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| Product | Description | |
|---|---|---|
| Native Bovine Tautomerase | In enzymology, phenylpyruvate tautomerase or Macrophage migration inhibitory factor (EC 5.3.2.1) is an enzyme that catalyzes the chemical reaction:keto-phenylpyruvate<-> enol-phenylpyruvate. Phenylpyruvate tautomerase has also been found to exhibit the same keto-enol tautomerism for 4-Hydroxyphenylpyruvic acid, which is structurally similar to phenylpyruvate but contains an additional hydroxyl moiety in the para position of the aromatic ring. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting keto-and enol-groups. This enzyme participates in tyrosine metabolism and phenylalanine metabolism. Applications: Tautomerase from bovine kidney has been used in a study to assess tritium isotope effects in the reaction catalyzed by 4-hydroxyphenylpyruvate dioxygenase. tautomerase from bovine kidney has also been used in a study to investigate human macrophage migration inhibitory factor. Group: Enzymes. Synonyms: Tautomerase; phenylpyruvate tautomerase; EC 5.3.2.1; phenylpyruvic keto-. Enzyme Commission Number: EC 5.3.2.1. CAS No. 9023-54-5. Tautomerase. Activity: 1-4 units/mg protein (Lowry), ~10 units/mL. Storage: -20°C. Form: aqueous solution. Source: Bovine kidney. Species: Bovine. Tautomerase; phenylpyruvate tautomerase; EC 5.3.2.1; phenylpyruvic keto-enol isomerase; 9023-54-5. Cat No: NATE-0691. |  |
| Native Bovine Thrombin | Thrombin is a serine protease that in humans is encoded by the F2 gene. Prothrombin (coagulation factor II) is proteolytically cleaved to form thrombin in the coagulation cascade, which ultimately results in the reduction of blood loss. Thrombin in turn acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzing many other coagulation-related reactions. Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects. Applications: Thrombin is used for site specific cleavage of recombinant fusion proteins containing an accessible thrombin recognition site for removal of ...Ia; E thrombin; β-thrombin; γ-thrombin. Enzyme Commission Number: EC 3.4.21.5. CAS No. 9002-4-4. Thrombin. Activity: 600-2,000 NIH units/mg protein (biuret) or > 2,000 NIH units/mg protein (E1%/280 = 19.5); > 125 NIH units/mg protein (biuret). Form: Type I, Lyophilized from saline sodium Citrate buffer, pH 6.5; Type II, buffered aqueous solution, In 0.05 M phosphate buffer, pH 7.0. Source: Bovine plasma. Species: Bovine. thrombin; 9002-04-4; EC 3.4.21.5; fibrinogenase; thrombase; thrombofort; topical; thrombin-C; tropostasin; activated blood-coagulation factor II; blood-coagulation factor IIa; factor IIa; E thrombin; β-thrombin; γ-thrombin. Cat No: NATE-0698. | |
| Native Bovine Thyroglobulin | Thyroglobulin is a glycoprotein consisting of two polypeptide dimers of molecular weight 330,000. Each molecule contains 115 tyrosine residues which are available for iodination. The tyrosine residues in the thyroglobulin molecule is iodinated in the thyroid gland which eventually leads to the synthesis of the thyroid hormones. Group: Others. Synonyms: Thyroglobulin; Bovine thyroglobulin. Purity: Not less than 90% as determined by electrophoresis in 4% polyacrylamide gels. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Bovine Thyroid Gland. Species: Bovine. Thyroglobulin; Bovine thyroglobulin. Cat No: NATE-1882. | |
| Native Bovine Trypsin | Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized. Trypsin consists of a single chain polypeptide of 223 amino acid residues, produced by the remova...te is dependent primarily on the cell type and the age of the culture. trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestions. additional applications include assessing crystallization by membrane-based techniques and in a study to determine that protein folding rates and yields can be limited by the presence of kinetic traps. trypsin can be used to release adherent cells from tissue culture plates for passaging. trypsin has been used in a study to assess the effects of macromolecular crowding on the structural stability of human α-lactalbumin. trypsin has also been use | |
| Native Bovine Trypsin Acetylated | Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized. The trypsin molecule has two domains: one is related to the enzyme active site and the trypt...e bacterial multidrug atp-binding cassette transporter. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin; Acetyltrypsin. Enzyme Commission Number: EC 3.4.21.4. Trypsin. Activity: > 8,500 BAEE units/mg protein (biuret). Storage: -20°C. Source: Bovine pancreas. Species: Bovine. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin; Acetyltrypsin. Cat No: NATE-0720. | |
| Native Bovine Trypsin & Chymotrypsin Mixtures | Native Bovine Trypsin & Chymotrypsin Mixtures. Creative enzymes is a world leading producer of trypsin / chymotrypsin mixtures. trypsin and chymotrypsin are extracted from bovine pancreas and pancreatic juices using multiple precipitation, fractionation, and filtration steps. creative enzymes products are not intended for use in pharmaceutical applications. Applications: In combination with chymotrypsinogen and ribonuclease it is used to formulate anti-inflammatory tablets /treatment of wounds (internal and external) / mixtures of trypsin and chymotrypsin in different ratios frequently are used in digestive aids and food. Group: Enzymes. Synonyms: Trypsin & Chymotrypsin. Trypsin-Chymotrypsin. Activity: >1000 :1000 NF U/mg. Storage: Store at <-15°C. Source: Bovine pancreas. Species: Bovine. Trypsin & Chymotrypsin. Cat No: NATE-0719. | |
