Enzyme
Enzyme inhibitors are molecules that bind to enzymes and decrease their activity. These inhibitors are widely used in research to study enzyme kinetics, regulation, and the role of specific enzymes in metabolic pathways. Enzyme inhibitors are also crucial in drug development, as many therapeutic agents function by inhibiting enzymes involved in disease processes. By targeting enzymes, these inhibitors can modulate biochemical pathways and offer potential treatments for various diseases. At CymitQuimica, we provide a comprehensive selection of high-quality enzyme inhibitors to support your research in biochemistry, pharmacology, and drug discovery.
Subcategories of "Enzyme"
- Carbonic Anhydrase(196 products)
- Hydroxylase(36 products)
- MPO(2 products)
- Reductase(51 products)
- Tyrosinase(71 products)
Found 3620 products of "Enzyme"
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α-Arbutin
CAS:α-Arbutin (4-hydroxyphenyl-D-lucopyranoside) is a synthetic and functional active ingredient for skin lightening.Formula:C12H16O7Purity:99.82% - 99.94%Color and Shape:Solid PowderMolecular weight:272.25D-Tyrosine
CAS:D-Tyrosine inhibits melanin production and biofilm formation, promoting biofilm dispersal without hindering bacterial growth.Formula:C9H11NO3Purity:99.86%Color and Shape:White CrystalsMolecular weight:181.193-O-Ethyl-L-ascorbic acid
CAS:3-O-Ethyl-L-ascorbic acid is a cosmetic tyrosinase inhibitor with whitening ability and is a stabilized vitamin C derivative.Formula:C8H12O6Purity:97.35% - 99.99%Color and Shape:White To Very Pale Yellow Crystalline Powder Solid PowderMolecular weight:204.18Benzenesulfonamide
CAS:Benzenesulfonamide (Benzosulfonamide) ia an inhibitor of carbonic anhydrases.Formula:C6H7NO2SPurity:99.42% - 99.99%Color and Shape:White Crystalline PowderMolecular weight:157.19Telotristat
CAS:Telotristat, active metabolite of LX1606, is an oral tryptophan hydroxylase inhibitor with potential antiserotonergic effects.Formula:C25H22ClF3N6O3Purity:99.70%Color and Shape:SolidMolecular weight:546.93Ref: TM-T21506
5mg46.00€10mg62.00€25mg119.00€50mg187.00€100mg304.00€200mg424.00€1mL*10mM (DMSO)52.00€Urokinase/uPA Protein, Rat, Recombinant (His)
Urokinase/uPA Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.Purity:> 95 % as determined by SDS-PAGE - > 95 % as determined by SDS-PAGEColor and Shape:Lyophilized PowderMolecular weight:47.3 kDa (predicted)Necrostatin-1
CAS:Controlled ProductApplications Necroptosis is a regulated caspase-independent cell death mechanism that results in morphological features resembling necrosis. Necrostatin-1 is an inhibitor of RIP1 kinase that prevents the death of TNF-α-treated FADD-deficient Jurkat cells. Necrostatin-1 has been used to investigate the pathological importance of necroptosis in ischemic brain injury and myocardial infarction.
References Foresti, R., et al: J. Biol. Chem., 272, 18411 (1997); Cardenas, A., et al.: J. Neurochem., 74, 2041 (2000); Degterev, et al.: Nat. Chem. Biol., 1, 112 (2005); Hitomi, J., et al.: Cell, 135, 1311 (2008);Formula:C13H13N3OSColor and Shape:NeatMolecular weight:259.33PfLDH 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 antimalarialPurity:96.1%Color and Shape:Lyophilized PowderMolecular weight:34.9 kDa (predicted)CDK2 Protein, Human, Recombinant (His)
CDK2 is a member of the Ser/Thr protein kinase family.Color and Shape:Lyophilized PowderMolecular weight:35 kDa (predicted); 33 kDa (reducing conditions)Ref: TM-TMPY-04542
5µg95.00€10µg153.00€20µg245.00€50µg486.00€100µg837.00€200µg1,468.00€500µg3,037.00€HER3/ERBB3 Protein, Human, Recombinant (His)
HER3/ERBB3 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.Purity:SDS-PAGE: 98.5%; SEC-HPLC: 97.6%Color and Shape:Lyophilized PowderMolecular weight:70.2 kDa (predicted); 100-110 kDa (reducing condition, due to glycosylation)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 developmentColor and Shape:Lyophilized PowderMolecular weight:96.19 kDa (predicted). Due to glycosylation, the protein migrates to 110-130 kDa based on Tris-Bis PAGE result.TPSAB1 protein, Cynomolgus, Recombinant (His)
TPSAB1, namely tryptase alpha/beta-1, is a serine protease with trypsinlike activity.Color and Shape:Lyophilized PowderMolecular weight:28.57kDa (predicted). The protein migrates to 30-33kDa 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).Purity:92.1% - > 90 % as determined by SDS-PAGEColor and Shape:Lyophilized PowderMolecular weight: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.Formula:C14H18O4Purity:99.88%Color and Shape:SolidMolecular weight:250.29EUCODIS® 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 immunoassaysColor and Shape:PowderMolecular weight: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.Purity: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 pageFormula:CrO4PPurity:Min. 1200 Usp U/MgMolecular weight: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.Purity: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:Purity:Corresponds To RequirementsColor and Shape: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.Purity: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.Color and Shape: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 acidPurity:Min. 95%Color and Shape: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.
