Enzima
Los inhibidores enzimáticos son moléculas que se unen a las enzimas y disminuyen su actividad. Estos inhibidores se utilizan ampliamente en la investigación para estudiar la cinética enzimática, la regulación y el papel de enzimas específicas en las vías metabólicas. Los inhibidores enzimáticos también son cruciales en el desarrollo de fármacos, ya que muchos agentes terapéuticos funcionan inhibiendo enzimas involucradas en procesos patológicos. Al dirigirse a las enzimas, estos inhibidores pueden modular las vías bioquímicas y ofrecer tratamientos potenciales para diversas enfermedades. En CymitQuimica, ofrecemos una amplia selección de inhibidores enzimáticos de alta calidad para apoyar su investigación en bioquímica, farmacología y descubrimiento de fármacos.
Subcategorías de "Enzima"
- Anhídrido carbónico(196 productos)
- Hidroxilasa(36 productos)
- MPO(2 productos)
- Reductasa(51 productos)
- Tirosinasa(71 productos)
Se han encontrado 3620 productos de "Enzima"
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LacBuster™-L 1000 (β-lactamase)
CAS:Ready to use beta-lactamase solution targeting beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. According to US Pharmacopeia (USP <71>) and EP, LacBusterTM-L is suitable for sterility testing methods such as membrane filtration and direct inoculation.neutral Endopeptidase, liquid, food grade
CAS:Neutral Endopeptidase is an enzymatic product in liquid form, classified as food grade, which is derived from microbial fermentation or animal sources. Its primary mode of action involves the hydrolysis of peptide bonds within proteins, resulting in the breakdown of these macromolecules into smaller peptides and amino acids. This process is facilitated through the enzyme's specificity for neutral pH environments, where it effectively cleaves internal bonds within a protein chain.Endonuclease, liquid, food grade
CAS:Endonuclease, liquid, food grade is a biochemical enzyme, which is derived from microbial or bovine sources, with precision in hydrolyzing phosphodiester bonds within nucleic acids. This endonuclease cleaves the internal bonds of DNA and RNA, enabling the breakdown of these molecules into smaller nucleotide fragments. Its catalytic action is particularly useful in the controlled degradation of nucleic acids without affecting other macromolecules in the substrate.CalB 02
CAS:CalB 02 is a lipase enzyme, which is a biocatalyst derived from the yeast Candida antarctica. It functions primarily by catalyzing the hydrolysis of ester bonds. This enzymatic action is due to the unique structure of the active site, which allows for precise substrate specificity and stereoselectivity.Endoglycosidase H, liquid, recombinant
CAS:Endoglycosidase H (systematic name glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase, EC 3.2.1.96) is a highly specific enzyme, that cleaves asparagine-linked mannose rich oligosaccharides. One unit of Endoglycosidase H will remove >95% of the carbohydrate from 10μg of denatured RNase B in 1 hour at 37°C in a total reaction volume of 10μl.The product EEH01.7 is available as a large-scale bulk supply of liquid enzyme solution and is intended for use in the chemical, diagnostic, pharmaceutical and related industries.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)Proteinase K, high-quality, liquid, recombinant
CAS:Proteinase K, high-quality, liquid, recombinant is an advanced enzymatic product, which is a serine protease derived through recombinant DNA technology. It cleaves peptide bonds to facilitate protein digestion with broad substrate specificity. Its robust proteolytic activity is optimal under various conditions, including a wide range of temperatures and pH levels, making it incredibly versatile.LacBuster™-L bulk (β-lactamase)
CAS:Ready to use beta-lactamase solution targeting beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. According to US Pharmacopeia (USP <71>) and EP, LacBusterTM-L is suitable for sterility testing methods such as membrane filtration and direct inoculation.Proteinase K, freeze-dried, recombinant
CAS:Proteinase K, freeze-dried, recombinant is an enzyme preparation used extensively in molecular biology and biochemistry. It is derived through recombinant DNA technology, producing a highly pure enzyme that is expressed in a non-pathogenic host. Its mode of action involves the non-specific cleavage of peptide bonds in proteins, making it a critical tool for protein digestion.Lipase 006
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 CR 02
CAS:Lipase CR 02 is a high-purity enzyme preparation, which is derived from the microbial fermentation of selected fungal strains. With a mechanism involving the hydrolysis of ester bonds in lipids, Lipase CR 02 facilitates the conversion of triglycerides into glycerol and free fatty acids. This catalytic activity positions it as an essential tool in various biochemical and industrial applications.Lipase 076
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™-L 100 (β-lactamase)
CAS:Ready to use beta-lactamase solution targeting beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. According to US Pharmacopeia (USP <71>) and EP, LacBusterTM-L is suitable for sterility testing methods such as membrane filtration and direct inoculation.beta lactamase I activity - min. 25.0 IU/mLbeta lactamase II activity - min. 10.0 IU/mLLipase 012
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.6-Phosphogluconic dehydrogenase from yeast
CAS:6-Phosphogluconic dehydrogenase is an enzyme from yeast, which is a key component of the oxidative phase of the pentose phosphate pathway. It catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate, with the concurrent reduction of NADP+ to NADPH. This enzyme is sourced from yeast, a model organism extensively used in biochemical studies due to its eukaryotic nature and ease of genetic manipulation.Pureza:Min. 95%Carboxypeptidase G from pseudomonas sp.
