Enzyme
Les inhibiteurs d'enzymes sont des molécules qui se lient aux enzymes et diminuent leur activité. Ces inhibiteurs sont largement utilisés en recherche pour étudier la cinétique enzymatique, la régulation et le rôle spécifique des enzymes dans les voies métaboliques. Les inhibiteurs d'enzymes sont également cruciaux dans le développement de médicaments, car de nombreux agents thérapeutiques agissent en inhibant les enzymes impliquées dans les processus pathologiques. En ciblant les enzymes, ces inhibiteurs peuvent moduler les voies biochimiques et offrir des traitements potentiels pour diverses maladies. Chez CymitQuimica, nous offrons une sélection complète d'inhibiteurs d'enzymes de haute qualité pour soutenir vos recherches en biochimie, pharmacologie et découverte de médicaments.
Sous-catégories appartenant à la catégorie "Enzyme"
- Anhydrase carbonique(196 produits)
- Hydroxylase(36 produits)
- MPO(2 produits)
- Réductase(51 produits)
- Tyrosinase(71 produits)
3620 produits trouvés pour "Enzyme"
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Urate oxidase (from Yeast)
CAS :Urate Oxidase, also known as uricase, catalizes the following reaction: Uric acid + O2 + H2O → 5-hydroxyisourate + H2O2.Formule :C18H26N5O14PDegré de pureté :Min. 95%Masse moléculaire :567.4 g/molalpha Amylase enzyme
Alpha Amylase (Amylase, α-Amylase, 1,4-α-D-glucan glucanohydrolase, glycogenase, systematic name 4-α-D-glucan glucanohydrolase; EC 3.2.1.1, CAS Number [9000-90-2]) 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. 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. Human pancreatic Alpha Amylase is supplied as clear, colorless to light yellow liquid solution at ≥400U/mL, specific activity ≥100 U/mg protein.Store at 2-8 °C on arrival.Degré de pureté :Min. 95%Ribonuclease A
CAS :Ribonuclease A (RNase A) is widely used to break down RNA in DNA purification. RNase A catalyzes the endonucleolytic cleavage of phosphodiester bonds of RNA.Serratiopeptidase
CAS :Serratiopeptidase (serratio peptidase, serratia peptidase, serrapeptidase, serratia E-15 protease, serralysin, serrapeptase; EC 3.4.24.40) is a proteolitic enzyme (proteinase) that is produced by Serratia marcescens.Degré de pureté :Min. 95%Couleur et forme :PowderEUCODIS® CalB01 IA, engineered variant of Candida antarctica Lipase B, immobilized by adsorption on hydrophobic carrier - ELCB01IA
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 CalB01 IA lipase has been immobilized on a hydrophobic carrier by adsorption. The immobilized CalB01 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.Butyrylcholinesterase
Butyrylcholinesterase (BCHE, BuChE, PCHE, pseudocholinesterase, plasma cholinesterase, Acylcholine acyl-hydrolase, Choline esterase; EC 3.1.1.8, CAS No [9001-08-5]) is an enzyme that made in the liver and found mainly in blood plasma. It catalyzes the following reaction: Acylcholine + H2O → choline + carboxylic acidOne unit of Butyrylcholinesterase will change absorbance by 0.2 milliunits (mA) per minute at optimal buffer conditions and 37 ̊C. Equine serum butyrylcholinesterase is supplied as white to pale grey-green powder with activity of ≥50U/mg and specific activity of ≥300U/mg protein. It can be dissolved at 5 mg/mL concentration in 50 mM Tris-HCl pH 7.3 - 7.5, giving colorless to slightly green solution. Equine serum butyrylcholinesterase is activated by Ca2+, optimum pH 7-8, KM=18 µM (butyrylthiocholine at 25°C). Store at -20°C on arrival.Aminopeptidase I from streptomyces griseus
CAS :Aminopeptidase I is a specialized proteolytic enzyme derived from the actinobacterium Streptomyces griseus. This enzyme functions by catalyzing the cleavage of amino acids from the N-terminus of peptides, which plays a pivotal role in protein metabolism and regulation. The source of this enzyme, Streptomyces griseus, is well-regarded for producing a variety of bioactive compounds owing to its rich genetic and biochemical repertoire.Alcohol Oxidase - vacuum-dried powder, >0.6 units/mg solid
CAS :Alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the following chemical reaction: a primary alcohol + O2 + H2O ⇌ an aldehyde + H2O2 One unit of alcohol oxidase will oxidize 1.0 µmole of methanol to formaldehyde per min at pH 7.5 and 25 °C.Lipoprotein lipase
CAS :Lipoprotein lipase is a critical enzyme used to modulate lipid processing, primarily sourced from mammalian tissues. It functions by hydrolyzing triglycerides present in circulating chylomicrons and very low-density lipoproteins. This enzymatic process liberates free fatty acids, which can subsequently be utilized as energy by peripheral tissues or stored in adipose tissue. Lipoprotein lipase is pivotal in lipid metabolism, participating in maintaining homeostasis of plasma lipid levels.Degré de pureté :Min. 95%Plasmin
CAS :Plasmin, human is a serin protease which present in the blood and is involved in the cleavage of cross-linked fibrin, a process known as fibrinolysis.One unit will produce one micromole of P-Nitroanilide from D-Val-Leu-Lys-P-Nitroanilide per minute at pH 7.5 at 37°CProtease from Streptomyces griseus
CAS :Protease enzymes break down proteins and are essential for many biological processes, including digestion, cellular regulation and blood clotting. They are also used in many industrial and biotechnological applications for example in food processing and in detergents.
