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(197 produits)
- Hydroxylase(36 produits)
- MPO(2 produits)
- Réductase(51 produits)
- Tyrosinase(71 produits)
3621 produits trouvés pour "Enzyme"
Trier par
Degré de pureté (%)
0
100
|
0
|
50
|
90
|
95
|
100
Chloramphenicol acetyltransferase from escherichia coli
CAS :Chloramphenicol acetyltransferase from escherichia coli (EC 2.3.1.28) detoxfies the antibiotic Chloramphenicol by attaching aceryl group. This renders chroramphenicol inactive, as it looses its ability to bind and inactivate ribosomes. One unit of Chloramphenicol acetyltransferase will convert 1 nmol of chloramphenicol and acetyl-CoA to chloramphenicol 3-acetate and CoA per min at pH 7.8 and 25 °C.Degré de pureté :Min. 95%LacBuster® - L 1000 IU, β-lactamase I & II, sterile liquid, EBL011.3
LacBuster®-L is a novel liquid and ready-to-use sterile beta-lactamase formulation with a broad substrate range against beta-lactam antibiotics including carbapenems, cephalosporins up to 5th generation and penicillins. LacBuster®-L is especially well suited for the direct innoculation method and membrane filtration tests according to US Pharmacopeia (USP <71>) and European Pharmacopeia (EP <2.6.1>). 1 Piece contains 10 vials.
Couleur et forme :Clear LiquidPyroglutamate aminopeptidase from pyrococcus furiosus, recombinant from E. coli
CAS :Pyroglutamate aminopeptidase from Pyrococcus furiosus, recombinant from E. coli, is an enzymatic product that specifically targets N-terminal pyroglutamyl residues in peptide chains. This enzyme is derived from the hyperthermophilic archaeon Pyrococcus furiosus, which allows it to exhibit high thermal stability and activity across a broad range of temperatures. Being produced recombinantly in E. coli ensures consistent availability and purity suitable for scientific applications.Degré de pureté :Min. 95%EUCODIS® Lipase 038, screening grade, recombinant, from microbial sources - EL038
Lipase 38 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 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 38 was shown to hydrolyze p-Nitrophenyl esters of acetate (27 % activity compared to butyrate), butyrate (100 %), octanoate (9 %) and caprate (5 %).Phospholipase A2, liquid, food-grade
CAS :Phospholipase A2, liquid, food-grade, is an enzymatic product derived from natural sources, typically microbial or animal tissues, utilized in various lipid modification processes. This enzyme specifically targets phospholipids, catalyzing the hydrolysis of the sn-2 ester bond, which releases free fatty acids and lysophospholipids. Its precise and efficient mode of action allows for targeted alterations in the lipid structure, offering potential benefits in modifying texture, flavor, and stability of food products.Degré de pureté :One Unit Of Enzyme Activity Is Defined As That Amount Of Enzyme That Causes The Release Of One5′-Nucleotidase human
CAS :5′-Nucleotidase (EC 3.1.3.5) is an enzyme that catalyzes hydrolysis of 5' nucleotides, removing the phosphate group: AMP + H2O ⇌ adenosine + Pi One unit of 5′-Nucleotidase will generate 1.0 μmole of phosphate ions per minute in the presence of AMP under optimal reaction conditions.rec HIV-1 Protease (expressed in E. coli)
A proteolytic enzyme synthesized by the HIV cell as part of the GagPol polyproteinSPM-1 (β-Lactamase)
CAS :SPM-1 (β-Lactamase) is an enzyme, which is a type of metallo-beta-lactamase enzyme, derived from bacterial origins, specifically from pathogens associated with nosocomial infections. This enzyme acts by hydrolyzing the amide bond in the beta-lactam ring of antibiotics, rendering β-lactam antibiotics ineffective. SPM-1 participates in antibiotic resistance by facilitating the degradation of a wide range of β-lactam antibiotics, including penicillins and cephalosporins, thereby nullifying their therapeutic effects.
KPC-1 (β-Lactamase)
CAS :KPC-1 (β-Lactamase) is an enzyme that breaks down β-lactam antibiotics, rendering them ineffective. It originates from strains of bacteria, particularly Klebsiella pneumoniae, which are significant sources of hospital-acquired infections. The mode of action involves hydrolyzing the β-lactam ring found in antibiotics such as penicillins and cephalosporins, neutralizing their antibacterial effects.VIM-15 (β-Lactamase)
CAS :VIM-15 (β-Lactamase) is a metallo-β-lactamase enzyme, which is derived from bacterial sources, particularly Gram-negative bacteria. Its mode of action involves the hydrolysis of β-lactam antibiotics, facilitating bacterial resistance. This enzyme employs zinc ions as cofactors to break the β-lactam ring, rendering these antibiotics ineffective against the bacteria that produce the enzyme. The hydrolysis process disrupts the antibiotic's structural integrity, crucial for its antibacterial activity, thereby nullifying its therapeutic effects.NMCA (β-Lactamase)
CAS :NMCA (β-Lactamase) is an enzyme that hydrolyzes β-lactam antibiotics, a type of product crucial for studies in antibiotic resistance mechanisms. This enzyme is derived from bacterial sources, specifically those strains known for their role in beta-lactam drug resistance. The mode of action of β-Lactamase involves the enzymatic breakdown of the β-lactam ring found in penicillins and cephalosporins, thereby neutralizing the antibiotic's efficacy. This catalytic process is an essential focus for researchers studying bacterial defense mechanisms and the development of resistant strains.
