
Enzimas em Proteínas Recombinantes
Foram encontrados 3319 produtos de "Enzimas em Proteínas Recombinantes"
ODC1 Protein, Human, Recombinant (His)
Ornithine decarboxylase (ODC1) is an enzyme which belongs to the Orn/Lys/Arg decarboxylase class-II family.Cor e Forma:Lyophilized PowderPeso molecular:25 &58 KDa (reducing condition)Ref: TM-TMPJ-00839
1mg2.535,00€5µg90,00€10µg130,00€20µg193,00€50µg381,00€100µg600,00€200µg947,00€500µg1.765,00€Glutaminase from escherichia coli
CAS: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.Pureza:Min. 95%Poly(ADP-ribose) glycohydrolase
CAS: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.
EUCODIS® Nitrilhydratase 10, recombinant enzyme - ENH010
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.Beta Lactamase Kit, 6 enzymes of 200 mg, recombinant - EBL_Kit01
Beta lactamase kit consisting of six different beta-lactamases with individual substrate specificity profiles against a broad range of beta-lactam antibiotics including penicilins, cephalosporins as well as carbapenems. The kit is especially designed for screening and finding the most well suited beta-lactamase for your specific process. Each vial contains at least 1000 IU beta I activity. Our beta-lactamases have been optimized for sterility testing and environmental monitoring in the manufacture and dosage formulation of beta-lactam antibiotics and for specific diagnostic purposes.Kit components:Pureza:Min. 95%Nitrilhydratase Kit, 10 recombinant enzymes with different substrate specificities - ENH Kit
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.EUCODIS® Nitrilhydratase 19, recombinant enzyme - ENH019
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.
EUCODIS® Nitrilhydratase 14, recombinant enzyme - ENH014
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.LacBuster® - S 2000 IU, beta-lactamase I & II, lyophilized, gamma irradiated - EBL023.2
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.Enteropeptidase
CAS: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.Pureza:Min. 95%EUCODIS® Nitrilhydratase 05, recombinant enzyme - ENH005
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.Neuraminidase from Vibrio Chloerae
CAS: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.Fórmula:C21H25NO11Pureza:(Activity U/Ml) ≥ 0.00Peso molecular:467.42 g/molL-Glutamic dehydrogenase (nadp) from proteus sp.
CAS: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.
Pureza:Min. 95%Peso molecular:300 g/molSucrose phosphorylase, recombinant, expressed in E. coli, ≥45 units/mg
CAS: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.Carboxypeptidase A from bovine pancreas
CAS: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.Thioglucosidase from Sinapis alba (white mustard) seed
CAS: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.Carbonodithioic Acid O-(Octahydro-4,7-methano-1H-inden-5-yl) Ester Potassium Salt
CAS:Produto ControladoFórmula:C11H15KOS2Cor e Forma:NeatPeso molecular:266.464Proteinase, 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.Pureza:Min. 95%Cor e Forma:PowderSuperoxide 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.
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.Urate oxidase (from Yeast)
CAS:Urate Oxidase, also known as uricase, catalizes the following reaction: Uric acid + O2 + H2O → 5-hydroxyisourate + H2O2.Fórmula:C18H26N5O14PPureza:Min. 95%Peso molecular:567.4 g/molGlutathione 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.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.Fórmula:C17H16N8ZnPureza:Min. 95%Peso molecular:397.74 g/molC. 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.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.
