Source: Corn. phosphopyruvate (phosphate) carboxylase; PEP carboxylase; phosphoenolpyruvic carboxylase; PEPC; PEPCase; phosphate:oxaloacetate carboxy-lyase (phosphorylating); EC 4.1.1.31; 9067-77-0. Cat No: NATE-0543. | |
| Native Corynebacterium glutamicum 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. 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. CAT. Activity: > 500000 U/mL. Storage: 2-8°C. Form: solution. contains ~30% glycerol, 10% ethanol. Source: Corynebacterium glutamicum. EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase; 9001-05-2. Cat No: NATE-0106. | |
| Native Corynebacterium lilium Creatinine Deiminase | Hydrolase for creatinine determination that catalyzes the conversion of creatinine to N-methylhydantoin and ammonia. Rely on the proven diagnostic quality of this product. Applications: Use creatinine deaminase in diagnostic tests for the determination of creatinine in combination with n-carbamoylsarcosine amidase, n-methylhydantoinase (atp-hydrolysing) and sarcosine oxidase. Group: Enzymes. Synonyms: Creatinine hydrolase; creatinine desiminase. Creatinine Deiminase. Activity: 45.0-90.0 U/mg lyophilizate. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Protect from light. Appearance: Beige lyophilizate. Source: Corynebacterium lilium. Creatinine hydrolase; Creatinine deaminase; EC 3.5.4.21; creatinine desiminase. Cat No: DIA-291. | |
| Native Crotalus adamanteus L-Amino Acid Oxidase | In enzymology, an L-amino acid oxidase (LAAO) (EC 1.4.3.2) is an enzyme that catalyzes the chemical reaction:an L-amino acid + H2O + O2<-> a 2-oxo acid + NH3 + H2O2. The enzyme was first described in 1944 by A. Zeller and A. Maritz. Not only are LAAOs quite variable in terms of molecular mass, they also vary widely regarding stability. In a similar vein, this enzyme performs in a myriad of biological activities including apoptosis-induction, edema-induction, hemorrhaging, and inhibition or induction of platelet aggregation. Applications: L-amino acid oxidase (laao) is used to convert l-amino acids to their corresponding α-keto acids. one unit will oxidatively de...w-injection pr ocedure with chemiluminescence detection for on-site determination of l-alanine. Group: Enzymes. Synonyms: L-amino acid oxidase; LAAO; L-AAO; EC 1.4.3.2; 9000-89-9; ophio-amino-acid oxidase; L-amino-acid:oxygen oxidoreductase (deaminating). Enzyme Commission Number: EC 1.4.3.2. CAS No. 9000-89-9. LAAO. Activity: Type I, > 0.3 unit/mg solid; Type II, > 3.0 units/mg protein (biuret). Storage: Type I, -20°C; Type II, 2-8°C. Form: Type I, dried venom; Type II, aqueous suspension. Source: Crotalus adamanteus. L-amino acid oxidase; LAAO; L-AAO; EC 1.4.3.2; 9000-89-9; ophio-amino-acid oxidase; L-amino-acid:oxygen oxidoreductase (deaminating). Cat No: NATE-0366. | |
| Native Crotalus adamanteus venom Phosphodiesterase I | Venom exonuclease (Phosphodiesterase I) successively hydrolyzes 5'-mononucleotides from 3'-OH-terminated ribo- and deoxyribo-oligonucleotides. The enzyme has an optimal pH range of 9.8-10.4 and a molecular weight of 115 kDa. Phosphodiesterase is inhibited by reducing agents such as glutathione, cysteine and ascorbic acids. It is completely inhibited by 5mM EDTA while ATP, ADP and AMP are partial inhibitors. The enzyme has an absolute requirement for Mg2+. Group: Enzymes. Synonyms: Phosphodiesterase I; EC 3.1.4.1; 5'-exonuclease; 5'-phosphodiesterase; 5'-nucleotide phosphodiesterase; oligonucleate 5'-nucleotidohydrolase; 5' nucleotide phosphodiesterase/alkaline phosphodiesterase I; 5'-NPDase; 5'-PDase; 5'-PDE; 5'NPDE; alkaline phosphodies. Enzyme Commission Number: EC 3.1.4.1. CAS No. 9025-82-5. PDE. Activity: > 20 units per mg dry weight. Storage: -20°C. Form: Lyophilized in vials. Source: Crotalus adamanteus venom. Phosphodiesterase I; EC 3.1.4.1; 5'-exonuclease; 5'-phosphodiesterase; 5'-nucleotide phosphodiesterase; oligonucleate 5'-nucleotidohydrolase; 5' nucleotide phosphodiesterase/alkaline phosphodiesterase I; 5'-NPDase; 5'-PDase; 5'-PDE; 5'NPDE; alkaline phosphodiesterase; nucleotide pyrophosphatase/phosphodiesterase I; orthophosphoric diester phosphohydrolase; PDE I; phosphodiesterase; exonuclease I. Cat No: NATE-0512. | |
| Native Crotalus adamanteus venom Pyrophosphatase, Nucleotide | In enzymology, a nucleotide diphosphatase (EC 3.6.1.9) is an enzyme that catalyzes the chemical reaction:a dinucleotide + H2O<-> 2 mononucleotides. Thus, the two substrates of this enzyme are dinucleotide and H2O, whereas its product is mononucleotide. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. This enzyme participates in 5 metabolic pathways:purine metabolism, starch and sucrose metabolism, riboflavin metabolism, nicotinate and nicotinamide metabolism, and pantothenate and coa biosynthesis. Group: Enzymes. Synonyms: nucleotide diphosphatase; EC 3.6.1.9; nucleotide pyrophosphatase; nucleotide-sugar pyrophosphatase; 9032-64-8. Enzyme Commission Number: EC 3.6.1.9. CAS No. 9032-64-8. Nucleotide Pyrophosphatase. Activity: 4-8 units/mg protein, vial of ~25 units. Storage: -20°C. Form: Lyophilized powder containing approx. 35% Tris buffer salts. Source: Crotalus adamanteus venom. nucleotide diphosphatase; EC 3.6.1.9; nucleotide pyrophosphatase; nucleotide-sugar pyrophosphatase; 9032-64-8. Pack: vial of ~25 units. Cat No: NATE-0493. | |
| Native Crotalus atrox L-Amino Acid Oxidase | In enzymology, an L-amino acid oxidase (LAAO) (EC 1.4.3.2) is an enzyme that catalyzes the chemical reaction:an L-amino acid + H2O + O2<-> a 2-oxo acid + NH3 + H2O2. The enzyme was first described in 1944 by A. Zeller and A. Maritz. Not only are LAAOs quite variable in terms of molecular mass, they also vary widely regarding stability. In a similar vein, this enzyme performs in a myriad of biological activities including apoptosis-induction, edema-induction, hemorrhaging, and inhibition or induction of platelet aggregation. Applications: L-amino acid oxidase is used to convert l-amino acids to their corresponding α-keto acids. this product is from crotalus atrox. one unit will oxidatively deaminate 1.0 μmole of l-phenylalanine per min at ph 6.5 at 37°c. l-amino acid oxidase, from creative enzymes, has been used in leucine aminopeptidase (lap) activity assays. Group: Enzymes. Synonyms: L-amino acid oxidase; LAAO; L-AAO; EC 1.4.3.2; 9000-89-9; ophio-amino-acid oxidase; L-amino-acid:oxygen oxido. Enzyme Commission Number: EC 1.4.3.2. CAS No. 9000-89-9. LAAO. Activity: > 0.10 unit/mg solid. Storage: -20°C. Form: dried venom. Source: Crotalus atrox (Western Diamondback Rattlesnake). L-amino acid oxidase; LAAO; L-AAO; EC 1.4.3.2; 9000-89-9; ophio-amino-acid oxidase; L-amino-acid:oxygen oxidoreductase (deaminating). Cat No: NATE-0367. | |
