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| Product | Description | |
|---|---|---|
| Native Penicillium camemberti Lipase | Triacylglycerol lipase is an enzyme with system name triacylglycerol acylhydrolase. This enzyme catalyses the following chemical reaction:triacylglycerol + H2O<-> diacylglycerol + a carboxylate. Group: Enzymes. Synonyms: EC 3.1.1.3; 9001-62-1; Lipase; Triacylglycerol acylhydrolase; Triacylglycerol lipase; butyrinase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969-4-9; Meito MY 30; Tweenesterase; GA. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Stability: 2-8°C. Form: powder, slightly beige. Source: Penicillium camemberti. 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-0402. |  |
| Native Penicillium citrinum Nuclease P1 | Nuclease P1 from Penicillium citrinum is a zinc-dependent endonuclease that exhibits increased activity in the presence of low concentrations of urea. Applications: Nuclease p1 from penicillium citrinum has been used in a study to assess crystal structures using ammonium sulphate or polyethylene glycol 4000 as a precipitating agent. it has also been used in a study to investigate a method for the direct sequence analysis 20-25 nucleotides from the terinini of 5? or 3? end group labeled rna. nuclease p1 is used to improve the sensitivity of a 32p-labeling method for the detection of dna adducts. the enzyme has an optimal temperature of approximately 70 oc, but for a long incubation, a temperature below 60 oc is more suitable. it is stable in the ph range of 5-8. Group: Enzymes. Synonyms: Endonuclease P1; EC 3.1.30.1; 54576-84-0; Nuclease P1; P1 nuclease. Enzyme Commission Number: EC 3.1.30.1. CAS No. 54576-84-0. Nuclease. Mole weight: 42-50 kDa. Activity: > 200 units/mg protein (E1%/280, 3?-5?-Phosphodiesterase). Storage: 2-8°C. Form: lyophilized powder. Source: Penicillium citrinum. Endonuclease P1; EC 3.1.30.1; 54576-84-0; Nuclease P1; P1 nuclease. Pack: vial of > 250 units (using RNA substrate). Cat No: NATE-0491. | |
| Native Penicillium janthinellum Carboxypeptidase P | Membrane Pro-Xaa carboxypeptidase (EC 3.4.17.16, carboxypeptidase P, microsomal carboxypeptidase) is an enzyme. This enzyme catalyses the following chemical reaction:Release of a C-terminal residue other than proline, by preferential cleavage of a prolyl bond. This is one of the renal brush border exopeptidases. Applications: Membrane pro-xaa carboxypeptidase (ec 3.4.17.16, carboxypeptidase p, microsomal carboxypeptidase) is an enzyme.[1][2][3] this enzyme catalyses the following chemical reaction release of a c-terminal residue other than proline, by preferential cleavage of a prolyl bond this is one of the renal brush border exopeptidases. Group: Enzymes. Synonyms: Aminoacylproline Carboxypeptidase; CPP; Penicillocarboxypeptidase S-1; Proline Carboxypeptidase; EC 3.4.17.16; Membrane Pro-Xaa carboxypeptidase; carboxypeptidase P; microsomal carboxypeptidase. Enzyme Commission Number: EC 3.4.17.16. CAS No. 9075-64-3. CPP. Storage: -20°C. Form: Lyophilized powder containing sodium Citrate. Source: Penicillium janthinellum. Aminoacylproline Carboxypeptidase; CPP; Penicillocarboxypeptidase S-1; Proline Carboxypeptidase; EC 3.4.17.16; Membrane Pro-Xaa carboxypeptidase; carboxypeptidase P; microsomal carboxypeptidase. Pack: vial of > 100 units. Cat No: NATE-0157. | |
| Native Penicillium sp. α-Rhamnosidase | A thermostable Alpha-L-Rhamnosidase (Naringinase, RhamA) that catalyzes the cleavage of the bond between terminal L (+)-rhamnose and the aglycone of rhamnose-containing glycosides. The enzyme is very active on naringin but has also substantial activity with hesperidin as substrate. Group: Enzymes. Synonyms: glycoside hydrolase; RhamA; naringinase; hesperidinase; α-L-rhamnosidase A; α-L-rhamnosidase N; α-L-rhamnoside rhamnohydrolase; EC 3.2.1.40. Enzyme Commission Number: EC 3.2.1.40. CAS No. 37288-35-0. RhamA. Activity: >0.2 u/mg. Appearance: Tan Powder. Storage: 4°C. Source: Penicillium sp. glycoside hydrolase; RhamA; naringinase; hesperidinase; α-L-rhamnosidase A; α-L-rhamnosidase N; α-L-rhamnoside rhamnohydrolase; EC 3.2.1.40. Cat No: NATE-1164. | |
| Native Penicillium sp. Dextranase | An endodextranase that hydrolyzes-(1,6)-glucosidic linkages in dextran. Dextrans are undesirable compounds synthesized from sucrose by microbial contaminants during sugar production that increase viscosity of the flow and decrease industrial recovery. Dextranase has been used for hydrolyzing dextran at sugar mills in order to improve efficiency of sugar production. Applications: Dextranase from penicillium has been used in a study to assess the purification properties of an extracellular dextranase from penicillium janthinellum. dextranase from penicillium has also been used in a study to investigate the carbohydrate component of penicillium funiculosum dextranase. it has been used for the hydrolysis of carbohydate polymers, during the study of polysaccharide synthesis by phanerochaete chrysosporium. it has also been used in the synthesis of new enzymatically degradable thermo-responsive nanogels. Group: Enzymes. Synonyms: EC 3.2.1.11, dextran hydrolase; endodextranase; dextran. Enzyme Commission Number: EC 3.2.1.11. CAS No. 9025-70-1. Dextranase. Activity: 3,000 units/mg. Storage: 2-8°C. Form: lyophilized powder. Source: Penicillium sp. 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-0194. | |
| Native Phosphofructokinase from Thermophillic bacteria | Phosphofructokinase is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis. The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes. One enzyme that utilizes this reaction is phosphofructokinase (PFK), which catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the glycolytic pathway. PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains) and as an octomer in yeast (where there are 4 alpha-(PFK1) and 4 beta-chains (PFK2), the latter, like the mammalian monomers, possessing 2 similar domains). This protein may use the morpheein model of allosteric regulation. Applications: Diagnostic tests. Group: Enzymes. Synonyms: PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Enzyme Commission Number: EC 2.7.1.11. CAS No. 9001-80-3. PFK. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Cat No: DIA-403. | |
| Native Phosphotransacetylase from Leuconostoc mesenteroides | Phosphotransacetylase converts CoA to acetyl CoA. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. This enzyme participates in 3 metabolic pathways:taurine and hypotaurine metabolism, pyruvate metabolism, and propanoate metabolism. Group: Enzymes. Synonyms: phosphate acetyltransferase; phosphotransacetylase; phosphoacylase; PTA; EC 2.3.1.8; 9029-91-8. Enzyme Commission Number: EC 2.3.1.8. CAS No. 9029-91-8. PTA. Activity: > 5,000 units/mg. Storage: Below -20°C. Form: Ammonium sulfate suspension. Source: Leuconostoc mesenteroides. phosphate acetyltransferase; phosphotransacetylase; phosphoacylase; PTA; EC 2.3.1.8; 9029-91-8. Cat No: NATE-1040. | |