Color and Shape: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.Purity: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.Formula:C21H25BrN2O3Purity:(%) 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.Color and Shape: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.Purity:(Sds-Page) Min. 80%Color and Shape: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.Purity: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.Formula:C8H17N2O5PMolecular weight: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.Purity: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.
Color and Shape: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.Formula: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.Purity:Min. 95%Molecular weight: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.Color and Shape:PowderTyrosinase
CAS:Copper-containing enzyme that catalyzes the first step in the synthesis of melanin
Color and Shape: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.
Purity:(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.
Color and Shape:Clear LiquidElastase
CAS:Elastase (EC 3.4. 21.36) is a serine protease that breaks down elastin fibers. One unit of Elastase release 1 nmol of p-nitrophenol per sec from BOC-L-alanine p-nitrophenyl ester at pH 6.5 and 37°C
EUCODIS® Lipase 001, screening grade, recombinant, from microbial sources - EL001
Lipase 01 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7 and temp. optimum at 25-45°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 01 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (57 %), laurate (13 %), palmitate (9 %), stearate (6 %), arachidate (2 %) and behenate (0.1 %).Deoxyribonuclease II from porcine spleen
CAS:Deoxyribonuclease II (DNase II, deoxyribonucleate 3'-nucleotidohydrolase, acid deoxyribonuclease, acid DNase, EC 3.1.22.1) is an endonuclease that cleaves DNA, yielding 3'-phosphate-terminated polynucleotides with a free hydroxyl group on position 5'. One unit of the DNase II will increase the absorbance of 260nm light at a rate of 0.001/minute in 1 ml reaction volume at pH 4.6 and 25°C.Purity:Min. 95%L-Glutamate oxidase from streptomyces sp.
CAS:L-Glutamate oxidase is a deaminating oxidoreductase that catalyzes the conversion of L-glutamate to ketoglutarate, ammonia and hydrogen peroxide. The enzyme has been shown to have significant potential for immobilization on an insoluble support such as silica gel, which would allow it to be used in assays requiring higher concentrations of substrate. This property is important for industrial applications such as biosensor development for clinical biochemistry and the food industry.Purity:Min. 95%Color and Shape:PowderMutanolysin - lyophilized powder, >4000 units/mg
CAS:A N-Acetyl Muramidase enzyme that cleaves N-acetylmuramyl-β(1-4)-N-acetylglucosamine linkage in peptidoglycan within the bacterial cell wall.Purity:Min. 95%Catalase ECAT01™, EUCODIS® Patent: US 9951306 and EP2861715
CAS:A proprietary potent and stable alternative to chemical neutralizers such as pyruvate - for the utilization in environmental monitoring applications. Use of catalase as a supplement in media plates offers a more effective and reliable solution for safe and secure environmental monitoring of sterilization in clean rooms, isolators or production facilities by also removing remaining traces and spots of high concentration of H2O2. Currently, agar plates for monitoring disinfection or sterilization are supplemented with pyruvate, which is consumed during the neutralization of hydrogen peroxide. One of the main benefits of this catalase is its high stability in agar media at 50°C, which allows easy preparation of media and processing into plates. Due to the high stability no special storage conditions are needed and a shelf-life of > 6 months at 4-25°C can be guaranteed. Key features are:α Amylase, Porcine Pancreatic