| Native Bovine Xanthine Oxidase | Xanthine oxidase is a molybdenum-containing enzyme that is found in the cytosol, and may be strongly inhibited by flavonoids. It plays a vital role in the metabolism of some drugs, as well as purines and pyrimidines. It is also known to be a biological source of reactive oxygen species. Xanthine oxidase was shown to be involved in the reduction of cytochrome c by the generation of superoxide anions following the oxidation of xanthine. These free radicals are responsible for reducing cytochrome c. Formerly e.c. 1.1.3.22. Group: Enzymes. Synonyms: Xanthine oxidase; XO; xanthine oxidoreductase; EC 1.17.3.2; 9002-17-9; XOD; Xanthine:oxygen oxidoreductase; hypoxanthine oxidase; hyp...in. Storage: 2-8°C. Form: Type I, Type II, ammonium sulfate suspension; Suspension in 2.3 M (NH4)2SO4 containing 1 mM sodium salicylate; Type III, ammonium sulfate suspension, Suspension in 2.3 M (NH4)2SO4, 10 mM sodium phosphate buffer, pH 7.8, containing 1 mM EDTA and 1 mM sodium salicylate; Type IV, lyophilized powder, Contains 0.5% sodium salicylate. Source: Bovine milk. Species: Bovine. Xanthine oxidase; XO; xanthine oxidoreductase; EC 1.17.3.2; 9002-17-9; XOD; Xanthine:oxygen oxidoreductase; hypoxanthine oxidase; hypoxanthine:oxygen oxidoreductase; Schardinger enzyme; hypoxanthine-xanthine oxidase; xanthine:O2 oxidoreductase; xanthine:xanthine oxidase. Cat No: NATE-0732. | |
| Native Brewer's bottom yeast Orotidine-5'-monophosphate pyrophosphorylase | Orotate phosphoribosyltransferase (OPRTase) or Orotic acid phosphoribosyltransferase is an enzyme involved in pyrimidine biosynthesis. It catalyzes the formation of orotidine 5'-monophosphate (OMP) from orotate and phosphoribosyl pyrophosphate. In yeast and bacteria, orotate phosphoribosyltransferase is an independent enzyme with a unique gene coding for the protein, whereas in mammals and other multicellular organisms, the catalytic function is carried out by a domain of the bifunctional enzyme UMP synthase. Applications: This is the preferred enzyme for assaying orotidine 5?-monophosphate and for the production of omp analogs from the corresponding orot...ty: ~25 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: Lyophilized powder containing approx. 50% buffer salts. Source: Brewer's bottom yeast. orotidylic acid phosphorylase; orotidine-5'-phosphate pyrophosphorylase; OPRTase; orotate phosphoribosyl pyrophosphate transferase; orotic acid phosphoribosyltransferase; orotidine 5'-monophosphate pyrophosphorylase; orotidine monophosphate pyrophosphorylase; orotidine phosphoribosyltransferase; orotidylate phosphoribosyltransferase; orotidylate pyrophosphorylase; orotidylic acid pyrophosphorylase; orotidylic phosphorylase; orotidylic pyrophosphorylase; EC 2.4.2.10; 9030-25-5. Cat No: NATE-0498. | |
| Native Burkholderia sp. Lipoprotein Lipase | Lipoprotein lipase (LPL) (EC 3.1.1.34) is a member of the lipase gene family, which includes pancreatic lipase, hepatic lipase, and endothelial lipase. It is a water-soluble enzyme that hydrolyzes triglycerides in lipoproteins, such as those found in chylomicrons and very low-density lipoproteins (VLDL), into two free fatty acids and one monoacylglycerol molecule. It is also involved in promoting the cellular uptake of chylomicron remnants, cholesterol-rich lipoproteins, and free fatty acids. LPL requires ApoC-II as a cofactor. LPL is attached to the luminal surface of endothelial cells in capillaries by the protein glycosylphosphatidylinositol HDL-binding protein 1 (GPI...rin in rats. Group: Enzymes. Synonyms: lipoprotein lipase; clearing factor lipase; diglyceride lipase; diacylglycerol lipase; postheparin esterase; diglyceride lipase; postheparin lipase; diacylglycerol hydrolase; lipemia-clearing factor; EC 3.1.1.34; 9004-02-8; LPL. Enzyme Commission Number: EC 3.1.1.34. CAS No. 9004-2-8. LPL. Activity: > 50,000 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Burkholderia sp. lipoprotein lipase; clearing factor lipase; diglyceride lipase; diacylglycerol lipase; postheparin esterase; diglyceride lipase; postheparin lipase; diacylglycerol hydrolase; lipemia-clearing factor; EC 3.1.1.34; 9004-02-8; LPL. Cat No: NATE-0417. | |
| Native Cabbage Phospholipase D | Phospholipase D is a phospholipid hydrolyzing enzyme and an important component of receptor-mediated signal transduction responses and regulated secretion. Hydrolyzes the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid. Phospholipase D is involved in conferring drought susceptibility in peanuts, which increases the risk of aflatoxin contamination. Applications: Phospholipase d (pld) is used to hydrolyze the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid. it has also been used to study metabolic labeling and direct imaging of choline phospholipids in vivo by measuring propargyl-cho incorporation. furthermore, pld is used in purification and kinetic studies. the enzyme has been used for the preparation of bodipy-phosphatidylcholine during the preparation of fluorescently labelled lipids. Group: Enzymes. Synonyms: Phospholipase D; EC 3.1.4.4; lipophosphodiesterase II; lecithinase D; choline phosphatase; PLD; 9001-87-0. Enzyme Commission Number: EC 3.1.4.4. CAS No. 9001-87-0. PLD. Activity: > 100 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Cabbage. Phospholipase D; EC 3.1.4.4; lipophosphodiesterase II; lecithinase D; choline phosphatase; PLD; 9001-87-0. Cat No: NATE-0595. | |