| Native Photinus pyralis (firefly) Luciferase | Firefly luciferase is an enzyme that catalyzes production of light from luciferin in the presence of Mg2+-ATP and oxygen. The reaction of this enzyme with luciferin, ATP, and O2 results in the emission of light. Luciferase activity can be inhibited by general anesthetics including isoflurane and ketamine/medetomidine thereby affecting the sensitivity of bioluminescence imaging. Applications: The reaction of this enzyme with luciferin, atp, and o2 results in the emission of light. luciferase can be used to detect trace amounts of atp. firefly luciferase is also one of the most commonly utilized reporter genes for the study of gene expression. the bioluminescent reaction ... been used in a study to identify the different characteristics of reporter genes in whole-cell bacterial sensors. luciferase from photinus pyralis has also been used in a study to develop a novel bioluminogenic assay for α-chymotrypsin. Group: Enzymes. Synonyms: Photinus-luciferin 4-monooxygenase (ATP-hydrolysing); firefly luciferase; luciferase (firefly luciferin); Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing); firefly luciferin luciferase; Photinus pyralis luciferase; EC 1.13.12.7; 61970-00-1. Enzyme Commission Number: EC 1.13.12.7. CAS No. 9014-00-0. Luciferase. Mole weight: mol wt 120 kDa (two subunits). Form: Lyophilized powder appr | |
| Native Photobacterium phosphoreum (Lux) Bacterial Luciferase | P. phosphoreum. Applications: Bacterial luciferase is purified from a photobacterium phosphoreum strain isolated from squid by our team and selected for its brightest luminescence. the luxab gene was amplified by pcr and cloned. the sequences of cloned α and β subunits have shown 94% and 92% identity to p24113 and p12744 proteins of photobacterium phosphoreum (swissprot entry). Group: Enzymes. Synonyms: aldehyde monooxygenase; luciferase; Vibrio fischeri luciferase; alkanal,reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing); alkanal,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing); alkanal monooxygenase (FMN); aldehyde,FMNH2:ox... presence of limiting concentrations of NADH substrate, light intensity is proportional to NAD(P)H concentration. The coupling of bacterial luciferase to FMN-NAD(P)H oxidoreductase has been used to provide ultrasensitive analytical tools for the quantification of NAD(P)H and the substrates of NADH-, NADPH- dependent enzymes (e.g. glucose, lactate, malate, ethanol, sorbitol, oxaloacetate).Bacterial Luciferase can be used for NAD(P)H quantification or in dehydrogenase-coupled assays.The enzyme is provided lyophilized, alone or with lyophilized FMN-reductase. Species: Luciferase. aldehyde monooxygenase; luciferase; Vibrio fischeri luciferase; alkanal,reduced-FMN:ox | |
| Native Pichia pastoris Alcohol Oxidase | In enzymology, an alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the chemical reaction:a primary alcohol + O2? an aldehyde + H2O2. Thus, the two substRates of this enzyme are primary alcohol and O2, whereas its two products are aldehyde and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. It employs one cofactor, FAD. Applications: Alcohol oxidase may be used to study protein translocation into peroxisomes. this product is from pichia pastoris. it has been used for the bacterial expression and immunological verification of hv-p68 cdna clones. Group: Enzymes. Synonyms: EC 1.1.3.13; 9073-63-6; alcohol oxidase; ethanol oxidase; Alcohol:oxygen oxidoreductase. Enzyme Commission Number: EC 1.1.3.13. CAS No. 9073-63-6. Activity: 10-40 units/mg protein (biuret). Storage: -20°C. Form: Buffered aqueous solution. Solution in 30% sucrose with 0.1 M phosphate buffer at pH 8.0. Source: Pichia pastoris. EC 1.1.3.13; 9073-63-6; alcohol oxidase; ethanol oxidase; Alcohol:oxygen oxidoreductase. Cat No: NATE-0047. | |
| Native Pigeon Carnitine Acetyltransferase | Carnitine acetyltransferase maintains the cellular and mitochondrial levels of acetyl-CoA, a key cofactor required for oxidative metabolism, by catalyzing an equilibrium between acetyl-CoA and acetyl-L-carnitine, a storage form of activated acetate. Carnitine acetyltransferase also maintains the pool of acetyl-CoA required for neuronal and nonneuronal acetylcholine production. Protein determined by biuret. Group: Enzymes. Synonyms: acetyl-CoA-carnitine O-acetyltransferase; acetylcarnitine transferase; carnitine acetyl coenzyme A transferase; carnitine acetylase; carnitine acetyltransferase; carnitine-acetyl-CoA transferase; CATC; 9029-90-7; carnitine O-acetyltransferase; EC 2.3.1.7; CRAT; CAT. Enzyme Commission Number: EC 2.3.1.7. CAS No. 9029-90-7. CRAT. Activity: > 70 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Crystalline suspension in 3.2 M (NH4)2SO4 solution, 50 mM potassium phosphate, 1 mM dithiothreitol, pH 7.0. Source: Pigeon breast muscle. Species: Pigeon. acetyl-CoA-carnitine O-acetyltransferase; acetylcarnitine transferase; carnitine acetyl coenzyme A transferase; carnitine acetylase; carnitine acetyltransferase; carnitine-acetyl-CoA transferase; CATC; 9029-90-7; carnitine O-acetyltransferase; EC 2.3.1.7; CRAT; CAT. Cat No: NATE-0159. | |
| Native Pigeon Citrate Synthase | Citrate synthase catalyses the conversion of Citrate to acetyl-CoA in the presence of coenzyme-A with the release of H2O and oxaloacetate. The enzyme has a molecular weight of 85 kDa and a pI of 6.1-6.6. It is inhibited by fluoroacetyl-CoA, palmitoyl-CoA, and citroyl-CoA. It is also inhibited when it is acetylated by acetic anhydride or iodinated by iodine. Group: Enzymes. Synonyms: CS; EC 4.1.3.7; EC 2.3.3.1; 9027-96-7; Citrate (Si)-synthase; (R)-citric synthase; Citrate oxaloacetate-lyase [(pro-3S)-CH2COO-->acetyl-CoA]. Enzyme Commission Number: EC 4.1.3.7. CAS No. 9027-96-7. CS. Activity: 80-150 units/mg protein (modified Warburg-Christian). Storage: 2-8°C. Form: ammonium sulfate suspension. Crystalline suspension in 2.2 M (NH4)2SO4 solution, pH 7.0, containing 6 mM phosphate and 0.5 mM Citrate. Source: Pigeon breast muscle. Species: Pigeon. CS; EC 4.1.3.7; EC 2.3.3.1; 9027-96-7; Citrate (Si)-synthase; (R)-citric synthase; Citrate oxaloacetate-lyase [(pro-3S)-CH2COO-->acetyl-CoA]. Cat No: NATE-0165. | |