Pureza:Min. 95%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.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.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.Pureza:Min. 95%Aminopeptidase, 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.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.eXrase DNA Endonuclease, tech-grade
CAS:eXrase DNA endonuclease from enGenes is a recombinant endonuclease from Serratia marcescens produced in E. coli. Effectively and efficiently degrades all forms of DNA and RNA, reducing sample viscosity without proteolytic activity. As effective and efficient as other nucleases on the market, eXrase DNA endonuclease is the most cost-effective way to improve proteins yields and improve sample handing. Presented as a ready to use colourless liquid, formulated in Tris buffer at pH 8.0 with 50 % glycerol (v/v). This tech grade version is our most cost effective endonuclease for R&D applications. eXrase DNA endonuclease is suitable for the effective breakdown of nucleic acids in numerous biotech settings: • Removal of residual host DNA from biotechnological products to meet regulatory standards • Reduction of viscosity and streamlined purification in downstream processing of fermentation procedures. • Reduction of viscosity in in upstream fermentation processes • Extraction and/or synthesis of flavouring nucleotides • Enhanced bioavailability of nucleotides in specific feed products • DNA degradation for the removal or prevention of biofilm formationeXrase DNA endonuclease from enGenes is made by a proprietary microbial fermentation process utilizing Escherichia coli cells. This enzyme facilitates the hydrolysis of phosphodiester bonds in various forms of DNA and RNA, including single-stranded, double-stranded, linear, circular, or supercoiled configurations, yielding smaller oligonucleotides typically composed of 2-4 base pairs. Unit-Definition: One unit (U) of the enzyme is defined as the amount required to digest calf thymus DNA, yielding acid-soluble oligonucleotides equivalent to a ΔA260nm of 1.0 within a 30-minute timeframe at pH 8.0 and 37°C. This standardization allows for consistent measurement of enzymatic activity across different batches.eXrase DNA Endonuclease, research-grade
CAS:eXrase DNA endonuclease from enGenes is a recombinant endonuclease from Serratia marcescens produced in E. coli. Effectively and efficiently degrades all forms of DNA and RNA, reducing sample viscosity without proteolytic activity. As effective and efficient as other nucleases on the market, eXrase DNA endonuclease is the most cost-effective way to improve proteins yields and improve sample handing. Presented as a ready to use colourless liquid, formulated in Tris buffer at pH 8.0 with 50 % glycerol (v/v). This research grade eXrase has low endotoxin, max 0.25 EU/kU.eXrase DNA endonuclease is suitable for the effective breakdown of nucleic acids in numerous biotech settings: • Removal of residual host DNA from biotechnological products to meet regulatory standards • Reduction of viscosity and streamlined purification in downstream processing of fermentation procedures. • Reduction of viscosity in in upstream fermentation processes • Extraction and/or synthesis of flavouring nucleotides • Enhanced bioavailability of nucleotides in specific feed products • DNA degradation for the removal or prevention of biofilm formationeXrase DNA endonuclease from enGenes is made by a proprietary microbial fermentation process utilizing Escherichia coli cells. This enzyme facilitates the hydrolysis of phosphodiester bonds in various forms of DNA and RNA, including single-stranded, double-stranded, linear, circular, or supercoiled configurations, yielding smaller oligonucleotides typically composed of 2-4 base pairs. Unit-Definition: One unit (U) of the enzyme is defined as the amount required to digest calf thymus DNA, yielding acid-soluble oligonucleotides equivalent to a ΔA260nm of 1.0 within a 30-minute timeframe at pH 8.0 and 37°C. This standardization allows for consistent measurement of enzymatic activity across different batches.
β-1,4-Galactosyltransferase 1
β-1,4-Galactosyltransferase 1 is an enzyme that catalyzes the synthesis of the glycosaminoglycan-protein linkage in proteoglycans.Aminoacyl tRNA synthetase-IN-1
CAS:Enzyme involved in protein translation and catalyzes the aminoacylation reactionFórmula:C16H25N7O7SPureza:Min. 95%Cor e Forma:PowderPeso molecular:459.48 g/molPyruvate kinase (from Rabbit muscle), ammonium sulfate suspension
CAS:Pyruvate kinase (from Rabbit muscle), ammonium sulfate suspension is an enzyme product, which is a purified protein extracted from the muscle tissue of rabbits. This enzyme plays a crucial role in glycolysis, specifically catalyzing the transphosphorylation of phosphoenolpyruvate (PEP) to pyruvate, generating ATP from ADP in the process. This step is a key regulatory point in the glycolytic pathway, which is essential for cellular energy production.
Pureza:Min. 95%Luciferase from Vibrio fischeri
CAS:Luciferase enzymes sourced from Vibrio fischeriCor e Forma:PowderEUCODIS® 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.
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.
Pureza:Min. 95%Malate 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.Pureza: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°CAsparaginase, 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.L-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.Pureza:Min. 95%Acid phosphatase
CAS:One unit will hydrolyse 1.0μmol of 4-nitrophenyl phosphate per minute at 37°C and pH 4.8. Substrate for enzyme analysis is the 4-nitrophenyl phosphate disodium hexahydrate (EN08508).Fórmula:C6H10O2Pureza:Min. 95%Peso molecular:114.14 g/molProtein 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.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.alpha 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.Pureza:Min. 95%