| Native Caldariomyces fumago Chloroperoxidase | Chloroperoxidase (CPO) is a 42 kDa Da extracellular heme glycoenzyme containing ferriprotoporphyrin IX as the prosthetic group. CPO is secreted from fungus and exhibits a broad spectrum of chemical reactivities. It is a peroxide-dependent chlorinating enzyme. It also catalyzes peroxidase-, catalase-and cytochrome P450-type reactions of dehydrogenation, H2O2 decomposition and oxygen insertion, respectively. The enzyme has magnetic and spectroscopic properties similar to that of cyctochrome P-450. CPO from the fungus Caldariomyces fumago has the capacity to chlorinate aromatic hydrocarbons, including polycyclic aromatic hydrocarbons (PAHs). Applications: A useful alternative to lactoperoxidase for 131i ion labeling studies, for bromination of proteins, and for cl labeling of macromolecules in long-term isolation procedures. Group: Enzymes. Synonyms: Chloroperoxidase; CPO; Vanadium halopero. Enzyme Commission Number: EC 1.11.1.10. CAS No. 9055-20-3. CPO. Activity: 1,000-2,000 units/mg protein (E1%/280); > 3,000 units/mL; >10,000 U/mL. Storage: 2-8°C. Form: buffered aqueous suspension. Purified suspension in 0.1 M sodium phosphate solution, pH approx. 4.5. Source: Caldariomyces fumago. Chloroperoxidase; CPO; Vanadium haloperoxidase; EC 1.11.1.10; 9055-20-3; Chloride Peroxidase; Chloride:hydrogen-peroxide oxidoreductase. Cat No: NATE-0156. | |
| Native Calf Adenosine Deaminase | Adenosine deaminase is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system. Group: Enzymes. Synonyms: ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Enzyme Commission Number: EC 3.5.4.4. CAS No. 9026-93-1. ADA. Mole weight: 33 kDa (SDS-PAGE). Activity: 150~200U/mg protein. Storage: Storage: Temperature 2-8 centigrade. Source: Calf Spleen. Species: Calf. ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Cat No: DIA-271. | |
| Native Calf 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. 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. Activity: > 2,000 units/mg protein. Storage: 2-8°C. Form: Freeze dried powder. Source: Calf intestine. Species: Calf. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Cat No: NATE-0054. | |
| Native Calf Enterokinase | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Applications: Enterokinase is used for the cleavage of fusion proteins at definite cleavage sites. for the processing of recombinant proteins, the desired protein is fused with enterokinase recognition sequence. after purification of the entire fusion protein, the protein or peptide is released by incubation with enterokinase. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; restriction protease enterokinase. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 150 kDa. Storage: Store at 2-8°C. Form: Lyophilized. Source: Calf intestine. Species: Calf. enterokinase; enteropeptidase; EC 3.4.21.9; restriction protease enterokinase. Cat No: NATE-0872. | |
| Native Calf Rennin | Rennin, a 323 amino acid chain, is secreted as an inactive precursor which is then converted into an active enzyme through limited proteolysis. It cleaves the peptide bond between phenylalanine and methionine in K-Casein. Applications: Rennin, also known as chymosin, is a milkclotting acid proteinase produced in the stomach of a calf. it is used in cheesemaking and to study neonatal gastric digestion. Group: Enzymes. Synonyms: chymosin; rennin; EC 3.4.23.4; 9001-98-3. Enzyme Commission Number: EC 3.4.23.4. CAS No. 9001-98-3. Rennin. Activity: > 20 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing sodium chloride. Source: Calf stomach. Species: Calf. chymosin; rennin; EC 3.4.23.4; 9001-98-3. Cat No: NATE-0651. | |
| Native Calf Terminal Transferase | Bovine terminal transferase (TdT) is a primer-dependent polymerase that catalyzes the addition of deoxynucleotides to the 3'-OH terminus of DNA molecules with the release of inorganic phosphate. TdT reacts preferentially with either single-stranded DNA molecules or double-stranded-DNA with 3' overhangs, but procedures have been developed to label blunt ends or 3'-recessive ends. In a reaction mixture, the divalent ion (Co2+, Mn2+, Mg2+) will influence purine and pyrimidine polymerization rate. Activities of TdT are also affected by the bases (dATP, dCTP, dGTP and dTTP) present. Bovine terminal transferase (tdt) is a primer-dependent polymerase that catalyzes the addition of d...ed dna with non-radioactive or radioactive labels o carrying out in vitro mutagenesis by adding single nucleotides to dna o use in tunel assays. Group: Enzymes. Synonyms: DNA nucleotidylexotransferase; terminal deoxyribonucleotidyltransferase; terminal addition enzyme; addase; deoxynucleotidyl terminal transferase; deoxyribonucleic acid nucleotidyltransferase; deoxyribonucleic nucleotidyltransferase; terminal deoxynucleotide transferase; TdT; EC 2.7.7.31; 9027-67-2. Enzyme Commission Number: EC 2.7.7.31. CAS No. 9027-67-2. TdT. Mole weight: mol wt 60 kDa. Storage: -20°C. Form: buffered aqueous glycerol solution. Source: Calf thymus. Species: Calf. DNA nucleotidylexotransferas | |
