Enzimi nelle Proteine Ricombinanti

<p>Endoglycosidase H (systematic name glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase, EC 3.2.1.96) is a highly specific enzyme, that cleaves asparagine-linked mannose rich oligosaccharides. One unit of Endoglycosidase H will remove &gt;95% of the carbohydrate from 10μg of denatured RNase B in 1 hour at 37°C in a total reaction volume of 10μl.The product EEH01.7 is available as a large-scale bulk supply of liquid enzyme solution and is intended for use in the chemical, diagnostic, pharmaceutical and related industries.For removal of all N-linked carbohydrates from proteins see Cymit Quimica's PNGase F enzymes (PNG01.3 - vials for research and PNG01.7 - large-scale bulk supply)</p>

<p>L-Leucine dehydrogenase (Leucine dehydrogenase, systematic name L-leucine:NAD+ oxidoreductase (deaminating); EC 1.4.1.9) is an enzyme that catalyzes the following reaction:  L-leucine + H2O + NAD+ ⇌ 4-methyl-2-oxopentanoate + NH3 + NADH + H+  One unit of L-Leucine dehydrogenase will convert 1.0 µmole of L‑leucine into 4-methyl-2-oxopentanoate per min at pH 10.5 and 37 °C in the presence of NAD+. The enzyme requires NAD+ as a cofactor, it is available here.</p>

<p>LacBuster™-S 50 is a beta-lactamase formulation, which is an enzyme of microbial origin with the ability to hydrolyze beta-lactam antibiotics. This enzymatic product is derived from specific bacterial species known for their resistance mechanisms, providing a robust capability to deactivate compounds such as penicillins and cephalosporins. Its mode of action involves the cleavage of the beta-lactam ring, a crucial structural component of these antibiotics, effectively neutralizing their antibacterial properties.</p>

<p>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 %).</p>

<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.</p>

<p>20mg/ml aq. solution.  Proteinase K is used for the general digestion of proteins and removal of protein contamination in nucleic acids. Addition of Protease K also stabilizes nucleic acids but degrading any nucleases present. Proteinase K is active in wide range of pH range, in the presence of SDS, urea and Guanidinium chloride at low to moderate concentrations. Proteinase K is also known under names of protease K and endopeptidase K.</p>

<p>Lipase CR 01 is an enzymatic product, which is derived from microbial sources, specifically selected strains of microorganisms. It exhibits a highly efficient mode of action by catalyzing the hydrolysis of triglycerides into glycerol and free fatty acids. This reaction is facilitated by its ability to target the ester bonds within lipid molecules, improving lipid solubilization and breakdown.</p>

<p>Adenosine deaminase catalyzes deamination of adenosine, converting it to inosine. It happens by the substituting of the amino group by a keto group. One Unit of the enzyme converts one micromole of adenosine to inosine per minute at 25°C, pH 7.4. Adenosine deaminase is also known by names of adenosine aminohydrolase, and ADA, EC 3.5.4.4.</p>

<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.</p>

<p>Lipase 06 recombinantly expressed in E. coli comes in a freeze-dried formulation. It has its pH optimum at 7 and temp. optimum at 30-45°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 06 was shown to hydrolyze p-Nitrophenyl esters of butyrate (91 % activity compared to octanoate), octanoate (100 %), laurate (13 %), palmitate (1 %), stearate (2 %), arachidate (0.3 %) and behenate (1 %).</p>

<p>Penicillin G acylase, 10mg/ml aqueous solution, is a biocatalytic enzyme used in pharmaceutical research and production. This enzyme is typically sourced from various microbial species, predominantly bacteria, through fermentation processes. