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(195 produits)
- Hydroxylase(35 produits)
- MPO(2 produits)
- Réductase(50 produits)
- Tyrosinase(71 produits)
3616 produits trouvés pour "Enzyme"
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EUCODIS® CalB01, engineered variant of Candida antarctica Lipase B - ELCB01
<p>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 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.</p>Sphingomyelinase from bacillus cereus
CAS :<p>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.</p>Degré de pureté :Min. 95%Serratiopeptidase
CAS :<p>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.</p>Degré de pureté :Min. 95%Couleur et forme :PowderAsparaginase, 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.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.Secreted Phospholipase A2-IIA, human, recombinant
The secreted phospholipase A2-IIA (sPLA2-IIA, PLA2, systematic name phosphatidylcholine 2-acylhydrolase; EC 3.1.1.4) is an enzyme that catalyses the hydrolysis of glycerophospholipids at the sn2 position, yielding 1-acylglycerophosphocholine and a fatty acid. One unit of secreted phospholipase A2-IIA will hydrolyze 1.0 μmole of substrate per min under optimal conditions.Degré de pureté :Min. 95%Citrate synthase
CAS :<p>Citrate synthase (E.C. 2.3.3.1) is an enzyme that catalyzes the following reaction: acetyl-CoA + oxaloacetate + H2O → citrate + CoA-SHOne unit of citrate synthase will form 1.0 μmole of citrate from acetyl-CoA and oxalacetate per min at pH 8.0 and 37 °C.Origin is porcine heart.Molecular weight ~ 49kDa (monomer) and ~ 98kDa (dimer)</p>Formule :C197H238O43S6Couleur et forme :PowderMasse moléculaire :3,486 g/molAminopeptidase, Aeromonas proteolytica
CAS :One unit of Aminopeptidase (3.4.11.10) will hydrolyze 1.0 μmole of L-leucine p-nitroanilide to p-nitroaniline and L-leucine per min at pH 8.0 and 25 °C.Cytochrome C oxidase
CAS :<p>Cytochrome C oxidase (originally assigned EC 1.9.3.1, now re-assigned EC 7.1.1.9) is an enzyme that catalyzes the following reaction: 4 Fe2+ – cytochrome c + 4 H+ + O2 → 4 Fe3+ – cytochrome c + 2 H2O</p>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%EUCODIS® 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.Ubiquitin thiolesterase UCHL1
CAS :<p>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.</p>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%Glutathione Reductase, baker's yeast
CAS :<p>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.</p>EUCODIS® CalB02, engineered variant of Candida antarctica Lipase B - ELCB02
<p>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 CalB02 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.</p>Alcohol dehydrogenase, from yeast
CAS :<p>Alcohol dehydrogenase (EC 1.1.1.1) is the enzyme that catalyzes interconversion between alcohols and aldehydes or ketones, using NAD+/NADH as a cofactor in the following reaction: CH3CH2OH + NAD+ ⇔ CH3CHO + NADH + H+ One unit of alcohol dehydrogenase will convert 1.0 µmol of ethanol to acetaldehyde per minute at pH 8.8 and 25 °C.</p>Plasmin
CAS :<p>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°C</p>Recombinant Isocitrate Dehydrogenase
CAS :<p>Recombinant Isocitrate Dehydrogenase is a bioengineered enzyme, which is derived from microbial or eukaryotic expression systems designed to mirror its naturally occurring form. This enzyme catalyzes the oxidative decarboxylation of isocitrate to alpha-ketoglutarate, utilizing NADP+ as a cofactor in the process. Its mode of action involves the conversion of isocitrate to alpha-ketoglutarate with the concomitant reduction of NADP+ to NADPH.</p>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/molAconitase (human recombinant)
CAS :<p>Aconitase catalyzes isomerization of citrate to isocitrate via cis-aconitate. Systemic enzyme name is aconitate hydratase; EC 4.2.1.3.</p>Degré de pureté :Min. 95%