| Native Canavalia ensiformis β-N-Acetylglucosaminidase | This enzyme, sometimes called β-N-acetylhexosaminidase, is reported to liberate terminal β-linked N-acetylglucosamine and N-acetylgalactosamine from a variety of substrates. The activity of β-N-actylglucosaminidase may be determined with the chromogenic substrate p-nitrophenyl-N-acetyl-β-D-glucosaminide. β-N-actylglucosaminidase hydrolyzes the terminal nonreducing N-acetyl-D-hexosamine residues. This enzyme contains two predominant isozymes, Hex A, a heterodimer, and Hex B, a homodimer. N-acetylglucosamine, acetamide, N-2-acetamido-2-deoyglucosylamine, N-acetylnojirimycin, and N-acetyldeoxynojirmycin are known inhibitors. At ph 4.0, p-nit...ta;-acetylaminodeoxyhexosidase; N-acetyl-β-D-hexosaminidase; N-acetyl-beta-hexosaminidase; β-hexosaminidase; β-acetylhexosaminidinase; β-D-N-acetylhexosaminidase; β-N-acetyl-D-hexosaminidase; β-N-acetylglucosaminidase; hexosaminidase A; N-acetylhexosaminidase; β-D-hexosaminidase; EC 3.2.1.52; 9012-33-3. Enzyme Commission Number: EC 3.2.1.52. CAS No. 9012-33-3. β-N-Acetylhexosaminidase. Activity: > 15 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 2.5 M (NH4)2SO4, pH 7.0. Source: Canavalia ensiformis. hexosaminidase; β-acetylaminodeoxyhexosidase; N-acetyl-β-D-hexosaminidase; N-ac | |
| Native Canavalia ensiformis (Jack bean) α-Mannosidase | α-Mannosidase is an acid hydrolase which is located in plant vacuoles and is thought to be involved with the turnover of N-linked glycoproteins. α-Mannosidase has been shown to inhibit the proliferation of B-lymphocytes. α-Mannosidase from Canavalia ensiformis is a tretamer composed of two subunits that each contain two components at 44 and 66 kDa. Applications: Liberates mannose from a variety of synthetic and natural α-mannosides. α-mannosidase can be used to liberate mannose from a variety of synthetic and natural α-mannosides. it has also been used in a study to investigate the causes of neurodegeneration in mucolipidosis ii ?knock-in? mice. Group: Enzymes. Synonyms: α-mannosidase; α-D-mannosidase; p-nitrophenyl-α-mannosidase; α-D-mannopyranosidase; 1,2-&a. Enzyme Commission Number: EC 3.2.1.24. CAS No. 9025-42-7. Mannosidase. Activity: > 15 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.0 M (NH4)2SO4 and 0.1 mM zinc acetate, pH 7.5. Source: Canavalia ensiformis (Jack bean). α-mannosidase; α-D-mannosidase; p-nitrophenyl-α-mannosidase; α-D-mannopyranosidase; 1,2-α-mannosidase; 1,2-α-D-mannosidase; exo-α-mannosidase; EC 3.2.1.24; 9025-42-7; Mannosidase. Cat No: NATE-0754. | |
| Native Candida boidinii Formate Dehydrogenase | Formate dehydrogenase is involved in the stress response of plants and catalyzes the reduction of NAD+ to NADH. Fdh is an abundant enzyme from yeast candida boidinii (cbfdh) that plays an important role in the energy supply of methylotrophic microorganisms and in the stress response of plants. Applications: Formate dehydrogenase (fdh) is used for diagnostics in large scale industrial pr ocesses. its used in the production of an unnatural amino acid, tert-l-leucine, a component of some hiv protease and matrix metalloprotease inhibitors. Group: Enzymes. Synonyms: EC 1.2.1.2; 9028-85-7; formate-NAD oxidoreductase; FDH; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate. Enzyme Commission Number: EC 1.2.1.2. CAS No. 9028-85-7. FDH. Activity: Type I, 5.0-15.0 units/mg protein; Type II, 0.3-0.6 units/mg; Type III, ~50 U/mL. Storage: -20°C. Form: Type I, lyophilized powder; Type II, powder; Type III, clear brown liquid. Source: Candida boidinii. EC 1.2.1.2; 9028-85-7; formate-NAD oxidoreductase; FDH; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Cat No: NATE-0254. | |
| Native Candida cylindracea Cholesterol Esterase | Cholesterol esterase (CE) is a reversible enzyme that can hydrolyze or synthesize fatty acid esters of cholesterol and other sterols. Hydrolysis of water insoluble long chain fatty acid esters requires bile salt activation. Hydrolysis of water soluble esters of short chain fatty acids and lysophospholipids does not require activation by bile salts. It also hydrolyzes tri-, di-, and mono-acylglycerols, phospholipids, lysophospholipids, and ceramide. This monomeric glycoprotein may have multiple functions in lipid and lipoprotein metabolism, as well as in atherosclerosis. Hydrolase that splits fatty acids from sterols. rely on the proven diagnostic quality of this product. Applications: Use cholesterol esterase in diagnostic tests for the determination of cholesterol in combination with cholesterol oxidase. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester s. Cholesterol Esterase. Activity: >10.5 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: Almost white lyophilizate. Source: Candida cylindracea. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; 9026-00-0; sterol esterase; CE. Cat No: NATE-0984. | |