Degré de pureté :Min. 95%Couleur et forme :PowderCellulose catalase
Cellulose catalase is an enzyme-based product, designed specifically to act as a catalyst in the oxidative processes associated with cellulose applications. It is derived from a microbial source, where bacilli or fungi are employed to produce robust catalase enzymes in a fermentation process. The mode of action involves the catalase enzyme’s ability to facilitate the decomposition of hydrogen peroxide into water and oxygen, thereby reducing oxidative damage during cellulose processing.
C. rugosa Lipase 02, CRL 2 from Candida rugosa - ELCR02
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 02 from the yeast Candida rugosa has a temperature optimum in the 30 - 50 °C range and pH optimum between pH 7 and 8.Transglutaminase from guinea pig liver
CAS :Transglutaminase (2.3.2.13) is an enzyme that catalyzes formation of isopeptide bonds between the γ-carboxamide groups ( -(C=O)NH2 ) of glutamine side chains and amino groups. The donor of the amino group is usually (but not always) an ε-amino group ( -NH2 ) of lysine residue. The reaction also releases ammonia: Gln-(C=O)NH2 + NH2-Lys → Gln-(C=O)NH-Lys + NH3One unit of transglutaminase will catalyze the formation of 1.0 μmole transglutamination product per min at pH 6.0 and 37 °C.Degré de pureté :Min. 95%Chloroperoxidase, aqueous suspension
CAS :Chloroperoxidase (also known as chloride peroxidase, systemic name chloride:hydrogen-peroxide oxidoreductase, EC 1.11.1.10) is an enzyme that catalyzes chlorination of organic compounds. Overall reaction is the following:R-H + Cl− + H2O2 + H+ → R-Cl + 2 H2O; reaction intermediate is hypochlorous acid (HOCl). One unit of chloroperoxidase will convert 1.0 μmole of substrate per minute.
Couleur et forme :PowderL-Asparaginase
CAS :L-Asparaginase (EC 3.5.1.1) is an enzyme that catalyzes the following reaction: L-Asparagine + H2O → L-Aspartate + NH4+ One unit will yield 1.0 μmole of ammonia from L-asparagine per min at pH 8.6 and 37 °C.Degré de pureté :Min. 95%Chymase
CAS :Chymase (alternative names mast cell protease 1, mast cell serine proteinase, skeletal muscle protease, EC 3.4.21.39) is a serine protease, found in mast cells and basophil granulocytes.Degré de pureté :Min. 95%EUCODIS® Nitrilhydratase 23, recombinant enzyme - ENH023
Nitrile hydratase 23 recombinantly expressed in E. coli comes in a freeze-dried formulation. Nitrile hydratases can be utilized to convert nitriles into their corresponding amides, e.g. to produce acrylamide from acrylonitrile. Additional applications include the removal of nitriles from industrial wastewater. Our nitrile hydratases have been tested for hydrolysis of the following substrates:cyclohexanecarbonitrile, cinnamonitrile, benzonitrile, methacrylonitrile, pivalonitrile.
Sphingomyelinase from bacillus cereus
CAS :Sphingomyelinase (SMase, Sphingomyelin phosphodiesterase, systematic name sphingomyelin cholinephosphohydrolase; EC 3.1.4.12) is an enzyme that hydrolyses sphingomyelin into phosphocholine and ceramide. One unit of sphingomyelinase will hydrolyze 1.0 µmole of chromogenic substrate analogue per minute at pH 7.4 and 37 °C.Degré de pureté :Min. 95%Cathepsin B from human placenta
CAS :Cathepsin B is a lysosomal proteolytic enzyme of the cysteine protease family. It is present in all mammalian cells. It is essential for the intracellular protein turnover. Cathepsin B may be a useful tool in Alzheimer′s research, as it may have a role in the natural defense against the disease.Degré de pureté :Min. 95%Phosphorylase B from rabbit muscle
CAS :Phosphorylase B is an enzymatic protein, specifically an isoform of glycogen phosphorylase, derived from rabbit muscle. This enzyme plays a critical role in glycogen metabolism by catalyzing the phosphorolytic cleavage of α(1→4) glycosidic bonds in glycogen, releasing glucose-1-phosphate. The rabbit muscle source provides a well-studied model due to its high enzyme activity and availability, facilitating in-depth biochemical and structural analysis.
Degré de pureté :Min. 95%Glutathione peroxidase
CAS :Glutathione peroxidase (EC 1.11.1.9) is an enzyme that reduces peroxides to limit oxidative damage, by catalyzing the following reaction: 2 GSH + H2O2 → GS–SG + 2 H2O One unit of glutathione peroxidase will catalyze the conversion of 1.0 µmole of H2O2 per minute at pH 7.0 and 25 °C in the presence of reduced glutathione. Reduced glutahione is available here.Degré de pureté :Min. 95%Masse moléculaire :84,500 g/molα-Mannosidase
CAS :α-Mannosidase (α-D-mannopyranosidase, 1,2-α-mannosidase, 1,2-α-D-mannosidase, exo-α-mannosidase, α-D-mannosidase, systematic name α-D-mannoside mannohydrolase; EC 3.2.1.24) is an enzyme that cleaves α-mannose to produce glucose. One unit of α-Mannosidase will hydrolyze 1.0 µmole of chromogenic phosphate mimic p-nitrophenyl-α-p-mannoside to p-nitrophenol in 1 minute at pH 5.0 and 37°C.
Masse moléculaire :65.4 g/molFormaldehyde Dehydrogenase
CAS :Formaldehyde dehydrogenase (EC 1.2.1.46) is an enzyme that catalyzes the following reaction: formaldehyde + NAD+ + H2O ⇌ formate + NADH + H+ One unit of formaldehyde dehydrogenase will convert 1.0 µmole of formaldehyde to formic acid per minute at pH 7.5 and 37°C in the presence of NAD+.NAD+ is available here.Asparaginase, from E.coli, recombinant, lyophilized - EASP001
Asparaginase (EC 3.5.1.1) is an enzyme that catalyzes the following reaction: Asparagine + H2O → Aspartate + NH4+ Industrially, asparaginase is used to reduce the formation of acrylamide in starch-containing food ingredients and products during production processes. Asparaginase has a temperature optimum in the 30 – 50 °C range and pH optimum between pH 8 and 9. One unit will yield 1.0 μmole of ammonia from asparagine per min.Proteinase, Bacillus subtilis, sutilain
CAS :Proteinase, Bacillus subtilis, sutilain is a proteolytic enzyme, which is derived from the bacterium Bacillus subtilis. This enzyme exhibits a serine-type mechanism of action, characterized by its ability to cleave peptide bonds in proteins efficiently. It catalyzes the hydrolysis of proteins into peptides and amino acids, facilitating the breakdown of complex proteins into simpler, soluble forms.Degré de pureté :Min. 95%Couleur et forme :PowderOxalate Oxidase, freeze-dried, from Wheat
CAS :Oxalate Oxidase, freeze-dried, from Wheat is an enzyme preparation which is derived from wheat and functions through the oxidative degradation of oxalate. This enzyme catalyzes the conversion of oxalate into carbon dioxide and hydrogen peroxide, utilizing oxygen as a co-substrate in the process. The activity of Oxalate Oxidase is crucial in biological and biochemical applications where oxalate degradation is required.Ref: 3D-ETS012.6
10U711,00€1KU4.680,00€25U551,00€2KU8.189,00€50U914,00€100U1.044,00€0.1KU1.020,00€0.5KU2.925,00€1000U5.429,00€2000U9.481,00€0.25KU1.802,00€β-Glucanase 2, thermostable
CAS :Thermostable β-Glucanase 2 is an enzyme that hydrolases β-Glucans into glucose. One unit of β-Glucanase 2 will produce 1.0 μmole of glucose from β-glucan per minute at pH 5.8 and 70 °C.Degré de pureté :Min. 95%Lactase - >300U/mg
