
Enzima
Subcategorias de "Enzima"
- Anidrase carbónica(196 produtos)
- Hidroxilase(36 produtos)
- MPO(2 produtos)
- Redutase(51 produtos)
- Tirosinase(71 produtos)
Foram encontrados 3620 produtos de "Enzima"
PfLDH Protein, P. falciparum, Recombinant (His)
Plasmodium falciparum lactate dehydrogenase (PfLDH) is a key enzyme for energy generation of malarial parasites and is considered to be a potential antimalarialPureza:96.1%Cor e Forma:Lyophilized PowderPeso molecular:34.9 kDa (predicted)HER3/ERBB3 Protein, Human, Recombinant (His)
HER3/ERBB3 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.Pureza:SDS-PAGE: 98.5%; SEC-HPLC: 97.6%Cor e Forma:Lyophilized PowderPeso molecular:70.2 kDa (predicted); 100-110 kDa (reducing condition, due to glycosylation)TPSAB1 protein, Cynomolgus, Recombinant (His)
TPSAB1, namely tryptase alpha/beta-1, is a serine protease with trypsinlike activity.Cor e Forma:Lyophilized PowderPeso molecular:28.57kDa (predicted). The protein migrates to 30-33kDa based on Tris-Bis PAGE result.ENPP3 Protein, Canine, Recombinant (His)
Ectonucleotide pyrophosphatase-phosphodiesterase 3 (ENPP3), a protein detected in the human uterus, has been found to play an important role in the developmentCor e Forma:Lyophilized PowderPeso molecular:96.19 kDa (predicted). Due to glycosylation, the protein migrates to 110-130 kDa based on Tris-Bis PAGE result.COX-2 Protein, Human, Recombinant (His)
PTGS2, also known as COX-2, is s component of Prostaglandin-endoperoxide synthase (PTGS).Pureza:92.1% - > 90 % as determined by SDS-PAGECor e Forma:Lyophilized PowderPeso molecular:68.5 kDa (predicted); 66 kDa (reducing conditions)Ref: TM-TMPY-01736
5µg162,00€10µg250,00€20µg400,00€50µg743,00€100µg1.190,00€200µg1.848,00€500µg3.518,00€(R)-Trolox
CAS:(R)-Trolox is a selective tyrosinase inhibitor used in food, cosmetics, and pharmaceutical products.Fórmula:C14H18O4Pureza:99.88%Cor e Forma:SolidPeso molecular:250.29Urokinase/uPA Protein, Rat, Recombinant (His)
Urokinase/uPA Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.Pureza:> 95 % as determined by SDS-PAGE - > 95 % as determined by SDS-PAGECor e Forma:Lyophilized PowderPeso molecular:47.3 kDa (predicted)EUCODIS® Lipase 013, screening grade, recombinant, from microbial sources - EL013
Lipase 13 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 35-45°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 13 was shown to hydrolyze p-Nitrophenyl esters of butyrate (87 % activity compared to octanoate), octanoate (100 %), palmitate (44 %), stearate (21 %) and arachidate (2 %).Y. lipolytica Lipase, from Yarrowia lipolytica - ELYL01
Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. The lipase from the yeast Y. lipolytica has a temperature optimum in the 30 - 40 °C range and pH optimum between pH 7 and 8.