| Native Candida Rugosa Cholesterol Esterase | Cholesterol esterase (CE) is also known as cholesterol ester hydrolase. This enzyme catalyzes the following reaction: Sterol Ester --------> Sterol + Fatty Acid.Cholesterol esterase activity has been demonstrated in pancreas, intestine, liver and kidney. The enzyme is inactivated by proteolytic enzymes but stabilized by proteolytic enzyme inhibitors and by bile salts. CE from rat pancreas has a molecular weight of 65,000-69,000. In the presence of bile salts, it aggregates to a hexamer which is possibly the active form of the enzyme. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; sterol esterase; CE. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Purity: 0.9. Cholesterol Esterase. Activity: 25-100 U/mg. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Candida Rugosa. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; sterol esterase; CE. Cat No: NATE-1679. | |
| Native Candida rugosa Lipase | Candida rugosa lipase is known to catalyze hydrolysis reactions, especially the production of ricinoleic acid. Group: Enzymes. Synonyms: EC 3.1.1.3; lipase; triglyceride lipase; tributyrase; butyrinase; glycerol ester hydrolase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969-4-9; Meito MY 30; Tweenesterase; GA 56; capalase L; triglyceride hydrolase; triolein hydrolase;. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Mole weight: Mr ~67 kDa. Activity: > 2 U/mg. Storage: 2-8°C. Form: powder, yellow-brown. Source: Candida rugosa. EC 3.1.1.3; lipase; triglyceride lipase; tributyrase; butyrinase; glycerol ester hydrolase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969-4-9; Meito MY 30; Tweenesterase; GA 56; capalase L; triglyceride hydrolase; triolein hydrolase; tween-hydrolyzing esterase; amano CE; cacordase; triglyceridase; triacylglycerol ester hydrolase; amano P; amano AP; PPL; glycerol-ester hydrolase; GEH; meito Sangyo OF lipase; hepatic lipase; lipazin; post-heparin plasma protamine-resistant lipase; salt-resistant post-heparin lipase; heparin releasable hepatic lipase; amano CES; amano B; tributyrase; triglyceride lipase; liver lipase; hepatic monoacylglycerol acyltransferase; 9001-62-1. Cat No: NATE-0399. | |
| Native Candida sp. Alcohol oxidase | In enzymology, an alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the chemical reaction a primary alcohol + O2 <-> an aldehyde + H2O2. Thus, the two substrates of this enzyme are primary alcohol and O2, whereas its two products are aldehyde and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. Native alcohol oxidase (ec 1.1.3.13) was purified from candida sp. Applications: Useful for enzymatic determination of blood alcohol. Group: Enzymes. Synonyms: ethanol oxidase; alcohol oxidase; EC 1.1.3.13; Methanol oxidase; 9073-63-6. Enzyme Commission Number: EC 1.1.3.13. CAS No. 9073-63-6. Alcohol Oxidase. Activity: 7~20 U/mg. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Light yellow powder. Source: Candida sp. ethanol oxidase; alcohol oxidase; EC 1.1.3.13; Methanol oxidase; 9073-63-6. Cat No: DIA-123. | |
| Native Candida sp. Invertase | Invertase is an enzyme that catalyzes the hydrolysis (breakdown) of sucrose (table sugar). The resulting mixture of fructose and glucose is called inverted sugar syrup. Related to invertases are sucrases. Invertases and sucrases hydrolyze sucrose to give the same mixture of glucose and fructose. Invertases cleave the O-C(fructose) bond, whereas the sucrases cleave the O-C(glucose) bond. Applications: This enzyme is useful for enzymatic determination of saccharose and for the structure investigation of carbohydrates containing ss-d-fructofuranoside residue. Group: Enzymes. Synonyms: EC 3.2.1.26; saccharase; glucosucrase; beta-h-fructosidase; beta-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase; beta-fructofuranosidase. Enzyme Commission Number: EC 3.2.1.26. CAS No. 9001-57-4. Invertase. Mole weight: approx. 260 kDa. Activity: Grade? 100U/mg-solid or more (containing approx. 70% of stabilizer). Stability: Stable at-20°C for at least one year. Appearance: White amorphous powder, lyophilized. Source: Candida sp. EC 3.2.1.26; saccharase; glucosucrase; beta-h-fructosidase; beta-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase; beta-fructofuranosidase. Cat No: DIA-205. | |
| Native Candida sp. Uricase | The enzyme urate oxidase (UO), or uricase or factor-independent urate hydroxylase, absent in humans, catalyzes the oxidation of uric acid to 5-hydroxyisourate: Uric acid + O2 + H2O ? 5-hydroxyisourate + H2O2 ? allantoin + CO2. Applications: This enzyme is useful for enzymatic determination of uric acid in clinical analysis. Group: Enzymes. Synonyms: urate oxidase; uric acid oxidase; uricase; uricase; urate: oxygen oxidoreductase; EC 1.7.3.3; uricase II. Enzyme Commission Number: EC 1.7.3.3. CAS No. 9002-12-4. UO. Mole weight: approx. 120 kDa. Activity: Grade? 4.0U/mg-solid or more (containing approx.20% of stabilizers). Stability: Stable at-20°C for at least one year. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Candida sp. urate oxidase; uric acid oxidase; uricase; uricase; urate: oxygen oxidoreductase; EC 1.7.3.3; uricase II. Cat No: DIA-175. | |
