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	Suppliers Website
Native Bovine L-Lactic Dehydrogenase Quick inquiry Where to buy	A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: For use in enzymatic determination of lactate or pyruvate. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nL. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 2-8°C. Form: Type I, Suspension in 2.2 M ammonium sulfate; Type II, buffered aqueous glycerol solution, Solution in 50% glycerol containing 0.025 M potassium phosphate buffer, pH 7.5; Type III, ammonium sulfate suspension, Crystalline suspension in 2.1 M (NH4)2SO4 solution, pH 6.0; Type IV, buffered aqueous glycerol solution, Solution in 50% glycerol containing 0.025 M potassium phosphate buffer, pH 7.5. Source: Bovine heart. Species: Bovine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0409.
Native Bovine Lysogangliosides Quick inquiry Where to buy	Lyso-gangliosides are prepared by removing glycolipid enzymatically from natural gangliosides. They can be used to analyze various cell function, such as cell proliferation, differentiation, apoptosis, signal transduction, etc. It can also be used as a material of ganglioside derivatives in RI labeling, fluorescence labeling, immobilization since they have free amino group in sphingosine. Group: Enzymes. Synonyms: Lyso-gangliosides; Lyso-GM3; Lysogangliosides. Purity: Greater than 95% by TLC. Lysogangliosides. Storage: -20°C. Form: Lyophilized. Source: Bovine milk ganglioside GM3. Species: Bovine. Lyso-gangliosides; Lyso-GM3; Lysogangliosides. Cat No: NATE-0870.
Native Bovine Malic Dehydrogenase Quick inquiry Where to buy	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 from bovine heart contains a histidine residue at the nad-binding active site which is critical for activity. when this histidine is mutated a loss in activity is observed. Applications: Malic dehydrogenase has been used in a study to assess a flow injection system for on-line monitoring of fumaric acid in biological pr ocesses. 1 it has also been used in a study to investigate a root-knot nematode parasitizing peanut in...001-64-3. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Activity: 2000-4000 units/mg protein (modified Warburg-Christian). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3 M (NH4)2SO4-0.01 M KH2PO4 solution, pH 7.3. Source: Bovine heart. Species: Bovine. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate (NAD) dehydrogenase; NAD-dependent malate dehydrogenase; NAD-specific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; EC 1.1.1.37; 9001-64-3. Cat No: NATE-0445.
Native Bovine Mucopolysaccharidase Quick inquiry Where to buy	Native Bovine Mucopolysaccharidase. Creative enzymes, is a leading producer of high potency hyaluronidase and mucopolysaccharidase and supplies the diagnostics industry. we extract hyaluronidase and mucopolysaccharidase from either bovine or ovine testes using multiple precipitation, fractionation, and filtration steps. creative enzymes products are not intended for use in pharmaceutical applications. Applications: In anti-cellulite preparations / promotion of topical drug absorption / local anesthesia / dispersion and dissipation of fluids and edema /in tissue and cell dissociation. Group: Enzymes. Synonyms: Mucopolysaccharidase; 37326-33-3; Hyaluronate 4-glycanohydrolase. CAS No. 9031-30-5. Mucopolysaccharidase. Activity: > 40 U/mg. Storage: Store at <-15°C. Form: A freeze-dried material. Source: Bovine testes. Species: Bovine. Mucopolysaccharidase; 37326-33-3; Hyaluronate 4-glycanohydrolase. Cat No: NATE-0463.