| Native Crotalus atrox venom 5'-Nucleotidase | 5'-nucleotidase is an enzyme with system name 5'-ribonucleotide phosphohydrolase. This enzyme catalyses the following chemical reaction:a 5'-ribonucleotide + H2O<-> a ribonucleoside + phosphate. This enzyme has a wide specificity for 5'-nucleotides. Group: Enzymes. Synonyms: uridine 5'-nucleotidase; 5'-adenylic phosphatase; adenosine 5'-phosphatase; AMP phosphatase; adenosine monophosphatase; 5'-mononucleotidase; AMPase; UMPase; snake venom 5'-nucleotidase; thimidine monophosphate nucleotidase; 5'-AMPase; 5'-AMP nucleotidase; AMP phosphohydrolase; IMP 5'-nucleotidase; EC 3.1.3.5. Enzyme Commission Number: EC 3.1.3.5. CAS No. 9027-73-0. AMPase. Activity: > 200 units/mg protein. Storage: -20°C. Form: Lyophilized powder balance primarily trehalose, HEPES and CaCl2. Source: Crotalus atrox. uridine 5'-nucleotidase; 5'-adenylic phosphatase; adenosine 5'-phosphatase; AMP phosphatase; adenosine monophosphatase; 5'-mononucleotidase; AMPase; UMPase; snake venom 5'-nucleotidase; thimidine monophosphate nucleotidase; 5'-AMPase; 5'-AMP nucleotidase; AMP phosphohydrolase; IMP 5'-nucleotidase; EC 3.1.3.5. Cat No: NATE-0072. | |
| Native Crotalus atrox (Western Diamondback Rattlesnake) Phosphodiesterase I | Phosphodiesterase I breaks phosphodiester bonds and catalyzes the hydrolysis of various nucleotide polyphosphates. Phosphodiesterase I is released from eucaryotic plasma membranes by phosphatidylinositol-specific phospholipase C. Applications: Phosphodiesterase (pde) is any enzyme that is used to breaks phosphodiester bonds. phosphodiesterase i from western diamondback rattlesnake, is used in phosphodiesterase activation assays for calmodulin. it is added to hydrolyze amp. it is a membrane-bound glycoprotein that is used to catalyze the hydrolysis of various nucleotide polyphosphates. Group: Enzymes. Synonyms: Phosphodiesterase I; EC 3.1.4.1; 5'-exonuclease; 5'-phosphodiesterase; 5'-nucleotide phosphodi. Enzyme Commission Number: EC 3.1.4.1. CAS No. 9025-82-5. PDE. Activity: > 0.01 unit/mg solid. Storage: -20°C. Form: crude dried venom. Source: Crotalus atrox (Western Diamondback Rattlesnake). Phosphodiesterase I; EC 3.1.4.1; 5'-exonuclease; 5'-phosphodiesterase; 5'-nucleotide phosphodiesterase; oligonucleate 5'-nucleotidohydrolase; 5' nucleotide phosphodiesterase/alkaline phosphodiesterase I; 5'-NPDase; 5'-PDase; 5'-PDE; 5'NPDE; alkaline phosphodiesterase; nucleotide pyrophosphatase/phosphodiesterase I; orthophosphoric diester phosphohydrolase; PDE I; phosphodiesterase; exonuclease I. Cat No: NATE-0513. | |
| Native Crotalus durissus terrificus venom Phospholipase A2 | Phospholipase A2 (PLA2) hydrolyzes the β-ester bond of zwitterionic glycerophospholipids. Preferred substrates are phosphatidylcholine, phosphatidylethanolamine, and their plasmalogen analogues. Phosphatidylinositol and phosphatidylserine are also hydrolyzed. It aggressively attacks phospholipids in membranes of intact cells. PLA2 specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Group: Enzymes. Synonyms: Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Enzyme Commission Number: EC 3.1.1.4. CAS No. 9001-84-7. PLA2. Activity: ~200 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Crotalus durissus terrificus venom. Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Cat No: NATE-0584. | |
| Native Crotalus durissus venom L-Amino Acid Oxidase | In enzymology, an L-amino acid oxidase (LAAO) (EC 1.4.3.2) is an enzyme that catalyzes the chemical reaction:an L-amino acid + H2O + O2<-> a 2-oxo acid + NH3 + H2O2. The enzyme was first described in 1944 by A. Zeller and A. Maritz. Not only are LAAOs quite variable in terms of molecular mass, they also vary widely regarding stability. In a similar vein, this enzyme performs in a myriad of biological activities including apoptosis-induction, edema-induction, hemorrhaging, and inhibition or induction of platelet aggregation. Applications: L-amino acid oxidase (laao) is used to convert l-amino acids to their corresponding α-keto acids. this product is from crotalus durissus venom. l-amino acid oxidase, from creative enzymes, has been used in leucine aminopeptidase (lap) activity assays. Group: Enzymes. Synonyms: L-amino acid oxidase; LAAO; L-AAO; EC 1.4.3.2; 9000-89-9; ophio-amino-acid oxidase; L-amino-acid:ox. Enzyme Commission Number: EC 1.4.3.2. CAS No. 9000-89-9. LAAO. Activity: 3-8 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.2 M (NH4)2SO4 pH approx. 6. Source: Crotalus durissus venom. L-amino acid oxidase; LAAO; L-AAO; EC 1.4.3.2; 9000-89-9; ophio-amino-acid oxidase; L-amino-acid:oxygen oxidoreductase (deaminating). Pack: Package size based on protein content. Cat No: NATE-0368. | |
| Native Crotalus Phospholipase A2 | Phospholipases A2 (PLA2s) EC 3.1.1.4 are enzymes that release fatty acids from the second carbon group of glycerol. This particular phospholipase specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Upon downstream modification by cyclooxygenases, arachidonic acid is modified into active compounds called eicosanoids. Eicosanoids include prostaglandins and leukotrienes, which are categorized as anti-inflammatory and inflammatory mediators. Phospholipase a2 is a member of the class of heat-stable, calcium-dependent enzymes catalyzing the hydrolysis of the 2-acyl bond of 3-n-phosphoglycerides. a chromatographically purified, dialyzed, lyophilized powder. Group: Enzymes. Synonyms: EC 3.1.1.4; Phospholipases A2; PLA2s. Enzyme Commission Number: EC 3.1.1.4. CAS No. 9001-86-9. Purity: chromatographically purified, dialyzed. PLA2. Mole weight: 30 kDa (Wells 1969). Activity: > 200 units per mg dry weight. Stability: The enzyme is stable at 90°C and pH 3.0 for at least five minutes. (Uthe 1971; Saito 1962). Storage: Store at 2-8°C. Form: lyophilized powder. Source: Crotalus adamanteus Venom. Species: Crotalus. EC 3.1.1.4; Phospholipases A2; PLA2s. Cat No: NATE-0591. | |
| Native Cucumis melo α-Galactosidase I, Alkaline | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Applications: Alkaline α-galactosidase i was used to assay enzyme activity with 2 mmp-nitrophenyl-α-d-galactoside as substrate at ph 6.5 to compare with the enzyme activity of α-gal a isolated and purified from sf-9 insect cells infected with a recombinant baculovirus encoding normal α-gal a gene. Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. GLA. Mole weight: apparent mol wt ~84 kDa by SDS-PAGE. Storage: -20°C. Form: The product is supplied as a lyophilized powder containing Tris-HCl buffer salts, DTT, EDTA, and NaCl. Source: Cucumis melo. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Cat No: NATE-0291. | |
| Native Cucurbita sp. Ascorbate Oxidase | In enzymology, a L-ascorbate oxidase (EC 1.10.3.3) is an enzyme that catalyzes the chemical reaction:2 L-ascorbate + O2<-> 2 dehydroascorbate + 2 H2O. Thus, the two substRates of this enzyme are L-ascorbate and O2, whereas its two products are dehydroascorbate and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor with oxygen as acceptor. This enzyme participates in ascorbate metabolism. It employs one cofactor, copper. Applications: Ascorbate oxidase, from cucurbita sp., may be used to study oxidative stress and heat stress response and tolerance. ascorbate oxidase, from creative enzymes, has been used in ascorbic acid assays to study the heat stress response of arabidopsis. Group: Enzymes. Synonyms: ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; . Enzyme Commission Number: EC 1.10.3.3. CAS No. 9029-44-1. AAO. Activity: 1,000-3,000 units/mg protein. Storage: 2-8°C. Form: Lyophilized powder containing buffers and sucrose as stabilizer. Source: Cucurbita sp. ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; L-ascorbate:O2 oxidoreductase; AA oxidase; EC 1.10.3.3; 9029-44-1; L-ascorbate oxidase. Cat No: NATE-0012. | |
