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| Product | Description | |
|---|---|---|
| Native Porcine Lipoamide Dehydrogenase | Lipoamide dehydrogenase (or diaphorase) catalyzes the following reaction: Lipoamide + NADH + H+ ? Dihydrolipoamide + NAD+. The enzyme occurs in mammalian and microbial cells and it catalyzes a number of reactions which involve NAD+ or NADH. Lipoamide dehydrogenase from porcine heart contains two polypeptide chains which are similar. It has two molecules of tightly bound flavin adenine dinucleotide (FAD). The molecular weight of the porcine heart enzyme is between 100,000 and 114,000. Group: Enzymes. Synonyms: NADH: lipoamide oxidoreductase; EC 1.6.4.3; Lipoamide Dehydrogenase; LD. Enzyme Commission Number: EC 1.6.4.3. LD. Mole weight: 100-114 kDa. Activity: 25 U/mg protein. Stability: Store at -20°C (-4°F). Form: Freeze-dried powder. Source: Porcine Heart. Species: Porcine. NADH: lipoamide oxidoreductase; EC 1.6.4.3; Lipoamide Dehydrogenase; LD. Cat No: NATE-0894. |  |
| Native Porcine L-Lactate 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. Dehydrogenase that catalyzes the interconversion of specific for l(+)-lactate to pyruvate. apply this ready-to-use enzyme directly in your diagnostic test. rely on the proven diagnostic quality of this product. Applications: Use l-lactate dehydrogenase in a variety of diagnostic tests for the removal of pyruvate in determinations working with nadh (i.e., triglycerides, lipase,...ehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. CAS No. 9001-60-9. LDH. Activity: >550 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Appearance: White suspension in ammonium sulfate, 3.2 mol/l; Tris, 10 mmol/l, pH approximately 6.5. Source: Porcine muscle. Species: Porcine. 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-0982. | |
| Native Porcine 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; Suspension in ammonium sulfate and 0.1 M potassium phosphate, pH 7.0. Source: Porcine heart. Species: Porcine. 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-0412. | |
| Native Porcine Malate Dehydrogenase, IFCC Quality | Dehydrogenase that catalyzes the interconversion of malate to oxaloacetate. Rely on the proven diagnostic quality of this product. Tested according to the recommendations of the International Federation of Clinical Chemistry (IFCC). Applications: Use malate dehydrogenase in diagnostic tests for the determination of aspartate aminotransferase or in applications for citric and acetic acid testing. Group: Enzymes. Synonyms: Malate Dehydrogenase, IFCC Quality; malic dehydrogenase; L-malate dehydrogenase; malic acid dehydrogenase; MDH. MDH. Mole weight: 70 kDa. Activity: >70 U/mg lyophilizate. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White lyophilizate. Source: Porcine heart. Species: Porcine. Malate Dehydrogenase, IFCC Quality; malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; S-malate: NAD+ oxidoreductase; EC 1.1.1.37; Malate Dehydrogenase. Cat No: DIA-278. | |
| Native Porcine Malic Dehydrogenase | 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. Group: Enzymes. Synonyms: malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid deh. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Activity: Type I, ~1,000 units/mg protein (biuret); Type II, > 400 units/mg protein (biuret); Type III, > 600 units/mg protein (biuret); Type IV, 600-1000 units/mg protein (biuret). Storage: 2-8°C. Form: Type I, Type III, ammonium sulfate suspension; Suspension in 2.8 M (NH4)2SO4 solution, pH 6.0; Type II, ammonium sulfate suspension, Suspension in 3.2 M (NH4)2SO4, 0.1 M KH2PO4, pH 7.0; Type IV, buffered aqueous glycerol solution, Solution in 50% glycerol containing 0.05 M potassium phosphate buffer, pH 7.5. Source: Porcine heart. Species: Porcine. 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-0447. | |
| Native Porcine Mutarotase | In enzymology, an aldose 1-epimerase (EC 5.1.3.3) is an enzyme that catalyzes the chemical reaction:alpha-D-glucose<-> beta-D-glucose. Hence, this enzyme has one substrate, alpha-D-glucose, and one product, beta-D-glucose. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. This enzyme participates in glycolysis and gluconeogenesis. Applications: Clinical chemistry. Group: Enzymes. Synonyms: mutarotase; aldose mutarotase; galactose mutarotase; galactose 1-epimerase; D-galactose 1-epimerase; aldose 1-epimerase; EC 5.1.3.3. Enzyme Commission Number: EC 5.1.3.3. CAS No. 9031-76-9. Mutarotase. Storage: Store desiccated at-15°C or below. Allow to come to room temperature before opening. Before returning to storage, redesiccate under vacuum over silica gel for a minimum of four hours. Re-seal before returning to-15°C or below. Form: A freeze-dried material. Source: Porcine kidney. Species: Porcine. mutarotase; aldose mutarotase; galactose mutarotase; galactose 1-epimerase; D-galactose 1-epimerase; aldose 1-epimerase; EC 5.1.3.3. Cat No: NATE-0465. | |
| Native Porcine NADase | In enzymology, a NAD+ nucleosidase (EC 3.2.2.5) is an enzyme that catalyzes the chemical reaction:NAD+ + H2O<-> ADP-ribose + nicotinamide. Thus, the two substrates of this enzyme are NAD+ and H2O, whereas its two products are ADP-ribose and nicotinamide. This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. This enzyme participates in nicotinate and nicotinamide metabolism and calcium signaling pathway. Nadase is a glycohydrolase that catalyzes adp-ribose transfer. Applications: Nadase from porcine brain has been used in a study to investigate histidine and related compounds resulting from catalyzed adp-riboslyation. ...ous); NAD nucleosidase (ambiguous); DPN hydrolase (ambiguous); NADase (ambiguous); nga (gene name); EC 3.2.2.5; 9032-65-9. Enzyme Commission Number: EC 3.2.2.5. CAS No. 9032-65-9. NADase. Activity: > 0.007 unit/mg solid. Storage: -20°C. Form: Acetone-dried powder. Source: Porcine brain. Species: Porcine. NAD glycohydrolase; nicotinamide adenine dinucleotide glycohydrolase; β-NAD+ glycohydrolase; DPNase (ambiguous); NAD hydrolase (ambiguous); diphosphopyridine nucleosidase (ambiguous); nicotinamide adenine dinucleotide nucleosidase (ambiguous); NAD nucleosidase (ambiguous); DPN hydrolase (ambiguous); NADase (ambiguous); nga (gene name); EC 3.2.2.5; 9032-65-9. Cat No: NATE-0472. | |
| Native Porcine NAD(P)H Dehydrogenase (quinone) | DT Diaphorase is a flavoenzyme that catalyzes the oxidation of reduced di-and triphosphopyridine nucleotides. It contains one mole of FAD per mole of enzyme. The enzyme found in rat liver catalyzes the oxidation of NADH and NADPH by various dyes and quinones. The molecular weight is found to be approximately 48 kDa Da. The pH optimum of the enzyme purified from rat liver is found to be 5.0. It is a cytosolic enzyme that catalyzes the two-electron reduction of various quinones. It catalyzes the conversion of vitamin K to vitamin K hydroquinone for utilization in the post-translational γ-glutamyl carboxylation reactions. These reactions are necessary for several pr...hydrogenase; NAD (P)H menadione reductase; NAD (P)H-quinone dehydrogenase; NAD (P)H-quinone oxidoreductase; NAD (P)H: (quinone-acceptor)oxidoreductase. CAS No. 9032-20-6. Diaphorase. Activity: >25 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Appearance: Yellow suspension in ammonium sulfate, 3.2 mol/l. Source: Porcine heart. Species: Porcine. menadione reductase; phylloquinone reductase; quinone reductase; dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone); DT-diaphorase; flavoprotein NAD (P)H-quinone reductase; menadione oxidoreductase; NAD (P)H dehydrogenase; NAD (P)H menadione reductase; NAD (P)H-quinone dehydro | |
| Native Porcine Pancreatin | 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. Applications: Pancreatin from porcine pancreas has been used to assess the treatment of steatorrhea by lipase supplementation therapy, to investigate treatment options for pancreatic diabetes in patients experiencing the decompensated stage of chronic pancreatitis, and to safely and effectively remove formalin-fixed tissues from arterial grafts without leading to structural damage or loss in fiber integrity. Group: Enzymes. Synonyms: Pancreatin; 8049-47-6; pancreatic acid. CAS No. 8049-47-6. Pancreatin. Storage: -20°C. Form: powder. Source: Porcine pancreas. Species: Porcine. Pancreatin; 8049-47-6; pancreatic acid. Cat No: NATE-0504. | |