Native Bovine Nucleoside 5'-Diphosphate Kinase Quick inquiry Where to buy	Nucleoside-diphosphate kinases are enzymes that catalyze the exchange of phosphate groups between different nucleoside diphosphates. NDK activities maintain an equilibrium between the concentrations of different nucleoside triphosphates such as, for example, when GTP produced in the citric acid (Krebs) cycle is converted to ATP. Nucleoside Diphosphate Kinase exists in two isoforms in eukaryotic cells, NDK-A and NDK-B. These enzymes are found expressed both in the mitochondria and the cytoplasm. Nucleoside diphosphate kinase exists in two isoforms in eukaryotic cells, ndk-a and ndk-b. these enzymes are found expressed both in the mit ochondria and the cytoplasm. Applica...cleotide phosphate kinase; UDP kinase; uridine diphosphate kinase; ATP:nucleoside diphosphate phosphotransferase; NDPK; NDKs; NDP Kinase; EC 2.7.4.6; 9026-51-1. Enzyme Commission Number: EC 2.7.4.6. CAS No. 9026-51-1. NDPK. Activity: > 1,000 units/mg protein (biuret). Storage: 2-8°C. Form: buffered aqueous glycerol solution. Source: Bovine liver. Species: Bovine. nucleoside-diphosphate kinase; nucleoside 5'-diphosphate kinase; nucleoside diphosphate (UDP) kinase; nucleoside diphosphokinase; nucleotide phosphate kinase; UDP kinase; uridine diphosphate kinase; ATP:nucleoside diphosphate phosphotransferase; NDPK; NDKs; NDP Kinase; EC 2.7.4.6; 9026-51-1. Cat No: NATE-0477.
Native Bovine Nucleoside monophosphate kinase Quick inquiry Where to buy	This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Group: Enzymes. Synonyms: ATP : nucleoside-monophosphate phosphotransferase; NMP-kinase; EC 2.7.4.4; 9026-50-0; nucleoside-phosphate kinase. Enzyme Commission Number: EC 2.7.4.4. CAS No. 9026-50-0. Activity: Approximately 0.5 units per mg protein. Appearance: White to slightly beige lyophillized powder. Form: Lyophilized powder containing approximately 80% sacharose. Source: Bovine liver. Species: Bovine. ATP : nucleoside-monophosphate phosphotransferase; NMP-kinase; EC 2.7.4.4; 9026-50-0; nucleoside-phosphate kinase. Cat No: NATE-1722.
Native Bovine Pancreatin Quick inquiry Where to buy	Pancreatin is a mixture of several digestive enzymes produced by the exocrine cells of the pancreas. It is composed of amylase, lipase and protease. This mixture is used to treat conditions in which pancreatic secretions are deficient, such as surgical pancreatectomy, pancreatitis and cystic fibrosis. It has been claimed to help with food allergies, celiac disease, autoimmune disease, cancer and weight loss. Pancreatin is sometimes called "pancreatic acid", although it is neither a single chemical substance nor an acid. Protease, not < 100 units/mg, calculated on the dried basis. amylase, not < 100 units/mg, calculated on the dried basis. lipase, not < 8 units/mg, calculated on the dried basis. Applications: 1. in clinical, used for treating indigestion,loss of appetite, digestive disorders caused by pancreatic diseases anddiabetes indigestion, etc. 2. it could be used for the production of digestiondrug. Group: Enzymes. Synonyms: Pancreatin; 8049-47-6; pancreatic acid. CAS No. 8049-47-6. Pancreatin. Appearance: white or light yellow amorphous powder. Storage: Sealed, Dark, Preserved in a cool and dry place. Source: Bovine Pancreas. Species: Bovine. Pancreatin; 8049-47-6; pancreatic acid. Cat No: NATE-0503.
Native Bovine Phenylethanolamine N-Methyl Transferase Quick inquiry Where to buy	Phenylethanolamine N-methyltransferase (PNMT) is the enzyme which catalyzes the N-methylation of norepinephrine thereby resulting in the formation of epinephrine as shown below: Norepinephrine + S-Adenosyl methionine (SAM) -------> Epinephrine. The mechanism involves transfer of an active methyl group from S-adenosylmethionine (SAM) to the primary amino group of norepinephrine. Although it is primarily localized in the adrenal medulla, PNMT activity has also been demonstrated in the brain and heart tissues of several mammalian species including humans. PNMT purified from ox, rat and rabbit adrenal medulla have molecular weights in the range of 37,000-38,000. Analys...yl-L-methionine:phenylethanolamine-N-methyltransferase; EC 2.1.1.28. Enzyme Commission Number: EC 2.1.1.28. PNMT. Mole weight: 37-38 kDa. Activity: 50-100 U/mg protein. Stability: Store at -20°C (-4°F). Form: Freeze-dried powder. Source: Bovine Adrenal Medulla. Species: Bovine. phenylethanolamine N-methyltransferase; noradrenaline N-methyltransferase; noradrenalin N-methyltransferase; norepinephrine methyltransferase; norepinephrine N-methyltransferase; phenethanolamine methyltransferase; phenethanolamine N-methyltransferase; Phenylethanolamine N-Methyl Transferase; PNMT; S-adenosyl-L-methionine:phenylethanolamine-N-methyltransferase; EC 2.1.1.28. Cat No: NATE-0871.
