Enzimas em Proteínas Recombinantes
Foram encontrados 3322 produtos de "Enzimas em Proteínas Recombinantes"
Aldehyde dehydrogenase, ≥2.0 units/mg protein potassium-activated
CAS:Aldehyde dehydrogenase (EC 1.2.1.3) is the enzyme that catalyzes oxidation of aldehydes to carboxilic acids, using NAD+ as a cofactor in the following reaction: R-CHO + NAD+ + H2O → R-COOH + NADH + H+ One enzyme unit will oxidize 1.0 μmole of acetaldehyde to acetic acid per min at 25 °C at pH 8.0 in the presence of β-NAD+, potassium and thiols.
Cor e Forma:PowderEUCODIS® Lipase 067, screening grade, recombinant, from microbial sources - EL067
Lipase 67 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-8 and temp. optimum at 30°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 67 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (37 %), laurate (3 %) and palmitate (0.2 %).EUCODIS® Lipase 037, screening grade, recombinant, from microbial sources - EL037
Lipase 37 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 8-9 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 37 was shown to hydrolyze p-Nitrophenyl esters of butyrate (48 % activity), octanoate (100 %), laurate (85 %), palmitate (5 %) and stearate (1 %).
EUCODIS® Lipase 056, screening grade, recombinant, from microbial sources - EL056
Lipase 56 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 8 and temp. optimum at 40-50°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 56 was shown to hydrolyze p-Nitrophenyl esters of butyrate (79 % activity compared to octanoate), octanoate (100 %), laurate (51 %), palmitate (29 %), stearate (15 %), arachidate (0.2 %) and behenate (0.1 %).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.Cor e Forma:PowderCreatine 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%Phospholipase D 040 food grade
CAS:Test sample of 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. Product is a lyopholised solidPyroglutamate 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.Pureza:Min. 95%Urokinase
CAS:Urokinase (urokinase-type plasminogen activator, uPA; EC 3.4.21.73) is as serine protease. Its physiological substrate is plasminogen. Urokinase converts plasminogen into an active enzyme, plasmin, which is also a serine protease. In its active form plasmin plays an important role in dissolving blood clots. Despite its name, Urokinase is not a kinase.Fórmula:C21H25BrN2O3Pureza:(%) Min. 85%EUCODIS® Lipase 044, screening grade, recombinant, from microbial sources - EL044
Lipase 44 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-10 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 44 was shown to hydrolyze p-Nitrophenyl esters of butyrate (70 % activity compared to octanoate), octanoate (100 %), laurate (88 %), palmitate (6 %) and stearate (2 %).
α-Glucosidase, from yeast
CAS:α-Glucosidase (EC 3.2.1.20) is a glycoside hydrolase enzyme that hydrolyzes α-1,4-linked D-glucose residues (e.g. in starch or oligosaccharides) to produce α-D-glucose. One unit of α-Glucosidase will release 1.0 µmole of p-nitrophenol from the chromogenic substrate mimic 4-nitrophenyl α-D-glucopyranoside per minute at pH 6.8 and 37 °C.
Cor e Forma:White PowderLeucine aminopeptidase, microsomal from porcine kidney
CAS:Leucine aminopeptidase (L-leucine aminopeptidase, Leucyl aminopeptidase, leucyl peptidase, peptidase S; EC 3.4.11.1) is an exopeptidase enzyme. It preferentially catalyses the removal of N-terminal leucine residues from proteins and peptides.Fórmula:C12H24O2Pureza:Min. 95%Peso molecular:200.31 g/molBromelain
CAS:Bromelain is a group of proteolytic enzymes found in the fruit and stem of pineapple plants. It is used in a topical drug product approved by the FDA to treat severe burns. However, its oral consumption to treat sinusitis, postoperative pain after the extraction of wisdom teeth, and osteoarthritis is still being researched.Cor e Forma:PowderY. lipolytica Lipase, from Yarrowia lipolytica - ELYL01
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 from the yeast Y. lipolytica has a temperature optimum in the 30 - 40 °C range and pH optimum between pH 7 and 8.
Isoamylase 01
CAS:Isoamylase (also known as debranching enzyme, systemic name glycogen α-1,6-glucanohydrolase; EC 3.2.1.68) is the enzyme that cleaves α-1,6-glucosidic branch linkages in carbohydrates, namely amylopectin or glycogen.
X-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 (L-8093), 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.
Lipase 037
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.Dihydrofolate reductase
CAS:Dihydrofolate reductase (DHFR, 1.5.1.3) is a NADP+/NADPH-dependent oxidoreductase, that reduces dihydrofolate to tetrahydrofolate in the following reaction: dihydrofolate + NADPH + H+ ⇌ tetrahydrofolate + NADP+One unit of dihydrofolate reductase will convert 1.0 μmole of dihydrofolic acid into tetrahydrofolic acid in 1 minute at pH 7.5, 22°C and presence of NADPH.
Pureza:Min. 95%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.Immobilized lipase
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. Immobilized lipases can be utilized in various reaction types, and are optimal for all reactions in organic solvents or solvent-free systems.
Cor e Forma:Powder