Peroxidase, from horseradish
CAS:Catalyst for signal development in immunoassaysCor e Forma:PowderPeso molecular:44,000.00 g/molAmylase protein (Porcine)
Alpha Amylase (Amylase, α-Amylase, 1,4-α-D-glucan glucanohydrolase, glycogenase, PPA; systematic name 4-α-D-glucan glucanohydrolase; EC 3.2.1.1, CAS Number [9000-90-2]) is an enzyme that catalyzes hydrolysis of large polysaccharides into smaller fragments. Alpha amylase targets alpha bonds of 1→4 glycosidic linkages of poly- and oligosaccharides with three or more D-glucose units. One unit of Alpha Amylase will catalyze the hydrolysis of 1.0 μmol of 2-chloro-4-nitrophenyl-α-D-maltotrioside to yield 2-chloro-4-nitrophenol per minute at 37°C. Porcine pancreatic Alpha Amylase is supplied as lyophilized, off-white to white powder, lyophilized from tris chloride and mannitol, pH 7.2. Activity is ≥70U/mL, specific activity ≥100 U/mg protein. Store at -20°C on arrival.Pureza:Min. 95%α-Chymotrypsin, freeze-dried, from bovine pancreas
CAS:Please enquire for more information about alpha-Chymotrypsin, freeze-dried, from bovine pancreas including the price, delivery time and more detailed product information at the technical inquiry form on this pageFórmula:CrO4PPureza:Min. 1200 Usp U/MgPeso molecular:146.97 g/mol(R)-Mandelonitrile lyase
CAS:(R)-Mandelonitrile lyase (systematic name mandelonitrile benzaldehyde-lyase (hydrogen cyanide-forming), other names are D-oxynitrilase, D-alpha-hydroxynitrile lyase, (R)-oxynitrilase, oxynitrilase, mandelonitrile benzaldehyde-lyase, ydroxynitrile lyase; EC 4.1.2.10) is the enzyme that catalyzes the following reaction:mandelonitrile ⇌ hydrogen cyanide + benzaldehydeOne unit of (R)-mandelonitrile lyase will convert 1.0 μmol of mandelonitrile per minute under optimal conditions.Pureza:Min. 95%α Amylase, powder
CAS:Alpha Amylase, powder, is an enzyme preparation that acts as a catalyst for the hydrolysis of starch, breaking it down into simpler sugars like maltose and glucose. This enzyme is derived from microbial or fungal sources, commonly via fermentation processes using strains of bacteria or fungi specifically optimized for enzyme production.α-L-Iduronidase, recombinant, lyophilised
CAS:PAIRED PRODUCTS AVAILABLE:Pureza:Corresponds To RequirementsCor e Forma:PowderLipase CR 03
CAS:Lipase CR 03 is an industrial-grade enzyme product that is derived from microbial sources, specifically engineered for robust and efficient catalytic activity. The enzyme is extracted utilizing advanced fermentation techniques that capitalize on the prolific nature of specific strains known for lipase production. Its mode of action involves the hydrolysis of ester bonds in triglycerides, converting them into free fatty acids and glycerol. This catalytic process is critical in various biochemical pathways and industrial reactions.o-Glycosidase from streptococcus pneumoniae
CAS:o-Glycosidase (O-Glycanase, endo-a-acetylgalactosaminidase, endo-a-N-acetylgalactosaminidase; EC 3.2.1.97) is an enzyme that specifically removes N-acetylgalactosamine disaccharides, that were attached to serine's or threonine's side-chain oxygen (hence o-Glycosidase). One unit of o-Glycosidase will hydrolyze 1.0 mmole of of substrate per minute at 37 °C and pH 5.0.Pureza:Min. 95%Lipase immo Kit 01
CAS:Lipase immo Kit 01 is an advanced biochemical tool designed for the immobilization of lipase, an enzyme commonly sourced from microorganisms. This innovative kit utilizes a sophisticated immobilization matrix to enhance enzyme stability and reusability. By binding the enzyme to a solid support, the kit facilitates repeated and continuous use in various reactions without significant loss of activity.Cor e Forma:PowderPhospholipase D 040 food grade
CAS:Test sample of Cymit Quimica's Phospholipase D 040 Halal and Kosher Food grade bulk enzyme (EPLD840.6). With one of the most competitive activity rates on the global market and manufactured in Europe, this enzyme is perfect for use in food, diagnostic, therapeutic and nutraceutical industries worldwide. Phospholipase D is an enzyme that is expressed in almost all types of organisms and whose activity can be harnessed to synthesize critical raw materials, for example phosphatidylserine. Phosphatidylserine has shown itself to be an important functional ingredient in reducing cognitive dysfunction and dementia in the field of nutraceuticals. As a Halal and Kosher food grade enzyme, Cymit Quimica's Phospholipase D is an excellent candidate for a diverse variety of food industry applications. Furthermore our enzyme can be used in diagnostic assays, creating first-class drug delivery systems and APIs. Product is a lyopholised solidEUCODIS® Peroxidase 13, from bacterial, fungal and plant origin, recombinant - EP013
Peroxidase 013 belongs to the class of the heme-family peroxidases and can be utilized for catalyzing oxidation/epoxidation of unsaturated C-C bonds, N- or S-oxidation, ether cleavage and alcohol/aldehyde oxidation reactions. The Peroxidase 12 has a temperature optimum in the 20 - 40 °C range and pH optimum between pH 5 and 8.Xanthine oxidase
CAS:Xanthine oxidase is an enzyme that catalyzes the hydroxylation of hypoxanthine to xanthine and xanthine to uric acidPureza:Min. 95%Cor e Forma:PowderSialic acid aldolase - crystalline
CAS:Sialic acid aldolase - crystalline is a purified enzyme product, which is typically derived from microbial sources, such as certain bacteria, that have evolved to metabolize sialic acids. This enzyme catalyzes a reversible aldol reaction between sialic acid and pyruvate, facilitating the cleavage or formation of sialic acid from N-acetylmannosamine and pyruvate. By breaking the carbon-carbon bond in sialic acid, sialic acid aldolase plays a critical role in the degradation and biosynthesis pathways of sialic acid, which are key factors in numerous biological processes.