Native Bovine Phosphodiesterase 3',5'-Cyclic Nucleotide Activator-deficient Quick inquiry Where to buy	Hydrolyzes the 3',5'-phosphodiester bond in cyclic nucleotide monophosphates, such as cAMP and cGMP, to the corresponding nucleotide 5'-monophosphate. Applications: Cyclic nucleotide phosphodiesterase has been investigated for its mechanism of activation as a function of calmodulin and ca2+. it has also been used in a study to show that the binding of trifluoperazine to the activator of cyclic nucleotide phosphodiesterase increases the activity by over 10-fold. for use in calmodulin (p 0270) assay. activity is reduced to <50% without calmodulin present. Group: Enzymes. Synonyms: cyclic 3',5'-mononucleotide phosphodiesterase; PDE; cyclic 3',5'-nucleotide ...th added activator). Storage: -20°C. Form: lyophilized powder (contains imidazole buffer salts and magnesium sulfate). Source: Bovine heart. Species: Bovine. cyclic 3',5'-mononucleotide phosphodiesterase; PDE; cyclic 3',5'-nucleotide phosphodiesterase; cyclic 3',5'-phosphodiesterase; 3',5'-nucleotide phosphodiesterase; 3':5'-cyclic nucleotide 5'-nucleotidohydrolase; 3',5'-cyclonucleotide phosphodiesterase; cyclic nucleotide phosphodiesterase; 3', 5'-cyclic nucleoside monophosphate phosphodiesterase; 3':5'-monophosphate phosphodiesterase (cyclic CMP); cytidine 3':5'-monophosphate phosphodiesterase (cyclic CMP); cyclic 3',5-nucleotide monophosphate phosphod
Native Bovine Phosphodiesterase, 3',5'-cyclic-nucleotide-specific Quick inquiry Where to buy	Hydrolyzes the 3',5'-phosphodiester bond in cyclic nucleotide monophosphates, such as cAMP and cGMP, to the corresponding nucleotide 5'-monophosphate. Applications: May be used to assay the protein activator, calmodulin. Group: Enzymes. Synonyms: cyclic 3',5'-mononucleotide phosphodiesterase; PDE. Enzyme Commission Number: EC 3.1.4.17. CAS No. 9040-59-9. PDE. Mole weight: mol wt ~60 kDa. Activity: 15-30 units/mg protein (in the presence of 0.03 mM Ca2+ and a saturating level (10 units per ml) of calmodulin (P2277)). Storage: -20°C. Form: Lyophilized powder containing Tris-HCl buffer salts and lactose. Source: Bovine brain. Species: Bovine. cyclic 3',5'-mononucleotide phosphodiesterase; PDE; cyclic 3',5'-nucleotide phosphodiesterase; cyclic 3',5'-phosphodiesterase; 3',5'-nucleotide phosphodiesterase; 3':5'-cyclic nucleotide 5'-nucleotidohydrolase; 3',5'-cyclonucleotide phosphodiesterase; cyclic nucleotide phosphodiesterase; 3', 5'-cyclic nucleoside monophosphate phosphodiesterase; 3':5'-monophosphate phosphodiesterase (cyclic CMP); cytidine 3':5'-monophosphate phosphodiesterase (cyclic CMP); cyclic 3',5-nucleotide monophosphate phosphodiesterase; nucleoside 3',5'-cyclic phosphate diesterase; nucleoside-3',5-monophosphate phosphodiesterase; EC 3.1.4.17. Pack: Package size based on activated units. Cat No: NATE-0515.