| Native Cucurbita sp. L-ascorbate oxidase | In enzymology, a L-ascorbate oxidase (EC 1.10.3.3) is an enzyme that catalyzes the chemical reaction2 L-ascorbate + O2 ? 2 dehydroascorbate + 2 H2O. Thus, the two substrates of this enzyme are L-ascorbate and O2, whereas its two products are dehydroascorbate and H2O. Native l-ascorbate oxidase (ec 1.10.3.3) was purified from acremonium sp. Applications: This enzyme is useful for enzymatic determination of ascorbic acid and for eliminating the interference of ascorbic acid in clinical analysis. Group: Enzymes. Synonyms: ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; L-ascorbate: O2 oxidoreductase; AA oxidase; EC 1.10.3.3; 9029-44-1; L-ascorbate oxidase. Enzyme Commission Number: EC 1.10.3.3. CAS No. 9029-44-1. Activity: 200U/mg. Appearance: Light blue amorphous powder, lyophilized. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Light blue lyophilized powder. Source: Cucurbita sp. ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; L-ascorbate: O2 oxidoreductase; AA oxidase; EC 1.10.3.3; 9029-44-1; L-ascorbate oxidase. Cat No: DIA-124. | |
| Native Cystathionine-β-synthase | Cystathionine-β-synthase, also known as CBS, is an enzyme (EC 4.2.1.22) that in humans is encoded by the CBS gene. CBS uses the cofactor pyridoxal-phosphate (PLP) and can be allosterically regulated by effectors such as the ubiquitous cofactor S-adenosyl-L-methionine (adoMet). This enzyme belongs to the family of lyases, to be specific, the hydro-lyases, which cleave carbon-oxygen bonds. CBS is a multidomain enzyme composed of an N-terminal enzymatic domain and two CBS domains. The CBS gene is the most common locus for mutations associated with homocystinuria. Human cbs performs a crucial step in the biosynthetic pathway of cysteine by providing a regulatory control po...nates methyl groups to a variety of substrates, e.g., neurotransmitters, proteins, and nucleic acids. in mammals, cbs is a highly regulated enzyme, which contains a heme cofactor that functions as a redox sensor, that can modulate its activity in response to changes in the redox potential. if the resting form of cbs in the cell has ferrous heme, the potential exists for activating the enzyme under oxidizing conditions by conversion to the ferric state. Group: Enzymes. Synonyms: Cystathionine-β-synthase; CBS; EC 4.2.1.22; 9023-99-8. Enzyme Commission Number: EC 4.2.1.22. CAS No. 9023-99-8. CBS. Cystathionine-β-synthase; CBS; EC 4.2.1.22; 9023-99-8. Cat No: DIA-272. | |
| Native Dactylium dendroides Galactose Oxidase | Galactose oxidase is an extracellular copper-containing enzyme, secreted by the deuteromycete fungus Dactylium dendroides. It catalyzes the oxidation of a range of primary alcohols, including D-galactose, to the corresponding aldehyde, with reduction of oxygen to hydrogen peroxide. Galactose oxidase is an extracellular copper-containing enzyme, secreted by the deuteromycete fungus dactylium dendroides. it catalyzes the oxidation of a range of primary alcohols, including d-galactose, to the corresponding aldehyde, with reduction of oxygen to hydrogen peroxide. Applications: Galactose oxidase may be used as an analytical tool for the specific determination of d-galactose in blood plasma, plant extracts, and phospholipids. it could be used for the characterization of terminal d-galactoside units in several polymers. it may also be useful in the determination of lactose. Group: Enzymes. Synonyms: EC 1.1.3.9; D-galactose oxidase; β-galacto. Enzyme Commission Number: EC 1.1.3.9. CAS No. 9028-79-9. Galactose Oxidase. Activity: Type I, 500-1,500 units/mg protein; Type II, > 3000 units/g solid. Storage: -20°C. Form: Type I, Lyophilized, contains buffer salts and stabilizer; Type II, lyophilized powder. Source: Dactylium dendroides. EC 1.1.3.9; D-galactose oxidase; β-galactose oxidase; 9028-79-9; Galactose Oxidase. Cat No: NATE-0273. | |
| Native Diaphorase (NADPH) from Bacillus megaterium | In enzymology, a NADPH dehydrogenase (EC 1.6.99.1) is an enzyme that catalyzes the chemical reaction: NADPH + H+ + acceptor <-> NADP+ + reduced acceptor. The 3 substrates of this enzyme are NADPH, H+, and acceptor, whereas its two products are NADP+ and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with other acceptors. Applications: Useful for enzymatic determination of reduced nadp. Group: Enzymes. Synonyms: NADPH:acceptor oxidoreductase; NADPH2 diaphorase; NADPH diaph. Enzyme Commission Number: EC 1.6.99.1. CAS No. 9001-68-7. Diaphorase. Mole weight: 48 kDa (gel filtration). Activity: More than 5 U/mg solid. Appearance: Yellowish amorphous powder, lyophilized. Storage: At least one year at -20°C. Form: Freeze dried powder. Source: Bacillus megaterium. NADPH:acceptor oxidoreductase; NADPH2 diaphorase; NADPH diaphorase; OYE; diaphorase; dihydronicotinamide adenine dinucleotide phosphate dehydrogenase; NADPH-dehydrogenase; NADPH-diaphorase; NADPH2-dehydrogenase; old yellow enzyme; reduced nicotinamide adenine dinucleotide phosphate dehydrogenase; TPNH dehydrogenase; TPNH-diaphorase; triphosphopyridine diaphorase; triphosphopyridine nucleotide diaphorase; NADPH2 dehydrogenase; NADPH: (acceptor) oxidoreductase; NADPH dehydrogenase; EC 1.6.99.1. Cat No: NATE-1154. | |
| Native Diisopropyl-fluorophosphatase | In enzymology, a diisopropyl-fluorophosphatase (EC 3.1.8.2) is an enzyme that catalyzes the chemical reaction:diisopropyl fluorophosphate + H2O<-> diisopropyl phosphate + fluoride. Thus, the two substrates of this enzyme are diisopropyl fluorophosphate and H2O, whereas its two products are diisopropyl phosphate and fluoride. This enzyme belongs to the family of hydrolases, specifically those acting on ester bonds phosphoric-triester hydrolases. It employs one cofactor, divalent cation. At least one compound, Chelating agent is known to inhibit this enzyme. Group: Enzymes. Synonyms: EC 3.1.8.2, DFPase; tabunase; somanase; organophosphorus acid anhydrolase; organophosphate acid anhydrase; OPA anhydrase; diisopropylphosphofluoridase; dialkylfluorophosphatase; diisopropyl phosphorofluoridate hydrolase; isopropylphosphorofluoridase; diisopropylfluorophosphonate dehaloge. Enzyme Commission Number: EC 3.1.8.2. CAS No. 9032-18-2. DFPase. Activity: > 30 units/mg. EC 3.1.8.2, DFPase; tabunase; somanase; organophosphorus acid anhydrolase; organophosphate acid anhydrase; OPA anhydrase; diisopropylphosphofluoridase; dialkylfluorophosphatase; diisopropyl phosphorofluoridate hydrolase; isopropylphosphorofluoridase; diisopropylfluorophosphonate dehalogenase; 9032-18-2. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0183. | |