| Native Candida utilis Invertase | Invertase is an enzyme that catalyzes the hydrolysis (breakdown) of sucrose (table sugar). The resulting mixture of fructose and glucose is called inverted sugar syrup. Related to invertases are sucrases. Invertases and sucrases hydrolyze sucrose to give the same mixture of glucose and fructose. Invertases cleave the O-C (fructose) bond, whereas the sucrases cleave the O-C (glucose) bond. Typically used in manufacturing confectionaries, dietary supplements, and other food grade applications. Applications: This enzyme is useful for enzymatic determination of saccharose and for the structure investigation of carbohydrates containing β-d-fructofuranoside residue. Group: Enzymes. Synonyms: EC 3.2.1.26; invertase; saccharase; glucosucrase; β-h-fructosidase; β-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase; β-fructofuranosida. Enzyme Commission Number: EC 3.2.1.26. CAS No. 9001-57-4. Invertase. Mole weight: mol wt ~260 kDa. Activity: > 300 units/mg solid. Storage: -20°C. Source: Candida utilis. EC 3.2.1.26; invertase; saccharase; glucosucrase; β-h-fructosidase; β-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase; β-fructofuranosidase; β-D-fructofuranoside fructohydrolase; 9001-57-4. Cat No: NATE-0358. | |
| Native Candida utilis L-Glutamic Dehydrogenase (NADP) | L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate. Group: Enzymes. Synonyms: L-Glutamic Dehydrogenase; EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD (P)-glutamate dehydrogenase; NAD (P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP). Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. Activity: 50-200 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salt. Source: Candida utilis. L-Glutamic Dehydrogenase; EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD (P)-glutamate dehydrogenase; NAD (P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP). Cat No: NATE-0394. | |
| 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 Cellulomonas sp. 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. Phosphoryl moiety of atp to one of the primary hydroxyl group of glycerol, forming sn-glycerol-3-p. the enzyme has the highest specificity for glycerol, and also phosphorylates dihydroxyacetone and glyceraldehyde (table 1,2). mg++ is essentially required for the reaction. Applications: This enzyme is useful for enzymatic dete...1) and lactate dehydrogenase (lcd-209, lcd-211), lipoprotein lipase (lpl-311, lpl-314) in clinical analysis. 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. Mole weight: mol wt ~128 kDa ((by gel filtration). Activity: 25-75 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing phosphate buffer salts and sodium gluconate. Source: Cellulomonas sp. EC 2.7.1.30; glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase; 9030-66-4. Cat No: NATE-0287. | |
| Native Cellulomonas sp. 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: This enzyme is useful for enzymatic determination of glycerol and of triglyceride when coupled with lipoprotein lipase in clinical analysis. formation of nadh from the reaction of glycerol and nad+ was catalyzed by the enzyme glycerol dehydrogenase. 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. Mole weight: mol wt ~390 kDa. Activity: 50-125 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing bovine serum albumin. Source: Cellulomonas sp. EC 1.1.1.6; NAD+-linked glycerol dehydrogenase; glycerol:NAD+ 2-oxidoreductase; GDH; GlDH; GlyDH; 9028-14-2; glycerin dehydrogenase. Cat No: NATE-0283. | |
| Native Chaetomium erraticum Dextranase | An endodextranase that hydrolyzes-(1,6)-glucosidic linkages in dextran. Dextrans are undesirable compounds synthesized from sucrose by microbial contaminants during sugar production that increase viscosity of the flow and decrease industrial recovery. Dextranase has been used for hydrolyzing dextran at sugar mills in order to improve efficiency of sugar production. A fungal dextranase produced by submerged fermentation of chaetomium erraticum. stable in the ph range of 3-7 and at temperatures up to approx. 70 oc. for most applications, the preferred conditions are ph 5-6 and a temperature of 50-60°c. Applications: Dextranase from chaetomium erraticum has been used in a study to investigate the optimization of process conditions for enzymatic modification of alternan. dextranase from chaetomium erraticum has also been used in a study to investigate the immobilization of dextranase from chaetomium erraticum. Group: Enzymes. Synonyms: EC 3.2.1.11, dextran hydrolase; endodextranase; dextranase DL 2; DL 2; . Enzyme Commission Number: EC 3.2.1.11. CAS No. 9025-70-1. Dextranase. Storage: 2-8°C. Form: solution. Source: Chaetomium erraticum. EC 3.2.1.11, dextran hydrolase; endodextranase; dextranase DL 2; DL 2; endo-dextranase; α-D-1,6-glucan-6-glucanohydrolase; 1,6-α-D-glucan 6-glucanohydrolase; 9025-70-1; Dextranase. Cat No: NATE-0182. | |