Native Bovine Phosphodiesterase II Quick inquiry Where to buy	Phosphodiesterase (PDE) is any enzyme that is used to breaks phosphodiester bonds. The enzyme acts on poly (A), poly (U), and poly (I). Native DNA and poly (C) are quite resistant to the action of this enzyme. Hydrolyzes RNA, RNA-Core, 3'-alkyl-and 3'-aryl-nucleoside phosphates, and polydeoxyribonucleotides with 3'-phosphate end groups to 3'-mononucleotides. Polynucleotides having 5'-phosphomonoester end groups are not attacked. Applications: Phosphodiesterase (pde) is any enzyme that is used to breaks phosphodiester bonds. it is a membrane-bound glycoprotein that is used to catalyze the hydrolysis of various nucleotide polyphosphates. phosphodiesterase ii has been used in t...yloxobutyl (pob) base adducts from dna. furthermore, it has been used along with micr oc occal endonuclease to hydrolyze purified dna to 3-nucleoside monophosphates. Group: Enzymes. Synonyms: 3'-exonuclease; spleen phosphodiesterase; 3'-nucleotide phosphodiesterase; phosphodiesterase II; spleen exonuclease; EC 3.1.16.1; 9068-54-6; PDE2. Enzyme Commission Number: EC 3.1.16.1. CAS No. 9068-54-6. PDE. Activity: > 5.0 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Bovine spleen. Species: Bovine. 3'-exonuclease; spleen phosphodiesterase; 3'-nucleotide phosphodiesterase; phosphodiesterase II; spleen exonuclease; EC 3.1.16.1; 9068-54-6; PDE2. Cat No: NATE-0518.
Native Bovine Phospholipase A2 Quick inquiry Where to buy	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: > 20 units/mg protein. Storage: -20°C. Form: lyophilized powder; Contains Tris buffer salts. Source: Bovine pancreas. Species: Bovine. Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Cat No: NATE-0583.
Native Bovine Plasma Amine Oxidase Quick inquiry Where to buy	Amine oxidase (also known as histaminase) is an enzyme involved in the metabolism, oxidation, and inactivation of histamine within the digestive tract. Bovine plasma amine oxidase has a molecular weight of 170 kDa and an optimum pH of 6.2 for spermine and 7.2 for spermidine. Amine oxidases are divided into two classes:the pyridoxal and copper containing enzyme to which plasma amine oxidase belongs, and the FAD-containing amino oxidases. Natural substrates include catecholamines, tryptamine derivatives and other physiologically active amines. Plasma amine oxidase is used in research requiring nitrogen group transfers. The molecule is composed of two identical polypeptide chai...mM respectively). It was from bovine plasma. chromatographically purified through step five of the procedure of yamada, y., and yasunobu, k., jbc, 237, 1511 (1962). a lyophilized powder. (one iu=4,330 tabor units). Group: Enzymes. Synonyms: Amine oxidase; EC 1.4.3.21; histaminase; Plasma Amine Oxidase. Enzyme Commission Number: EC 1.4.3.21. Purity: Chromatographically purified. Amine Oxidase. Mole weight: 170 kDa. Activity: > 17 Tabor units/mg dw. Stability: Stable for 12 months at-20°C. Store at -20°C. Storage: Store at -20°C. Form: lyophilized powder. Source: Bovine Plasma. Species: Bovine. Amine oxidase; EC 1.4.3.21; histaminase; Plasma Amine Oxidase. Cat No: NATE-0069.