Cor e Forma:PowderCreatinine amidohydrolase, 150 units/mg solid, 250 U
CAS:Creatinine amidohydrolase (also sometimes reffered as creatininase, EC 3.5.2.10) is an enzyme that catalyses the following reaction: creatinine + H2O ⇌ creatine One unit of creatinine amidohydrolase will produce 1.0 µmole of creatine at pH 7.5 and 37 °C.Pureza:Min. 95%EUCODIS® Lipase 056, screening grade, recombinant, from microbial sources - EL056
Lipase 56 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 8 and temp. optimum at 40-50°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 56 was shown to hydrolyze p-Nitrophenyl esters of butyrate (79 % activity compared to octanoate), octanoate (100 %), laurate (51 %), palmitate (29 %), stearate (15 %), arachidate (0.2 %) and behenate (0.1 %).Urokinase
CAS:Urokinase (urokinase-type plasminogen activator, uPA; EC 3.4.21.73) is as serine protease. Its physiological substrate is plasminogen. Urokinase converts plasminogen into an active enzyme, plasmin, which is also a serine protease. In its active form plasmin plays an important role in dissolving blood clots. Despite its name, Urokinase is not a kinase.Fórmula:C21H25BrN2O3Pureza:(%) Min. 85%Lysozyme, lyophilized powder, min 45000 FIP U/mg
CAS:Lysozyme, lyophilized powder, min 45000 FIP U/mg, is an enzymatic product derived primarily from egg white. It is a versatile and potent enzyme known for its ability to hydrolyze the β(1-4) glycosidic bonds in the peptidoglycan layer of bacterial cell walls. This mechanism of action is particularly effective against Gram-positive bacteria due to the accessibility of their peptidoglycan layer.Cor e Forma:White PowderSARS-CoV-2 main protease
CAS:The main protease Mpro is a key protein in the lifecycle of the SARS-CoV-2 virus. Mpro cleaves the viral polyproteins at the C-terminal end of a glutamine residue in recognition sequences containing Leu-Gln-(Ser, Ala, Gly) motifs (Rut et al, 2020). As SARS-CoV-2 MPro has no closely related homologues in humans, it represents an attractive drug target (Ullrich and Nitsche, 2020). In summary, the Mpro protease is a chymotrypsin-like cysteine protease, requires homodimerisation for proteolytic activity, cleaves the viral polyproteins in 11 distinct sites, exclusively after a glutamine residue. A fluorogenic substrate for Mpro assays is Ac-Abu-Tle-Leu-Gln-AMC.The protein amount or better its concentration in solution is quantified using either A280 (absorption at 280 nm with its specific absorption coefficient) or using the Bradford assay (uses the dye Coomassie Brilliant Blue). Both of these methods quantify the total amount of protein in a sample, no matter what the oligomerization state is.Pureza:(Sds-Page) Min. 80%Cor e Forma:LyophilisateTrypsin, technical grade, freeze-dried
CAS:Trypsin (EC 3.4.21.4) is a protease that hydrolyses proteins by cleaving the peptide bond at the carboxyl side of the positively charged amino acid (Lysine or Arginine). Trypsin belongs to a family of serine proteases, as it has a serine in its active site. Trypsin can be inhibited by using trypsin inhibitor Alpha 1 Antitrypsin.Pureza:Min. 98%Carboxypeptidase P
CAS:Carboxypeptidase P (EC 3.4.17.16, also Membrane Pro-Xaa carboxypeptidase, microsomal carboxypeptidase) is a C-terminal exopeptidase, that preferentially cuts at C-terminal amino acid next to proline: ~-Pro-X → ~-Pro + X.Fórmula:C8H17N2O5PPeso molecular:252.2 g/molSucrose phosphorylase (from leuconostoc mesenteroides)
CAS:Sucrose phosphorylase (sucrose glucosyltransferase, disaccharide glucosyltransferase, systemic name Sucrose:orthophosphate α-D-glucosytransferase; EC 2.4.1.7) is an enzyme that catalyzes the following reaction:sucrose + Pi ⇌ D-fructose + α-D-glucose-1-phosphateOne unit of Sucrose phosphorylase will produce 1.0 μmole of D-fructose per minute in the presence of sucrose and phosphate under optimum conditions.Pureza:Min. 95%EUCODIS® Lipase 070, screening grade, recombinant, from microbial sources - EL070