| Native Porcine Pancreozymin | Cholecystokinin is a peptide hormone of the gastrointestinal system responsible for stimulating the digestion of fat and protein. Cholecystokinin, previously called pancreozymin, is synthesized by I-cells in the mucosal epithelium of the small intestine and secreted in the duodenum, the first segment of the small intestine, and causes the release of digestive enzymes and bile from the pancreas and gallbladder, respectively. It also acts as a hunger suppressant. Recent evidence has suggested that it also plays a major role in inducing drug tolerance to opioids like morphine and heroin, and is partly implicated in experiences of pain hypersensitivity during opioid withdrawal. Applications: Cholecystokinin (cck) is a peptide hormone of the gastrointestinal system responsible for stimulating the digestion of fat and protein. it is used to study brain, kidney and pancreatic functioning as well as reproductive behavior and glucose tolerance. Group: Enzymes. Synonyms: Cholecystokinin, CCK, CCK-PZ; 9011-97-6; Pancreozymin. CAS No. 9011-97-6. CCK. Activity: 2-6 Crick units/mg solid. Storage: 2-8°C. Source: Porcine intestine. Species: Porcine. Cholecystokinin, CCK, CCK-PZ; 9011-97-6; Pancreozymin. Cat No: NATE-0113. | |
| Native Porcine Pepsin | Pepsin is one of the principal protein degrading or proteolytic enzymes in the digestive system. During the process of digestion, Pepsin acts on the complex dietary protein and breaks up into peptides and amino acids which can be readily absorbed by the intestinal lining. It helps in digestive disturbance in general and as a result of impaired production of gastric juice. It acts as an adjunct in the treatment of anemic conditions, especially during slimming diet when protein intake increases. It is used as research tool in protein analysis and as digestive syrup in heart burn, acid indigestion and sour stomach. It is also used in tablets for increasing appetite and in the preparation of cheese and other protein-containing foods. Group: Enzymes. Synonyms: EC 3.4.23.1; pepsin; lactated pepsin; pepsin fortior; fundus-pepsin; elixir lactate of pepsin; P I; lactated pepsin elixir; P II; pepsin R; pepsin D; Pepsin A. Enzyme Commission Number: EC 3.4.23.1. CAS No. 9001-75-6. Pepsin. Activity: 10000U/g. Source: Porcine Stomach. Species: Porcine. EC 3.4.23.1; pepsin; lactated pepsin; pepsin fortior; fundus-pepsin; elixir lactate of pepsin; P I; lactated pepsin elixir; P II; pepsin R; pepsin D; Pepsin A. Cat No: PHAM-242. | |
| Native Porcine Pepsinogen | Pepsinogen is the zymogen of pepsin. It is processed by autocatalytic cleavage of 44 amino acids to generate active pepsin. Serum levels of pepsinogen have been measured to identify gastric cancer risk. Applications: Pepsin is an enzyme whose zymogen (pepsinogen) is released by the chief cells in the stomach and that degrades food proteins into peptides. it was discovered in 1836 by theodor schwann who also coined its name from the greek word π?ψΙ? pepsis, meaning "digestion" (from π?πτεΙν peptein "to digest"). it was the first enzyme to be discovered, and, in 1928, it became one of the first enzymes to be crystallized, by john h. northrop. ...rticular types of amino acids, collaborate to break down dietary proteins into their components, i.e., peptides and amino acids, which can be readily absorbed by the intestinal lining. pepsin is most efficient in cleaving peptide bonds between hydrophobic and preferably aromatic amino acids such as phenylalanine, tryptophan, and tyrosine. Group: Zymogens. Synonyms: pepsinogen; 9001-10-9; Pepsinogen from hog stomach. CAS No. 9001-10-9. Pepsinogen. Activity: ~3,000 units/mg protein (after activation to pepsin at pH 2.0 at 25°C). Storage: 2-8°C. Form: lyophilized powder. Source: Porcine Stomach. Species: Porcine. pepsinogen; 9001-10-9; Pepsinogen from hog stomach. Cat No: NATE-0547. | |
| Native Porcine Peptidase | 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. Applications: 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. Group: Enzymes. Synonyms: protease; peptidase; proteinase; 9031-96-3. CAS No. 9031-96-3. Peptidase. Activity: ≥ 500 U/g. Storage: -20°C. Source: Porcine intestinal mucosa. Species: Porcine. protease; peptidase; proteinase; 9031-96-3. Cat No: NATE-0548. | |
| Native Porcine Phosphodiesterase, 3',5'-Cyclic Nucleotide, Activator-deficient | PDE3 is a phosphodiesterase. The PDEs belong to at least eleven related gene families, which are different in their primary structure, substrate affinity, responses to effectors, and regulation mechanism. Most of the PDE families are composed of more than one gene. PDE3 is clinically significant because of its role in regulating heart muscle, vascular smooth muscle and platelet aggregation. PDE3 inhibitors have been developed as pharmaceuticals, but their use is limited by arrhythmic effects and they can increase mortality in some applications. Applications: May be used to assay the protein activator, calmodulin. Group: Enzymes. Synonyms: cyclic 3',5'-m...finity chromatography. PDE. Mole weight: mol wt ~60 kDa. Storage: -20°C. Form: Lyophilized preparation which has been depleted of calmodulin and containing buffer salts as Tris-HCl. Source: Porcine brain. Species: Porcine. 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 phosphodie | |
| Native Porcine 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: Type I, > 600 units/mg protein. Storage: -20°C. Form: Type I, ammonium sulfate suspension; Suspension in 3.2 M (NH4)2SO4 solution, pH 5.5; Type II, suspension, off-white. Source: Porcine pancreas. Species: Porcine. Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Cat No: NATE-0587. | |
| Native Porcine Prolidase | Prolidase is an enzyme that catalyzes the hydrolysis of the imide bond between an α-carboxyl group and proline or hydroxyproline. The protein forms a homodimer that hydrolyzes dipeptides or tripeptides with C-terminal proline or hydroxyproline residues. Applications: Prolidase is has an important role recycling of proline and collagen production. it is used to study mutations in the pepd gene that cause prolidase deficiency. it is used to hydrolyze proteins with c-terminal proline or hydroxyproline residues. prolidase from porcine kidney, has been used to hydrolyze peptide bonds from the amino terminus when studying enzymatic methylation of membrane proteins. Group: Enzymes. Synonyms: Xaa-Pro dipeptidase; prolidase; imidodipeptidase; proline dipeptidase; peptidase D; gamma-peptidase; X-Pro dipeptidase; EC 3.4.13.9; 9025-32-5. Enzyme Commission Number: EC 3.4.13.9. CAS No. 9025-32-5. Prolidase. Activity: > 100 units/mg protein. Storage: -20°C. Form: Supplied as a lyophilized powder containing Tris buffer salt and MnCl2. Source: Porcine kidney. Species: Porcine. Xaa-Pro dipeptidase; prolidase; imidodipeptidase; proline dipeptidase; peptidase D; gamma-peptidase; X-Pro dipeptidase; EC 3.4.13.9; 9025-32-5. Cat No: NATE-0627. | |
| Native Porcine Superoxide Dismutase | Superoxide dismutase (SOD) is one kind of metalloenzyme, it can be used in antioxidization, fight against senium and improve the immunologic function. Superoxide dismutase(SOD) can be used in health care food, cosmetics and beer, etc. Group: Enzymes. Synonyms: 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. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Mole weight: 32KD. Activity: 4500 U/mg. Storage: 2 years in dry and low temperature. Form: light blue green powder. Source: Porcine. Species: Porcine. 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-1925. | |
| Native Porcine 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. Applications: Diagnostic controls, calibrators & standards; immunoassays; testing/assay validation; life science; manufacturing; coagulation/anemia. Group: Enzymes. Synonyms: thrombin; alpha Subunit Thrombin. Thrombin. Mole weight: 362 kDa. Activity: > 1,000 NIH U/mg. Stability: 2 years. Storage: Store at -20°C. Form: Liquid in 0.05 M sodium Citrate, 0.2 M NaCl, 0.1% PEG-8,000, pH 6.5. Source: Porcine Plasma. Species: Porcine. thrombin; 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; alpha Subunit Thrombin. Cat No: NATE-0970. | |
| Native Porcine Trehalase | Trehalase is a glycoside hydrolase enzyme located in on the brush border of the small intestine that catalyzes the conversion of trehalose to glucose. It is found in most animals. The non-reducing disaccharide trehalose (α-D-glucopyranosyl-1,1-α-D-glucopyranoside) is one of the most important storage carbohydRates, which is present in almost all forms of life except mammals. The disaccharide is hydrolyzed into two molecules of glucose by the enzyme trehalase. There are two types of trehalases found in Saccharomyces cerevisiae, viz. neutral trehalase (NT) and acid trehalase (AT) classified according to their pH optima. NT has an optimum pH of 7.0, while that of AT is 4...mopara viticola-infected grapevine leaves. trehalase has also been used in a study to investigate growth arrest by trehalose-6-phosphate. Group: Enzymes. Synonyms: α,α-Trehalose glucohydrolase; Trehalase; EC 3.2.1.28; 9025-52-9; α,α-trehalase. Enzyme Commission Number: EC 3.2.1.28. CAS No. 9025-52-9. Trehalase. Activity: > 1.0 units/mg protein. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 1% Triton(TM) X-100 and 25 mM potassium phosphate, pH 6.5. Source: Porcine kidney. Species: Porcine. α,α-Trehalose glucohydrolase; Trehalase; EC 3.2.1.28; 9025-52-9; α,α-trehalase. Cat No: NATE-0717. | |