CAS :beta-Galactosidase (EC 3.2.1.23, shortly beta-Gal, also know as lactase) catalyses the hydrolysis of beta-d-galactoside in the presence of water to galactose and alcohol, or lactose into glucose and galactose. beta-Gal has a molecular weight of 540,000 and is composed of four identical subunits of MW 135,000, each with an independent active site. The enzyme has divalent metals as cofactors, with chelated Mg2+ ions required to maintain active site conformation. The molecule contains numerous sulfhydryl groups and is glycosylated.Nitrilase
CAS :Nitrilase (nitrile aminohydrolase; EC 3.5.5.1) in an enzyme that catalyzes hydrolysis of nitriles to carboxilic acids and ammonia: R-CN + 2 H2O → R-COO- + NH4+ One unit of nitrilase will yield 1.0 μmol of ammonia per minute under optimal reaction conditions using acrylonitrile as a substrate.
Degré de pureté :Min. 95%Protein disulfide isomerase from bovine liver
CAS :An enzyme that catalyzes the formation and breakage of disulfide bonds in the folding of proteinsFormule :C7H5Cl2NO5SDegré de pureté :Min. 95%Masse moléculaire :286.09 g/molMalate dehydrogenase,buffered aqueous glycerol solution, 600-1000 units/mg protein (biuret)
CAS :Malic dehydrogenase is a mitochondrial isozyme and an important catalyst in the tricarboxylic acid cycle. The enzyme catalyzes the following reaction: Oxaloacetate + β-NADH → L-Malate + β-NADOne unit will convert 1.0 μmole of oxalacetate and β-NADH to L-malate and β-NAD per min at pH 7.5 at 25 °C.Degré de pureté :Min. 95%Ubiquitin Conjugating enzyme E2C Human Recombinant
Ubiquitin Conjugating enzyme E2C (other names UBE2C, UBCH10, dJ447F3.2, ubiquitin conjugating enzyme E2 C; EC 2.3.2.24) is an essential mediator of mitotic destruction events and cell cycle progression. It catalyzes the destruction of cyclins A and B in conjunction with the anaphase-promoting complex, and therefore, plays an important role in the control of the cell exit from mitosis This activity is essential at then end of mitosis for the inactivation of their partner kinase Cdc2 and exit from mitosis into G1 of the next cell cycle. In addition, UBE2C bears homology to yeast PAS2, a gene that is essential for biogenesis of peroxisomes. UBE2C is useful for in vitro ubiquitinylation reactions.Deoxycytidine Kinase, human, recombinant
Deoxycytidine kinase (dCK, EC 2.7.1.74) is an enzyme that catalyzes the following reaction: dC + ATP → dCMP + ADP It can also use UTP as a donor of the phosphate group, and it can phosphorylate other deoxyribonucleosides (e.g. dA, dG) as well as nucleoside analogues (like clofarabine). One unit of dCK will convert 1.0 µmole of dC and ATP to dCMP and ADP per minute at pH 7.5 and 37°C.Degré de pureté :Min. 95%Diaphorase (from Clostridium kluyveri)
CAS :Diaphorase (lipoyl dehydrogenase, EC 1.8.1.4) is an NAD+/NADH-dependent oxidoreductase. One unit of diaphorase will convert 1.0 μmole NADH into NAD+ the presence of substrate at pH 7.5 and 25 °C.Degré de pureté :Min. 95%Lipoxidase
CAS :Lipoxidase is an enzyme, which is typically sourced from various plant tissues, animals, and some microorganisms. It functions by catalyzing the oxidation of polyunsaturated fatty acids in the presence of oxygen. This enzymatic action results in the formation of lipid hydroperoxides, which are key intermediates in various biochemical pathways, including those involved in cell signaling and the modulation of gene expression.Degré de pureté :Min. 95%Glutathione Reductase, baker's yeast
CAS :Glutathione Reductase, baker's yeast, is an enzyme derived from the yeast species *Saccharomyces cerevisiae*. This enzyme is sourced from baker's yeast, providing a renewable and consistent product for various biochemical applications. Its mode of action involves catalyzing the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione (GSH), using NADPH as an electron donor. This reaction is crucial for maintaining the intracellular redox balance by regenerating GSH, the primary cellular antioxidant.Superoxide dismutase PEG
Superoxide dismutase coupled to polyethylene glycol. Superoxide dismutase (EC 1.15.1.1) is an enzyme that catalyzes the following reaction: 2 H+ + 2 O2− → O2 + H2O2 thus converting an extremely reactive and cytotoxic superoxide radical into oxygen and (significantly less reactive) hydrogen peroxide.