| Native Pineapple Bromelain | Bromelain is a cysteine endopeptidase with broad specificity for cleavage of proteins. Bromelain may be from a stem or piece of fruit. Stem bromelain (SBM) (EC 3.4.22.32), a proteolytic enzyme, is a widely accepted phytotherapeutical drug member of the bromelain family of proteolytic enzymes obtained from Ananas comosus. Some of the therapeutic benefits of SBM are reversible inhibition of platelet aggregation, angina pectoris, bronchitis, sinusitis, surgical traumas, thrombophlebitis, pyelonephritis and enhanced absorption of drugs, particularly of antibiotics. Its anti-metastasis and anti-inflammatory activities are apparently independent of its proteolytic activity. Applications: Bromelain may be used to inhibit the biosysnthesis of proinflammatory prostaglandins. it may be used to reduce clotting efficiency. bromelain, from pineapple stem, has been used to make enzymatic hydrolysates of honeybee-collected pollen. Group: Enzymes. Synonyms: stem bromelain; EC 3.4.22.32; 37189-34-7; bromelain; pineappl. Enzyme Commission Number: EC 3.4.22.32. CAS No. 37189-34-7. Bromelain. Activity: > 3 units/mg protein; 5-15 units/mg protein. Form: Lyophilized powder containing mannitol and potassium phosphate buffer salts. Source: Pineapple stem. Species: Pineapple. stem bromelain; EC 3.4.22.32; 37189-34-7; bromelain; pineapple stem bromelain; SBM. Cat No: NATE-0665. | |
| Native Plant origin Diamine Oxidase | DAO is an enzyme (EC 1.4.3.22) composed of 642 amino acids. It is a homo-dimer of two identical subunits. Each subunit contains 2 disulfide bounds and a free cysteine with a theoretical molecular weight of 72,878 daltons per unit (a nominal molecular weight of 73 ±3 kDa is used for analytical purposes). DAO active site contains copper (II) and phenylalanine quinone: 2,4,5-trihydroxyphenylalanine quinone (TPQ). The products of the CuAO-catalysed oxidative deamination of amines such as histamine are various aldehydes, ammonia, and hydrogen peroxide. The copper is essential for activity and is believed to play a redox role in substrate turnover.Plant DAOs (histaminase) differs...oms, various plants, and animals. A review article by R. Medda, et al. in 1995 describes in detail research in this area. Applications: Dao catalyzes the oxidation of diamines (and some monoamines) to produce the aldehyde, ammonia, and h2o2. Group: Enzymes. Synonyms: EC 1.4.3.6; 9001-53-0; Amine:oxygen oxidoreductase (deaminating) (pyridoxal-containing); Diamine Oxidase; Amine oxidase (copper-containing). Enzyme Commission Number: EC 1.4.3.6. CAS No. 9001-53-0. Diamine Oxidase. Form: Tan Liquid. Source: Pisum sativum. EC 1.4.3.6; 9001-53-0; Amine:oxygen oxidoreductase (deaminating) (pyridoxal-containing); Diamine Oxidase; Amine oxidase (copper-containing). Cat No: NATE-0188. | |
| Native Plant Superoxide Dismutase | Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice by preventing the conversion of NO to peroxynitrate, an inducer of apoptosis. Group: Enzymes. Synonyms: Superoxide dismutases; EC 1.15.1.1; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; Cu,Zn-SOD; SOD. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Activity: 20,000u/g. Storage: at -4°C - 25°C, dry, dark conditions for 3 years. Form: Lyophilized powder. Source: Cactus. Superoxide dismutases; EC 1.15.1.1; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; Cu,Zn-SOD; SOD. Cat No: NATE-1868. | |
| Native Pleurotus ostreatus (mushroom) Laccase | Laccase is a blue copper oxidase that reduces molecular oxygen to water. Laccase oxidizes polyphenols, methoxy-substituted phenols and diamines, but not tyrosine. Oxidation by laccase is an one-electron reaction that generates a free radical. Applications: Laccase is polyphenol oxidase found in many plants, fungi and microorganisms. laccases may be useful in enzymatic biofuel systems, teeth whitening, textile dyeing, and in other applications that require the removal of oxygen. Group: Enzymes. Synonyms: Laccases; EC 1.10.3.2; 80498-15-3; urishiol oxidase; urushiol oxidase; p-diphenol oxidase; benzenediol:oxygen oxidoreductase. Enzyme Commission Number: EC 1.10.3.2. CAS No. 80498-15-3. Laccase. Activity: > 4.0 units/mg. Storage: -20°C. Source: Pleurotus ostreatus (mushroom). Laccases; EC 1.10.3.2; 80498-15-3; urishiol oxidase; urushiol oxidase; p-diphenol oxidase; benzenediol:oxygen oxidoreductase. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0372. | |
| Native Porcine Aconitase | Aconitase catalyses the stereo-specific isomerization of Citrate to Isocitrate via cis-aconitate in the tricarboxylic acid cycle. Aconitase is inhibited by cyanide, sulfide and copper and mercury at low concentRations. It is competitively inhibited by trans-aconitate. Aconitase contains an internal Fe-S cluster which is responsible for its activity. Crude preparation containing aconitase activity. Applications: Aconitase may be usefull in diabetes research as well as to study structural conservation between iron-responsive element binding proteins (ire-bp) and isomerases. Group: Enzymes. Synonyms: cis-aconitase; aconitase; Citrate hydro-lyase; Citrate (Isocitrate) hydro-lyase; EC 4.2.1.3; 9024-25-3; aconitate hydRatase. Enzyme Commission Number: EC 4.2.1.3. CAS No. 9024-25-3. Aconitase. Storage: -20°C. Source: Porcine heart. Species: Porcine. cis-aconitase; aconitase; Citrate hydro-lyase; Citrate (Isocitrate) hydro-lyase; EC 4.2.1.3; 9024-25-3; aconitate hydRatase. Cat No: NATE-0024. | |
| Native Porcine Acylase I | In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Protein determined by biuret. Applications: Acylase i from porcine kidney has been used to study the acylase i-catalyzed deacetylation of various s-alkyl-n-acetyl-l-cysteines and their carb...ort acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. ACY1. Activity: > 2,000 units/mg protein; 500-1,500 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Porcine kidney. Species: Porcine. aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-0031. | |
| Native Porcine Adenosine 5'-Triphosphatase | ATPases are a class of enzymes that catalyze the decomposition of ATP into ADP and a free phosphate ion. This dephosphorylation reaction releases energy, which the enzyme (in most cases) harnesses to drive other chemical reactions that would not otherwise occur. This process is widely used in all known forms of life. Some such enzymes are integral membrane proteins (anchored within biological membranes), and move solutes across the membrane, typically against their concentRation gradient. These are called transmembrane ATPases. Applications: Atpase is used to liberate inorganic phosphorus from atp. atpase, from porcine cerebral cortex, has been used in inhibition assays of na/k-atpase activity. Group: Enzymes. Synonyms: ATP phosphohydrolase; ATPase; Adenosine 5'-. Enzyme Commission Number: EC 3.6.1.3. CAS No. 9000-83-3. Adenosine 5'-Triphosphatase. Activity: > 0.3 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing 90% sucrose, 0.4% EDTA Na4 and 0.06% NaCl. Source: Porcine cerebral cortex. Species: Porcine. ATP phosphohydrolase; ATPase; Adenosine 5'-Triphosphatase; EC 3.6.1.3; adenylpyrophosphatase; ATP monophosphatase; triphosphatase; SV40 T-antigen; adenosine 5'-triphosphatase; ATP hydrolase, complex V (mitochondrial electron transport); (Ca2+ + Mg2+)-ATPase; HCO3--ATPase; adenosine triphosphatase. Cat No: NATE-0089. | |