| Native E. coli 1-5-Anhydroglucitol-6-Phosphate Dehydrogenase | Native E. coli 1-5-Anhydroglucitol-6-Phosphate Dehydrogenase. Ag6pdhii is an enzyme produced by microorganisms. this product shall be used for a diagnostics reagent. Applications: Useful for enzymatic determination of 1,5-ag. Group: Enzymes. Synonyms: AG6PDHII; EC 1.1.1.140; 1-5-Anhydroglucitol-6-Phosphate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.140. CAS No. 37250-69-4. AG6PDHII. Mole weight: 78 kDa (TSK gel G 3000 SWXL gel filtration); 40 kDa (SDS-PAGE). Activity: > 20 U/mg. Stability: Stable for 1 years under the freezing condition (-80°C). Appearance: White powder. Storage: Storage at-80°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Escherichia coli. AG6PDHII; EC 1.1.1.140; 1-5-Anhydroglucitol-6-Phosphate Dehydrogenase. Cat No: NATE-0039. | |
| Native E. coli 3-Deoxy-D-manno-octulosonate Aldolase | In enzymology, a 3-deoxy-D-manno-octulosonate aldolase (EC 4.1.2.23) is an enzyme that catalyzes the chemical reaction:3-deoxy-D-manno-octulosonate<-> pyruvate + D-arabinose. Hence, this enzyme has one substRate, 3-deoxy-D-manno-octulosonate, and two products, pyruvate and D-arabinose. This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. Group: Enzymes. Synonyms: 2-keto-3-deoxyoctonate aldolase; KDOaldolase; 3-deoxyoctulosonic aldolase; 2-keto-3-deoxyoctonic aldolase; 3-deoxy-D-manno-octulosonic aldolase; 3-deoxy-D-manno-octulosonate D-arabinose-lyase; EC 4.1.2.23; 3-Deoxy-D-manno-octulosonate Aldolase. Enzyme Commission Number: EC 4.1.2.23. CAS No. 9026-95-3. KDOaldolase. Activity: > 1.0 units/mg. Storage: -20°C. Source: E. coli. 2-keto-3-deoxyoctonate aldolase; KDOaldolase; 3-deoxyoctulosonic aldolase; 2-keto-3-deoxyoctonic aldolase; 3-deoxy-D-manno-octulosonic aldolase; 3-deoxy-D-manno-octulosonate D-arabinose-lyase; EC 4.1.2.23; 3-Deoxy-D-manno-octulosonate Aldolase. Cat No: NATE-0363. | |
| Native E. coli Alanine Aminotransferase | Alanine transaminase (ALT) is a transaminase enzyme (EC 2.6.1.2). It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate-pyruvate transaminase (SGPT) or serum glutamic-pyruvic transaminase (SGPT). ALT is found in plasma and in various body tissues, but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Group: Enzymes. Synonyms: Alanine transami. Enzyme Commission Number: EC 2.6.1.2. CAS No. 9000-86-6. Purity: > 95% (SDS-PAGE). ALT. Mole weight: 54,479 of subunit deduced from gene sequence. Activity: > 1,000 U/mL. Storage: -20°C. Form: Liquid. Source: E. coli. Alanine transaminase; ALT; EC 2.6.1.2; alanine aminotransferase; ALAT; glutamic-pyruvic transaminase; glutamic-alanine transaminase; GPT; β-alanine aminotransferase; alanine-α-ketoglutarate aminotransferase; alanine-pyruvate aminotransferase; glutamic acid-pyruvic acid transaminase; glutamic-pyruvic aminotransferase; L-alanine aminotransferase; L-alanine transaminase; L-alanine-α-ketoglutarate aminotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. Cat No: NATE-0064. | |
| Native E.coli Galactose 1-Dehydrogenase | In enzymology, a galactose 1-dehydrogenase (EC 1.1.1.48) is an enzyme that catalyzes the chemical reaction: D-galactose + NAD+ rightleftharpoons D-galactono-1,4-lactone + NADH + H+. Thus, the two substrates of this enzyme are D-galactose and NAD+, whereas its 3 products are D-galactono-1,4-lactone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in galactose metabolism. Dehydrogenase that catalyzes the oxidation of galactose to d-galactono-1,4-lactone. rely on the proven diagnostic quality of this recombinant enzyme. Applications: Use galactose 1-dehydrogenase in diagnostic tests for the determination of total galactose. Group: Enzymes. Synonyms: D-galactose:NAD+ 1-oxidoreductase; D-galactose dehydrogenase; beta-galactose dehydrogenase; NAD+-dependent D-galactose dehydrogenase; galactose 1-dehy. CAS No. 9028-54-0. Galactose dehydrogenase. Activity: >50 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Appearance: White lyophilizate. Source: E.coli. D-galactose:NAD+ 1-oxidoreductase; D-galactose dehydrogenase; beta-galactose dehydrogenase; NAD+-dependent D-galactose dehydrogenase; galactose 1-dehydrogenase; EC 1.1.1.48; Galactose dehydrogenase; Galactose 1-Dehydrogenase. Cat No: NATE-0979. | |
| Native E. coli Inorganic Pyrophosphatase | Pyrophosphatase (or inorganic pyrophosphatase) is an enzyme (EC 3.6.1.1) that catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. This is a highly exergonic reaction, and therefore can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The functionality of this enzyme plays a critical role in lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, and DNA synthesis,as well as other biochemical transformations. Applications: Increasing rna yield in transcription reaction; enhancing dna replication. Group: Enzymes. Synonyms: Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. CAS No. 9024-82-2. Inorganic pyrophosphatase. Form: 20 mM Tris-HCl, 100 mM NaCl, 1 mM Dithiothreitol, 0.1 mM EDTA, 50% Glycerol, pH 8.0 25°C. Store at -20°C. Source: E. coli. Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-1272. | |
| Native E. coli N-Carbamoylsarcosine Amidase | In enzymology, a N-carbamoylsarcosine amidase is an enzyme that catalyzes the chemical reaction: N-carbamoylsarcosine + H2O rightleftharpoons sarcosine + CO2 + NH3. Thus, the two substrates of this enzyme are N-carbamoylsarcosine and H2O, whereas its 3 products are sarcosine, CO2, and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in arginine and proline metabolism. Hydrolase that catalyzes the interconversion of n-carbamoylsarcosine to sarcosine. Applications: Use n-carbamoylsarcosine amidase in diagnostic tests for the determination of creatinine in combination with creatinine deaminase, n-methylhydantoinase (atp-hydrolysing) and sarcosine oxidase. Group: Enzymes. Synonyms: N-carbamoylsarcosine amidase; N-carbamoylsarcosine amidohydrolase; carbamoylsarcosine amidase. CAS No. 92767-52-7. N-Carbamoylsarcosine Amidase. Activity: 0.80-1.30 U/mg. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Protect from light. Appearance: White lyophilizate. Source: E. coli. Species: E. coli. N-carbamoylsarcosine amidase; N-carbamoylsarcosine amidohydrolase; carbamoylsarcosine amidase. Cat No: NATE-0876. | |
| Native E. coli PreScission Protease | PreScission Protease is a fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes a subset of sequences which include the core amino acid sequence Leu-Phe-Gln/Gly-Pro cleaving between the Gln and Gly residues. Substrate recognition and cleavage are likely to be dependent not only upon primary structural signals, but also upon the secondary and tertiary structures of the fusion protein as well. Applications: During cleavage reactions, it is recommended that samples be removed at various time points and analyzed by sds-page to estimate the yield, purity, and extent of digestion. the amount of prescission protease, temperature and length of incubation required for complete digestion of a given gst fusion partner may vary depending on the fusion partner. optimal conditions for each fusion should be determined in pilot experiments. digestion may be improved by adding triton x-100, tween 20, nonidet, or np40 to a concentration of 0.01%. concentrations of these detergents up to 1% do not inhibit prescission protease. Group: Enzymes. Synonyms: . Purity: >90% by SDS-PAGE. PSP. Activity: >10000 IU/mg. Appearance: Sterile colorless liquid. Storage: Should be stored in small aliquots at -20°C to -80°C for long term. Source: E. coli. PreScission Protease; PSP. Cat No: NATE-0877. | |