Lipase 70 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 35-45°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 70 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (62 %), laurate (15 %), palmitate (4 %), stearate (3 %), arachidate (2 %) and behenate (0.2 %).Immobilized lipase
CAS:Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Immobilized lipases can be utilized in various reaction types, and are optimal for all reactions in organic solvents or solvent-free systems.
Cor e Forma:PowderEUCODIS® Lipase 070 immobilized, screening grade, recombinant, from microbial sources, covalent immobilization, or immobilization by absorption - EL070-I
Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. The immobilized Lipase 070 has a temperature optimum at 45 °C and pH optimum between pH 5 and 8, and is covalently immobilized on a polymer resin. Immobilized lipases can be utilized in various reaction types, and are optimal for all reactions in organic solvents or solvent-free systems.LacBuster™-S bulk for plates (β-lactamase)
CAS:This product shows beta-lactamase activity against clinically relevant beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. This product may be of particular interest for laboratory teams who require the sterility testing of biological specimens or for environmental monitoring applications.
Creatinine deiminase
CAS:Creatinine deiminase (EC 3.5.4.21) in an enzyme that catalyzes the following reaction: Creatinine + H2O → N-Methylhydantoin + NH3 One unit of creatinine deiminase will hydrolyze 1.0 µmole of creatinine to N-methylhydantoin and ammonia per minute at pH 7.5 and 37°C.Fórmula:C20H32O3SHypoxanthine phosphoribosyltransferase, liquid
CAS:Please enquire for more information about Hypoxanthine phosphoribosyltransferase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this pageLacBuster™-S 1000 (β-lactamase)
CAS:LacBuster™-S 1000 is an enzymatic product derived from microbial sources, specifically engineered for precision and efficiency. It is a beta-lactamase, which catalyzes the hydrolysis of the beta-lactam ring found in beta-lactam antibiotics such as penicillins and cephalosporins, rendering them inactive. The enzyme achieves this by breaking the amide bond within the beta-lactam ring, a critical structural component necessary for antibiotic activity.Dextran dextrinase, liquid
CAS:Please enquire for more information about Dextran dextrinase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this pagePhosphoribosyl pyrophosphate synthase, liquid
CAS:Please enquire for more information about Phosphoribosyl pyrophosphate synthase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this pageEsterase, from porcine liver, ≥15 units/mg
CAS:Porcine liver esterase (EC 3.1.1.1) is an enzyme that catalyses ester hydrolysis, producing a fatty acid and an alcohol. One unit of esterase will hydrolyze 1.0 μmole of ethyl butyrate to butyric acid and ethanol per min at pH 8.0 and 25 °C. Ethyl butyrate is available here.LacBuster™-S 5000 (β-lactamase)
CAS:LacBuster™-S 5000 is an enzymatic product, specifically a beta-lactamase, which originates from microbial sources known for their ability to produce enzymes that break down antibiotics. This product functions by hydrolyzing the beta-lactam ring of relevant antibiotics, thereby neutralizing their antibacterial activity.Isoamylase 5MU, from Pseudomonase sp., recombinant, lyophilized - EIA01