| Native Chaetomium gracile Dextranase | An endodextranase that hydrolyzes-(1,6)-glucosidic linkages in dextran. Dextrans are undesirable compounds synthesized from sucrose by microbial contaminants during sugar production that increase viscosity of the flow and decrease industrial recovery. Dextranase has been used for hydrolyzing dextran at sugar mills in order to improve efficiency of sugar production. Group: Enzymes. Synonyms: EC 3.2.1.11, dextran hydrolase; endodextranase; dextranase DL 2; DL 2; endo-dextranase; α-D-1,6-glucan-6-glucanohydrolase; 1,6-α-D-glucan 6-glucanohydrolase; Dextranase. Enzyme Commission Number: EC 3.2.1.11. CAS No. 9025-70-1. Dextranase. Form: Liquid. Source: Chaetomium gracile. EC 3.2.1.11, dextran hydrolase; endodextranase; dextranase DL 2; DL 2; endo-dextranase; α-D-1,6-glucan-6-glucanohydrolase; 1,6-α-D-glucan 6-glucanohydrolase; Dextranase. Cat No: NATE-0873. | |
| Native Chicken 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. It was from chicken intestine partially purified. a dried powder. used in the nf/usp dexamethasone phosphate assay. 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. Purity: Partially purified. ALP. Mole weight: 140 kDa. Activity: > 0.9 units per mg dry weight (25°C pH 8.8. Stability: The lyophilized preparation is stable for 1-2 years at 2-8°C. Storage: Store at 2-8°C. Form: dried powder. Source: Chicken Intestine. Species: Chicken. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Cat No: NATE-0055. | |
| Native Chicken α-N-Acetylgalactosaminidase | α-N-acetylgalactosaminidase (EC 3.2.1.49) is a glycoside hydrolase from bacteria and animals, also known as nagalase. The human gene that codes for this enzyme is NAGA. Mutations in this gene and the deficiency in alpha-N-acetylgalactosaminidase activity have been identified as the cause of Schindler disease. Group: Enzymes. Synonyms: EC 3.2.1.49; 9075-63-2; α-N-acetylgalactosaminidase; Alpha-N-acetylgalactosaminidase; α-acetylgalactosaminidase; N-acetyl-α-D-galactosaminidase; N-acetyl-α-galactosaminidase; α-NAGAL; α-NAGA; α-GalNAcase. Enzyme Commission Number: EC 3.2.1.49. CAS No. 9075-63-2. α-NAGA. Source: Chicken Liver. Species: Chicken. EC 3.2.1.49; 9075-63-2; α-N-acetylgalactosaminidase; Alpha-N-acetylgalactosaminidase; α-acetylgalactosaminidase; N-acetyl-α-D-galactosaminidase; N-acetyl-α-galactosaminidase; α-NAGAL; α-NAGA; α-GalNAcase. Cat No: NATE-0755. | |
| Native Chicken Collagen Type II | Triplehelical domain of chicken sternum collagen type II. Gnd-HCl extraction, pepsin digestion, saltprecipitation, ion excange chromatography, gelfiltration. Group: Others. Synonyms: Chicken Collagen Type II; Collagen Type II; Type II collagen; collagen. Appearance: White or off white powder. Storage: Stored at room temperature and keep it clean, dry, ventilated warehouse, sun and moisture proof. Source: Chicken sternum. Species: Chicken. Chicken Collagen Type II; Collagen Type II; Type II collagen; collagen. Cat No: NATE-1165. | |
| Native Chicken 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; glyceraldehyde phos. Enzyme Commission Number: EC 1.2.1.12. CAS No. 9001-50-7. Glyceraldehyde-3-phosphate Dehydrogenase. Activity: > 40 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Citrate buffer salts. Source: Chicken muscle. Species: Chicken. 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-0279. | |
| Native Chicken L-Lactic Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 2-8°C. Form: ammonium sulfate suspension; Crystalline suspension in 1.3 M (NH4)2SO4, pH 6.0. Source: Chicken heart. Species: Chicken. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0411. | |
| Native Chicken Lysozyme chloride form | Lysozymes, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycoside hydrolases. These are enzymes (EC 3.2.1.17) that damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Lysozyme is abundant in a number of secretions, such as tears, saliva, human milk, and mucus. It is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in sequence ...lmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme; lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2. Enzyme Commission Number: EC 3.2.1.17. CAS No. 9001-63-2. Lysozyme. Mole weight: mol wt ~14.3 kDa. Activity: > 100,000 units/mg protein (E1%/280). Storage: -20°C. Form: Lyophilized powder containing sodium chloride and sodium acetate. Source: Chicken egg white. Species: Chicken. muramidase; globulin G; mucopeptide glucohydrolase; globulin G1; N,O-diacetylmuramidase; lysozyme g; L-7001; 1,4-N-acetylmuramidase; mucopeptide N-acetylmuramoylhydrolase; PR1-lysozyme; lysozyme; LYZ; LZM; EC 3.2.1.17; 9001-63-2. Cat No: NATE-0432. | |
| Native Chicken Malic Dehydrogenase (oxalacetate-decarboxylating) | Malic dehydrogenase (MDH) exists as two isoforms within eukaryotic cells, one that is expressed in the mitochondria and functions in the TCA cycle and one in the cytoplasm that converts malate from the mitochondria back into oxaloacetate. Malic dehydrogenase (mdh) exists as two isoforms within eukaryotic cells, one that is expressed in the mit ochondria and functions in the tca cycle and one in the cytoplasm that converts malate from the mit ochondria back into oxaloacetate. Applications: Malic dehydrogenase has been used in a study to assess the dietary manganese requirement of juvenile yellow catfish (pelteobagrus fulvidraco) and effects on whole body minera...ctivity: 10-30 units/mg protein (modified Warburg-Christian). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 2.9 M (NH4)2SO4 solution containing 10 mM potassium phosphate, 0.5 mM 2-mercaptoethanol, 10 mM manganese chloride, and 3 mM Na4EDTA, pH 6.0. Source: Chicken liver. Species: Chicken. malic enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); malate dehydrogenase (decarboxylating, NADP+); NADP+-linked decarboxylating malic enzyme; NADP+-malic enzyme; NADP+-specific malic enzyme; NADP-specific malate dehydrogenase; malate dehydrogenase (NADP+, decarboxylating); L-malate:NADP+oxidoreductase; EC 1.1.1.40; 9028-47-1. Cat No: NATE-0446. | |