Native Bovine Protamine Kinase, Cytosolic Quick inquiry Where to buy	Cytosolic protamine kinase is involved in the regulation of protein synthesis and is indirectly associated with numerous cellular processes. Cytosolic protamine kinase is a distinct insulin-stimulated kinase involved in the phosphorylation of eukaryotic Initiation Factor 4E (eIF4E) which is key to initiating translation by mRNA. This protein appears to be inactivated by protein phosphatase 2A family members and may also be inhibited by microcystin, okadeic acid, and ATP. The phosphorylation process is reversible and MBPK1 and MBPK2 (Myelin Basic Protein Kinase 1 and 2) may reactivate cytosolic protamine kinase. Applications: Cytosolic protamine kinase (cpk) is isolated from bovine kidney and has a molecular mass of approximately 45 kda. it phosphorylates the eukaryotic initiation factor 4e (eif4e), which initiates translation by mrna. it is used to study protein synthesis and various cellular processes. Group: Enzymes. Synonyms: Protamine Kinase, Cytosolic; Cytosolic protamine kinase; CPK; Cpk. Purity: >90% (SDS-PAGE). CPK. Activity: > 15,000 units/mg protein. Form: buffered aqueous glycerol solution. Source: Bovine kidney. Species: Bovine. Protamine Kinase, Cytosolic; Cytosolic protamine kinase; CPK; Cpk. Cat No: NATE-0155.
Native Bovine Protease Quick inquiry Where to buy	A protease (also called peptidase or proteinase) is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in animals, plants, bacteria, archaea and viruses. Derived from new zealand-sourced pancreas. Applications: Protease is an enzyme used to break down proteins by hydrolyzing peptide bonds. protease is used to degrade proteins, to study protease inhibitors and to study thermal inactivation kinetics. this product is from bovine pancreas. protease from bovine pancrease (type i) has been used for the extraction of hemicellulose. Group: Enzymes. Synonyms: Protease; peptidase; proteinase; 9001-92-7. CAS No. 9001-92-7. Protease. Activity: > 5 units/mg solid. Storage: -20°C. Source: bovine pancreas. Species: Bovine. Protease; peptidase; proteinase; 9001-92-7. Cat No: NATE-0628.
Native Bovine Protein Disulfide Isomerase Quick inquiry Where to buy	Protein Disulfide Isomerase (PDI) has the C-terminal ER retention sequence Lys-Asp-Glu-Leu. It has active, intracellular traffic to different cell compartments. PDI supports internalization of Chlamydia, cholera and diphtheria toxins in some hosts. PDI is required for Sindbis virus infection and aids in reducing HIV gp120 protein thiols. PDI facilitates formation of the correct disulfide bonds by promoting rapid reshuffling of disulfide pairings. Protein disulfide isomerase (pdi) from bovine liver is a homodimer with a molecular weight of 107 kda (gel filtration) and the molecular weight of the monomer has been reported at 57 kda (sds-page). the enzyme is a glycoprotein ... is mainly l ocated in the er, where it assists in protein-folding and thiol-disulfide exchanges. it is used to study functional role of pdi in parasite infection and the interaction between macrophage pdi and l. chagasi. Group: Enzymes. Synonyms: Protein disulfide isomerase; PDI; EC 5.3.4.1; 37318-49-3; S-S rearrangase. Enzyme Commission Number: EC 5.3.4.1. CAS No. 37318-49-3. Purity: >95% (SDS-PAGE). PDI. Activity: 100-400 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts and stabilizer. Source: Bovine liver. Species: Bovine. Protein disulfide isomerase; PDI; EC 5.3.4.1; 37318-49-3; S-S rearrangase. Cat No: NATE-0533.
Native Bovine Protein Kinase A Quick inquiry Where to buy	Protein Kinase A (PKA) catalyzes the transfer of the terminal phosphate of ATP to threonine or serine residues in a variety of protein substrates. The enzyme is composed of two subunit types: a catalytic subunit and a regulatory subunit. In the absence of cAMP, the two subunits are bound to each other and no catalysis can take place. In the presence of cAMP, the regulatory subunit binds cAMP, thus releasing the catalytic subunit. Group: Enzymes. Synonyms: Protein kinase A; PKA; Protein Kinase; 3',5'-cyclic-AMP-dependent Protein Kinase. Enzyme Commission Number: EC 2.7.11.11. CAS No. 9026-43-1. PKAC. Activity: >0.4 units/μg protein. Storage: Store the product at -20 °C. The dry solid is shipped at ambient temperature with minimal loss in activity. When stored at -20 °C with desiccant, the protein will lose <10% activity per year. Form: Lyophilized from a solution containing: 5-10% potassium phosphate buffer, pH 7.5, 5-10% EDTA, and 80-90% protein (biuret assay). Source: Bovine heart. Species: Bovine. Protein kinase A; PKA; Protein Kinase; 3',5'-cyclic-AMP-dependent Protein Kinase. Cat No: NATE-1944.
Native Bovine Protein Kinase G Iα Quick inquiry Where to buy	Protein Kinase G 1a is a native isoform of protein kinase G type I (cGK-I) isolated from bovine lung. It is a serine-threonine protein kinase found naturally in high concentrations in the cerebellar Purkinje cells, smooth muscle cells, and human platelets. > 95% (sds-page), buffered aqueous glycerol solution. Group: Enzymes. Synonyms: Protein Kinase G Iα; PKG Iα; cGK Iα; cyclic Guanosine Monophosphate Protein Kinase I α; EC 2.7.1.37; PKG1A; cGMP-dependent protein kinase. Enzyme Commission Number: EC 2.7.1.37. Purity: >95% (SDS-PAGE). PKC. Mole weight: mol wt 74 kDa (monomer). Stability: -20°C. Form: buffered aqueous glycerol solution. Source: bovine lung. Species: Bovine. Protein Kinase G Iα; PKG Iα; cGK Iα; cyclic Guanosine Monophosphate Protein Kinase I α; EC 2.7.1.37; PKG1A; cGMP-dependent protein kinase. Cat No: NATE-0579.
Native Bovine Protein Phosphatase 2A1 Quick inquiry Where to buy	Protein Phosphatase 2A1 is a trimer consisting of the A, B, and C subunits of the PP2A family. It has a total molecular weight of 192 kDa. Protein Phosphatase 2A is a cytoplasmic protein, which colocalizes with mictotubule proteins and is involved in the dephosphorylation of the tau protein and oncoprotein 18. Protein Phosphatase 2A1 binds to polymerized microtubule proteins and may be targeted by tubulin in modulating phosphatase activity. Applications: Protein phosphatase 2a1 is a divalent cation-dependent protein serine/threonine phosphatase implicated as a growth suppressor and is associated with dis-regulation in cancer. the enzyme is involved in regulating numerous cellular processes and is used to study cell cycle, growth, and differentiation. the protein phosphatase 2a1 has been used to treat human fibroblast cells prior to western blot analysis. Group: Enzymes. Synonyms: Protein Phosphatase 2A1; PP2A1; PPA2A1. Purity: >90% (SDS-PAGE). Protein Phosphatase. Activity: > 1500 units/mg protein. Stability: -70°C. Form: Solution in 50 mM Tris-HCl, pH 7.0, containing 14 mM 2-mercaptoethanol, 1 mM benzamidine, 0.1 mM PMSF, 1 mM EDTA, and 50% glycerol. Source: Bovine. Protein Phosphatase 2A1; PP2A1; PPA2A1. Pack: vial of 1 μg. Cat No: NATE-0616.
Native Bovine Protein Phosphatase 2A2 Quick inquiry Where to buy	Protein phosphatase 2A (PP2A) is a specific protamine-kinase-inactivating phosphatase, one common physiological form of which is PP2A2. Protein Phosphatase 2A2 from bovine kidney was shown to be a unique inhibitor of protamine kinase while other phosphatases in the same family including PP1, PP2B, PP2C did not show any inhibition. Protein phosphatase 2a (pp2a) is a specific protamine-kinase-inactivating phosphatase, one common physiological form of which is pp2a2. Applications: Protein phosphatase 2a2 has been used in a study to investigate two heat-stable protein inhibitors. it has also been used in a study to describe the purification and properties of a protamine kinase from bovine kidney microsomes. Group: Enzymes. Synonyms: Protein Phosphatase 2A2; PP2A2. Protein Phosphatase. Activity: ~2.0 U/vial. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: Bovine kidney. Species: Bovine. Protein Phosphatase 2A2; PP2A2. Cat No: NATE-0617.