| Native Porcine 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 cleaves peptides on the c-terminal side of lysine and arginine residues. the rate of hydr... others, will inhibit trypsin. Applications: For use in immunohistochemical procedures to enhance staining and to unmask antigens after routine fixation and processing. for trypsin digestion of peptides, use a ratio of about 1:100 to 1:20 for trypsin:peptide. the typical use for this product is in removing adherent cells from a culture surface. the concentration of trypsin necessary to dislodge cells from their substrate 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 digestionsns+. additional applications inclu | |
| Native Potato Acid Phosphatase | Acid phosphatases (APase) are a family of enzymes that non-specifically catalyze the hydrolysis of monoesters and anhydrides of phosphoric acid to produce inorganic phosphate at an optimum pH of 4 to 7. Acid phosphatase from potatoes is a 111 kDa diner consisting of two subunits at 41 and 35 kDa. This phosphatase has also been shown to cleave DNA. Acid phosphatase from potatoes is a 111 kda diner consisting of two subunits at 41 and 35 kda. this phosphatase has also been shown to cleave dna. Applications: Phosphatase acid from potato has been used in a study to develop a method of efficient enzymatic hydrolysis of polyprenyl pyrophosphates. it has also been used in a study to ...ase. Activity: Type I, > 200 units/mg protein (biuret); Type II, 0.5-3.0 unit/mg solid; Type III, 3.0-10.0 units/mg solid; Type IV, > 10.0 units/mg protein (modified Warburg-Christian). Storage: 2-8°C. Form: Type I, Type IV, ammonium sulfate suspension; Suspension in 1.8 M (NH4)2SO4, 10 mM MgCl2, pH 5.5; Type II, Type III, lyophilized powder. Source: Potato. acid phosphatase; 9001-77-8; acid phosphomonoesterase; phosphomonoesterase; glycerophosphatase; acid monophosphatase; acid phosphohydrolase; acid phosphomonoester hydrolase; uteroferrin; acid nucleoside diphosphate phosphatase; orthophosphoric-monoester phosphohydrolase (acid optimum); EC 3.1.3.2; APase. Cat No: NATE-0083. | |
| Native Potatoes Apyrase | Apyrase is found in all eukaryotes and some prokaryotes. Apyrase, from potato, has a crucial role in regulating growth and development. Apyrase is involved in the inactivation of synaptic ATP as a neurotransmitter following nerve stimulation and in the inhibition of ADP induced platelet aggregation to prevent thrombosis. Divalent metal ions are required for activity and best activity is observed with calcium ion at 5 mM. Applications: At least two isoenzymes are found in different varieties of s. tuberosum:4,5 one with a high atpase/adpase ratio (~10) and another with a low ratio (~1). reaction: atp ? adp+pi ? amp+2pi.apyrase is used to hydrolyze nucleoside triphosphates and diphosphates. for hydrolysis of organic di and triphosphates, the optimal ph is 6, and for inorganic substrates, the optimal ph is 5.1. apyrase, from creative enzymes, has been used in inhibition studies of platelet-aggregation. Group: Enzymes. Synonyms: ATP-diphosphatase; adenosine diphosphatase. Enzyme Commission Number: EC 3.6.1.5. CAS No. 9000-95-7. Apyrase. Activity: > 200 units/mg protein; > 600 units/mg protein. Storage: -20°C. Form: lyophilized powder. Partially purified, lyophilized powder containing potassium succinate buffer salts. Source: Potatoes. ATP-diphosphatase; adenosine diphosphatase; ADPase; ATP diphosphohydrolase; apyrase; EC 3.6.1.5; 9000-95-7. Cat No: NATE-0085. | |
| Native Propionibacterium freudenreichii (shermanII) Fructose-6-phosphate Kinase, Pyrophosphate-dependent | Fructose-1,6-bisphosphatase (FBP) is an important enzyme in glucose metabolism. It catalyzes the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate. Fructose-6-phosphate kinase converts fructose-6-phosphate into fructose 1,6-bisphophate in the rate limiting step of the glycolysis cycle. Applications: Fbp was used to study the kinetic mechanism of pyrophosphate-dependent phosphofructokinase from propionibacterium freudenreichii. Group: Enzymes. Synonyms: EC 2.7.1.90; 6-phosphofructokinase (pyrophosphate); pyrophosphate-fructose 6-phosphate 1-phosphotransferase; inorganic pyrophosphate-dependent phosphofructokinase; inorganic pyrophosphate-phosphofructokinase; pyrophospha. Enzyme Commission Number: EC 2.7.1.90. CAS No. 55326-40-4. FBP. Activity: 4.0-8.0 units/mg protein. Storage: -20°C. Form: lyophilized powder; Contains imidazole salts and stabilizer. Source: Propionibacterium freudenreichii (shermanII). EC 2.7.1.90; 6-phosphofructokinase (pyrophosphate); pyrophosphate-fructose 6-phosphate 1-phosphotransferase; inorganic pyrophosphate-dependent phosphofructokinase; inorganic pyrophosphate-phosphofructokinase; pyrophosphate-dependent phosphofructo-1-kinase; pyrophosphate-fructose 6-phosphate phosphotransferase; 55326-40-4. Cat No: NATE-0253. | |
| Native Protein Methylase II | Methylation of proteins is one of the key reactions in the post-translational modification of protein amino acid residues in the cell. It has been established that the basic and acidic amino acid residues of certain proteins are methylated in vivo. Protein methylase II methylates the free carboxyl groups of dicarboxylic acid residues in a protein molecule. Existence of this enzyme, in mammalian tissues, was first reported by Liss and Edelstein. Protein methylase II from ox brain has been purified by Iqbal and Steenson. Group: Enzymes. Synonyms: S-adenosylmethionine:protein Carboxyl O-methyltransferase; EC 2.1.1.24; Protein Methylase II. Enzyme Commission Number: EC 2.1.1.24. Protein Methylase II. S-adenosylmethionine:protein Carboxyl O-methyltransferase; EC 2.1.1.24; Protein Methylase II. Cat No: NATE-0895. | |
| Native Proteus sp. Glutamate Dehydrogenase (NADP-dependent) | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Applications: This enzyme is useful for enzymatic determination of nh3, α-ketoglutaric acid and l-glutamic acid, and for assay of leucine aminopeptidase and urea...lutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Enzyme Commission Number: EC 1.4.1.4. Mole weight: approx. 300 kDa. Activity: 300U/mg-protein or more (9,000U/ml or more). Appearance: Solution with 50mM Tris-HCl buffer containing 0.05% NaN3 and 5.0mM EDTA, pH 7.8. Form: Freeze dried powder. Source: Proteus sp. glutamate dehydrogenase (NADP+); 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); EC 1.4.1.4; GLDH. Cat No: DIA-196. | |
| Native Proteus sp. L-Glutamic Dehydrogenase (NADP) | L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate. Applications: This enzyme is useful for enzymatic determination of nh3, α-ketoglutaric acid and l-glutamic acid, and for assay of leucine aminopeptidase and urease. this enzyme is also used for enzymatic determination of urea when coupled with urease (urh-201) in clinical analysis. 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 de. Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. Mole weight: mol wt ~300 kDa. Activity: > 400 units/mg protein (biuret). Storage: 2-8°C. Form: buffered aqueous solution; Solution in 50 mM Tris HCl, pH 7.8, 5 mM Na2EDTA containing 0.05% sodium azide. Source: Proteus sp. 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-0395. | |
| Native Proteus vulgaris Chondroitinase ABC | Chondroitinase ABC catalyzes the eliminative degradation of polysaccharides containing (1-4)-β-D-hexosaminyl and (1-3)-β-D-glucuronosyl or (1-3)-α-L-iduronosyl linkages to disaccharides containing 4-deoxy-β-D-gluc-4-enuronosyl groups. It acts on chondroitin 4-sulfate, chondroitin 6-sulfate, and dermatan sulfate, and acts slowly on hyaluronate. The molecular weight is found to be approximately 120 kDa with 2 non-identical subunits of molecular masses 86 kDa and 32 kDa. The pH optimum is found to be 8.0 with chondroitin sulfate and 6.8 with hyaluronic acid and tempeRature optimum is 37°C. 1 mM Zn2+ acts as an inhibitor, while 0.05 M acetate is an activ...BC lyase; ChS ABC lyase; chondroitin sulfate ABC endoeliminase; chondroitin sulfate ABC endolyase; ChS ABC lyase I; 9024-13-9. Enzyme Commission Number: EC 4.2.2.4. CAS No. 9024-13-9. Chondroitinase ABC. Activity: 50-250 units/mg protein (using chondroitin sulfate C as substrate); 0.3-3 units/mg solid (using chondroitin sulfate C as substrate). Storage: -20°C. Form: lyophilized powder. Source: Proteus vulgaris. EC 4.2.2.4, chondroitinase; chondroitin ABC eliminase; chondroitinase ABC; chondroitin ABC lyase; chondroitin sulfate ABC lyase; ChS ABC lyase; chondroitin sulfate ABC endoeliminase; chondroitin sulfate ABC endolyase; ChS ABC lyase I; 9024-13-9. Cat No: NATE-0131. | |