C. rugosa Lipase 03, CRL 3 from Candida rugosa - ELCR03
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 03 from the yeast Candida rugosa has a temperature optimum in the 30 - 50 °C range and pH optimum between pH 7 and 8.Protein phosphatase 2C
CAS :Protein phosphatase 2C is a key enzyme, which is a serine/threonine-specific phosphatase, derived from various organisms including humans, plants, and bacteria. This enzyme plays a pivotal role in cellular signaling by removing phosphate groups from serine and threonine residues on target proteins, a process known as dephosphorylation. This action is crucial for the regulation of diverse cellular functions, including stress responses, cell division, and apoptosis.Amidase, from Rhodococcus sp., recombinant, lyophilized - EAM02
CAS :Amidase (EC 3.5.1.4) is a hydrolase acting on carbon-nitrogen bonds in linear amides and can be used in the hydrolysis of amides to acids. Amidase 02 is of bacterial origin (R. erythropolis and has been produced in E.coli).α-N-Acetylglucosaminidase
CAS :α-N-Acetylglucosaminidase (recombinant Human NAGLU Protein), degrades heparan sulfate by hydrolysis of terminal GlcNAc resides in N-acetyl-alpha-D-glucosaminides of heparan sulfate.Activity is measured by its ability to hydrolyse 4-Nitrophenyl 2-acetamido-2-deoxy-a-D-glucopyranoside EN03208 or EM31027. The specific activity is >900 pmol/min/μg, as measured under the decribed conditions.Degré de pureté :(Sds-Page) Min. 95%Creatinase from pseudomonas sp.
CAS :Creatinase (EC 3.5.3.3) is an enzyme that catalyzes the fellowing reaction: creatine + H2O ⇌ sarcosine + ureaOne unit of creatinase will hydrolyze 1.0 µmole of creatine into sarcosine and urea per min at pH 7.5 and 37 °C.Degré de pureté :Min. 95%Adenylate Kinase 1, human, recombinant
Adenylate kinase 1 (EC 2.7.4.3) catalyzes interconversion between ATP, ADP and AMP by catalyzing the following reaction: ATP + AMP ⇔ 2 ADP One unit of Adenylate kinase 1 will convert 1.0 µmol ATP and 1.0 µmol AMP to 2.0 µmol ADP per min at optimum conditions.Degré de pureté :Min. 95%Chitinase
CAS :Chitinase (systematic name (1→4)-2-acetamido-2-deoxy-β-D-glucan glycanohydrolase, EC 3.2.1.14) is a hydrolase that breaks down glycosidic bonds in chitin. One unit of chitinase will yield 1.0 mg of N-acetyl-D-glucosamine from chitin per hour at pH 6.0 and 25 °C.Formule :C17H16N8ZnDegré de pureté :Min. 95%Masse moléculaire :397.74 g/molCasein Kinase 2
Casein kinase 2 (CK2, CSNK2; EC 2.7.11.1) is a constitutively active serine and threonine protein kinase. It plays a role in a range of cellular processes, including DNA repair, cell cycle control, metabolic regulation, circadian rhythms and more. Its known substrates include hundreds of proteins. One unit of CK2 will phosphorylate of 1 pmol of of peptide substrate in 1 minute at 30°C and presence of ATP.Formule :C45H73N19O24Degré de pureté :Min. 95%Masse moléculaire :1,264.17 g/molUbiquitin thiolesterase UCHL1
CAS :Ubiquitin thiolesterase UCHL1 (Ubiquitin carboxy-terminal hydrolase L1; EC 3.1.2.15) is an enzyme that hydrolyses small C-terminal ubiquitin adducts to regenerate ubiquitin.
