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(177 productos)
- Hidroxilasa(30 productos)
- MPO(2 productos)
- Reductasa(52 productos)
- Tirosinasa(67 productos)
Se han encontrado 3586 productos de "Enzima"
Ordenar por
Pureza (%)
0
100
|
0
|
50
|
90
|
95
|
100
L-Glutamic dehydrogenase (nadp) from proteus sp.
CAS:<p>L-Glutamic dehydrogenase (NADP+ dependent, from proteus sp., EC 1.4.1.4) is an enzyme that catalyzes the following reaction: L-glutamate + H2O + NADP+ ⇌ 2-oxoglutarate + NH3 + NADPH + H+ One unit of L-Glutamic dehydrogenase will generate 1.0 μmole of 2-oxoglutarate from L-glutamate per min at pH 8.3, 30 °C and the presence of NADPH and ammonium. NADP+ is available here and NADPH is available here, depending on whether you require the reaction to proceed from left to right or from righ to left, respectively.</p>Pureza:Min. 95%Peso molecular:300 g/molNeuraminidase from Vibrio Chloerae
CAS:<p>Neuraminidase (Exo-α-sialidase, sialidase, systematic name acetylneuraminyl hydrolase; EC 3.2.1.18) is an enzyme that catalyzes hydrolysis of glycosidic linkages of neuraminic acids. As it is exo-hydrolase, it hydrolyzes terminal N- or O- acylneuramic acid units, that are linked by α2,3-, α2,6-, and α2,8- glycosidic bonds. One unit of neuraminidase will hydrolyze 1 μmol N-acetyl-neuraminosyl-D-lactose under optimal conditions.</p>Fórmula:C21H25NO11Pureza:(Activity U/Ml) ≥ 0.00Peso molecular:467.42 g/molEUCODIS® Nitrilhydratase 05, recombinant enzyme - ENH005
<p>Nitrile hydratase 05 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.</p>EUCODIS® Nitrilhydratase 17, recombinant enzyme - ENH017
<p>Nitrile hydratase 17 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.</p>Thioglucosidase from Sinapis alba (white mustard) seed
CAS:<p>Thioglucosidase (thioglucoside glucohydrolase, Myrosinase, sinigrinase, sinigrase; EC 3.2.1.147) is an enzyme that cleaves thio-linked glucosides:a thioglucoside + H2O ⇌ a sugar + a thiol (the thiol formed is usually unstable and undergoes spontaneous re-arrangement into a isothiocyanate through a loss of a sulfate group)One unit will produce 1.0 μmole glucose per min from sinigrin (a thio-linked glucoside) at pH 6.0 and 25 °C.</p>EUCODIS® Nitrilhydratase 19, recombinant enzyme - ENH019
<p>Nitrile hydratase 19 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.</p>EUCODIS® Nitrilhydratase 01, recombinant enzyme - ENH001
<p>Nitrile hydratase 01 recombinantly expressed in E. coli comes in a freeze-dried formulation. Nitrile hydratases can be utilized to convert nitriles into their corresponding amidese, 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.</p>Enteropeptidase
CAS:<p>Enteropeptidase (historic name entorokinase; EC 3.4.21.9) is a proteolytic enzyme (proteinase) that activates trypsinogen into its active form, trypsin. One unit of enteropeptidase will produce 1.0 nmole of trypsin from trypsinogen per min at pH 5.6 and 25 °C.</p>Pureza:Min. 95%Sucrose phosphorylase, recombinant, expressed in E. coli, ≥45 units/mg
CAS:<p>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-phosphate One unit of Sucrose phosphorylase will produce 1.0 μmole of D-fructose per minute in the presence of sucrose and phosphate at pH 7.6 and 25 °C.</p>Aldolase from rabbit muscle
CAS:<p>One unit of aldolase (EC 4.1.2.13) will convert 1.0 µmol of Fructose-1,6-Diphosphate to Dihydroxyacetone phosphate and Glyceraldehyde-3-phosphate per min at 25 °C and pH 7.4. Lyophilized Powder.</p>Peso molecular:161 g/molUrease from Canavalia ensiformis
CAS:<p>Urease from Canavalia ensiformis (Jack bean urease, EC 3.5.1.5) is an enzyme that catalyses the following reaction: (NH2)2CO + H2O → CO2 + 2 NH3 One unit of urease will yield 1.0 µmole of NH3 from urea per min at pH 7.0 and 25 °C.</p>Peso molecular:480 g/molEUCODIS® Nitrilhydratase 14, recombinant enzyme - ENH014