| Native Pseudomonas aeruginosa Elastase | Pancreatic elastase is a form of elastase that is produced in the acinar cells of the pancreas, initially produced as an inactive zymogen and later activated in the duodenum by trypsin. Elastases form a subfamily of serine proteases, characterized by a distinctive structure consisting of two beta barrel domains converging at the active site that hydrolyze amides and esters amongst many proteins in addition to elastin, a type of connective tissue that holds organs together. Pancreatic elastase 1 is a serine endopeptidase, a specific type of protease that has the amino acid serine at its active site. Group: Enzymes. Synonyms: EC 3.4.21.36, pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase; elastase-1; pancreatopeptidase; ELA1. Enzyme Commission Number: EC 3.4.24.26. CAS No. 9004-6-2. Purity: > 90% by SDS-PAGE. ELA1. Mole weight: 33000. Stability: Following reconstitution, aliquot and freeze (-20°C) for long-term storage or refrigerate (4°C) for short-term storage. Stock solutions are stable for up to 1 week at 4°Cor for up to 2 months at-20°C. Appearance: Lyophilized. Storage: Storage at-20°C. Source: Pseudomonas aeruginosa. EC 3.4.21.36, pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase; elastase-1; pancreatopeptidase; ELA1. Cat No: NATE-0212. | |
| Native Pseudomonas atlantica Agarase | Agarase is an enzyme with system name agarose 4-glycanohydrolase. It found in agarolytic bacteria and is the first enzyme in the agar catabolic pathway. It is responsible for allowing them to use agar as their primary source of Carbon and enables their ability to thrive in the ocean. Agarases are classified as either α-agarases or β-agarases based upon whether they degrade αor β linkages in agarose, breaking them into oligosaccharides. When secreted, α-agarases yield oligosaccharides with 3.6 anhydro-L-galactose at the reducing end whereas β-agarases result in D-galactose residues. Group: Enzymes. Synonyms: agarase; AgaA; AgaB; endo-β-agarase; agarose 3-glycanohydrolase; EC 3.2.1.81; 37288-57-6. Enzyme Commission Number: EC 3.2.1.81. CAS No. 37288-57-6. Agarase. Activity: > 5,000 units/mg protein (Lowry). Storage: 2-8°C. Form: lyophilized powder. Contains phosphate buffer salts. May contain bovine serum albumin to standardize protein content. Source: Pseudomonas atlantica. agarase; AgaA; AgaB; endo-β-agarase; agarose 3-glycanohydrolase; EC 3.2.1.81; 37288-57-6. Cat No: NATE-0040. | |
| Native Pseudomonas fluorescens β-Lactamase | β--lactamase inactivates β-lactam antibiotics by breaking open the β-lactam ring. Group: Enzymes. Synonyms: β-lactamase; penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase; EC 3.5.2.6; 9073-60-3. Enzyme Commission Number: EC 3.5.2.6. CAS No. 9073-60-3. β-Lactamase. Storage: 2-8°C. Form: Lyophilized powder containing potassium phosphate and sodium bicarbonate. Source: Pseudomonas fluorescens. β-lactamase; penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase; EC 3.5.2.6; 9073-60-3. Cat No: NATE-0775. | |
| Native Pseudomonas fluorescens 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. Protein determined by biuret. Applications: Cholesterol esterase from pseudomonas fluorescens has...iterpenol 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. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Cholesterol Esterase. Activity: > 10,000 units/g protein. Storage: -20°C. Form: lyophilized powder. Source: Pseudomonas fluorescens. 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-0116. | |
| Native Pseudomonas fluorescens Galactose 1-Dehydrogenase | In enzymology, a galactose 1-dehydrogenase (EC 1.1.1.48) is an enzyme that catalyzes the chemical reaction: D-galactose + NAD+ rightleftharpoons D-galactono-1,4-lactone + NADH + H+. Thus, the two substrates of this enzyme are D-galactose and NAD+, whereas its 3 products are D-galactono-1,4-lactone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in galactose metabolism. Dehydrogenase that catalyzes the oxidation of galactose to d-galactono-1,4-lactone. rely on the proven diagnostic quality of this recombinant enzyme. apply this ready-t...uctase; D-galactose dehydrogenase; beta-galactose dehydrogenase; NAD+-dependent D-galactose dehydrogenase; galactose 1-dehydrogenase; Galactose dehydrogenase. CAS No. 9028-54-0. Galactose dehydrogenase. Activity: >5 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Appearance: White suspension in ammonium sulfate solution, 3.2 mol/l; EDTA, 1 mmol/l; pH approximately 6. Source: Pseudomonas fluorescens. D-galactose:NAD+ 1-oxidoreductase; D-galactose dehydrogenase; beta-galactose dehydrogenase; NAD+-dependent D-galactose dehydrogenase; galactose 1-dehydrogenase; EC 1.1.1.48; Galactose dehydrogenase; Galactose 1-Dehydrogenase. Cat No: NATE-0980. | |
| Native Pseudomonas fragi Acyl-CoA Synthetase | The Long chain fatty acyl-CoA synthetase enzyme is a member of the ligase family that activates the breakdown of complex fatty acids. Long chain fatty acyl-CoA synthetase plays a crucial role in intermediary metabolism by catalyzing the formation of fatty acyl-CoA by a two-step process proceeding through an adenylated intermediate. It is an enzyme present in all organisms from bacteria to humans. It catalyzes the pre-step reaction for β-oxidation of fatty acids or can be incorporated in phospholipids. Acs is an enzyme produced by microorganisms. this product shall be used for a diagnostics reagent. Applications: Useful in the enzymatic determination of fatty acid when coupled with acyl-coa oxidase. Group: Enzymes. Synonyms: EC 6.2.1.3; ACS; acyl-CoA synthetase; fatty acid thiokinase (long chain. Enzyme Commission Number: EC 6.2.1.3. CAS No. 9013-18-7. ACS3. Mole weight: 60 kDa (Sephadex G-150) SDS-PAGE 62 kDa. Activity: 2-8 U/mg. Stability: At least one year at-20°C. Appearance: White powder. Storage: Keep in freezer (-20°C to-80°C), dry place in well-closed containers and away from direct sun light). Form: Freeze dried powder. Source: Pseudomonas fragi. EC 6.2.1.3; ACS; acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetase; ac | |
| Native Pseudomonas fragi mutant strain Endoproteinase Asp-N | Peptidyl-Asp metalloendopeptidase (EC 3.4.24.33, endoproteinase Asp-N, peptidyl-Asp metalloproteinase) is an enzyme. This enzyme catalyses the following chemical reaction:Cleavage of Xaa-Asp, Xaa-Glu and Xaa-cysteic acid bonds. This metalloenzyme is isolated from Pseudomonas fragi. Group: Enzymes. Synonyms: endoproteinase Asp-N; peptidyl-Asp metalloproteinase; EC 3.4.24.33; 9001-92-7; peptidyl-Asp metalloendopeptidase. Enzyme Commission Number: EC 3.4.24.33. CAS No. 9001-92-7. Endoproteinase Asp-N. Storage: 2-8°C. Form: lyophilized powder. Source: Pseudomonas fragi mutant strain. endoproteinase Asp-N; peptidyl-Asp metalloproteinase; EC 3.4.24.33; 9001-92-7; peptidyl-Asp metalloendopeptidase. Pack: vial of 2 μg. Cat No: NATE-0222. | |
| Native Pseudomonas lemoignei β-Hydroxybutyrate Dehydrogenase | In mammalian systems, β-hydroxybutyrate dehydrogenase is localized on the inner mitochondrial membrane and requires phosphatidyl choline for activity. In contrast, the enzyme from Pseudomonas is a soluble cytosolic enzyme that does not require a phospholipid allosteric activator. The enzyme is required for the utilization of ketone bodies as a source of metabolic energy. It catalyzes the oxidation of 3-hydroxybutyrate to acetoacetate, the first step in the conversion of ketone bodies to citric acid, which is then further metabolized via the tricarboxylic acid cycle (Krebs cycle). Applications: Suitable for the determination of acetoacetate and d (-)-3-hy...1.1.30; 9028-38-0. Enzyme Commission Number: EC 1.1.1.30. CAS No. 9028-38-0. 3-HBDH. Activity: > 200 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing sucrose, β-NAD and Tris buffer salts. Source: Pseudomonas lemoignei. 3-hydroxybutyrate dehydrogenase; 3-HBDH; NAD-β-hydroxybutyRate dehydrogenase; hydroxybutyRate oxidoreductase; β-hydroxybutyRate dehydrogenase; D-β-hydroxybutyRate dehydrogenase; D-3-hydroxybutyRate dehydrogenase; D-(-)-3-hydroxybutyRate dehydrogenase; β-hydroxybutyric acid dehydrogenase; 3-D-hydroxybutyRate dehydrogenase; β-hydroxybutyric dehydrogenase; EC 1.1.1.30; 9028-38-0. Cat No: NATE-0003. | |