| Native Chicken Myokinase | Adenylate kinase (EC 2.7.4.3) (also known as ADK or myokinase) is a phosphotransferase enzyme that catalyzes the interconversion of adenine nucleotides, and plays an important role in cellular energy homeostasis. Mutational analysis of the amino acid proline 17 of myokinase from chicken muscle is critical for structural stability, substrate binding and enzyme activity. Applications: Myokinase from chicken muscle has been used in a study to assess the release of enzymes via acute myositis and neurogenic atrophy in muscles. it has also been used in a study to investigate the development of sarcoplasmic reticulum membranes in chicken pectoralis muscle cells. Group: Enzymes. Synonyms: Adenylate kinase; EC 2.7.4.3; ADK; myokinase; 9013-02-9; Adenylic kinase; Adenylokinase. Enzyme Commission Number: EC 2.7.4.3. CAS No. 9013-2-9. Myokinase. Activity: 1,500-3 ,000 units/mg protein (biuret). Storage: -20°C. Form: essentially salt-free, lyophilized powder. Source: Chicken muscle. Species: Chicken. Adenylate kinase; EC 2.7.4.3; ADK; myokinase; 9013-02-9; Adenylic kinase; Adenylokinase. Cat No: NATE-0037. | |
| Native Chicken Phosphoglucomutase | Phosphoglucomutase (EC 5.4.2.2) is an enzyme that transfers a phosphate group on an α-D-glucose monomer from the 1' to the 6' position in the forward direction or the 6' to the 1' position in the reverse direction. More precisely, it facilitates the interconversion of glucose 1-phosphate and glucose 6-phosphate. Group: Enzymes. Synonyms: EC 5.4.2.2; PGM; phosphoglucomutase; α-D-Glucose-1,6-bisphosphatase, α-D-Glucose-1-phosphate phosphotransferase, Phosphoglucomutase-1, PGM-1, PGM 1, Glucose phosphomutase 1; Glucose phosphomutase; Phosphoglucose mutase. Enzyme Commission Number: EC 5.4.2.2. CAS No. 9001-81-4. Phosphoglucomutase. Activity: > 10 Units / mg. Storage: Below -20°C. Form: Frozen Liquid. Source: Chicken Muscle. Species: Chicken. EC 5.4.2.2; PGM; phosphoglucomutase; α-D-Glucose-1,6-bisphosphatase, α-D-Glucose-1-phosphate phosphotransferase, Phosphoglucomutase-1, PGM-1, PGM 1, Glucose phosphomutase 1; Glucose phosphomutase; Phosphoglucose mutase. Cat No: NATE-1032. | |
| Native Chicken Sulfite Oxidase | Sulfite oxidase (EC 1.8.3.1) is an enzyme in the mitochondria of all eukaryotes.[citation needed] It oxidizes sulfite to sulfate and, via cytochrome c, transfers the electrons produced to the electron transport chain, allowing generation of ATP in oxidative phosphorylation. This is the last step in the metabolism of sulfur-containing compounds and the sulfate is excreted. Sulfite oxidase is a metallo-enzyme that utilizes a molybdopterin cofactor and a heme group. It is one of the cytochromes b5 and belongs to the enzyme super-family of molybdenum oxotransferases that also includes DMSO reductase, xanthine oxidase, and nitrite reductase. Group: Enzymes. Synonyms: sulfite oxidase; EC 1.8.3.1; 9029-38-3. Enzyme Commission Number: EC 1.8.3.1. CAS No. 9029-38-3. Purity: > 85% (SDS-PAGE). Sulfite Oxidase. Mole weight: 110 kDa. Activity: 30-70 U/mg. Storage: -20°C. Form: Lyophilized. Source: Chicken Liver. Species: Chicken. sulfite oxidase; EC 1.8.3.1; 9029-38-3. Cat No: NATE-0689. | |
| Native Chromobacterium viscosum Lipase | Triacylglycerol lipase is an enzyme with system name triacylglycerol acylhydrolase. This enzyme catalyses the following chemical reaction:triacylglycerol + H2O<-> diacylglycerol + a carboxylate. Group: Enzymes. Synonyms: EC 3.1.1.3; 9001-62-1; Lipase; Triacylglycerol acylhydrolase; Triacylglycerol lipase; butyrinase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Activity: > 2,000 units/mg protein. Stability: -20°C. Form: lyophilized powder. Source: Chromobacterium viscosum. EC 3.1.1.3; 9001-62-1; Lipase; Triacylglycerol acylhydrolase; Triacylglycerol lipase; butyrinase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969-4-9; Meito MY 30; Tweenesterase; GA 56; capalase L; triglyceride hydrolase; triolein hydrolase; tween-hydrolyzing esterase; amano CE; cacordase; triglyceridase; triacylglycerol ester hydrolase; amano P; amano AP; PPL; glycerol-ester hydrolase; GEH; meito Sangyo OF lipase; hepatic lipase; lipazin; post-heparin plasma protamine-resistant lipase; salt-resistant post-heparin lipase; heparin releasable hepatic lipase; amano CES; amano B; tributyrase; triglyceride lipase; liver lipase; hepatic monoacylglycerol acyltransferase. Cat No: NATE-0400. | |
| 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. | |
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