| Native E. coli RNA Polymerase, Holoenzyme | E. coli RNA Polymerase, Holoenzyme is the core enzyme saturated with sigma factor 70. The Holoenzyme initiates RNA synthesis from sigma 70 specific bacterial and phage promoters. E. coli RNA Polymerase, Core Enzyme consists of 5 subunits designated α, α, β?, β, and &omega. The enzyme is free of sigma factor and does not recognize any specific bacterial or phage DNA promoters. The enzyme retains the ability to transcribe RNA from nonspecific initiation sequences. Addition of sigma factors will allow the enzyme to initiate RNA synthesis from specific bacterial and phage promoters. Applications: Rna synthesis from e. coli promoter transcription initiation studies in vitro translation with purexpress. Group: Enzymes. Synonyms: E. coli RNA Polymerase, Holoenzyme; E. coli RNA Polymerase; RNA Polymerase; RNAP; RNApol; DNA-dependent RNA polymerase. RNAP. Mole weight: 400 kDa. Storage: at -20°C. Form: 20 mM Tris-HCl, pH 7.5, 100 mM NaCl, 0.1 mM EDTA, 1 mM dithiothreitol (DTT) and 50% glycerol. Source: E. coli. E. coli RNA Polymerase, Holoenzyme; E. coli RNA Polymerase; RNA Polymerase; RNAP; RNApol; DNA-dependent RNA polymerase. Cat No: NATE-1262. | |
| Native E.coli Sarcosine Oxidase | Oxidoreductase that catalyzes the demethylation of sarcosine to glycine. Use Sarcosine Oxidase in your preferred creatinine reagent mix and rely on the proven diagnostic quality of this product. Applications: Use sarcosine oxidase in diagnostic tests for the determination of creatinine. this can be done using one of two methods: (1) in combination with creatinase and creatininase. (2) in combination with creatinine deaminase, n-carbamoylsarcosine amidase and n-methylhydantoinase (atp-hydrolyzing). Group: Enzymes. Synonyms: Sarcosine Oxidase; SAO. CAS No. 9029-22-5. SAO. Mole weight: 40 kD. Activity: 22-40 U/mg lyophilizate; >45 U/mg protein. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Protect from light. Appearance: Yellow lyophilizate. Source: E. coli. Sarcosine Oxidase; EC 1.5.3.1; SAO. Cat No: DIA-290. | |
| Native E. coli Transketolase | Transketolase is highly specific for ketol donor substrates and is stereospecific and enantioselective to hydroxyaldehyde substrates with an (R) configuration. It specifically catalyzes the irreversible transfer of one ketol unit from α-hydroxypyruvic acid to an aldehyde to produce a D-threo (3S,4R)ketose. Applications: Transketolase is widely used in organic synthesis. Group: Enzymes. Synonyms: Transketolase; EC 2.2.1.1; 9014-48-6; glycolaldehydetransferase; Glycolaldehyde Transferase. Enzyme Commission Number: EC 2.2.1.1. CAS No. 9014-48-6. Transketolase. Activity: > 0.1 units/mg. Storage: -20°C. Source: E. coli. Transketolase; EC 2.2.1.1; 9014-48-6; glycolaldehydetransferase; Glycolaldehyde Transferase. Cat No: NATE-0716. | |
| Native Electrophorus electricus (electric eel) 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. Type vi-s, lyophilized powder, 200-1000 units/mg protein; type v-s, lyophilized powder, > 1000 units/mg protein. Applications: The enzyme has been used as a reference to to evaluate the effect of aspartame metabolites on hippocampal acetylcholinesterase activity. the enzyme has also been used in immobilization studies for the rapid detection of acetylthiocholine chloride. Group: Enzymes. Synonyms: true c. Enzyme Commission Number: EC 3.1.1.7. CAS No. 9000-81-1. Acetylcholinesterase. Mole weight: 280 kDa. Activity: > 1 ,000 units/mg protein; 200-1 ,000 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Electrophorus electricus (electric eel). 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-0018. | |
| Native Elizabethkingia meningoseptica PNGase F | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Applications: Used to deglycosylate protein. proteomics grade pngase f has been extensively purified and lyophilized from dilute potassium phosphate buffer to prod...eptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. Purity: > 95% (SDS-PAGE). PNGase F. Mole weight: ~36 kDa. Storage: 2-8°C. Source: Elizabethkingia meningoseptica. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-0601. | |
| Native Elizabethkingia miricola PNGase F | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Applications: Used to deglycosylate protein. Group: Enzymes. Synonyms: glycopeptide N-glycosida. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. PNGase F. Mole weight: 36 kDa. Activity: > 20,000 units/mg protein and > 5,000 units/ml. Stability: The product remains active for at least 12 months when stored properly. Exposure for several days to ambient temperatures will not reduce activity. Do Not Freeze. Storage: 2-8°C. Form: Supplied as a solution in 20 mM Tris HCl, pH 7.5, 50 mM NaCl and 1 mM EDTA. Source: Elizabethkingia miricola. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-0602. | |
| Native Enterobacter aerogenes Glycerol Dehydrogenase | Glycerol dehydrogenase is an enzyme in the oxidoreductase family that utilizes the NAD+ to catalyze the oxidation of glycerol to form glycerone (dihydroxyacetone). Applications: Glycerol dehydrogenase was used in the kinetic enzymatic determination of glycerol in wine and beer. Group: Enzymes. Synonyms: EC 1.1.1.6; NAD+-linked glycerol dehydrogenase; glycerol:NAD+ 2-oxidoreductase; GDH; GlDH; GlyDH; 9028-14-2; glycerin dehydrogenase. Enzyme Commission Number: EC 1.1.1.6. CAS No. 9028-14-2. GDH. Activity: 20-80 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Enterobacter aerogenes. EC 1.1.1.6; NAD+-linked glycerol dehydrogenase; glycerol:NAD+ 2-oxidoreductase; GDH; GlDH; GlyDH; 9028-14-2; glycerin dehydrogenase. Cat No: NATE-0284. | |
| Native Enterobacter aerogenes myo-Inositol Dehydrogenase | In enzymology, an inositol 2-dehydrogenase (EC 1.1.1.18) is an enzyme that catalyzes the chemical reaction:myo-inositol + NAD+<-> 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+. Thus, the two substrates of this enzyme are myo-inositol and NAD+, whereas its 3 products are 2,4,6/3,5 pentahydroxycyclohexanone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in inositol metabolism and inositol phosphate metabolism. Group: Enzymes. Synonyms: myo-inositol 2-dehydrogenase; myo-inositol:NAD+ oxidoreductase; inositol dehydrogenase; myo-inositol dehydrogenase; EC 1.1.1.18; 9028-25-5. Enzyme Commission Number: EC 1.1.1.18. CAS No. 9028-25-5. myo-Inositol Dehydrogenase. Activity: > 10 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing buffer salts and stabilizers. Source: Enterobacter aerogenes. myo-inositol 2-dehydrogenase; myo-inositol:NAD+ oxidoreductase; inositol dehydrogenase; myo-inositol dehydrogenase; EC 1.1.1.18; 9028-25-5. Cat No: NATE-0467. | |