CAS:Carboxypeptidase G (EC 3.4.17.11, alternative name γ-Glutamyl hydrolase) is a protease that cuts γ-glutamyl bonds with high specificity. One unit of Carboxypeptidase G will hydrolyze (+)amethopterin to generate 1.0 μmole of L-glutamic acid.Pureza:Min. 95%Lipase CalA, wildtype, freeze-dried, recombinant, from Candida antarctica
CAS:Lipase CalA, wildtype, freeze-dried, recombinant, from Candida antarctica is an enzymatic product, which is a highly purified form of lipase enzyme. It is derived from the yeast species Candida antarctica through recombinant DNA technology, ensuring consistency and purity by expressing the enzyme in a controlled microbial system.Endopeptidase, powder
CAS:Endopeptidase, powder, is a proteolytic enzyme, which is typically derived from microbial, plant, or animal sources, each imparting unique specificities. This enzyme functions by cleaving peptide bonds within polypeptide chains, rather than terminal bonds, thereby facilitating the breakdown of proteins into smaller, more manageable peptide fragments. The mode of action involves recognizing specific amino acid sequences within the substrate, leading to targeted bond hydrolysis.Ultra nuclease, liquid, recombinant
CAS:Ultra nuclease (EC 3.1.30.2) is an enzyme that digests DNA and RNA in any form: single- and double-stranded, linear, circular and supercoiled. The ultimate reaction product is 5'-monophosphate oligonucleatides that are mostly three, four and five bases long. Please enquire for more information about Ultra nuclease, liquid, recombinant including the price, delivery time and more detailed product information at the technical inquiry form on this pageEUCODIS® Lipase 031, screening grade, recombinant, from microbial sources - EL031
Lipase 31 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 40-80°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 31 was shown to hydrolyze p-Nitrophenyl esters of acetate (100 % activity) and butyrate (23 %).
LacBuster™-L concentrate
CAS:Beta-lactamase solution targeting beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. According to US Pharmacopeia (USP <71>) and EP, LacBusterTM-L is suitable for sterility testing methods such as membrane filtration and direct inoculation.
CalB 01
CAS:CalB 01 is an industrial biocatalyst that is derived from microbial sources, specifically engineered through recombinant DNA technology. Its primary component is the lipase enzyme from the yeast Candida antarctica, which has been optimized for high performance in various biotransformations. This enzyme functions by catalyzing the hydrolysis and synthesis of esters, facilitating transesterification and resolution of chiral molecules. The mode of action involves the selective cleavage of ester bonds in aqueous and non-aqueous media, which is crucial for modifying substrates in complex chemical reactions.CalB 10
CAS:CalB 10 is an industrial enzyme, specifically a lipase, which is derived from microbial sources, most commonly expressing the lipase B from Candida antarctica. It operates through the hydrolysis of ester bonds in lipids, enabling the conversion of triglycerides into glycerol and free fatty acids. This catalytic action is facilitated via its active site, where the nucleophilic serine residue attacks the carbonyl carbon of the substrate, forming a tetrahedral intermediate that eventually results in bond cleavage and product release.Lipase 017
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 065, screening grade, recombinant, from microbial sources - EL065
Lipase 65 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-8 and temp. optimum at 30-40°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 65 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (87 %), laurate (5 %), palmitate (0.2 %) and stearate (0.1 %).