Porcine Pancreatic Alpha Amylase is an enzyme that catalyses hydrolysis of large polysacharides into smaller fragments. Alpha amylase targets alpha bonds of 1→4 glycosidic linkages of poly- and oligosaccharides with three or more D-glucose units. Systematic name of alpha-amylase is 4-α-D-glucan glucanohydrolase, EC 3.2.1.1. One unit of Alpha Amylase will produce 1.0 mg of maltose from starch in 1 minute at pH 4.9 and 40 °C. Please enquire for more information about Alpha Amylase, Porcine Pancreatic including the price, delivery time and more detailed product information at the technical inquiry form on this pageProtein kinase LATS2
CAS:Protein kinase LATS2 is a serine/threonine kinase, which is a crucial component sourced intrinsically from cellular kinase cascades involved in cell regulation. This protein kinase is pivotal in the Hippo signaling pathway, which regulates cell growth, apoptosis, and stem cell renewal. LATS2 is part of the core kinase cascade that, upon activation, phosphorylates and inhibits the activity of the transcriptional co-activators YAP and TAZ, thereby controlling their transcriptional activity. This inhibition is key to maintaining proper cell proliferation and preventing uncontrolled cell growth that could lead to tumorigenesis.Purity:Min. 95%α Amylase, Porcine Pancreatic
Alpha Amylase is an enzyme that catalyses hydrolysis of large polysacharides into smaller fragments. Alpha amylase targets alpha bonds of 1→4 glycosidic linkages of poly- and oligosaccharides with three or more D-glucose units. Systematic name of alpha-amylase is 4-α-D-glucan glucanohydrolase, EC 3.2.1.1. One unit of Alpha Amylase will produce 1.0 mg of maltose from starch in 1 minute at pH 4.9 and 40 °C.Collagenase
CAS:Collagenase is an enzymes that is responsible for breaking peptide bonds in collagen
Formula:C12H18ClNO3Color and Shape:Brown Slightly Yellow PowderMolecular weight:259.73 g/molXylanase, powder
CAS:Xylanase is an enzymatic product, which is typically derived from microbial sources such as fungi or bacteria. Its primary function involves catalyzing the hydrolysis of xylan, a major hemicellulose component found in plant cell walls. Through breaking down xylan into xylose and other oligosaccharides, xylanase significantly modifies plant material structure.Cellulase, powder
CAS:Cellulase, powder is an enzymatic product derived from microbial fermentation, specifically sourced from fungi or bacteria known for their cellulolytic activity. Cellulase acts by catalyzing the hydrolysis of cellulose, breaking it down into smaller polysaccharides and glucose. This decomposition occurs through synergistic action by three main components: endoglucanases, exoglucanases, and β-glucosidases, each targeting specific bonds in the cellulose structure, resulting in its complete breakdown.PNGaseF, wildtype, liquid, recombinant, from Elizabethkingia miricola
CAS:PNGase F is an endoglycosidase that can remove all N-linked carbohydrates from proteins, which is useful if you are uncertain whether the carbohydrate is N-linked or O-linked to the protein or is a high mannose type. It is also the enzyme of choice when you need to study or use the naked protein in your application. PNGase functions as a glycoamidase and hydrolyzes the amide bond between the innermost GlcNac of mammalian asparagine-linked mannose oligosaccharides, whether they are high, complex or hybrid. Specifically, the glycan is removed from the asparagine residue which through the deamination reactions becomes aspartic acid.This enzyme is available as a large-scale bulk supply of liquid enzyme solution. See our PNGase F available as vials for research applications with pre-defined quantities (>250 kU/vial) of liquid enzyme solution.Also available is our endoH enzymes (EEH01.3 - research quantities and EEH01.7 - large scale bulk supply).Streptodornase
CAS:Streptodornase is a DNase that is often present as in the streptokinase preparations as an impurity.