| Native Enterobacter cloacae β-Lactamase | β--lactamase inactivates β-lactam antibiotics by breaking open the β-lactam ring. Protein determined by biuret. Applications: Β-lactamase is used to inactivate β-lactam antibiotics by breaking open the β-lactam ring. β-lactamase is used to study antibiotic resistance and resistance suppression1. this product is produced from enterobacter cloacae. Group: Enzymes. Synonyms: β-lactamase; penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase; EC . Enzyme Commission Number: EC 3.5.2.6. CAS No. 9073-60-3. β-Lactamase. Activity: 6-18 units/mg protein (using benzylpenicillin); 0.2-0.6 units/mg protein (using benzylpenicillin). Storage: 2-8°C. Form: Lyophilized powder containing sodium phosphate and sodium Citrate buffer salts. Source: Enterobacter cloacae. β-lactamase; penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase; EC 3.5.2.6; 9073-60-3. Cat No: NATE-0774. | |
| Native environmental DNA α-Fucosidase | In enzymology, an alpha-L-fucosidase (EC 3.2.1.51) is an enzyme that catalyzes the chemical reaction:an alpha-L-fucoside + H2O<-> L-fucose + an alcohol. Thus, the two substRates of this enzyme are alpha-L-fucoside and H2O, whereas its two products are L-fucose and alcohol. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O-and S-glycosyl compounds. This enzyme participates in n-glycan degradation and glycan structures-degradation. Group: Enzymes. Synonyms: alpha-L-fucoside fucohydrolase; alpha-fucosidase; EC 3.2.1.51; alpha-L-fucosidase. Enzyme Commission Number: EC 3.2.1.51. CAS No. 9037-65-4. FUCA. Source: Proprietary environmental DNA. Species: environmental DNA. alpha-L-fucoside fucohydrolase; alpha-fucosidase; EC 3.2.1.51; alpha-L-fucosidase. Cat No: NATE-0749. | |
| Native Environmental DNA Pustulanase (β-glucanase) | A thermostable β-1,6-endoglucanase or pustulanase (E.C. 3.2.1.75) which catalyses the cleavage of β-1,6 bonds in pustulan and other beta-glucans containing 1,6 linked glucose units. The enzyme is now a component in a standard assay for beta-glucan from Bakers yeast as documented in US Pharmacopeia Food and Chemicals Index. Group: Enzymes. Synonyms: EC 3.2.1.75; glycoside hydrolase; pustulanase; glucan endo-1,6-β-glucosidase; 6-β-D-glucan glucanohydrolase; endo-1,6-β-glucanase; β-1?6)-β-D-glucanase; β-1,6-glucanase-pustulanase; β-1,6-glucan hydrolase; β-1,6-glucan 6-glucanohydrolase; 1,6-β-D-glucan glucanohydrolase. Enzyme Commission Number: EC 3.2.1.75. CAS No. 37278-39-0. Pustulanase. Source: Proprietary metagenome environmental DNA. Species: Environmental DNA. EC 3.2.1.75; glycoside hydrolase; pustulanase; glucan endo-1,6-β-glucosidase; 6-β-D-glucan glucanohydrolase; endo-1,6-β-glucanase; β-1?6)-β-D-glucanase; β-1,6-glucanase-pustulanase; β-1,6-glucan hydrolase; β-1,6-glucan 6-glucanohydrolase; 1,6-β-D-glucan glucanohydrolase. Cat No: NATE-0645. | |
| Native Equine Butyrylcholinesterase | Butyrylcholinesterase (BChE) is a serine hydrolase that is structurally similar to acetylcholinesterase (AChE), but differs in substRate specificities and inhibitor sensitivities. BChE can, unlike AChE, efficiently hydrolyze larger esters of choline such as butyrylcholine and benzoylcholine. The enzyme is a tetrameric glycoprotein with four equal subunits (110 kDa each). The enzyme is activated by Ca2+ and Mg2+ and the activity is constant over the pH range 6.0-8.0. It is inhibited by Betaine, nicotine, organophosphates, carbamates. This product is prepared from equine serum using ammonium sulfate fractionation and supplied as a lyophilized powder. Applications: Butyrylchol...vestigations into selective inhibitors may provide a clearer picture of the physiological role of bche in both healthy and diseased individuals. this product has been used for the screening of cholineesterase inhibitors in selected fruits and vegetables, for restoring cognitive function and improving memory. it has also been used to develop a butyrylcholinesterase and choline oxidase immobilized bio-sniffer for the detection of nicotine. nicotine inhibits bche activity. a decrease in the byproducts of bche activity reflects the volume of nicotine. Group: Enzymes. Synonyms: Butyrylcholinesterase; BCHE; BuChE; pseudocholinesterase; plasma cholinesterase; EC 3.1.1.8; 9001-08-5; | |
| Native Equine Ferritin | Ferritin is a highly specialized protein whose main function is to store excess iron intracellularly. It is widely distributed throughout the animal and plant kingdoms. In mammalian tissues, ferritin is present in concentrated form in spleen, liver and the intestinal mucosa. Ferritin is not a structurally homogeneous protein since purified preparations, when examined by polyacrylamide gel electrophoresis, show multiple bands. Immunologically, ferritins appear to be species specific but not organ specific. Iron: 30% (bipyridyl method). Group: Others. Purity: Not less than 90% as determined by electrophoresis on 4% polyacrylamide gels. Storage: Store at 4° C; Do not freeze. Form: Saline buffer. Source: Equine Spleen. Species: Equine. Ferritin. Cat No: NATE-1876. | |
| Native Equine γ-Glutamyltranspeptidase | γ-glutamyl transferase is an enzyme that transfers gamma-glutamyl functional groups. It is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker. GGT catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification. Other lines of evidence indicate that GGT can also exert a prooxidant role, with regulatory effects at various levels in cellular signal transduction and cellular pathophysiology. Group: Enzymes. Synonyms: EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; . Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. Activity: 5-12 units/mg solid. Storage: -20°C. Source: Equine kidney. Species: Equine. EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Cat No: NATE-0791. | |
| Native Equine Glutathione S-Transferase | Glutathione S-transferases are a family of proteins that catalyze the conjugation of reduced glutathione with a variety of hydrophobic chemicals containing electrophilic centers. Group: Enzymes. Synonyms: EC 2.5.1.18; glutathione S-transferase; glutathione S-alkyltransferase; glutathione S-aryltransferase; S-(hydroxyalkyl)glutathione lyase; glutathione S-aralkyltransferase; glutathione S-alkyl transferase; GST; 50812-37-8. Enzyme Commission Number: EC 2.5.1.18. CAS No. 50812-37-8. Glutathione S-Transferase. Mole weight: mol wt 45-50 kDa. Activity: > 25 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris and phosphate buffer salts, reduced glutathione and EDTA. Source: Equine liver. Species: Equine. EC 2.5.1.18; glutathione S-transferase; glutathione S-alkyltransferase; glutathione S-aryltransferase; S-(hydroxyalkyl)glutathione lyase; glutathione S-aralkyltransferase; glutathione S-alkyl transferase; GST; 50812-37-8. Cat No: NATE-0325. | |