Tyrosinase
CAS:Tyrosinase (EC 1.14.18.1) is an enzyme that oxydises phenol derivatives (e.g. tyrosine, dopamine). One unit of tyrosinase dissolved in 3mL reaction mixture will cause the absorbance at 280nm to increase by 0.001 in the presence of L-tyrosine at pH 6.5 and 25 °C. L-tyrosine is available here.Lyophilized, from mushroom. Activity ≥1000 unit/mgForma y color:PowderBspQI, 10U/μL buffer solution
BspQI is a Type IIS restriction endonuclease which only cleave one strand when binding to a DNA sequence.Sialic acid aldolase - Aqueous solution
CAS:Sialic acid aldolase - Aqueous solution is an enzyme preparation used extensively in biochemical and biotechnological applications. It is derived from microbial sources, where it is expressed and purified to high levels for research purposes. Sialic acid aldolase acts by catalyzing the reversible aldol reaction between N-acetylneuraminic acid (sialic acid) and pyruvate, facilitating the cleavage or synthesis of sialic acid.Forma y color:PowderEUCODIS® Peroxidase 13, from microbial origin, recombinant
CAS:Peroxidases can be utilized as enzymes catalyzing e.g. aromatic ring hydroxylation, epoxidation, halogenation, N- or S-oxidation, ether cleavage and alcohol/aldehyde oxidation reactions.Lipase 070
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.Triosephosphate Isomerase, freeze-dried, from rabbit Muscle
CAS:Triose-phosphate isomerase (TPI, TIM; EC 5.3.1.1) is an enzyme that catalyzes the reversible isomerization of dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate: DHAP ⇌ GADP The reaction mechanism involves the formation of an enediol intermediate. One unit of Triose-phosphate isomerase will convert 1.0 μmole glyceraldehyde 3-phosphate to dihydroxyacetone phosphate per min at pH 7.6 and 25 °C. Please enquire for more information about Triosephosphate Isomerase, freeze-dried, from rabbit Muscle including the price, delivery time and more detailed product information at the technical inquiry form on this pageCytrate Lyase, freeze-dried, Klebsiella Pneumoniae
CAS:Citrate lyase (also known as ATP citrate synthase, EC 2.3.3.8) is an enzyme that catalyzes the following reaction:citrate + ATP + CoA → oxaloacetate + Acetyl-CoA + ADP + PiGlucose-6-phosphate dehydrogenase
CAS:Glucose-6-phosphate dehydrogenase (G6PD, G6PDH; EC 1.1.1.49) is an enzyme that catalises the following reaction: D-glucose 6-phosphate + NADP+ + H2O ⇌ 6-phospho-D-glucono-1,5-lactone + NADPH + H+ One unit of G6PD will oxidize 1.0 µmole of D-glucose 6-phosphate to 6-phospho-D-glucono-1,5-lactone per min in the presence of NAD+ at pH 7.8 and 30 °C. NADP+ is available here.Forma y color:Clear LiquidPectinase from aspergillus niger
CAS:Pectin is an enzyme that breaks down pectin, a complex polysaccharide found in plant cell walls. It widely used in food and beverage, wine and brewing and textile and paper industriesFórmula:C20H43NForma y color:PowderPeso molecular:297.33955Penicillin G acylase, 10mg/ml aqueous solution
CAS:Penicillin G acylase, 10mg/ml aqueous solution, is a biocatalytic enzyme used in pharmaceutical research and production. This enzyme is typically sourced from various microbial species, predominantly bacteria, through fermentation processes. Its primary mode of action involves the hydrolysis of penicillin G, catalyzing the cleavage of the side chain amide bond to produce 6-aminopenicillanic acid (6-APA), a core building block for the synthesis of a variety of semi-synthetic penicillins.Pureza:Min. 1000 U/MlForma y color:Brown Clear LiquidPenicillin amidase from escherichia coli
CAS:As a member of the family of hydrolases this enzyme acts on carbon-nitrogen bonds and may be used in the commercial production of semisynthetic penicillin.