| Native Porcine Alkaline Phosphatase | Alkaline phosphatase (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Applications: Alkaline phosphatase is used for conjugation to antibodies and other proteins for elisa, western blotting, and hist ochemical detection. alkaline phosphatase is also used to prevent dna self ligation and for radiolabeling. 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: >100U/mg. Storage: -20°C. Form: Freeze dried powder. Source: Porcine kidney. Species: Porcine. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Pack: Package size based on DEA units. Cat No: NATE-0059. | |
| Native Porcine α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. this product is from porcine pancreas and is type i-a. α-amylase, from creative enzymes, has been used in various plant studies, such as metabolism studies in arabidopsis. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Mole weight: 51-54 kDa. Activity: > 1000 units/mg protein (E1%/280); > 10 units/mg solid; 700-1400 units/mg protein (E1%/280). Storage: 2-8°C. Form: saline suspension. Suspension in 2.9 M NaCl solution containing 3 mM CaCl2. Source: Porcine pancreas. Species: Porcine. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0745. | |
| Native Porcine α-Ketoglutarate Dehydrogenase | The oxoglutarate dehydrogenase complex (OGDC) or α-ketoglutarate dehydrogenase complex is an enzyme complex, most commonly known for its role in the citric acid cycle. Group: Enzymes. Synonyms: 2-ketoglutarate dehydrogenase; 2-oxoglutarate dehydrogenase; 2-oxoglutarate:lipoate oxidoreductase; 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-succinylating); α-k. Enzyme Commission Number: EC 1.2.4.2. CAS No. 9031-2-1. AKGDH. Activity: 0.1-1.0 units/mg protein (Lowry). Storage: -20°C. Form: buffered aqueous glycerol solution. Supplied as a 50% glycerol solution containing ~9 mg per mL bovine serum albumin, 30% sucrose, 1.5 mM EDTA, 1.5 mM EGTA, 1.5 mM 2-mercaptoethanol, 0.3% TRITON(TM) X-100, 0.003% sodium azide, and 15 mM potassium phosphate, pH 6.8. Source: Porcine heart. Species: Porcine. 2-ketoglutarate dehydrogenase; 2-oxoglutarate dehydrogenase; 2-oxoglutarate:lipoate oxidoreductase; 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-succinylating); α-ketoglutarate dehydrogenase; αketoglutaric acid dehydrogenase; α-ketoglutaric dehydrogenase; α-oxoglutarate dehydrogenase; AKGDH; OGDC; ketoglutaric dehydrogenase; oxoglutarate decarboxylase; oxoglutarate dehydrogenase; oxoglutarate dehydrogenase (lipoamide); EC 1.2.4.2; 9031-02-1. Cat No: NATE-0495. | |
| Native Porcine Aminopeptidase M | Native amino peptidase M from porcine kidney. Metalloprotease that hydrolyzes N-terminal amino acids from almost all unsubstituted oligopeptides. Does not cleave X-Pro bonds or N-blocked amino acids. Useful in peptide sequencing. Inhibited by EDTA, bestatin, and amastatin. Group: Enzymes. Synonyms: Aminopeptidase M. Enzyme Commission Number: EC 3.4.11.2. CAS No. 9054-63-1. Aminopeptidase M. Activity: > 50 units/ml. Stability: Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 4 months at -20°C. Appearance: White crystalline suspension. Storage: 2 - 8°C. Source: Porcine kidney. Species: Porcine. Aminopeptidase M. Cat No: NATE-1912. | |
| Native Porcine 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. Ace is a monomer with molecular weight of ~170 kda ph range for activity: 7-8.5 temperature optimum: 37°c zinc is...-82-1. Angiotensin Converting Enzyme. Activity: > 10 units/mg protein (Bradford). Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Porcine kidney. Species: Porcine. 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 N | |
| Native Porcine Apo D-Amino Acid Oxidase | Apo-D-amino acid oxidase is entirely present as a monomeric protein, while the reconstituted holoenzyme is a dimer of 79 kDa. Group: Enzymes. Synonyms: Apo D-Amino Acid Oxidase; D-Amino Acid Oxidase; DAAO; Apo DAAO. Enzyme Commission Number: EC 1.4.3.3. CAS No. 9000-88-8. Purity: 0.9. DAAO. Activity: 25-30 U/mg protein. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Porcine Kidney. Species: Porcine. Apo D-Amino Acid Oxidase; D-Amino Acid Oxidase; DAAO; Apo DAAO. Cat No: NATE-1872. | |
| Native Porcine Calpain 1 | Caplain 1 is a neutral calcium-dependent cysteine protease containing the EF-hand motif. The protease consists of two subunits; the larger subunit has four domains that are homologous with papain and calmodulin. The smaller subunit has one domain that shares homology with calmodulin. It is activated by micromolar levels of calcium and hence, it is also called as micro-calpain. Its activation leads to cellular protein degradation, neuronal cell degeneRation, and autoimmune demyelinating diseases such as multiple sclerosis. Group: Enzymes. Synonyms: μ-calpain; calcium-activated neutral protease I; EC 3.4.22.52. Purity: > = 95% by SDS-PAGE. Calpain 1. Mole weight: 110000. Stability: > 1 year. Storage: -70°C or lower; avoid freeze/thaw cycles. Form: Frozen. Source: Porcine Erythrocytes. Species: Porcine. calpain 1, μ-calpain; calcium-activated neutral protease I; EC 3.4.22.52. Cat No: NATE-1625. | |
| Native Porcine Carboxypeptidase B | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Protein determined by biuret. Applications: Carboxypeptidase b has been used in a study to develop a non-invasive...ith carboxypeptidase b, which is a c-terminal lysine-specific endopeptidase, is measured using flow cytometry analysis. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. CAS No. 9025-24-5. CPB1. Storage: -20°C. Form: lyophilized powder. Contains HEPES buffer salts and carbohydrate. Source: Porcine pancreas. Species: Porcine. carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Cat No: NATE-0152. | |
| Native Porcine Catechol-O-methyl Transferase | Catechol-O-methyltransferase (COMT; EC 2.1.1.6) is one of several enzymes that degrade catecholamines such as dopamine, epinephrine, and norepinephrine. In Humans, catechol-O-methyltransferase protein is encoded by the COMT gene. As the regulation of catecholamines is impaired in a number of medical conditions, several pharmaceutical drugs target COMT to alter its activity and therefore the availability of catecholamines. COMT was first discovered by the biochemist Julius Axelrod in 1957. Group: Enzymes. Synonyms: catechol O-methyltransferase; COMT; COMT I; COMT II; S-COMT (soluble form of catechol-O-methyltransferase); MB-COMT (membrane-bound form of catechol-O-methyltransferase); catechol methyltransferase; catecholamine O-methyltransferase; EC 2.1.1.6; 9012-25-3; Py. Enzyme Commission Number: EC 2.1.1.6. CAS No. 9012-25-3. COMT. Activity: > 150 units/mg protein. Form: Lyophilized powder containing phosphate buffer and dithiothreitol. Source: Porcine liver. Species: Porcine. catechol O-methyltransferase; COMT; COMT I; COMT II; S-COMT (soluble form of catechol-O-methyltransferase); MB-COMT (membrane-bound form of catechol-O-methyltransferase); catechol methyltransferase; catecholamine O-methyltransferase; EC 2.1.1.6; 9012-25-3; Pyrocatechol-O-methyl Transferase; S-Adenosyl-L-methionine:catechol O-methyltransferase. Cat No: NATE-0148. | |