| Native Equine Spleen Apoferritin | Native apo-ferritin from equine spleen is a native protein shell of ferritin molecule lacking iron. Group: Enzymes. Synonyms: Ferritin, Apo-; Apoferritin; Ferritin; Apo-Ferritin; Apo ferritin. CAS No. 9013-31-4. Purity: 0.95. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Equine Spleen. Species: Equine. Ferritin, Apo-; Apoferritin; Ferritin; Apo-Ferritin; Apo ferritin. Cat No: NATE-1873. | |
| Native Escherichia coli Acetate Kinase | In molecular biology, acetate kinase (EC 2.7.2.1), which is predominantly found in micro-organisms, facilitates the production of acetyl-CoA by phosphorylating acetate in the presence of ATP and a divalent cation. Short-chain fatty acids (SCFAs) play a major role in carbon cycle and can be utilized as a source of carbon and energy by bacteria. The enzyme is important in the process of glycolysis, enzyme levels being increased in the presence of excess glucose. The growth of a bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme is involved in excretion of excess carbohydRate. A related enzyme, butyRate kinase, facili...rom escherichia coli has been used as part of an atp-regenerating system to study the kinetics of agonist-stimulated transphosphatidylatio. Group: Enzymes. Synonyms: Acetate kinase (phosphorylating); Acetic kinase; Acetokinase; AK; EC 2.7.2.1; 9027-42-3; Acetate kinase. Enzyme Commission Number: EC 2.7.2.1. CAS No. 9027-42-3. Acetate kinase. Activity: > 150 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized powder containing trehalose with small amounts of potassium phosphate, magnesium chloride, and dithiothreitol. Source: Escherichia coli. Acetate kinase (phosphorylating); Acetic kinase; Acetokinase; AK; EC 2.7.2.1; 9027-42-3; Acetate kinase. Cat No: NATE-0017. | |
| Native Escherichia coli Alkaline Phosphatase | Alkaline phosphatase (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Applications: Alkaline phosphatase is used for conjugation to antibodies and other proteins for elisa, western blotting, and hist ochemical detection. it may be used for protein labeling when high sensitivity is required. Group: Enzymes. Synonyms: Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Enzyme Commission Number: EC 3.1.3.1. CAS No. 9001-78-9. ALP. Activity: Type I, >30 units per mg protein; Type II, >20 units per mg protein; Type III, >10 units per mg protein. Storage: 2-8°C. Form: A suspension in 2.6M ammonium sulfate, pH 8.0. Source: Escherichia coli. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Cat No: NATE-0056. | |
| Native Escherichia coli Apotryptophanase | Apotryptophanase hydrolizes tryptophan and is capable of catalyzing α,β-elimination reactions with a number of substituted amino acids, including S-methyl-, S-ethyl-and S-benzyl-L-cysteine. DTNB inactivates tryptophanase. Applications: Apotryptophanase is used for the quantitative determination of pyridoxal-phosphate. apotryptophanase, from creative enzymes, has been used to study pregnancy-associated plp deficiency and vitamin b-6 deficiency. Group: Enzymes. Synonyms: L-tryptophanase; L-tryptophan indole-lyase (deaminating); TNase; EC 4.1.99.1; 9024-00-4. Enzyme Commission Number: EC 4.1.99.1. CAS No. 9024-00-4. TNase. Activity: 75-150 units/mg solid. Storage: -20°C. Form: soluble powder. Source: Escherichia coli. L-tryptophanase; L-tryptophan indole-lyase (deaminating); TNase; EC 4.1.99.1; 9024-00-4. Cat No: NATE-0706. | |
| Native Escherichia coli Asparaginase | Asparaginase (EC 3.5.1.1, USAN) or Colaspase (BAN) is an enzyme that catalyzes the hydrolysis of asparagine to aspartic acid. Asparaginases are enzymes expressed and produced by microorganisms. Applications: Asparaginase is used in enzymatic assays and to convert asparagine to aspartic acid. asparaginase is used to reduce the formation of acrylamide in starchy food products. it is also used as a chemotherapy agent for acute lymphoblastic leukemia. product is from escherichia coli and is provided as a lyophilized powder containing sodium chloride. Group: Enzymes. Synonyms: EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Enzyme Commission Number: EC 3.5.1.1. CAS No. 9015-68-3. Asparaginase. Storage: 2-8°C. Form: lyophilized powder. Source: Escherichia coli. EC 3.5.1.1; Asparaginase; Colaspase; L-asparaginase; L-asparagine amidohydrolase. Cat No: PHAM-226. | |
| Native Escherichia coli β-Galactosidase | β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Applications: This enzyme is useful for structural investigation of carbohydrates, the determination of lactose (foodstuff analysis) and as an enzyme label for enzyme immunoassay. Group: Enzymes. Synonyms: β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.23. CAS No. 9031-11-2. β-gal. Mole weight: 540 kDa. Activity: Grade? 500U/mg-solid or more. Stability: Stable at-20°C for at least 6 months. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Escherichia coli. β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. Cat No: DIA-189. | |
| Native Escherichia coli β-Galactosidase-biotin labeled | β-galactosidase is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Applications: Β-galactosidase was used as a control antigen in the selection of human antibody fragments by phage display. Group: Enzymes. Synonyms: β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. β-gal. Activity: 350-1200 units/mg protein. Form: Lyophilized powder containing Tris-acetate, DTT, MgCl2, and isopropyl β-D-thiogalactopyranoside. Source: E. coli. β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase; β-Galactosidase-biotin labeled; biotin β-gal. Cat No: NATE-1585. | |
| Native Escherichia coli β-Glucuronidase | β-glucuronidase catalyzes the breakdown of complex carbohydrates. In humans it converts conjugated bilirubin into the unconjugated form, making bilirubin suitable for reabsorption. Type ix-a, 1,000-5,000 units/mg protein; type vii-a, lyophilized powder, 5,000-20,000 units/mg protein. Applications: Β-glucuronidase is used as a reporter gene in gus assays to monitor gene expression. Group: Enzymes. Synonyms: β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase; EC 3.2.1.31; 9001-45-0; β-D-glucuronoside glucuronosohydrolase; GUSB. Enzyme Commission Number: EC 3.2.1.31. CAS No. 9001-45-0. GUSB. Form: lyophilized powder. Source: Escherichia coli. β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase; EC 3.2.1.31; 9001-45-0; β-D-glucuronoside glucuronosohydrolase; GUSB. Cat No: NATE-0330. | |