Pureza:Min. 95%Immobilized penicillin G acylase
CAS:Hydrolytic enzyme; biocatalyst in production of beta-lactam antibioticsForma y color:White Beige PowderLipase CR 01
CAS:Lipase CR 01 is an enzymatic product, which is derived from microbial sources, specifically selected strains of microorganisms. It exhibits a highly efficient mode of action by catalyzing the hydrolysis of triglycerides into glycerol and free fatty acids. This reaction is facilitated by its ability to target the ester bonds within lipid molecules, improving lipid solubilization and breakdown.Creatine phosphokinase, type I, lyophilized powder, ≥150 units/mg protein
CAS:Creatine kinase (also known phosphocreatine kinase or creatine phosphokinase, EC 2.7.3.2) in an enzyme that catalyzes the following reaction:creatine + ATP ⇌ phosphocreatine + ADPOne unit of creatine kinase will transfer 1.0 μmole of phosphate from phosphocreatine to ADP per min at pH 7.4 and 30 °C.Pureza:Min. 95%Trypsin
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.Pureza:Min. 250 Usp U/MgEUCODIS® Lipase 006, screening grade, recombinant, from microbial sources - EL006
Lipase 06 recombinantly expressed in E. coli comes in a freeze-dried formulation. It has its pH optimum at 7 and temp. optimum at 30-45°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 06 was shown to hydrolyze p-Nitrophenyl esters of butyrate (91 % activity compared to octanoate), octanoate (100 %), laurate (13 %), palmitate (1 %), stearate (2 %), arachidate (0.3 %) and behenate (1 %).EUCODIS® Lipase 009, screening grade, recombinant, from microbial sources - EL009
Lipase 09 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7 and temp. optimum at 35-55°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 09 was shown to hydrolyze p-Nitrophenyl esters of acetate (18 % activity compared to octanoate), butyrate (80 %), octanoate (100 %) and capate (40 %).Hexokinase
CAS:Hexokinase (EC 2.7.1.1) in an enzyme that catalyses the following reaction: Glucose + ATP → Glucose-6-phosphate + ADP One unit of hexokinase will phosphorylate 1.0 µmole of glucose per min at pH 7.6 and 25 °C in the presence of ATP. The product is a lyophilized powder, ≥30 units/mg protein.Pureza:(%) Min. 90%Forma y color:PowderX-Shining™ Luciferase, lyophilised
CAS:Supplied as lyophilisate containing 1% w/w X-Shining™ Luciferase. The improved, thermostable X-Shining™ 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 termostable luciferase X-Shining™ 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-Shining™ Luciferase is supplied as a lyophilisate (1% w/w X-Shining™ Luciferase) or as aqueous solution with glycerol (BX174908), 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.Pureza:(Spec. Activity. U/Mg) Min. 10^7Forma y color:PowderPenase (Penicillinase) bulk
CAS:Penase (Penicillinase) is an enzyme, which is a type of β-lactamase sourced from various bacterial strains capable of deactivating penicillin. It accomplishes this by targeting the β-lactam ring, a crucial structural component of penicillin antibiotics, and hydrolyzing it, thereby neutralizing the antibiotic effect. This enzymatic action is a defense mechanism employed by certain bacteria to survive in environments saturated with penicillin-based antibiotics.EUCODIS® Lipase 020, screening grade, recombinant, from microbial sources - EL020
Lipase 20 recombinantly expressed in P. pastoris comes in a spray-dried formulation. It has its pH optimum at 7-8. 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 20 was shown to hydrolyze p-Nitrophenyl esters of butyrate (3 % activity compared to octanoate), octanoate (100 %), laurate (85 %), palmitate (52 %), stearate (29 %), arachidate (22 %) and behenate (8 %).
CS2 hydrolase from Acidianus sp., aqueous solution with glycerol
CS2 hydrolase (Carbon disulfide hydrolase; E.C. 3.13.1.5) is an enzyme that catalyzes the following reaction: CS2 + 2 H2O → CO2 + 2 H2S thus converting carbon disulfide into hydrogen sulfide and carbon dioxide.Fórmula:C1101H1721N305O320S6Peso molecular:43,345.4 g/molEUCODIS® Lipase 008, screening grade, recombinant, from microbial sources - EL008
Lipase 08 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 20-60°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 08 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (60 %), laurate (7 %), palmitate (0.5 %), stearate (0.2 %), arachidate (0.1 %) and behenate (0.1 %).Recombinant enterokinase
CAS:Entorokinase (also known as enteropeptidase; EC 3.4.21.9) is a proteolytic enzyme (proteinase) that activates trypsinogen into its active form, trypsin. One unit of Entorokinase will produce 1.0 nmole of trypsin from trypsinogen per min at pH 5.6 and 25 °C.