Isoamylase (also known as debranching enzyme, systemic name glycogen α-1,6-glucanohydrolase; EC 3.2.1.68) is an enzyme from the family of carbohydrolases acting specifically on α-1,6-glucosidic branch linkages in polysaccharides such as amylopectin or glycogen, but rarely hydrolyzes such bonds in pullulan. Isoamylase has been obtained from P. amyloderamosa and has a temperature optimum in the 30 – 40 °C range and pH optimum between pH 3 and 4.Amidase, from Pseudomonase aeruginosa, recombinant, lyophilized - EAM01
CAS:Amidase is a hydrolase acting on carbon-nitrogen bonds in linear amides, and can be used in hydrolysis of amides to acids. Amidase 01 is of bacterial origin (P. aeruginosa) and has been produced in E.coli.Adenosine deaminase, type X, buffered aqueous glycerol solution, >130units/mg
CAS:Adenosine deaminase catalyzes deamination of adenosine, converting it to inosine. It happens by the substituting of the amino group by a keto group. One Unit of the enzyme converts one micromole of adenosine to inosine per minute at 25°C, pH 7.4. Adenosine deaminase is also known by names of adenosine aminohydrolase, and ADA, EC 3.5.4.4.Pureza:Min. 95%Peso molecular:1,000 g/molα-Glucosidase from bacillus stearothermophilus, lyophilized powder, 300000U/g
CAS:α-Glucosidase (EC 3.2.1.20) is a glycoside hydrolase enzyme that hydrolyzes α-1,4-linked D-glucose residues to produce α-D-glucose. This enzyme has been isolated from Bacillus stearothermophilus and is used as an industrial catalyst in the production of glucose syrups. One Unit of α-Glucosidase will release 1.0 µmole of p-nitrophenol from the chromogenic substrate mimic 4-nitrophenyl α-D-glucopyranoside per minute under optimum conditions.Cor e Forma:PowderTyrosinase
CAS:Copper-containing enzyme that catalyzes the first step in the synthesis of melanin
Cor e Forma:PowderSuperoxide dismutase, porcine erythrocytes
CAS:Please enquire for more information about Superoxide dismutase, porcine erythrocytes including the price, delivery time and more detailed product information at the technical inquiry form on this pageeconoLuciferase, buffered aqueous solution
CAS:Cymit Quimica’s econoLuciferase™ (econoLuc Cymit Quimica Cat. No. L-8090) is a recombinant luciferase from the firefly Luciola lateralis that has been expressed as a luciferase-GFP fusion protein in E. coli.The luciferase enzyme has been optimized for increased thermo-stability by genetic modification to be stable for one hour at 37°C and up to two days at room temperature.Stabilized econoLuciferase™ thus overcomes the disadvantages and limitations of wild-type Luciferase, notably its short active life, outperforming enzyme from the Photinus pyralis firefly for both performance and stability.This optimized luciferase is the perfect enzyme for ATP detection assays in hygiene control, microbial tests using caged luciferins and it is the luciferase of choice for biochemical tests measuring ATP consumption and production in diverse enzymatic reactions.The product L-8090 is available on a large scale and is intended for use in the chemical, diagnostic, pharmaceutical and related industries.
Pureza:(Spec. Activity. U/Mg) Min. 5 X 10^8Isoamylase 01
CAS:Isoamylase (also known as debranching enzyme, systemic name glycogen α-1,6-glucanohydrolase; EC 3.2.1.68) is the enzyme that cleaves α-1,6-glucosidic branch linkages in carbohydrates, namely amylopectin or glycogen.
Proteinase K Solution
CAS:20mg/ml aq. solution. Proteinase K is used for the general digestion of proteins and removal of protein contamination in nucleic acids. Addition of Protease K also stabilizes nucleic acids but degrading any nucleases present. Proteinase K is active in wide range of pH range, in the presence of SDS, urea and Guanidinium chloride at low to moderate concentrations. Proteinase K is also known under names of protease K and endopeptidase K.
Cor e Forma:Clear Liquid