<p>Nitrile hydratase 14 recombinantly expressed in E. coli comes in a freeze-dried formulation. Nitrile hydratases can be utilized to convert nitriles into their corresponding amidese, 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.</p>Poly(ADP-ribose) glycohydrolase
CAS:<p>Poly(ADP-ribose) glycohydrolase is an enzyme, which is derived from various organisms, including eukaryotic cells. It plays a crucial role in the regulation of poly(ADP-ribose) (PAR) metabolism. This enzyme functions by hydrolyzing the glycosidic bonds in poly(ADP-ribose) chains, thereby regulating the cellular levels of PAR by converting it back to ADP-ribose units.</p>Glutamic pyruvic transaminase
CAS:<p>Glutamic pyruvic transaminase (also Alanine transaminase, alanine aminotransferase; E.C. 2.6.1.2) is an enzyme that catalyzes the following reaction: L-alanine + α-ketoglutarate ⇌ pyruvate + L-glutamate One unit of Glutamic pyruvic transaminase will catalyze the conversion of 1.0 µmole per minute of L-alanine and α-ketoglutarate to L-glutamate and pyruvate, at 37°C and pH 7.4.</p>Forma y color:PowderPeso molecular:272.25 g/molEUCODIS® Nitrilhydratase 10, recombinant enzyme - ENH010
<p>Nitrile hydratase 10 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.</p>Carboxypeptidase A from bovine pancreas
CAS:<p>Carboxypeptidase A (EC 3.4.17.1) is an exopeptidase enzyme. It hydrolyzes peptide bonds of C-terminal residues with aliphatic or aromatic side-chains. One unit of Carboxypeptidase A will hydrolyze 1.0 μmole of hippuryl-L-phenylalanine per min at pH 7.5 and 25 °C.</p>EUCODIS® Nitrilhydratase 20, recombinant enzyme - ENH020
<p>Nitrile hydratase 20 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.</p>Pureza:Min. 95%EUCODIS® Nitrilhydratase 22, recombinant enzyme - ENH022
<p>Nitrile hydratase 22 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.</p>Pureza:Min. 95%Nitrilhydratase Kit, 10 recombinant enzymes with different substrate specificities - ENH Kit
<p>Kit of 10 unique, nitrile hydratases recombinantly expressed in E. coli for screening. 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. Please note, that the kit enzymes can also be supplied as whole cell biocatalysts in large scale.</p>Glutaminase from escherichia coli
CAS:<p>Glutaminase (glutaminase I, L-glutaminase, glutamine aminohydrolase; EC 3.5.1.2) is an enzyme that catalyzes the following reaction: L-glutamine + H2O → L-glutamate + NH4+ One unit of glutaminase will convert 1.0 μmole of L-glutamine into L-glutamate per min at pH 4.9 and 37 °C.</p>Pureza:Min. 95%D-Ribulose 1,5-diphosphate carboxylase from spinach
CAS:<p>D-Ribulose 1,5-diphosphate carboxylase, commonly known as RuBisCO, is an essential enzyme that catalyzes the first major step of carbon fixation, a process by which inorganic carbon from the atmosphere is converted into organic molecules. This enzyme is derived from spinach, a common model organism used in plant biology research due to its accessibility and well-characterized photosynthetic pathways.</p>Pureza:Min. 95%ODC1 Protein, Human, Recombinant (His)
<p>Ornithine decarboxylase (ODC1) is an enzyme which belongs to the Orn/Lys/Arg decarboxylase class-II family.</p>Forma y color:Lyophilized PowderPeso molecular:25 &58 KDa (reducing condition)LacBuster® - S 2000 IU, β-lactamase I & II, lyophilized, γ irradiated - EBL023.2
<p>LacBuster®-S 2000 is a solid and Gamma-irradiated, freeze-dried, broad range beta-lactamase formulation with 2000 IU beta-lactamase II and 20000 IU beta-lactamase I activity per vial.</p>Carbonodithioic Acid O-(Octahydro-4,7-methano-1H-inden-5-yl) Ester Potassium Salt