| Native Porcine Cholesterol Esterase | The enzyme is found primarily in pancreas and pancreatic secretions, but in other tissues as well. Bile salts, such as cholate and its conjugates, act as stabilizers of the native polymeric form of the enzyme and can protect it from proteolytic degradation in the intestine. Applications: Determination of cholesterol in serum and plasma, with cholesterol oxidase or peroxidase synthesis of optically active alcohols and carboxylic acids (via ester hydrolysis, esterification, or transesterification). 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; 9026-00-0; sterol esterase; CE. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Cholesterol Esterase. Activity: > 300 units per gram dry weight. Storage: Store at -20°C. Form: Lyophilized powder. Source: Porcine pancreas. Species: Porcine. 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-0115. | |
| Native Porcine Citrate Synthase | Citrate synthase catalyses the conversion of Citrate to acetyl-CoA in the presence of coenzyme-A with the release of H2O and oxaloacetate. The enzyme has a molecular weight of 85 kDa and a pI of 6.1-6.6. It is inhibited by fluoroacetyl-CoA, palmitoyl-CoA, and citroyl-CoA. It is also inhibited when it is acetylated by acetic anhydride or iodinated by iodine. Group: Enzymes. Synonyms: CS; EC 4.1.3.7; EC 2.3.3.1; 9027-96-7; Citrate (Si)-synthase; (R)-citric synthase; Citrate oxaloacetate-lyase [(pro-3S)-CH2COO-->acetyl-CoA]. Enzyme Commission Number: EC 4.1.3.7. CAS No. 9027-96-7. CS. Activity: > 100 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.2 M (NH4)2SO4 solution, pH 7.0. Source: Porcine heart. Species: Porcine. CS; EC 4.1.3.7; EC 2.3.3.1; 9027-96-7; Citrate (Si)-synthase; (R)-citric synthase; Citrate oxaloacetate-lyase [(pro-3S)-CH2COO-->acetyl-CoA]. Cat No: NATE-0166. | |
| Native Porcine Colipase | Colipase is a protein co-enzyme required for optimal enzyme activity of pancreatic lipase. It is secreted by the pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by trypsin. Its function is to prevent the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides. In humans, the colipase protein is encoded by the CLPS gene. Applications: Pancreatic colipase is a required co-factor for pancreatic lipase, being necessary for its activity during hydrolysis of dietary triglycerides in the presence of bile salts. Group: Enzymes. Synonyms: CLPS; colipase; pancreatic colipase. CLPS. Activity: 10 KU-20 KU/mL. Appearance: Colourless liquid. Form: Liquid. Source: Porcine pancreas. Species: Porcine. CLPS; colipase; pancreatic colipase. Cat No: NATE-0144. | |
| Native Porcine Creatine Kinase | Creatine Kinase is an enzyme present in muscle, brain, and other tissues of vertebrates that catalyzes the reversible conversion of ADP and phosphocreatine into ATP and creatine. Elevated levels of creatine phosphokinase indicates possible Brain injury or stroke, convulsions, delirium tremens, Dermatomyositis or polymyositis, electric shock, Heart attack, Inflammation of the heart muscle (myocarditis), Lung tissue death (pulmonary infarction), Muscular dystrophies and Myopathy. Group: Enzymes. Synonyms: EC 2.7.3.2; ATP:creatine phosphotransferase; CK; CPK; creatine phosphokinase; creatine phosphotransferase; phosphocreatine kinase; adenosine triphosphate-creatine transphosphorylase; 9001-15-4. Enzyme Commission Number: EC 2.7.3.2. CAS No. 9001-15-4. Activity: > 300 U/mg. Appearance: Reddish to pink lyophilized powder. Storage: Store at -20° C. Form: Lyophilized from tris acetate, DTT and EDTA, pH: 7.0. Source: Porcine Heart. Species: Porcine. EC 2.7.3.2; ATP:creatine phosphotransferase; CK; CPK; creatine phosphokinase; creatine phosphotransferase; phosphocreatine kinase; adenosine triphosphate-creatine transphosphorylase; 9001-15-4. Cat No: NATE-1884. | |
| Native Porcine Creatine Kinase BB | Creatine Kinase BB is concentrated in the brain and lungs Because the CKBB isoenzyme, CPK-1 isoenzyme is predominately found in the brain and lungs, injury to either of these organs (for example, stroke or lung injury due to a pulmonary embolism) are associated with elevated levels of this isoenzyme. Applications: Diagnostic controls, calibrators & standards; immunoassays; clinical chemistry; testing/assay validation; life science; manufacturing. Group: Enzymes. Synonyms: CPK-1; CKBB isoenyzme; CK-BB; CKB; creatine kinase, brain; CKBB; creatine kinase B-type; creatine kinase-B; creatine kinase B chain; B-CK; Brain-type creatine kinase; Creatine Kinase BB; BB-CK. Enzyme Commission Number: EC 2.7.3.2. CAS No. 9001-15-4. CK. Activity: > 100 U/mg. Stability: 3 years. Storage: Store at -20°C. Form: Lyophilized from 10 mM tris-succinate, 2 mM DTT, 2 mM EDTA, pH 6.5. Source: Porcine Brain. Species: Porcine. CPK-1; CKBB isoenyzme; CK-BB; CKB; creatine kinase, brain; CKBB; creatine kinase B-type; creatine kinase-B; creatine kinase B chain; B-CK; Brain-type creatine kinase; Creatine Kinase BB; BB-CK. Cat No: NATE-0958. | |
| Native Porcine Creatine Kinase MM | Creatine kinase, muscle also known as CKM is a creatine kinase that in humans is encoded by the CKM gene. In the figure to the right, the crystal structure of the muscle-type M-CK monomer is shown. In vivo, two such monomers arrange symmetrically to form the active MM-CK enzyme. In heart, in addition to the MM-CK homodimer, also the heterodimer MB-CK consisting of one muscle (M-CK) and one brain-type (B-CK) subunit is expressed. The latter may be an important serum marker for myocardial infarction, if released from damaged myocardial cells into the blood where it can be detected by clinical chemistry. Applications: Diagnostic controls, calibrators & standards; clinical chemistry; testing/assay validation; life science; manufacturing. Group: Enzymes. Synonyms: CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; M-CK; MM-CK. Purity: > 90% (SDS-PAGE). CK. Mole weight: 43 kDa. Stability: 2 years. Storage: Store at -20°C. Form: Liquid; 50% Glycerol, 50 mM TrisCl, 2.5 mM b-mercaptoethanol, 0.05% NaN3. Source: Porcine Skeletal Muscle. Species: Porcine. CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; M-CK; MM-CK. Cat No: NATE-0959. | |
| Native Porcine Creatine Phosphokinase | Creatine phosphokinase (CPK) is widely distributed and is primarily involved with ATP regeneration in conjunction with the contractile and transport systems. The enzyme is dimeric and exists in three isoenzyme forms: MM (muscle), MB (heart) and BB (brain). CPK from rabbit muscle has a molecular weight of 81,000 The hybrid isoenzyme (MB) has the highest concentration in the heart muscle. Therefore, determination of the serum CPK level of this isoenzyme has been used as a sensitive index for the diagnosis of myocardial infarction. Elevated levels of the BB isoenzyme of CPK have been reported in the serum of patients immediately following cardiac surgery. The CPK-BB levels in serum returned to normal by the fourth post-operative day. This may be a more sensitive diagnostic tool than the serum levels of CPK-MB isoenzyme in cardiac patients. Group: Enzymes. Syn. Enzyme Commission Number: EC 2.7.3.2. CAS No. 9001-15-4. Purity: 0.95. CK. Activity: >300 U/mg protein. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Porcine Heart. Species: Porcine. 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; Creatine kinase. Cat No: NATE-1869. | |