| Native Pseudomonas sp. Acyl-coenzyme A Synthetase | The Long chain fatty acyl-CoA synthetase enzyme is a member of the ligase family that activates the breakdown of complex fatty acids. Long chain fatty acyl-CoA synthetase plays a crucial role in intermediary metabolism by catalyzing the formation of fatty acyl-CoA by a two-step process proceeding through an adenylated intermediate. It is an enzyme present in all organisms from bacteria to Humans. It catalyzes the pre-step reaction for β-oxidation of fatty acids or can be incorpoRated in phospholipids. Acyl coenzyme A synthetase proteins are involved in regulating and facilitating long-chain fatty acid transport in mammalian cells. Applications: Acyl-coenzyme a synthetase may be used to study fatty acid metabolism and lipid metabolism. it has been used to study its interaction with fatty acid transport proteins, which has been found to be involved in the efficient cellular uptake of long-chain fatty acids in adipocyte. Group: Enzymes. Synonyms: acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating. Enzyme Commission Number: EC 6.2.1.3. CAS No. 9013-18-7. ACS3. Activity: > 2 units/mg protein. Storage: -20°C. Source: Pseudomonas sp. acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetase; acyl coenzyme A synt | |
| Native Pseudomonas sp. Carboxypeptidase G | Carboxypeptidase G is a lysosomal, thiol-dependent protease, which progressively cleaves γ-glutamyl pteroyl poly-γ-glutamate yielding pteroyl-α-glutamate (folic acid) and free glutamate. It is considered highly specific for the γ-glutamyl bond, but not for the C-terminal amino acid of the leaving group.1 Molecular mass of this homodimer is approximately 90 kDa. The enzyme is activated by Zn2+ ions. Applications: Carboxypeptidase g from pseudomonas sp., or γ-glutamyl hydrolase, has been used in a study to assess the role of the putidaredoxin cooh-terminus in p-450cam (cytochrome m) hydroxylations. carboxypeptidase g from pseudomonas sp. has also been used in a study to investigate the effects of nitric oxide on pemetrexed cytotoxicity via no-cgmp signaling in lung adenocarcinoma cells. Group: Enzymes. Synonyms: γ-Glutamyl hydrolase; EC 3.4.17.11; 9074-87-7; glutamate carboxypeptidas. Enzyme Commission Number: EC 3.4.17.11. CAS No. 9074-87-7. Carboxypeptidase G. Activity: > 3 units/mg protein. Storage: -20°C. Form: lyophilized powder contains sodium acetate salt. Source: Pseudomonas sp. γ-Glutamyl hydrolase; EC 3.4.17.11; 9074-87-7; glutamate carboxypeptidase; carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; glutamyl carboxypeptidase; N-pteroyl-L-glutamate hydrolase. Cat No: NATE-0102. | |
| Native Pseudomonas sp. Cholesterol Esterase | Sterol esterase belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is steryl-ester acylhydrolase. This enzyme participates in bile acid biosynthesis. Applications: This enzyme is useful for enzymatic determination of total cholesterol when coupled with cholesterol oxidase in clinical analysis. Group: Enzymes. Synonyms: 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; Sterol esterase. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Cholesterol Esterase. Mole weight: approx. 300 kDa. Activity: GradeIII 100U/mg-solid or more (containing approx. 40% of stabilizers). Stability: Stable at-20°C for at least one year. Appearance: Light brown amorphous powder, lyophilized. Source: Pseudomonas sp. 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; Sterol esterase. Cat No: DIA-134. | |
| Native Pseudomonas sp. Cholesterol Oxidase | Recombinant Cholesterol Oxidase belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. This enzyme participates in bile acid biosynthesis. Recombinant cholesterol oxidase produced in e.coli has a molecular mass of about 34,000 da. Group: Enzymes. Synonyms: Cholesterol-O2 oxidoreductase; 3 beta-Hydroxy steroid oxidoreductase; 3β-hydroxysteroid: oxygen oxidoreductase; cholesterol: oxygen oxidoreductase; cholesterol oxidase; EC 1.1.3.6. Enzyme Commission Number: EC 1.1.3.6. CAS No. 9026-00-0. CHOD. Mole weight: about 34 kDa (gel filtration). Activity: Grade ? 15 U/mg-solid or more(contg. approx. 40% of stabilizers). Stability: Stable at-20°C for at least 6 months. Appearance: Yellowish amorphous powder, lyophilized. Source: Pseudomonas sp. Cholesterol-O2 oxidoreductase; 3 beta-Hydroxy steroid oxidoreductase; 3β-hydroxysteroid: oxygen oxidoreductase; cholesterol: oxygen oxidoreductase; cholesterol oxidase; EC 1.1.3.6. Cat No: DIA-136. | |
| Native Pseudomonas sp. Creatinine amidohydrolase | Creatinine Amidohydrolase catalyzes the hydrolytic reaction converting creatinine to creatine. The enzyme is purified from a microorganism. The molecular size of the enzyme is approximately 175,000. The enzyme is useful for the enzy-matic assay of creatinine when coupled with other related enzymes. Creatinine + H2O ? Creatine. Creatininase from pseudomonas sp. is a homohexameric enzyme with a molecular mass of 28.4 kda per subunit. it is a cyclic amidohydrolase catalysing the reversible conversion of creatinine to creatine. each monomer contains a binuclear zinc centre near the c termini of the β-strands and the n termini of the main α-helices. these zinc ions indicate the location of the active site. Applications: This enzyme is useful for enzymatic determination of creatinine when coupled with creatine amidinohydrolase, sarcosine dehydrogenase or sarcosine oxidase and formaldehyde dehydrogenase in clinical analysis. Group: Enzymes. Synonyms: creatininase; creatinine hydrolase; creatinine . Enzyme Commission Number: EC 3.5.2.10. CAS No. 9025-13-2. Creatininase. Mole weight: 175 kDa. Activity: > 250U/mg protein. Storage: 2-8°C. Form: Lyophilized powder containing sucrose and BSA as stabilizers. Source: Pseudomonas sp. creatininase; creatinine hydrolase; creatinine amidohydrolase; EC 3.5.2.10; 9025-13-2. Cat No: DIA-130. | |
| Native Pseudomonas sp. D-3-hydroxybutyrate dehydrogenase | In enzymology, a 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) is an enzyme that catalyzes the chemical reaction: (R)-3-hydroxybutanoate + NAD+ <-> acetoacetate + NADH + H+. Thus, the two substrates of this enzyme are (R)-3-hydroxybutanoate and NAD+, whereas its three products are acetoacetate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in synthesis and degradation of ketone bodies and butanoate metabolism. Applications: This enzyme is useful for enzymatic determination of ketone bodies (d-3-hydroxybutyrate and acetoacetate) in...ission Number: EC 1.1.1.30. CAS No. 9028-38-0. 3-HBDH. Mole weight: approx. 130 kDa (by gel filtration). Activity: Grade? 100U/mg-solid or more. Stability: Stable at-20°C for at least one year. Appearance: White amorphous powder, lyophilized. Source: Pseudomonas sp. (R)-3-hydroxybutanoate: NAD+ oxidoreductase; NAD+-beta-hydroxybutyrate dehydrogenase; hydroxybutyrate oxidoreductase; beta-hydroxybutyrate dehydrogenase; D-beta-hydroxybutyrate dehydrogenase; D-3-hydroxybutyrate dehydrogenase; D-(-)-3-hydroxybutyrate dehydrogenase; beta-hydroxybutyric acid dehydrogenase; 3-D-hydroxybutyrate dehydrogenase; beta-hydroxybutyric dehydrogenase; EC 1.1.1.30. Cat No: DIA-204. | |
| Native Pseudomonas sp. Formaldehyde Dehydrogenase | Formaldehyde dehydrogenase catalyzes the conversion of formaldehyde to formate. Applications: Formaldehyde dehydrogenase is used as a biosensor for the presence of formaldehyde in pharmaceuticals, waste water, vaccines and industrial products. it was also used in coupled pectin methyl esterase (pme) enzyme assay. Group: Enzymes. Synonyms: EC 1.2.1.46; Formaldehyde Dehydrogenase; NAD-linked formaldehyde dehydrogenase; NAD-dependent formaldehyde dehydrogenase; 9028-84-6. Enzyme Commission Number: EC 1.2.1.46. CAS No. 9028-84-6. Formaldehyde Dehydrogenase. Activity: 1.0-6.0 units/mg solid. Storage: -20°C. Form: Lyophilized powder containing ~70% stabilizers as Mg2+, Ca2+, bovine serum albumin, glycine, and lysine. Source: Pseudomonas sp. EC 1.2.1.46; Formaldehyde Dehydrogenase; NAD-linked formaldehyde dehydrogenase; NAD-dependent formaldehyde dehydrogenase; 9028-84-6. Cat No: NATE-0257. | |
| Native Pseudomonas sp. Glucose dehydrogenase | In enzymology, a glucose 1-dehydrogenase (EC 1.1.1.47) is an enzyme that catalyzes the chemical reaction:beta-D-glucose + NAD (P)+<-> D-glucono-1,5-lactone + NAD (P)H + H+. The 3 substrates of this enzyme are beta-D-glucose, NAD+, and NADP+, whereas its 4 products are D-glucono-1,5-lactone, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. Group: Enzymes. Synonyms: EC 1.1.1.47; D-glucose dehydrogenase (NAD (P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD (P)+ 1-oxidoreductase; glucose 1-dehydrogenase; Glucose dehydrogenase; 9028-53-9. Enzyme Commission Number: EC 1.1.1.47. CAS No. 9028-53-9. Glucose Dehyrogenase. Activity: > 200 units/mg. Storage: -20°C. Form: powder; white. Source: Pseudomonas sp. EC 1.1.1.47; D-glucose dehydrogenase (NAD (P)+); hexose phosphate dehydrogenase; β-D-glucose:NAD (P)+ 1-oxidoreductase; glucose 1-dehydrogenase; Glucose dehydrogenase; 9028-53-9. Cat No: NATE-0305. | |