Native Bovine Protein Phosphatase 2Ac Quick inquiry Where to buy	Divalent cation-independent catalytic subunit of protein phosphatase 2A. Useful for functional studies of the A and B subunit of the phosphatase. Group: Enzymes. Synonyms: Protein Phosphatase 2Ac; PP2Ac. Protein Phosphatase. Activity: ~2 U/vial. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: Bovine kidney. Species: Bovine. Protein Phosphatase 2Ac; PP2Ac. Cat No: NATE-0618.
Native Bovine Protein Phosphatase 2C Quick inquiry Where to buy	Protein Phosphatase 2C is a Mg2+-dependent serine/threonine protein phosphatase with a molecular mass of 42-45 kDa, involved in regulating numerous cellular processes. It is ubiquitously expressed and has been isolated from many mammalian tissues including liver, brain, skeletal muscle, retina, and blood platelets. There are two major isotypes associated with this enzyme, 2C1 and 2C2, also known as 2Ca and 2Cb, respectively. Both isozymes appear to be equally Mg2+-dependent and respond similarly to specific substrates. Both are monomers that demonstrate ~75% sequence homology. The molecular masses are similar; 44 kDa and 42 kDa for 2C1 and 2C2, respectively. Additional Type 2C serine/threonine protein phosphatases include 2Cg, 2Cd, Wip1, and NERPP2C, many of which have multiple isozyme members. Group: Enzymes. Synonyms: Protein Phosphatase 2C; PP2C. Protein Phosphatase. Activity: ~1000 units/mg protein. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: Bovine kidney. Species: Bovine. Protein Phosphatase 2C; PP2C. Pack: vial of 1 μg. Cat No: NATE-0619.
Native Bovine Pyruvate Carboxylase Quick inquiry Where to buy	Pyruvate carboxylase catalyzes the carboxylation of pyruvate to oxaloacetate. Pyruvate carboxylase is a mitochondrial protein that has a biotin prosthetic group that requiries magnesium or manganese and acetyl CoA. Applications: Pyruvate is critical for gluconeogenesis, lipogenesis, glyceroneogenesis, neurotransmitter biosynthesis and glucose-induced insulin, and is used to study these pr ocesses. the enzyme from creative enzymes has been used as a positive control during the assay of pyruvate carboxylase activity in cell-free extracts of corynebacterium glutamicum. Group: Enzymes. Synonyms: Pyruvate carboxylase; PC; EC 6.4.1.1; 9014-19-1; pyruvic carboxylase. Enzyme Commission Number: EC 6.4.1.1. CAS No. 9014-19-1. PC. Activity: 5-25 units/mg protein (BCA). Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 0.05 M Tris-HCl, pH 7.4, 2 mM magnesium acetate and 1 mM EDTA. Source: Bovine liver. Species: Bovine. Pyruvate carboxylase; PC; EC 6.4.1.1; 9014-19-1; pyruvic carboxylase. Cat No: NATE-0508.
Native Bovine Rhodanese Quick inquiry Where to buy	Rhodanese (RHOD) is the principal enzyme involved in hydrogen sulphide (H2S) detoxication in the colonic luman. Applications: Rhodanese (rhod) is an enzyme that converts cyanide to thi ocyanate. rhod may be useful in ulcerative colitis (uc) research as it has been shown to have detoxifying properties in the colon. rhodanese is used to study sulfur energy metabolism. Group: Enzymes. Synonyms: Rhodanese; EC 2.8.1.1; 9026-04-4; thiosulfate cyanide transsulfurase; thiosulfate thiotransferase; rhodanese; RHOD. Enzyme Commission Number: EC 2.8.1.1. CAS No. 9026-4-4. RHOD. Activity: 100-300 units/mg solid. Storage: -20°C. Form: essentially salt-free, lyophilized powder. Source: Bovine liver. Species: Bovine. Rhodanese; EC 2.8.1.1; 9026-04-4; thiosulfate cyanide transsulfurase; thiosulfate thiotransferase; rhodanese; RHOD. Cat No: NATE-0654.
