
Enzima
Sottocategorie di "Enzima"
- Anidrasi carbonica(197 prodotti)
- Idrossilasi(36 prodotti)
- MPO(2 prodotti)
- Riduttasi(51 prodotti)
- Tirosinasi(71 prodotti)
Trovati 3623 prodotti di "Enzima"
EUCODIS® Peroxidase 13, from bacterial, fungal and plant origin, recombinant - EP013
Peroxidase 013 belongs to the class of the heme-family peroxidases and can be utilized for catalyzing oxidation/epoxidation of unsaturated C-C bonds, N- or S-oxidation, ether cleavage and alcohol/aldehyde oxidation reactions. The Peroxidase 12 has a temperature optimum in the 20 - 40 °C range and pH optimum between pH 5 and 8.Xanthine oxidase
CAS:Xanthine oxidase is an enzyme that catalyzes the hydroxylation of hypoxanthine to xanthine and xanthine to uric acidPurezza:Min. 95%Colore e forma:PowderSialic acid aldolase - crystalline
CAS:Sialic acid aldolase - crystalline is a purified enzyme product, which is typically derived from microbial sources, such as certain bacteria, that have evolved to metabolize sialic acids. This enzyme catalyzes a reversible aldol reaction between sialic acid and pyruvate, facilitating the cleavage or formation of sialic acid from N-acetylmannosamine and pyruvate. By breaking the carbon-carbon bond in sialic acid, sialic acid aldolase plays a critical role in the degradation and biosynthesis pathways of sialic acid, which are key factors in numerous biological processes.
Colore e forma:PowderCreatinine amidohydrolase, 150 units/mg solid, 250 U
CAS:Creatinine amidohydrolase (also sometimes reffered as creatininase, EC 3.5.2.10) is an enzyme that catalyses the following reaction: creatinine + H2O ⇌ creatine One unit of creatinine amidohydrolase will produce 1.0 µmole of creatine at pH 7.5 and 37 °C.Purezza:Min. 95%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 %).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.
Colore e forma:White PowderUrokinase
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.Formula:C21H25BrN2O3Purezza:(%) Min. 85%Lysozyme, lyophilized powder, min 45000 FIP U/mg
CAS:Lysozyme, lyophilized powder, min 45000 FIP U/mg, is an enzymatic product derived primarily from egg white. It is a versatile and potent enzyme known for its ability to hydrolyze the β(1-4) glycosidic bonds in the peptidoglycan layer of bacterial cell walls. This mechanism of action is particularly effective against Gram-positive bacteria due to the accessibility of their peptidoglycan layer.Colore e forma:White PowderSARS-CoV-2 main protease
CAS:The main protease Mpro is a key protein in the lifecycle of the SARS-CoV-2 virus. Mpro cleaves the viral polyproteins at the C-terminal end of a glutamine residue in recognition sequences containing Leu-Gln-(Ser, Ala, Gly) motifs (Rut et al, 2020). As SARS-CoV-2 MPro has no closely related homologues in humans, it represents an attractive drug target (Ullrich and Nitsche, 2020). In summary, the Mpro protease is a chymotrypsin-like cysteine protease, requires homodimerisation for proteolytic activity, cleaves the viral polyproteins in 11 distinct sites, exclusively after a glutamine residue. A fluorogenic substrate for Mpro assays is Ac-Abu-Tle-Leu-Gln-AMC.The protein amount or better its concentration in solution is quantified using either A280 (absorption at 280 nm with its specific absorption coefficient) or using the Bradford assay (uses the dye Coomassie Brilliant Blue). Both of these methods quantify the total amount of protein in a sample, no matter what the oligomerization state is.Purezza:(Sds-Page) Min. 80%Colore e forma:LyophilisateTrypsin, technical grade, freeze-dried
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. Trypsin can be inhibited by using trypsin inhibitor Alpha 1 Antitrypsin.Purezza:Min. 98%Carboxypeptidase P
CAS:Carboxypeptidase P (EC 3.4.17.16, also Membrane Pro-Xaa carboxypeptidase, microsomal carboxypeptidase) is a C-terminal exopeptidase, that preferentially cuts at C-terminal amino acid next to proline: ~-Pro-X → ~-Pro + X.Formula:C8H17N2O5PPeso molecolare:252.2 g/molSucrose phosphorylase (from leuconostoc mesenteroides)
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-phosphateOne unit of Sucrose phosphorylase will produce 1.0 μmole of D-fructose per minute in the presence of sucrose and phosphate under optimum conditions.Purezza:Min. 95%EUCODIS® Lipase 070, screening grade, recombinant, from microbial sources - EL070
Lipase 70 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 35-45°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 70 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (62 %), laurate (15 %), palmitate (4 %), stearate (3 %), arachidate (2 %) and behenate (0.2 %).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.
Colore e forma:PowderEUCODIS® Lipase 070 immobilized, screening grade, recombinant, from microbial sources, covalent immobilization, or immobilization by absorption - EL070-I
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 070 has a temperature optimum at 45 °C and pH optimum between pH 5 and 8, and is covalently immobilized on a polymer resin. Immobilized lipases can be utilized in various reaction types, and are optimal for all reactions in organic solvents or solvent-free systems.LacBuster™-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.
Creatinine deiminase
CAS:Creatinine deiminase (EC 3.5.4.21) in an enzyme that catalyzes the following reaction: Creatinine + H2O → N-Methylhydantoin + NH3 One unit of creatinine deiminase will hydrolyze 1.0 µmole of creatinine to N-methylhydantoin and ammonia per minute at pH 7.5 and 37°C.Formula:C20H32O3SHypoxanthine phosphoribosyltransferase, liquid
CAS:Please enquire for more information about Hypoxanthine phosphoribosyltransferase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this pageLacBuster™-S 1000 (β-lactamase)
CAS:LacBuster™-S 1000 is an enzymatic product derived from microbial sources, specifically engineered for precision and efficiency. It is a beta-lactamase, which catalyzes the hydrolysis of the beta-lactam ring found in beta-lactam antibiotics such as penicillins and cephalosporins, rendering them inactive. The enzyme achieves this by breaking the amide bond within the beta-lactam ring, a critical structural component necessary for antibiotic activity.Dextran dextrinase, liquid
CAS:Please enquire for more information about Dextran dextrinase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this page