| Native Pseudomonas sp. Isoamylase | Isoamylase is an enzyme with system name glycogen 6-alpha-D-glucanohydrolase. This enzyme catalyses the following chemical reaction:Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins. This enzyme also readily hydrolyses amylopectin. Group: Enzymes. Synonyms: EC 3.2.1.68; debranching enzyme; glycogen alpha-1,6-glucanohydrolase; isoamylase. Enzyme Commission Number: EC 3.2.1.68. CAS No. 9067-73-6. Purity: Single major band on SDS-gel electrophoresis (MW = 71,500). Isoamylase. Activity: 180 U/mg protein (on oyster glycogen) at pH 4.0 and 40°C. 200 U/mL. Storage: 2-8°C. Form: ammonium sulfate suspension; Supplied as a suspension in 3.2 M ammonium sulfate. Source: Pseudomonas sp. EC 3.2.1.68; debranching enzyme; glycogen alpha-1,6-glucanohydrolase; isoamylase. Cat No: NATE-0360. | |
| Native Pseudomonas sp. Keratanase | Keratan-sulfate endo-1,4-beta-galactosidase (EC 3.2.1.103, endo-beta-galactosidase, keratan sulfate endogalactosidase, keratanase, keratan-sulfate 1,4-beta-D-galactanohydrolase) is an enzyme with system name keratan-sulfate 4-beta-D-galactanohydrolase. This enzyme catalyses the following chemical reaction:Endohydrolysis of (1->4)-beta-D-galactosidic linkages in keratan sulfate. Hydrolyses the 1,4-beta-D-galactosyl linkages adjacent to 1,3-N-acetyl-alpha-D-glucosaminyl residues. Group: Enzymes. Synonyms: Endo-β-galactosidase; endo-β-galactosidase; keratan sulfate endogalactosidase; keratanase; keratan-sulfate 1,4-β-D-galactanohydrolase; EC 3.2.1.103. Enzyme Commission Number: EC 3.2.1.103. CAS No. 55072-01-0. Endo-β-galactosidase. Storage: -20°C. Form: lyophilized powder. Source: Pseudomonas sp. Endo-β-galactosidase; endo-β-galactosidase; keratan sulfate endogalactosidase; keratanase; keratan-sulfate 1,4-β-D-galactanohydrolase; EC 3.2.1.103. Pack: vial of >10 units. Cat No: NATE-0364. | |
| Native Pseudomonas 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. Applications: This enzyme is useful for enzymatic determination of triglyceride in serum when coupled with l-α-glycerophosphate oxidase and glycerol kinase. usually, the reaction can be completed in 5 minutes at 37°c by using 2.5~3.0 units of the enzyme per test (3.0ml) at ph around 7.0. Group: Enzymes. Synonyms: Lipoprotein lipase; LPL; EC 3.1.1.34; Clearing factor lipase; Diacylglycerol lipas. Enzyme Commission Number: EC 3.1.1.34. CAS No. 9004-2-8. LPL. Mole weight: approx. 134 kDa. Activity: Grade??20U/mg-solid or more (containing approx. 80% of stabilizers). Stability: Stable at-20°C for at least one year. Appearance: Light brown amorphous powder, lyophilized. Source: Pseudomonas sp. Lipoprotein lipase; LPL; EC 3.1.1.34; Clearing factor lipase; Diacylglycerol lipase; Diglyceride lipase. Cat No: DIA-210. | |
| Native Pseudomonas sp. N-Acylhexosamine Oxidase | In enzymology, a N-acylhexosamine oxidase (EC 1.1.3.29) is an enzyme that catalyzes the chemical reaction:N-acetyl-D-glucosamine + O2<-> N-acetyl-D-glucosaminate + H2O2. Thus, the two substrates of this enzyme are N-acetyl-D-glucosamine and O2, whereas its two products are N-acetyl-D-glucosaminate and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. Group: Enzymes. Synonyms: N-acylhexosamine oxidase; EC 1.1.3.29; N-acyl-D-hexosamine oxidase; N-acyl-β-D-hexosamine:oxygen 1-oxidoreductase; N-acyl-D-hexosamine:oxygen 1-oxidoreductase. Enzyme Commission Number: EC 1.1.3.29. CAS No. 121479-58-1. N-Acylhexosamine Oxidase. Activity: > 20 units/mg protein. Storage: 2-8°C. Form: Suspension in 80% saturated ammonium sulfate. Source: Pseudomonas sp. N-acylhexosamine oxidase; EC 1.1.3.29; N-acyl-D-hexosamine oxidase; N-acyl-β-D-hexosamine:oxygen 1-oxidoreductase; N-acyl-D-hexosamine:oxygen 1-oxidoreductase. Cat No: NATE-0469. | |
| Native Pseudomonas sp. Oxaloacetate decarboxylase | Oxaloacetate decarboxylase is a carboxy-lyase involved in the conversion of oxaloacetate into pyruvate. It is categorized under EC 4.1.1.3. In some bacteria this enzyme is a trimer, composed of alpha, beta and gamma subunits. The beta and gamma subunits are integral membrane proteins. Native oxaloacetate decarboxylase (ec 4.1.1.3) was purified from pseudomonas sp. Applications: Useful for enzymatic determination of ast. Group: Enzymes. Synonyms: EC 4.1.1.3; Oxaloacetate decarboxylase; Oxalate beta-decarboxylase; Oxaloacetate carboxy-lyase. Enzyme Commission Number: EC 7.2.4.2 (Formerly EC 4.1.1.3). CAS No. 9024-98-0. Oxaloacetate decarboxylase. Activity: > 100 U/mg. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Pseudomonas sp. EC 4.1.1.3; Oxaloacetate decarboxylase; Oxalate beta-decarboxylase; Oxaloacetate carboxy-lyase. Cat No: DIA-161. | |
| Native Pseudomonas sp. p-Hydroxybenzoate Hydroxylase | In enzymology, a 4-hydroxybenzoate 3-monooxygenase (EC 1.14.13.2) is an enzyme that catalyzes the chemical reaction:4-hydroxybenzoate + NADPH + H+ + O2<-> protocatechuate + NADP+ + H2O. The 4 substrates of this enzyme are 4-hydroxybenzoate, NADPH, H+, and O2, whereas its 3 products are protocatechuate, NADP+, and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. Applications: This enzyme is useful for enzymatic...p-hydroxybenzoic acid hydroxylase; p-hydroxybenzoic hydroxylase; EC 1.14.13.2; 9059-23-8. Enzyme Commission Number: EC 1.14.13.2. CAS No. 9059-23-8. p-Hydroxybenzoate Hydroxylase. Mole weight: mol wt 55-~60 kDa. Activity: ~20 units/mg solid. Storage: -20°C. Form: lyophilized powder; Contains mannitol and stabilizers. Source: Pseudomonas sp. p-hydroxybenzoate hydrolyase; p-hydroxybenzoate hydroxylase; 4-hydroxybenzoate 3-hydroxylase; 4-hydroxybenzoate monooxygenase; 4-hydroxybenzoic hydroxylase; p-hydroxybenzoate-3-hydroxylase; p-hydroxybenzoic acid hydrolase; p-hydroxybenzoic acid hydroxylase; p-hydroxybenzoic hydroxylase; EC 1.14.13.2; 9059-23-8. Cat No: NATE-0564. | |
| Native Pseudomonas sp. Polymyxin Acylase | Polymyxin acylase, from Pseudomonas sp. deacylates polymyxin group antibiotics and long-chain fatty acyl groups of proteins. Polymyxin acylase has an affinity for long-chain fatty acyl proteins in human carcinoma cells. Applications: Polymyxin acylase, from pseudomonas sp., is a n-myristoyl cleaving enzyme that has been used to determine the n-myristoyl peptide sequence and may be useful in cancer research since it has antitumor activity against murine and human tumor cells. Group: Enzymes. Synonyms: Polymyxin Acylase; Peptide N-fatty acylase. CAS No. 111174-43-7. Polymyxin Acylase. Activity: > 0.1 units/mg solid. Stability: -20°C. Source: Pseudomonas sp. Polymyxin Acylase; Peptide N-fatty acylase. Cat No: NATE-0611. | |
| Native Pseudomonas sp. Protocatechuate 3, 4-dioxygenase | In enzymology, a protocatechuate 3,4-dioxygenase (EC 1.13.11.3) is an enzyme that catalyzes the chemical reaction: 3,4-dihydroxybenzoate + O2 <-> 3-carboxy-cis,cis-muconate. Thus, the two substrates of this enzyme are 3,4-dihydroxybenzoate (protocatechuic acid) and O2, whereas its product is 3-carboxy-cis,cis-muconate. This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). This enzyme participates in benzoate degradation via hydroxylation and 2,4-dichlorobenzoate degradation. It employs one cofactor, iron. Applications: This enzyme... protocatechuic 3,4-dioxygenase; protocatechuic 3,4-oxygenase. Enzyme Commission Number: EC 1.13.11.3. CAS No. 9029-47-4. Protocatechuate 3, 4-dioxygenase. Mole weight: approx. 700 kDa. Activity: Grade? 3.0U/mg-solid or more (containing approx. 40% of stabilizers). Stability: Store at -20°C (A decrease in activity of ca. 20% may occur within one year). Appearance: Light brown amorphous powder, lyophilized. Source: Pseudomonas sp. EC 1.13.11.3; Protocatechuate 3,4-dioxygenase; protocatechuate: oxygen 3,4-oxidoreductase (decyclizing); protocatechuate oxygenase; protocatechuic acid oxidase; protocatechuic 3,4-dioxygenase; protocatechuic 3,4-oxygenase. Cat No: DIA-214. | |
| Native Pseudomonas sp. Protocatechuate 3,4-Dioxygenase | In enzymology, a protocatechuate 3,4-dioxygenase (EC 1.13.11.3) is an enzyme that catalyzes the chemical reaction:3,4-dihydroxybenzoate + O2<-> 3-carboxy-cis,cis-muconate. Thus, the two substrates of this enzyme are 3,4-dihydroxybenzoate (protocatechuic acid) and O2, whereas its product is 3-carboxy-cis,cis-muconate. This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). This enzyme participates in benzoate degradation via hydroxylation and 2,4-dichlorobenzoate degradation. It employs one cofactor, iron. Applications: Prot ocatechua... has been used in the preparation of imaging buffer along with dmb-bsa (dynein motility buffer-bsa), atp and prot ocatechuate in single molecule motility assay. Group: Enzymes. Synonyms: protocatechuate 3,4-dioxygenase; protocatechuate oxygenase; protocatechuic acid oxidase; protocatechuic 3,4-dioxygenase; protocatechuic 3,4-oxygenase; 9029-47-4; EC 1.13.11.3; PCD. Enzyme Commission Number: EC 1.13.11.3. CAS No. 9029-47-4. Protocatechuate 3, 4-dioxygenase. Mole weight: mol wt ~700 kDa. Activity: > 3 units/mg solid. Storage: -20°C. Form: lyophilized powder; Supplied as lyophilized powder containing approx. 40% stabilizer. Source: Pseudomonas sp. protocatechuate 3,4- | |