| Native Porcine Cytochrome c Reductase | Cytochrome c reductase is a flavoprotein that completes the oxidation-reduction chain between hexosemonophosphate and cytochrome c. The molecular weight of cytochrome c reductase is found to be approximately 78 kDa Da. The prosthetic group of cytochrome c reductase is alloxazine mononucleotide. The enzyme is very unstable with respect to low pH and to denaturation by heat. Group: Enzymes. Synonyms: EC 1.6.99.3; cytochrome c reductase; type 1 dehydrogenase; β-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine . Enzyme Commission Number: EC 1.6.99.3. CAS No. 9027-14-9. Cytochrome c Reductase. Activity: > 1.0 units/mg protein. Storage: -20°C. Form: lyophilized powder. Crude, lyophilized powder containing potassium phosphate, pH approx. 7.0. Source: Porcine heart. Species: Porcine. EC 1.6.99.3; cytochrome c reductase; type 1 dehydrogenase; β-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine dinucleotide dehydrogenase; diphosphopyridine diaphorase; DPNH diaphorase; NADH diaphorase; NADH hydrogenase; NADH oxidoreductase; NADH-menadione oxidoreductase; reduced diphosphopyridine nucleotide diaphorase; NADH:cytochrome c oxidoreductase; NADH2 dehydrogenase; NADH: (acceptor) oxidoreductase; 9027-14-9. Cat No: NATE-0179. | |
| Native Porcine D-Amino Acid Oxidase | D-Amino Acid Oxidase isolated from porcine kidney is used in the measurement of D-alanine and FAD, and in the preparation of L-amino acids from racemic mixtures. Creative Enzymes products are not intended for use in pharmaceutical applications. Applications: The measurement of d-alanine and fad, and in the preparation of l-amino acids from racemic mixtures. life science. Group: Enzymes. Synonyms: DAAO; DAO; OXDA; DAMOX; D-Amino Acid Oxidase; EC 1.4.3.3; 9000-88-8; ophio-amino-acid oxidase; L-amino acid:O2 oxidoreductase; new yellow enzyme. Enzyme Commission Number: EC 1.4.3.3. CAS No. 9000-88-8. DAAO. Activity: > 6000 U/g. Storage: Store at <-15°C. Form: A freeze-dried material. Source: Porcine kidney. Species: Porcine. DAAO; DAO; OXDA; DAMOX; D-Amino Acid Oxidase; EC 1.4.3.3; 9000-88-8; ophio-amino-acid oxidase; L-amino acid:O2 oxidoreductase; new yellow enzyme. Cat No: NATE-0180. | |
| Native Porcine Deoxyribonuclease II | Deoxyribonuclease II, also called as acid DNAse, hydrolyzes deoxyribonucleotide linkages in native and denatured DNA yielding products with 3'-phosphates. In vitro, its optimum pH range is 4.5-5.0. It also acts upon p-nitrophenyl-phosphodiesters at pH 5.6-5.9. The molecular weight is approximately 38 kDa Da. Applications: Dnase ii from creative enzymes has been used to treat transformed cells during the purification of β-lactamase. it has also been used for the preparation of adenoma tissue in a study that investigated the effect of somatoprim on growth hormone secretion in human adenoma cell cultures (hsa). deoxyribonuclease ii from porcine spleen has been used in an immunohistological study of the immune system cells in paraffin-embedded tissues. deoxyribonuclease ii from porcine spleen has also been used in a study to investigate its reassociation with the lysosomal membrane. Group: Enzymes. Synony. Enzyme Commission Number: EC 3.1.22.1. CAS No. 9025-64-3. DNASE2. Activity: 2,000-6,000 Kunitz units/mg protein (biuret). Storage: -20°C. Form: lyophilized powder. Contains sodium chloride. Source: Porcine spleen. Species: Porcine. DNASE2; deoxyribonuclease II; EC 3.1.22.1; 9025-64-3; DNase II; pancreatic DNase II; deoxyribonucleate 3'-nucleotidohydrolase; DNase II; pancreatic DNase II; acid deoxyribonuclease; acid Dnase. Cat No: NATE-0202. | |
| Native Porcine Diamine Oxidase | Diamine oxidase from porcine kidney is a homodimer consisting of 2 equal subunits with a molecular weight of 87 kDa each. Each subunit contains one molecule of pyridoxal phosphate and one atom of copper. The molecular mass of the enzyme is found to be 170 kDa. The enzyme is a glycoprotein containing 5% hexose, 3.3% glucosamine, 2.6% N-acetylglucosamine, and 0.25% N-acetylneuraminic acid. The enzyme exhibits a high affinity for concanavalin A. It catalyzes the oxidation of monoamines, diamines, and histamine to aldehydes, ammonia, and hydrogen peroxide. Optimum pH with cadverine and histamine as substrates is found to be 6.3-7.4.2 The enzyme is classified as a copper amine oxid...a luminescence-based test for determining ornithine decarboxylase activity. diamine oxidase from porcine kidney has also been used in a study to investigate n-linked oligosaccharide structures in diamine oxidase. Group: Enzymes. Synonyms: EC 1.4.3.6; 9001-53-0; Amine:oxygen oxidoreductase (deaminating) (pyridoxal-containing); Diamine Oxidase; Amine oxidase (copper-containing). Enzyme Commission Number: EC 1.4.3.6. CAS No. 9001-53-0. Diamine Oxidase. Activity: > 0.05 unit/mg solid. Storage: -20°C. Source: Porcine kidney. Species: Porcine. EC 1.4.3.6; 9001-53-0; Amine:oxygen oxidoreductase (deaminating) (pyridoxal-containing); Diamine Oxidase; Amine oxidase (copper-containing). | |
| Native Porcine Dipeptidyl Peptidase IV | Native DPPIV is a ubiquitous type II transmembrane glycoprotein and a serine protease of the S9 prolyl-oligopeptidase family. In vivo, it is synthesized with a signal peptide, which functions as the membrane anchoring domain. There is an 88% sequence homology between the human and porcine kidney enzymes. Both exist as homodimers with a subunit molecular weight of ~30 kDa. The high mannose 100 kDa DPPIV precursor is processed in the Golgi to yield a 124 kDa heavily N-and O-linked mature glycoprotein. It is then sorted to the apical membrane through the concerted action of both N-and O-linked glycans and its association with lipid microdomains. The porcine enzyme contains 18...ukocyte antigen CD26; glycylprolyl dipeptidylaminopeptidase; dipeptidyl-peptide hydrolase; glycylprolyl aminopeptidase; dipeptidyl-aminopeptidase IV; DPP IV/CD26; amino acyl-prolyl dipeptidyl aminopeptidase; T cell triggering molecule Tp103; X-PDAP. Enzyme Commission Number: EC 3.4.14.5. CAS No. 54249-88-6. Purity: >94% by SDS-PAGE. DPP IV. Activity: 1.0 U/mg; Specific Activity >40 U/mg protein. Storage: at -70°C, Avoid freeze/thaw. Form: Liquid. In 20 mM Tris-HCl, 5 mM CaCl?, 1 uM ZnCl?, 0.05% NaN?, pH 8.0. Source: Porcine Kidney. Species: Porcine. EC 3.4.14.5; 54249-88-6; DPPIV; DPP4; dipeptidyl aminopeptidase IV; Xaa-Pro-dipeptidyl-aminopeptidase; Gly-Pro naphthylamidas | |