Heat Labile Uracil-DNA Glycosylase, 500 units
Heat Labile Uracil-DNA Glycosylase, 500 units, is an enzyme designed for molecular biology applications, primarily derived from a recombinant bacterial source. This enzyme effectively removes uracil from DNA molecules at temperatures that preserve the integrity of the DNA. With its heat-labile properties, the enzyme can be inactivated at moderately elevated temperatures, making it ideal for processes that require precise control over enzyme activity.PNGaseF, wildtype, liquid, recombinant, from Elizabethkingia miricola
CAS:PNGase F is an endoglycosidase that can remove all N-linked carbohydrates from proteins, which is useful if you are uncertain whether the carbohydrate is N-linked or O-linked to the protein or is a high mannose type. It is also the enzyme of choice when you need to study or use the naked protein in your application. PNGase functions as a glycoamidase and hydrolyzes the amide bond between the innermost GlcNac of mammalian asparagine-linked mannose oligosaccharides, whether they are high, complex or hybrid. Specifically, the glycan is removed from the asparagine residue which through the deamination reactions becomes aspartic acid.This enzyme is available as vials for research applications with pre-defined quantities (>250 kU/vial) of liquid enzyme solution . See our large-scale bulk supply of PNGase F for the deglycosylation of proteins in manufacture.Also available is our endoH enzymes (EEH01.3 - vials for research and EEH01.7 - large scale bulk supply).Xylanase 1, thermostable
CAS:Xylanase (Endo-1,4-β-xylanase, 1,4-β-D-Xylanxylanohydrolase, systematic name 4-β-D-xylan xylanohydrolase; EC 3.2.1.8) is an enzyme that digests polysaccharide xylan by hydrolyzing (1→4)-β-D-xylosidic linkages. One unit of Xylanase will hydrolyze 1.0 μmole of chromogenic substrate mimic per minute (available here) under optimal reaction conditions.
Color and Shape:Powderβ-Lactamase Kit 01
CAS:Beta-lactamase enzymes demonstrate 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.Lipase 009
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.EndoH, wildtype, liquid, recombinant, from Streptomyces plicatus
CAS:Endoglycosidase H (Endo H) is a highly specific enzyme that cleaves N-linked oligosaccharides from glycoproteins, targeting high-mannose and certain hybrid-type N-glycans. It does not act on complex-type N-glycans, which are typically processed further in the Golgi apparatus. Due to its specificity, Endo H is widely used in research to study intracellular protein trafficking and post-translational modifications, particularly those occurring during glycoprotein maturation.This product is available as vials for research applications with pre-defined quantities (>250 kU/vial) of liquid enzyme solutionSee our EndoH (EEH01.7) available for large-scale bulk supply of liquid enzyme solution for the deglycosylation of proteins in manufacture.For removal of all N-linked carbohydrates from proteins see Cymit Quimica's PNGase F enzymes (PNG01.3 - vials for research and PNG01.7 - large-scale bulk supply)EUCODIS® Lipase 064, screening grade, recombinant, from microbial sources - EL064
Lipase 64 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7 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 64 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (0.5 %) and laurate (0.1 %).Cocarboxylase tetrahydrate
CAS:Cocarboxylase tetrahydrate is a coenzyme form of vitamin B1; cofactor for enzymes involved in carbohydrate catabolismFormula:C12H18N4O7P2S·4H2OPurity:Min 96%Color and Shape:White PowderMolecular weight:496.37 g/molFructose-6-phosphate Kinase
CAS:Fructose-6-phosphate kinase (Phosphofructokinase, PFK, EC 2.7.1.11) is an enzyme that catalyzes the following reaction: F6P + ATP ⇌ F1,6BP + ATP One unit of PFK will convert 1.0 μmole of fructose 6-phosphate and ATP to fructose 1,6-diphosphate and ADP per minute at pH 9.0 at 30 °C.Purity:Min. 95%Glucose oxidase from aspergillus niger - activity > 6000 u/g
CAS:Glucose oxidase is an enzyme thata catalyses the rapid conversion of glucose into non-fermentable gluconic acid in the presence of oxygen (O2). Its used is widely expanded with many applications in the chemical and pharmaceutical industry, food and beverage, clinical studies and biotechnology, among others. It medical diagnosis, glucose oxidase serves as a biosensor for detecting and determining the different levels of glucose in blood samples.Formula:C6H12O6Color and Shape:PowderMolecular weight:180.16 g/molLipase