| Native Pseudomonas sp. Sarcosine Dehydrogenase | In enzymology, sarcosine dehydrogenase (EC 1.5.99.1) is a mitochondrial enzyme that catalyzes the chemical reaction N-demethylation of sarcosine to give glycine. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with other acceptors. Sarcosine dehydrogenase is closely related to dimethylglycine dehydrogenase, which catalyzes the demethylation reaction of dimethylglycine to sarcosine. Both sarcosine dehydrogenase and dimethylglycine dehydrogenase use FAD as a cofactor. Sarcosine dehydrogenase is linked by electron-transferring flavoprotein (ETF) to the respiratory redox chain. Group: Enzymes. Synonyms: sarcosine dehydrogenase; EC 1.5.99.1; sarcosine N-demethylase; monomethylglycine dehydrogenase; sarcosine: (acceptor) oxidoreductase (demethylating); 37228-65-2; EC 1.5.8.3. Enzyme Commission Number: EC 1.5.99.1. CAS No. 37228-65-2. Sarcosine dehydrogenase. Activity: 0.5-1.5 units/mg protein. Storage: 2-8°C. Form: Lyophilized powder containing approx. 60% sucrose, 10% potassium phosphate buffer salts and trace EDTA. Source: Pseudomonas sp. sarcosine dehydrogenase; EC 1.5.99.1; sarcosine N-demethylase; monomethylglycine dehydrogenase; sarcosine: (acceptor) oxidoreductase (demethylating); 37228-65-2; EC 1.5.8.3. Cat No: NATE-0663. | |
| Native Pseudomonas sp. Sphingolipid ceramide N-deacylase | Sphingolipid ceramide N-deacylase (SCDase) is derived from Pseudomonas and hydrolyzes the N-acyl linkage between fatty acids and sphingosine bases in ceramides of various sphingolipids. The enzyme also catalyzes the reverse reaction and possesses transacylation activity. SCDase acts on various acidic and neutral glycosphingolipids and sphingomyelin; however, it exhibits low activity with ceramides. Applications: Hydrolysis of n-acyl linkages between fatty acids and sphingosine bases sphingolipid hydrolysis. Group: Enzymes. Synonyms: SCDase; Sphingolipid ceramide N-deacylase. SCDase. Storage: Store at -20°C until use. Store reconstituted solution in aliquots at -20°C. Avoid freeze-thaw. Form: Solution in 50 mM sodium acetate (pH 6.0) containing 0.1% Lubrol PX. Source: Pseudomonas sp. Species: Pseudomonas sp. SCDase; Sphingolipid ceramide N-deacylase. Cat No: NATE-0896. | |
| Native Pseudomonas testosteroni 3α-Hydroxysteroid Dehydrogenase | In enzymology, a 3alpha-hydroxysteroid dehydrogenase (B-specific) (EC 1.1.1.50) is an enzyme that catalyzes the chemical reaction:androsterone + NAD (P)+<-> 5alpha-androstane-3,17-dione + NAD (P)H + H+. The 3 substRates of this enzyme are androsterone, NAD+, and NADP+, whereas its 4 products are 5alpha-androstane-3,17-dione, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor, more specifically it is part of the group of hydroxysteroid dehydrogenases. Group: Enzymes. Synonyms: hydroxyprostaglandin dehydrogenase; 3α-hydroxysteroid oxidoreductase; sterognost 3α; 3α-hydroxysteroid dehydrogenase (B-specific); 3α-hydroxysteroid 3-dehydrog. Enzyme Commission Number: EC 1.1.1.50. CAS No. 9028-56-2. 3α-Hydroxysteroid Dehydrogenase. Activity: > 15 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salt and EDTA. Source: Pseudomonas testosteroni. hydroxyprostaglandin dehydrogenase; 3α-hydroxysteroid oxidoreductase; sterognost 3α; 3α-hydroxysteroid dehydrogenase (B-specific); 3α-hydroxysteroid 3-dehydrogenase (B-specific); 3α-hydroxysteroid:NAD (P)+ 3-oxidoreductase (B-specific); EC 1.1.1.50. Cat No: NATE-0007. | |
| Native Pyruvate decarboxylase from Thermophillic bacteria | Pyruvate decarboxylase (PDC) is a homotetrameric enzyme that catalyses the decarboxylation of pyruvic acid to acetaldehyde and carbon dioxide in the cytoplasm. Pyruvate decarboxylase depends on cofactors thiamine pyrophosphate (TPP) and magnesium. PDC contains a β-α-β structure, yielding parallel β-sheets. Applications: C-c bond formation: ligation of two aldehyde molecules enantioselectively to 2-hydroxy ketones; preparation of (r)-phenylacetylcarbinol (pac). Group: Enzymes. Synonyms: Pyruvate decarboxylase; EC 4.1.1.1; α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase; 9001-04-1; 2-Oxo-acid carboxy-lyase; PDC. Enzyme Commission Number: EC 4.1.1.1. CAS No. 9001-4-1. PDC. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. Pyruvate decarboxylase; EC 4.1.1.1; α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase; 9001-04-1; 2-Oxo-acid carboxy-lyase; PDC. Cat No: NATE-1159. | |
| Native Pyruvate Kinase from Thermophillic bacteria | Pyruvate kinase is an enzyme involved in glycolysis. It catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to ADP, yielding one molecule of pyruvate and one molecule of ATP. Applications: Atp regeneration in biocatalysis. Group: Enzymes. Synonyms: Pyruvate kinase; EC 2.7.1.40; 9001-59-6; phosphoenolpyruvate kinase; phosphoenol transphosphorylase; pyruvate kinase (phosphorylating); fluorokinase; fluorokinase (phosphorylating); pyruvic kinase; pyruvate phosphotransferase; ATP:pyruvate 2-O-phosphotransferase. Enzyme Commission Number: EC 2.7.1.40. CAS No. 9001-59-6. Pyruvate Kinase. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. Pyruvate kinase; EC 2.7.1.40; 9001-59-6; phosphoenolpyruvate kinase; phosphoenol transphosphorylase; pyruvate kinase (phosphorylating); fluorokinase; fluorokinase (phosphorylating); pyruvic kinase; pyruvate phosphotransferase; ATP:pyruvate 2-O-phosphotransferase. Cat No: NATE-1158. | |
| Native Rabbit Aldolase | Fructose-bisphosphate aldolase (EC 4.1.2.13), often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate. Gluconeogenesis and the Calvin cycle, which are anabolic pathways, use the reverse reaction. Glycolysis, a catabolic pathway, uses the forward reaction. Aldolase is divided into two classes by mechanism. Applications: Aldolase is used to convert fructose 1,6-diphosphate to dihydroxyacetone p...aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Enzyme Commission Number: EC 4.1.2.13. CAS No. 9024-52-6. Aldolase. Activity: Type I, lyophilized powder, > 8.0 units/mg protein; Type II, ammonium sulfate suspension, 10-20 units/mg protein. Storage: -20°C. Form: lyophilized powder. Essentially sulfate-free containing Citrate buffer salts. Source: Rabbit muscle. Species: Rabbit. aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Cat No: NATE-0048. | |
| Native Rabbit 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. ALP. Activity: 0.2-0.6 unit/mg solid (in glycine buffer). Storage: -20°C. Source: Rabbit intestine. Species: Rabbit. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Cat No: NATE-0060. | |
| Native Rabbit α-Glycerophosphate Dehydrogenase | α-glycerophosphate dehydrogenase catalyzes the conversion of dihydroxyacetone to glycerol phosphate. Protein determined by biuret. Group: Enzymes. Synonyms: α-glycerol phosphate dehydrogenase (NAD); α-glycerophosphate dehydrogenase (NAD); glycerol 1-phosphate dehydr. Enzyme Commission Number: EC 1.1.1.8. CAS No. 9075-65-4. GPDH. Activity: 100-300 units/mg protein; > 100 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Crystalline suspension in 3.2 M (NH4)2SO4 and 0.1 g/L EDTA solution, pH 6.0. Source: Rabbit muscle. Species: Rabbit. α-glycerol phosphate dehydrogenase (NAD); α-glycerophosphate dehydrogenase (NAD); glycerol 1-phosphate dehydrogenase; glycerol phosphate dehydrogenase (NAD); glycerophosphate dehydrogenase (NAD); hydroglycerophosphate dehydrogenase; L-α-glycerol phosphate dehydrogenase; L-α-glycerophosphate dehydrogenase; L-glycerol phosphate dehydrogenase; L-glycerophosphate dehydrogenase; NAD-α-glycerophosphate dehydrogenase; NAD-dependent glycerol phosphate dehydrogenase; NAD-dependent glycerol-3-phosphate dehydrogenase; NAD-L-glycerol-3-phosphate dehydrogenase; NAD-linked glycerol 3-phosphate dehydrogenase; NADH-dihydroxyacetone phosphate reductase; glycerol-3-phosphate dehydrogenase (NAD); EC 1.1.1.8; 9075-65-4; α-GDH. Cat No: NATE-0750. | |
| Native Rabbit α-Glycerophosphate Dehydrogenase-Triosephosphate Isomerase | α-glycerophosphate dehydrogenase catalyzes the conversion of dihydroxyacetone to glycerol phosphate. Applications: Α-glycerophosphate dehydrogenase was used in 2-deoxy-ribose 5-phosphate aldolase (dera) cleavage (retroaldol) assay. Group: Enzymes. Synonyms: α-glycerol phosphate dehydrogenase (NAD); α-glyceropho. Enzyme Commission Number: EC 1.1.1.8. CAS No. 9075-65-4. GPDH. Activity: TPI 750-2000 units/mg protein, GDH 75-200 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension. Mixed crystalline suspension in 3.2 M (NH4)2SO4, pH 6. Source: Rabbit muscle. Species: Rabbit. α-glycerol phosphate dehydrogenase (NAD); α-glycerophosphate dehydrogenase (NAD); glycerol 1-phosphate dehydrogenase; glycerol phosphate dehydrogenase (NAD); glycerophosphate dehydrogenase (NAD); hydroglycerophosphate dehydrogenase; L-α-glycerol phosphate dehydrogenase; L-α-glycerophosphate dehydrogenase; L-glycerol phosphate dehydrogenase; L-glycerophosphate dehydrogenase; NAD-α-glycerophosphate dehydrogenase; NAD-dependent glycerol phosphate dehydrogenase; NAD-dependent glycerol-3-phosphate dehydrogenase; NAD-L-glycerol-3-phosphate dehydrogenase; NAD-linked glycerol 3-phosphate dehydrogenase; NADH-dihydroxyacetone phosphate reductase; glycerol-3-phosphate | |