| Native Porcine 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 3.4.21.36. CAS No. 39445-21-1. ELA1. Activity: Type I, > 15 units/mg; Type II, > 4.0 units/mg protein; Type III, > 1 units/mg protein (biuret). Storage: -20°C. Form: Type I, white powder; Type II, Type III, lyophilized powder, Contains sodium carbonate. Source: Porcine pancreas. Species: Porcine. EC 3.4.21.36, pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase; elastase-1; pancreatopeptidase; ELA1. Pack: Package size based on protein content. Cat No: NATE-0211. | |
| Native Porcine Enterokinase | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Applications: Enterokinase from porcine intestine has been used in a study to report a new experimental model of the anomalous pancreatico-biliary junction. enterokinase from porcine intestine has also ...peptide. the enzyme from creative enzymes has been used for the activation of trypsinogen in order to measure the activity of trypsin in hog pancreas. the study showed that antimicrobial treatment reduces intestinal microflora and improves protein digestive capacity without changes in villous structure of weanling pigs. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Activity: Type I, > 20 units/mg protein. Storage: -20°C. Form: salt-free, lyophilized powder. Source: Porcine intestine. Species: Porcine. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Cat No: NATE-0225. | |
| Native Porcine Esterase | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Porcine liver esterase is used to catalyze the hydrolysis of pentaacetyl catechin and epicatechin for use in pharmaceutical and industrial applications. pig liver esterase is commonly used for kinetic resolutions and assymetric synthesis in organic chemistry. esterase from porcine liver has been used in a study to assess the effect of 5-aminolaevulinic acid peptide prodrugs on photosensitization for photodynamic therapy. esterase from porcine liver has also been used in a study to investigate how site-specific atherogenic gene expression correlates with subsequent variable lesion development in c...ms: 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. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: Type I, > 15 units/mg solid; Type II, > 50 units/mg; Type III, > 150 units/mg protein (biuret). Storage: -20°C. For | |
| Native Porcine Fumarase | Fumarase catalyzes the reversible hydration of fumarate to malate. In its mitochondrial form, fumarate is involved in the Krebs Cycle, while the cytosolic form is involved in amino acid metabolism. Fumarase (fh in human) is a well-known tricarboxylic-acid-cycle enzyme found in both the cytoplasm and mit ochondria of all eukaryotes. Applications: Fumarase is used as a protein calibration standard in the purification of intact dna polymerase a/primase from mouse cells. Group: Enzymes. Synonyms: EC 4.2.1.2; fumarase; L-malate hydro-lyase; (S)-malate hydro-lyase; 9032-88-6. Enzyme Commission Number: EC 4.2.1.2. CAS No. 9032-88-6. Fumarase. Activity: 300-500 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.2 M (NH4)2SO4, 0.05 M KH2PO4, pH 7.5, 0.014 M 2-mercaptoethanol. Source: Porcine heart. Species: Porcine. EC 4.2.1.2; fumarase; L-malate hydro-lyase; (S)-malate hydro-lyase; 9032-88-6. Cat No: NATE-0267. | |
| Native Porcine γ-Glutamyltranspeptidase | γ-glutamyl transferase is an enzyme that transfers gamma-glutamyl functional groups. It is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker. GGT catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification. Other lines of evidence indicate that GGT can also exert a prooxidant role, with regulatory effects at various levels in cellular signal transduction and cellul...ase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. Activity: 2.0-6.0 units/mg solid. Storage: -20°C. Source: Porcine kidney. Species: Porcine. EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Cat No: NATE-0793. | |
| Native Porcine Glutamic-Oxalacetic Transaminase | Aspartate transaminase (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or serum glutamic oxaloacetic transaminase (SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme (EC 2.6.1.1). AST catalyzes the reversible transfer of an α-amino group between aspartate and glutamate and, as such, is an important enzyme in amino acid metabolism. AST is found in the liver, heart, skeletal muscle, kidneys, brain, and red blood cells. Serum AST level, serum ALT (alanine transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Group: Enzymes. Synonyms: EC 2.6.1.1; glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutaRate-glutamate aminotransferase; aspartate α-ketoglutaRate transaminase; aspartate aminotransferase; aspartate-2-oxoglutaRate transaminase; aspartic acid aminotr. Enzyme Commission Number: EC 2.6.1.1. CAS No. 9000-97-9. Activity: > 100 U/mg. Storage: 2-8°C. Source: Porcine heart. Species: Porcine. EC 2.6.1.1; glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutaRate-glutamate aminotransferase; aspartate α-ketoglutaRate transaminase; aspartate aminotransferase; aspartate-2-oxoglutaRate transa | |
| Native Porcine Glutamic-Pyruvic Transaminase | Alanine transaminase (ALT) is a transaminase enzyme (EC 2.6.1.2). It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate-pyruvate transaminase (SGPT) or serum glutamic-pyruvic transaminase (SGPT). ALT is found in plasma and in various body tissues, but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Group: Enzymes. Synonyms: Alanine transaminase; ALT; EC 2.6.1.2; alanine aminotransferase; ALA. Enzyme Commission Number: EC 2.6.1.2. CAS No. 9000-86-6. Activity: 100 U/mg. Storage: -20°C. Form: Freeze dried powder. Source: Porcine heart. Species: Porcine. Alanine transaminase; ALT; EC 2.6.1.2; alanine aminotransferase; ALAT; glutamic-pyruvic transaminase; glutamic-alanine transaminase; GPT; β-alanine aminotransferase; alanine-α-ketoglutarate aminotransferase; alanine-pyruvate aminotransferase; glutamic acid-pyruvic acid transaminase; glutamic-pyruvic aminotransferase; L-alanine aminotransferase; L-alanine transaminase; L-alanine-α-ketoglutarate aminotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. Cat No: NATE-0068. | |
| Native Porcine Guanylate Kinase | In enzymology, a guanylate kinase (EC 2.7.4.8) is an enzyme that catalyzes the chemical reaction:ATP + GMP<-> ADP + GDP. Thus, the two substrates of this enzyme are ATP and GMP, whereas its two products are ADP and GDP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. This enzyme participates in purine metabolism. Group: Enzymes. Synonyms: guanylate kinase; deoxyguanylate kinase; 5'-GMP kinase; GMP kinase; guanosine monophosphate kinase; ATP:GMP phosphotransferase; EC 2.7.4.8; 9026-59-9. Enzyme Commission Number: EC 2.7.4.8. CAS No. 9026-59-9. GMP kinase. Activity: > 10 units/mg protein (modified Warburg-Christian). Storage: 2-8°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol, 1 mM potassium phosphate, pH approx. 7.0, containing 0.1 mm EDTA. Source: Porcine brain. Species: Porcine. guanylate kinase; deoxyguanylate kinase; 5'-GMP kinase; GMP kinase; guanosine monophosphate kinase; ATP:GMP phosphotransferase; EC 2.7.4.8; 9026-59-9. Cat No: NATE-0310. | |