Native Bovine Ribonuclease A Quick inquiry Where to buy	Ribonuclease A is an endoribonuclease that cleaves single stranded RNA after pyrimidine nucleotides. It attacks at the 3 phosphate end. Ribonucleases do not hydrolyze DNA, because the DNA lacks 2'-OH groups essential for the formation of cyclic intermediates. RNase can hydrolyze RNA from protein samples. Pancreatic RNase A specifically cleaves at the 3'-side of pyrimidine (uracil or cytosine) phosphate bonds. Ribonucleases do not hydrolyze dna, because the dna lacks 2?-oh groups essential for the formation of cyclic intermediates. rnase can hydrolyze rna from protein samples. pancreatic rnase a specifically cleaves at the 3?-side of pyrimidine (uracil or cytosine) phosphate bon...y to investigate particle-based and monolithic columns for cation exchange protein displacement chromatography. Group: Enzymes. Synonyms: Pancreatic ribonucleases; EC 3.1.27.5; RNase; RNase I; RNase A; pancreatic RNase; ribonuclease I; endoribonuclease I; ribonucleic phosphatase; alkaline ribonuclease; ribonuclease; gene S glycoproteins; Ceratitis capitata alkaline ribonuclease; SLSG glycoproteins; gene S locus-specific glycoproteins; S-genotype-asssocd. glycoproteins; ribonucleate 3'-pyrimidino-oligonucleotidohydrolase; 9001-99-4. Enzyme Commission Number: EC 3.1.27.5. CAS No. 9001-99-4. Rnase. Mole weight: mol wt ~13.7 kDa. Activity: Type I, 50-150 Kunitz units/mg solid; Type
Native Bovine Ribonuclease B Quick inquiry Where to buy	Native RNase BS generated by subtilisin digestion of native RNase B comprising of amino acid residues 21-124 of RNase B, is sensitive to PNGase F digestion. Intramolecular N-glycans of bovine pancreatic RNase B function like chaperone. RNase B is found to be much faster than RNase A, while RNase A is liable to aggregate during regeneration. The stimulatory effect of Asn-oligosaccharide (which corresponds to the most predominant sugar chain of RNase B) reveals that the N-glycans of RNase B facilitates the transformation of bulky intermediates into folded, compact species. Group: Enzymes. Synonyms: Pancreatic ribonucleases; EC 3.1.27. glycoproteins; ribonucleate 3'-pyrimidino-oligonucleotidohydrolase; 9001-99-4. Enzyme Commission Number: EC 3.1.27.5. CAS No. 9001-99-4. Purity: > 80% (SDS-PAGE). Rnase. Activity: > 50 Kunitz units/mg protein. Storage: -20°C. Source: Bovine pancreas. Species: Bovine. Pancreatic ribonucleases; EC 3.1.27.5; RNase; RNase I; RNase B; pancreatic RNase; ribonuclease I; endoribonuclease I; ribonucleic phosphatase; alkaline ribonuclease; ribonuclease; gene S glycoproteins; Ceratitis capitata alkaline ribonuclease; SLSG glycoproteins; gene S locus-specific glycoproteins; S-genotype-asssocd. glycoproteins; ribonucleate 3'-pyrimidino-oligonucleotidohydrolase; 9001-99-4. Pack: Package size based on protein content. Cat No: NATE-0656.
Native Bovine Superoxide Dismutase Quick inquiry Where to buy	Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice by preventing the conversion of NO to peroxynitrate, an inducer of apoptosis. Group: Enzymes. Synonyms: Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide di. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Mole weight: mol wt 32.5 kDa. Activity: Type I, > 3 ,000 units/mg protein; Type II, > 4,500 units/mg protein; Type III, 2,500-7 ,000 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Bovine erythrocytes. Species: Bovine. Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuperoxide dismutase; superoxide dismutase I; superoxide dismutase II; SOD; Cu,Zn-SOD; Mn-SOD; Fe-SOD; SODF; SODS; SOD-1; SOD-2; SOD-3; SOD-4; hemocuprein; erythrocuprein; cytocuprein; cuprein ; hepatocuprein; 9054-89-1. Cat No: NATE-0675.
Native Bovine Tautomerase Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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) Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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) Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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 Quick inquiry Where to buy	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.

Would you like to list your products on USA Chemical Suppliers?

Our database is helping our users find suppliers everyday.

Add Your Products