| Native Rabbit Angiotensin Converting Enzyme | Angiotensin-converting enzyme (EC 3.4.15.1), or "ACE" indirectly increases blood pressure by causing blood vessels to constrict. It does that by converting angiotensin I to angiotensin II, which constricts the vessels. For this reason, drugs known as ACE inhibitors are used to lower blood pressure. ACE, angiotensin I and angiotensin II are part of the renin-angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. ACE is secreted in the lungs and kidneys by cells in the endothelium (inner layer) of blood vessels. Group: Enzymes. Synonyms: ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dip. Enzyme Commission Number: EC 3.4.15.1. CAS No. 9015-82-1. Angiotensin Converting Enzyme. Activity: > 2.0 units/mg protein (modified Warburg-Christian). Form: lyophilized powder. Source: Rabbit lung. Species: Rabbit. ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dipeptidyl carboxypeptidase I; peptidase P; dipeptide hydrolase, peptidyl dipeptidase; angiotensin converting enzyme; kininase II; angiotensin I-converting enzyme; carboxycathepsin; dipeptidyl carboxypeptidase; "hypertensin converting enzyme" peptidyl dipeptidase I; peptidyl-dipeptide hydrolase; peptidyldipeptide hydrolase; endothelial cell peptidyl dipeptidase; peptidyl dipeptidase-4; PDH; peptidyl dipeptide hydrolase; DCP. Cat No: NATE-0015. | |
| Native Rabbit Creatine Phosphokinase | Creatine kinase plays a key role in the energy metabolism of cells with intermittently high and fluctuating energy requirements. Examples of such cells include cardiac or skeletal muscle cells and neural tissues of brain and retina. The enzyme catalyzes the reversible transfer of the phosphoryl group from phosphorylcreatine to ADP, in order to generate ATP.1 The molecular mass of the protein is found to be approximately 80 kDa Da. It is made up of 2 subunits, each having a molecular weight of 40 kDa ± 2000. The lighter subunit is present in larger amounts. Protein determined by biuret. Applications: Molecular weight: ~81 kda creatine phosphokinase is a dimer composed predom... CK; CPK; MM-CK; MB-CK; BB-CK; creatine phosphokinase; creatine phosphotransferase; phosphocreatine kinase; adenosine triphosphate-creatine transphosphorylase; Mi-CK; CK-BB; CK-MM; CK-MB; CKMiMi; MiMi-CK; 9001-15-4. Enzyme Commission Number: EC 2.7.3.2. CAS No. 9001-15-4. CK. Activity: > 150 units/mg protein. Storage: -20°C. Form: salt-free, lyophilized powder. Source: Rabbit muscle. Species: Rabbit. EC 2.7.3.2; ATP:creatine phosphotransferase; CK; CPK; MM-CK; MB-CK; BB-CK; creatine phosphokinase; creatine phosphotransferase; phosphocreatine kinase; adenosine triphosphate-creatine transphosphorylase; Mi-CK; CK-BB; CK-MM; CK-MB; CKMiMi; MiMi-CK; 9001-15-4. Cat No: NATE-0138. | |
| Native Rabbit Cytochrome P450 Reductase induced with phenobarbital | The enzyme catalyses electron transfer to cytochrome P450. This system plays a major role in detoxification of drugs and xenobiotics, activation of carcinogens, and metabolism of endogenous substrates such as steroids. Group: Enzymes. Synonyms: EC 1.6.2.4; NADPH:ferrihemoprotein oxidoreductase; NADPH:hemoprotein oxidoreductase; NADPH:P450 oxidoreductase; P450 reductase; CPR; 9039-06-9; FAD-cytochrome c reductase; NADPH-dependent cytochrome c reductase; NADPH:P-450 reductase. Enzyme Commission Number: EC 1.6.2.4. CAS No. 9023-82-9. Purity: ~90% (SDS-PAGE). CPR. Mole weight: mol wt ~80 kDa. Activity: 25-75 units/mg protein (Bradford). Storage: -20°C. Form: buffered aqueous glycerol solution. Solution in 30 mM potassium phosphate buffer, pH 7.7, and 0.1 mM EDTA containing 50% (v/v) glycerol. Source: Rabbit liver. Species: Rabbit. EC 1.6.2.4; NADPH:ferrihemoprotein oxidoreductase; NADPH:hemoprotein oxidoreductase; NADPH:P450 oxidoreductase; P450 reductase; CPR; 9039-06-9; FAD-cytochrome c reductase; NADPH-dependent cytochrome c reductase; NADPH:P-450 reductase. Cat No: NATE-0158. | |
| Native Rabbit Esterase | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Esterase from rabbit liver has been used in a study to investigate a toxic effect of carbamate insecticides. esterase from rabbit liver has also been used in a study to investigate the effect of simvastatin on expression and activity of a lipoprotein-ass ociated phospholipase a. the enzyme from creative enzymes has been used to study the effect of divalent metal ions on the activity of esterase. Group: Enzymes. Synonyms: EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; ca. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 75 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Rabbit liver. Species: Rabbit. EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase; 9016-18-6. Cat No: NATE-0238. | |
| Native Rabbit Glucose-6-Phosphatase | Glucose 6-phosphatase (EC 3.1.3.9, G6Pase) is an enzyme that hydrolyzes glucose-6-phosphate, resulting in the creation of a phosphate group and free glucose. Glucose is then exported from the cell via glucose transporter membrane proteins. This catalysis completes the final step in gluconeogenesis and glycogenolysis and therefore plays a key role in the homeostatic regulation of blood glucose levels. Applications: Glucose-6-phosphatase was used to study the effects of clausena anisata (wild hook leaf) extracts on selected diabetes-related metabolizing enzymes. Group: Enzymes. Synonyms: EC 3.1.3.9; glucose 6-phosphate phosphatase; G6Pase; 9001-39-2; glucose-6-phosphatase. Enzyme Commission Number: EC 3.1.3.9. CAS No. 9001-39-2. Purity: Protein ~30 % (balance mostly sucrose). G6Pase. Activity: > 0.05 units/mg protein. Storage: -20°C. Form: powder with sucrose. Source: Rabbit liver. Species: Rabbit. EC 3.1.3.9; glucose 6-phosphate phosphatase; G6Pase; 9001-39-2; glucose-6-phosphatase. Cat No: NATE-0269. | |
| Native Rabbit 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 phospha. Enzyme Commission Number: EC 1.2.1.12. CAS No. 9001-50-7. Glyceraldehyde-3-phosphate Dehydrogenase. Activity: > 75 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Citrate buffer salts. Source: Rabbit muscle. Species: Rabbit. 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-0281. | |
| Native Rabbit Glycerol-3-phosphate dehydrogenase | Glycerol-3-phosphate dehydrogenase (GPDH) is an enzyme that catalyzes the reversible redox conversion of dihydroxyacetone phosphate (aka glycerone phosphate, outdated) to sn-glycerol 3-phosphate. Glycerol-3-phosphate dehydrogenase serves as a major link between carbohydrate metabolism and lipid metabolism. It is also a major contributor of electrons to the electron transport chain in the mitochondria. Group: Enzymes. Synonyms: Glycerol-3-phosphate dehydrogenase; GPDH; alpha glycerol-3-phosphate dehydrogenase; alphaGPDH; glycerolphosphate dehydrogenase; EC 1.1.1.8; 9075-65-4; α-glycerol phosphate dehydrogenase (NAD); α-glycerophos. Enzyme Commission Number: EC 1.1.1.8. CAS No. 9075-65-4. Purity: Purified. GPDH. Mole weight: 75200. Activity: > 15 U/mg solid. Appearance: White to off-white powder. Storage: -20°C. Form: Lyophilized. Source: Rabbit Muscle. Species: Rabbit. Glycerol-3-phosphate dehydrogenase; GPDH; alpha glycerol-3-phosphate dehydrogenase; alphaGPDH; glycerolphosphate dehydrogenase; EC 1.1.1.8; 9075-65-4; α-glycerol phosphate dehydrogenase (NAD); α-glycerophosphate dehydrogenase (NAD); glycerol 1-phosphate dehydrogenase; glycerol phosphate dehydrogenase (NAD); glycerophosphate dehydrogenase (NAD); hydroglycerophosphate dehydrogenase; L-α-glycerol phosphate dehydrogenase; L-α-glyceroph | |
| Native Rabbit Lactate 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: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Mole weight: 140 kDa. Activity: > 250 units per mg protein. Source: Rabbit Muscle. Species: Rabbit. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: DIA-268. | |
| Native Rabbit 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. Lactic dehydrogenase (ldh) has a total molecular weight of 140 kda and is composed of 4 subunits which are designated m subunit (muscle) and h subunit (heart). these subunits may be mixed in any of 5 combinations (m4, m3h1, m2h2, mh3, and h4). skeletal muscle contains ldh that is predominately m4 with some small amounts of m3h and traces of h2h2. the h and m subunits are quite ...reductase; 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: Type I, lyophilized powder; Type II, ; Type III, ammonium sulfate suspension, Crystalline suspension in 3.2 M (NH4)2SO4 solution, pH 6.0. Source: Rabbit muscle. Species: Rabbit. 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-0413. | |
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