CAS:Producto controladoFórmula:C11H15KOS2Forma y color:NeatPeso molecular:266.464Chymase
CAS:<p>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.</p>Pureza:Min. 95%β-Glucanase 2, thermostable
CAS:<p>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.</p>Pureza:Min. 95%α-Mannosidase
CAS:<p>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.</p>Peso molecular:65.4 g/molAspartic acid proteinase
CAS:<p>Aspartic acid proteinase is a type of proteolytic enzyme, which originates from various biological sources including humans, fungi, and plants. It is characterized by its action via two critical aspartic acid residues in the active site, which facilitate the hydrolysis of peptide bonds in proteins. This enzyme operates optimally in acidic environments, making it crucial in processes like digestion and protein processing within cellular compartments such as lysosomes.</p>Luciferase from Vibrio fischeri
CAS:<p>Luciferase enzymes sourced from Vibrio fischeri</p>Forma y color:PowderSerratiopeptidase
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>Pureza:Min. 95%Forma y color:PowderAminopeptidase I from streptomyces griseus
CAS:<p>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.</p>β-1,4-Galactosyltransferase 1
<p>β-1,4-Galactosyltransferase 1 is an enzyme that catalyzes the synthesis of the glycosaminoglycan-protein linkage in proteoglycans.</p>Aminopeptidase, Aeromonas proteolytica
CAS:<p>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.</p>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:<p>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.</p>Pureza:Min. 95%EUCODIS® CalB01 IA, engineered variant of Candida antarctica Lipase B, immobilized by adsorption on hydrophobic carrier - ELCB01IA
<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 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.</p>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>Immobilized Lipase Kit, 7 unique immobilized EUCODIS® Lipases, immobilized by adsorption and covalent binding - ELIM Kit
<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 immobilized Lipase kit contains 7 different lipases, immobilised on a hydrophobic carrier either by adsorption or covalent linkage. Immobilized lipases can be utilized in various reaction types, and are optimal for all reactions in organic solvents or solvent-free systems.</p>3,4-Dihydroxybenzylamine hydrobromide
CAS:<p>3,4-Dihydroxybenzylamine hydrobromide inhibits DNA polymerase and melanoma growth, varying with tyrosinase activity.</p>Fórmula:C7H10BrNO2Pureza:98.49%Forma y color:Light Beige Crystalline PowderPeso molecular:220.06Deoxycytidine Kinase, human, recombinant
<p>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.</p>Pureza:Min. 95%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>Pureza:Min. 95%Asparaginase, from E.coli, recombinant, lyophilized - EASP001
<p>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.</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>Protein disulfide isomerase from bovine liver
CAS:<p>An enzyme that catalyzes the formation and breakage of disulfide bonds in the folding of proteins</p>Fórmula:C7H5Cl2NO5SPureza:Min. 95%Peso molecular:286.09 g/molAmidase, from Rhodococcus sp., recombinant, lyophilized - EAM02
CAS:<p>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).</p>Adenylate Kinase 1, human, recombinant
<p>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.</p>Pureza:Min. 95%α Amylase enzyme
<p>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.</p>Pureza:Min. 95%Transglutaminase from guinea pig liver
CAS:<p>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.</p>Pureza:Min. 95%