CAS:Porcine pancreatic lipase is an enzyme that has been shown to have antioxidative properties. It is used as an additive in biodiesel production, where it prevents the formation of trans fatty acids and reduces the amount of free radicals. This enzyme has been shown to have lipase, protease, and amylase activities by using surface methodology. Porcine pancreatic lipase can be used for the treatment of autoimmune diseases such as multiple sclerosis and rheumatoid arthritis. This enzyme interacts with other enzymes such as lipases, proteases, and amylases to catalyze reactions on surfaces. It can be used for asymmetric synthesis by hydrogen bonding or by forming an intermediate complex with metal ions.Purity:Min. 95%Color and Shape:SolidAdenosine deaminase, type X, buffered aqueous glycerol solution
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.Molecular weight:1,000 g/molLacBuster™ TSA broad range β-lactamase contact plates, 10 plates per pack, barcoded
CAS:A general purpose growth medium supplemented with LacBuster™ to effectively neutralize beta-lactam antibiotics. This product is suitable for the cultivation of a wide variety of microorganisms for environmental monitoring within the pharmaceutical industry and for high performance monitoring of your isolators and clean rooms during beta lactam manufactureLacBuster™ TSA broad range β-lactamase settle plates, 10 plates per pack, barcoded
CAS:A general purpose growth medium supplemented with LacBuster™ to effectively neutralize beta-lactam antibiotics. This product is suitable for the cultivation of a wide variety of microorganisms for environmental monitoring within the pharmaceutical industry and for high performance monitoring of your isolators and clean rooms during beta lactam manufactureLuciferase - from Photinus pyralis (firefly)
CAS:Luciferase enzyme from Photinus pyralis (firefly), which catalyzes the oxidation of firefly luciferin. This reaction depends on the presence of oxygen and ATP and causes the bioluminescence seen in firefliesPurity:(Gel Electrophoresis) Min. 98%Color and Shape:PowderLacBuster™ TSA broad range β-lactamase contact plates, 10 plates per pack, barcoded
CAS:A general purpose growth medium supplemented with LacBuster™ to effectively neutralize beta-lactam antibiotics. This product is suitable for the cultivation of a wide variety of microorganisms for environmental monitoring within the pharmaceutical industry and for high performance monitoring of your isolators and clean rooms during beta lactam manufactureLipase 014
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.LacBuster™ TSA broad range β-lactamase settle plates, 10 plates per pack, barcoded
CAS:A general purpose growth medium supplemented with LacBuster™ to effectively neutralize beta-lactam antibiotics. This product is suitable for the cultivation of a wide variety of microorganisms for environmental monitoring within the pharmaceutical industry and for high performance monitoring of your isolators and clean rooms during beta lactam manufactureEUCODIS® Lipase 044, screening grade, recombinant, from microbial sources - EL044
Lipase 44 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-10 and temp. optimum at 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 44 was shown to hydrolyze p-Nitrophenyl esters of butyrate (70 % activity compared to octanoate), octanoate (100 %), laurate (88 %), palmitate (6 %) and stearate (2 %).
Phosphoenolpyruvate carboxylase
CAS:Phosphoenolpyruvate carboxylase is an enzyme, often found naturally in the cytosol of plant cells, which is derived primarily from various plant species. It plays a crucial role in the photosynthetic process, particularly in C4 and CAM plants. By catalyzing the irreversible carboxylation of phosphoenolpyruvate (PEP) to oxaloacetate, this enzyme facilitates the fixation of carbon dioxide, a vital step in the conversion of carbon dioxide into organic compounds during photosynthesis.Purity:Min. 95%Lipase 016
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.
Lipase 065
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.Lipase 038
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.Lipase 003
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.
EUCODIS® Lipase 003, screening grade, recombinant, from microbial sources - EL003
Lipase 03 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7 and temp. optimum at 20-50°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 03 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (90 %), laurate (28 %), palmitate (14 %), stearate (9 %), arachidate (2 %) and behenate (3 %).Lipase 044
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.Dihydrofolate reductase
CAS:Dihydrofolate reductase (DHFR, 1.5.1.3) is a NADP+/NADPH-dependent oxidoreductase, that reduces dihydrofolate to tetrahydrofolate in the following reaction: dihydrofolate + NADPH + H+ ⇌ tetrahydrofolate + NADP+One unit of dihydrofolate reductase will convert 1.0 μmole of dihydrofolic acid into tetrahydrofolic acid in 1 minute at pH 7.5, 22°C and presence of NADPH.
Purity:Min. 95%Lipase 037
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.