| Native Porcine heart 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. Applications: This enzyme is useful for enzymatic determination of numerous metabolites, e.g.atp, adp, glucose, creatinine, pyruvate, lactate and glycerol, and of enzyme activities, e.g.gpt, pk and cpk when coupled with the related enzymes. 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: 115 kDa±6,500. Activity: Grade? 2,000U/ml or more. Stability: Stable at 5°C for at least one year. Appearance: Crystalline suspension in 1.6M ammonium sulfate solution. Source: Porcine heart. Species: Porcine. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: DIA-206. | |
| Native Porcine Isocitric Dehydrogenase (NADP) | Isocitrate dehydrogenase (IDH) is an enzyme that catalyzes the oxidative decarboxylation of Isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2. This is a two-step process, which involves oxidation of Isocitrate (a secondary alcohol) to oxalosuccinate (a ketone), followed by the decarboxylation of the carboxyl group beta to the ketone, forming alpha-ketoglutarate. In humans, IDH exists in three isoforms:IDH3 catalyzes the third step of the citric acid cycle while converting NAD+ to NADH in the mitochondria. The isoforms IDH1 and IDH2 catalyze the same reaction outside the context of the citric acid cycle and use NADP+ as a cofactor instead of NAD+. They localize to the cytosol as well as the mitochondrion and peroxisome. Group: Enzymes. Synonyms: oxalosuccinate decarboxylase; Isocitrate dehyd. Enzyme Commission Number: EC 1.1.1.42. CAS No. 9028-48-2. IDH. Activity: Type I, 0.5-3.0 unit/mg solid; Type II, 3-20 units/mg protein. Storage: -20°C. Form: Type II, buffered aqueous glycerol solution, Solution in 50% glycerol in EDTA buffer salts, pH 6.0. Source: Porcine heart. Species: Porcine. oxalosuccinate decarboxylase; Isocitrate dehydrogenase (NADP); oxalsuccinic decarboxylase; Isocitrate (NADP) dehydrogenase; Isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; NADP-specific Isocitrate dehydrog | |
| Native Porcine Kallikrein | Tissue kallikrein is an enzyme. This enzyme catalyses the following chemical reaction:Preferential cleavage of Arg-bonds in small molecule substrates. It acts highly selectively to release kallidin (lysyl-bradykinin) from kininogen. This enzyme is formed from tissue prokallikrein by activation with trypsin. Group: Enzymes. Synonyms: tissue kallikrein; glandular kallikrein; pancreatic kallikrein; submandibular kallikrein; submaxillary kallikrein; kidney kallikrein; urinary kallikrein; kallikrein; salivary kallikrein; kininogenin; kininogenase; callicrein; glumorin; padreatin; padutin; kallidinogenase; bradykininogenase; depot-padutin; urokallikrein; dilminal D; onokrein P; 9001-01-8; EC 3.4.21.35. Enzyme Commission Number: EC 3.4.21.35. CAS No. 9001-1-8. Kallikrein. Activity: > 40 units/mg protein. Storage: 2-8°C. Source: Porcine pancreas. Species: Porcine. tissue kallikrein; glandular kallikrein; pancreatic kallikrein; submandibular kallikrein; submaxillary kallikrein; kidney kallikrein; urinary kallikrein; kallikrein; salivary kallikrein; kininogenin; kininogenase; callicrein; glumorin; padreatin; padutin; kallidinogenase; bradykininogenase; depot-padutin; urokallikrein; dilminal D; onokrein P; 9001-01-8; EC 3.4.21.35. Cat No: NATE-0362. | |
| Native Porcine 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. Applications: Diagnostic controls, calibrators & standards; clinical chemistry; testing/assay validation; life science; manufacturing. 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: ~136,700. Activity: > 100 U/mg. Stability: 2 years. Storage: Store at -20°C. Form: Lyophilized. Source: Porcine Muscle. Species: Porcine. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: NATE-0964. | |
| Native Porcine Leucine Aminopeptidase | Leucine aminopeptidase (LAP) is a proteolytic enzyme which hydrolyzes the peptide bond adjacent to a free amino group. It is called leucine aminopeptidase because it rapidly catalyzes the hydrolysis of leucine containing peptides. However, it also catalyzes the hydrolytic release of other amino acids located at the N-terminal end of various peptides and proteins. The enzyme from porcine kidney has been extensively studied. It has a molecular weight of 255,000 and it consists of four subunits each having one atom of zinc. Group: Enzymes. Synonyms: Leucine Aminopeptidase; 9054-63-1; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidas. Enzyme Commission Number: EC 3.4.11.1. Purity: 90% (biuret). LAP. Activity: >100 U/mg protein. Storage: Stable when stored at 4°C. Do not freeze. Form: Ammonium Sulfate. Source: Porcine Kidney. Species: Porcine. Leucine Aminopeptidase; 9054-63-1; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I; EC 3.4.11.1; leucyl aminopeptidase; LAP. Cat No: NATE-1879. | |
| Native Porcine Leucine Aminopeptidase, microsomal | Leucyl aminopeptidases are enzymes that preferentially catalyze the hydrolysis of leucine residues at the N-terminus of peptides and proteins. Other N-terminal residues can also be cleaved, however. LAPs have been found across superkingdoms. Identified LAPs include human LAP, bovine lens LAP, porcine LAP, Escherichia coli (E. coli) LAP (also known as PepA or XerB), and the solanaceous-specific acidic LAP (LAP-A) in tomato (Solanum lycopersicum). Group: Enzymes. Synonyms: Leucine Aminopeptidase, microsomal; 9054-63-1; leucine aminopeptidase; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL prot. Enzyme Commission Number: EC 3.4.11.1. CAS No. 9054-63-1. LAP. Activity: Type VI-S, > 12 units/mg protein (biuret); Type IV-S, 10-40 units/mg protein (Bradford). Form: Type VI-S, lyophilized powder; Type IV-S, ammonium sulfate suspension. Source: Porcine kidney. Species: Porcine. Leucine Aminopeptidase, microsomal; 9054-63-1; leucine aminopeptidase; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I; EC 3.4.11.1; leucyl aminopeptidase; LAP. Cat No: NATE-0378. | |
| Native Porcine Lipase | Triacylglycerol lipase is an enzyme with system name triacylglycerol acylhydrolase. This enzyme catalyses the following chemical reaction:triacylglycerol + H2O<-> diacylglycerol + a carboxylate. The pancreatic enzyme acts only on an ester-water interface. Applications: Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel. Group: Enzymes. Synonyms: EC 3.1.1.3; 9001-62-1; Lipase; Triacylglycerol acylhydrolase; Triacylglycerol lipase; butyrinase; tributyrinase;. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Activity: > 20,000 units/mg protein. Stability: -20°C. Form: lyophilized powder. Source: Porcine pancreas. Species: Porcine. 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; | |
| 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. | |
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