Enzymes dans les Protéines Recombinantes
3319 produits trouvés pour "Enzymes dans les Protéines Recombinantes"
Luciferase - from Photinus pyralis (firefly)
CAS :Luciferase enzyme from Photinus pyralis (firefly), which catalyzes the oxidation of firefly luciferin. This reaction depends on the presence of oxygen and ATP and causes the bioluminescence seen in firefliesDegré de pureté :(Gel Electrophoresis) Min. 98%Couleur et forme :Powderα-Chymotrypsin, freeze-dried, from bovine pancreas
CAS :Please enquire for more information about alpha-Chymotrypsin, freeze-dried, from bovine pancreas including the price, delivery time and more detailed product information at the technical inquiry form on this pageFormule :CrO4PDegré de pureté :Min. 1200 Usp U/MgMasse moléculaire :146.97 g/molEUCODIS® 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 %).Lipase 064
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 068
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 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 %).
Enolase, neuron specific
CAS :Enolase (phosphopyruvate hydratase, EC 4.2.1.11) is an enzyme that catalyses the following reaction: 2-phospho-D-glycerate ⇌ phosphoenolpyruvate + H2O One unit of enolase will convert 1.0 μmole of 2-phosphoglycerate to phosphoenolpyruvate per minute.
Degré de pureté :Min. 95%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/mLTrypsin
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.Degré de pureté :Min. 250 Usp U/MgLacBuster™-S bulk for plates (β-lactamase)
CAS :This product shows beta-lactamase activity against clinically relevant beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. This product may be of particular interest for laboratory teams who require the sterility testing of biological specimens or for environmental monitoring applications.
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.Lipase 032
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.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 056
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 038
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 032
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 016
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.
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.Glucose oxidase from aspergillus niger - activity > 6000 u/g
CAS :Glucose oxidase is an enzyme thata catalyses the rapid conversion of glucose into non-fermentable gluconic acid in the presence of oxygen (O2). Its used is widely expanded with many applications in the chemical and pharmaceutical industry, food and beverage, clinical studies and biotechnology, among others. It medical diagnosis, glucose oxidase serves as a biosensor for detecting and determining the different levels of glucose in blood samples.Formule :C6H12O6Couleur et forme :PowderMasse moléculaire :180.16 g/mol