| Native Escherichia coli Chloramphenicol Acetyltransferase | Chloramphenicol acetyltransferase (or CAT) is a bacterial enzyme (EC 2.3.1.28) that detoxifies the antibiotic chloramphenicol and is responsible for chloramphenicol resistance in bacteria. This enzyme covalently attaches an acetyl group from acetyl-CoA to chloramphenicol, which prevents chloramphenicol from binding to ribosomes. A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism. Applications: Chloramphenicol acetyltransferase from escherichia coli has been used in a study to assess the construction of a novel expression system in klebsiella pneumoniae and its application for 1,3-propanediol produ...etyl-CoA:chloramphenicol 3-O-acetyltransferase; CAT; 9040-07-7; chloramphenicol acetyltransferase; chloramphenicol acetylase; chloramphenicol transacetylase; CAT I; CAT II; CAT III. CAS No. 9040-7-7. Chloramphenicol Acetyltransferase. Mole weight: mol wt 75 kDa (three identical subunits). Activity: 50,000-150,000 units/mg protein (Lowry). Storage: -20°C. Form: Type I, lyophilized powder. Partially purified; contains Tris buffer salts; Type II, buffered aqueous glycerol solution. Clear, colorless solution in 50% glycerol containing 5 mM Tris-HCl, pH 7.8, and 0.5 mM 2-mercaptoethanol. Source: Escherichia coli. Acetyl-CoA:chloramphenicol 3-O-acetyltransferase; CAT; 9 | |
| Native Escherichia coli Diacylglycerol Kinase | Diacylglycerol kinase (DGK or DAGK) is a family of enzymes that catalyzes the conversion of diacylglycerol (DAG) to phosphatidic acid (PA) utilizing ATP as a source of the phosphate. In non-stimulated cells, DGK activity is low allowing DAG to be used for glycerophospholipid biosynthesis but on receptor activation of the phosphoinositide pathway, DGK activity increases driving the conversion of DAG to PA. As both lipids are thought to function as bioactive lipid signaling molecules with distinct cellular targets, DGK therefore occupies an important position, effectively serving as a switch by terminating the signalling of one lipid while simultaneously activating signa...n of dgka and plsb genes of phospholipid synthesis by multiple stress responses in escherichia coli. diacylglycerol kinase from escherichia coli has also been used in a study to identify an alcohol binding site in the first cysteine-rich domain of protein kinase cdelta. Group: Enzymes. Synonyms: Diacylglycerol Kinase; DGK; DAGK; EC 2.7.1.107; Diacylglycerol kinase (ATP); sn-1,2-Diacylglycerol kinase. Enzyme Commission Number: EC 2.7.1.107. CAS No. 60382-71-0. DAGK. Mole weight: mol wt 13.7 kDa. Stability: -70°C. Form: suspension. Source: E. coli. Diacylglycerol Kinase; DGK; DAGK; EC 2.7.1.107; Diacylglycerol kinase (ATP); sn-1,2-Diacylglycerol kinase. Cat No: NATE-0181. | |
| Native Escherichia coli Glutaminase | Glutaminase catalyzes the conversion of glutamine to glutamate. Glutaminase is an amidohydrolase enzyme that generates glutamate from glutamine. Glutaminase has tissue-specific isoenzymes. Glutaminase has an important role in glial cells. Glutaminase catalyzes the following reaction:Glutamine + H2O ? Glutamate + NH3. Group: Enzymes. Synonyms: EC 3.5.1.2; glutaminase I; L-glutaminase; glutamine aminohydrolase; Glutaminase; 9001-47-2. Enzyme Commission Number: EC 3.5.1.2. CAS No. 9001-47-2. Glutaminase. Activity: Type I, 500-1,500 units/mg protein; Type II, 50-200 units/mg protein. Storage: -20°C. Form: Type I, Lyophilized powder containing stabilizer and potassium succinate; Type II, Lyophilized powder containing potassium succinate and EDTA. Source: Escherichia coli. EC 3.5.1.2; glutaminase I; L-glutaminase; glutamine aminohydrolase; Glutaminase; 9001-47-2. Cat No: NATE-0307. | |
| Native Escherichia coli Glycerokinase | Glycerol kinase is a phosphotransferase enzyme involved in triglycerides and glycerophospholipids synthesis. Glycerol kinase catalyzes tge MgATP-dependent phosphorylation of glycerol to produce sn-glycerol-3-phosphate and is the rate limiting enzyme in the utilization of glycerol. It is also subject to feedback regulation by fructose-1,6-bisphosphate. Applications: Glycerol kinase (glpk) was used to study the effects of pain controlling neuropeptides on human fat cell lipolysis. Group: Enzymes. Synonyms: EC 2.7.1.30; glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase; 9030-66-4. Enzyme Commission Number: EC 2.7.1.30. CAS No. 9030-66-4. GK. Activity: Type I, 50-100 units/mg protein; Type II, 300-600 units/mL. Storage: -20°C. Form: Type I, lyophilized powder, Partially purified lyophilized powder, balance is primarily salts and EDTA; Type II, ammonium sulfate suspension, Suspension in 3.1 M (NH4)2SO4 pH 7.3, with 1% BSA and 2% trehalose. Source: Escherichia coli. EC 2.7.1.30; glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase; 9030-66-4. Cat No: NATE-0288. | |
| Native Escherichia coli L-Arginine Decarboxylase | In enzymology, an arginine decarboxylase (EC 4.1.1.19) is an enzyme that catalyzes the chemical reaction:L-arginine<-> agmatine + CO2. Hence, this enzyme has one substRate, L-arginine, and two products, agmatine and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. It employs one cofactor, pyridoxal phosphate. Group: Enzymes. Synonyms: arginine decarboxylase; EC 4.1.1.19; 9024-77-5; SpeA; L-arginine carboxylyase; L-Arginine Decarboxylase; ADC. Enzyme Commission Number: EC 4.1.1.19. CAS No. 9024-77-5. ADC. Activity: 5-15 units/mg protein. Storage: -20°C. Source: Escherichia coli. arginine decarboxylase; EC 4.1.1.19; 9024-77-5; SpeA; L-arginine carboxylyase; L-Arginine Decarboxylase; ADC. Cat No: NATE-0033. | |
| Native Escherichia coli L-Glutamine Synthetase | Glutamine synthetase (GS) (EC 6.3.1.2) is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine:Glutamate + ATP + NH3 ? Glutamine + ADP + phosphate. Glutamine Synthetase uses ammonia produced by Nitrate reduction, amino acid degradation, and photorespiration. The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites. Applications: L-glutamine synthetase may be used for the purification of proteases from escherichia coli. Group: Enzymes. Synonyms: glutamine synthetase; glutamylhydroxamic synthetase; L-glutamine synthetase; glutamate-ammonia ligase; L-Glutamate:ammonia ligase (ADP-forming); EC 6.3.1.2; GS; 9023-70-5. Enzyme Commission Number: EC 6.3.1.2. CAS No. 9023-70-5. Purity: affinity chromatography. GS. Activity: 400-2,000 units/mg protein. Storage: -20°C. Form: lyophilized powder; Contains potassium phosphate, sodium Citrate and magnesium acetate buffer salts. Source: Escherichia coli. glutamine synthetase; glutamylhydroxamic synthetase; L-glutamine synthetase; glutamate-ammonia ligase; L-Glutamate:ammonia ligase (ADP-forming); EC 6.3.1.2; GS; 9023-70-5. Cat No: NATE-0321. | |
| 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 Escherichia coli Nitrate Reductase (cytochrome) | Nitrate reductase (cytochrome) is an enzyme with system name ferrocytochrome:nitrate oxidoreductase. This enzyme catalises the following chemical reaction:2 ferrocytochrome + 2 H+ + nitrate<-> 2 ferricytochrome + nitrite. Group: Enzymes. Synonyms: Nitrate reductase (cytochrome); respiratory Nitrate reductase; benzyl viologen-Nitrate reductase; EC 1.9.6.1; 9029-42-9. Enzyme Commission Number: EC 1.9.6.1. CAS No. 9029-42-9. Nitrate reductase. Activity: > 5 units/g solid. Storage: -20°C. Form: lyophilized powder. Source: Escherichia coli. Nitrate reductase (cytochrome); respiratory Nitrate reductase; benzyl viologen-Nitrate reductase; EC 1.9.6.1; 9029-42-9. Cat No: NATE-0485. | |
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