OXA-11 (β-Lactamase)
CAS :OXA-11 is a β-lactamase enzyme, which is a type of protein produced by certain bacteria. These enzymes are derived from the bacterial source and are responsible for antibiotic resistance. The primary mode of action of OXA-11 is the hydrolysis of the β-lactam ring found in various antibiotics, such as penicillins and cephalosporins, rendering them ineffective. This enzymatic activity allows bacteria to survive exposure to these antimicrobial agents, posing a significant challenge in clinical settings.Penase (Penicillinase)
CAS :Penase is an enzyme, specifically a type of beta-lactamase, which is derived from bacterial sources. Its mode of action involves the hydrolysis of the beta-lactam ring present in penicillin molecules. This enzymatic activity renders penicillin inactive by breaking its critical structural component that is essential for its antibacterial activity.Phospholipase D 040 food grade
CAS :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.X-Shining™ Luciferase, 10 mg/mL aqueous solution with glycerol
CAS :The improved, thermostable X-ShiningTM Luciferase is suitable for any luciferin-luciferase-based assay using D-luciferin (dLuc) or synthetic pro-luciferins (caged luciferins). Examples of its typical applications include ATP tests in hygiene monitoring, ATP tests in drug screenings and bacteria identification in microbial assays. The thermostable luciferase X-ShiningTM has been optimised by genetic engineering for strongly increased thermostability and storage stability. In temperature stress tests, the enzyme survives temperatures of 60 °C for over an hour, whereas a wild type luciferase from firefly is inactivated after only a few minutes. The extraordinary stability makes it user-friendly and eliminates some of the main disadvantages and limitations of the commonly used wild type luciferase. X-ShiningTM Luciferase is supplied as aqueous solution with glycerol or as a lyophilisate (L-8095), and it may be stored for months at room temperature without significant loss of function. Find out more about our innovative X-Shining range here X-Shining | Innovation | Cymit Quimica Carbosynth.Degré de pureté :(Sds-Page) Min. 90%KPC-1 (β-Lactamase)
CAS :KPC-1 (β-Lactamase) is a specialized enzyme, which is produced by certain Gram-negative bacteria, notably Klebsiella pneumoniae. It functions by hydrolyzing the β-lactam ring found in a wide range of β-lactam antibiotics, such as penicillins and cephalosporins. This enzymatic action effectively neutralizes the antibiotic's antimicrobial properties, rendering the drugs ineffective against bacteria that produce KPC-1.SPM-1 (β-Lactamase)
CAS :SPM-1 (β-Lactamase) is a metallo-β-lactamase enzyme, which is derived from certain Gram-negative bacteria, such as Pseudomonas aeruginosa. This enzyme is characterized by its ability to hydrolyze a broad spectrum of β-lactam antibiotics, including penicillins, cephalosporins, and carbapenems, due to the presence of a zinc ion in its active site. The zinc ion plays a crucial role in the catalytic mechanism by facilitating the cleavage of the β-lactam ring, rendering the antibiotic ineffective against bacterial cell wall synthesis.Glucosyltransferase206-freeze dried
CAS :Glucosyltransferase206-freeze dried is an enzymatic preparation designed for specific biochemical applications. It is derived from microbial sources, where it is produced and purified through advanced biotechnological processes. The enzyme functions by catalyzing the transfer of glucosyl units from donor molecules to specific acceptors, thereby forming glycosidic bonds. This mode of action is crucial in various biosynthetic pathways, particularly in the production of polysaccharides and structural carbohydrates.Glucosyltransferase205-freeze dried
CAS :Glucosyltransferase205-freeze dried is an enzyme preparation that is commonly used in biochemical and molecular biology research. It is derived from microbial sources, often from bacteria or fungi that are known for producing extracellular enzymes. The primary mode of action of Glucosyltransferase205 involves catalyzing the transfer of glucose residues from donor molecules, such as UDP-glucose, to acceptor molecules, forming glycosidic bonds. This enzymatic activity is crucial in the biosynthesis of polysaccharides, which are essential components in various biological structures and processes.
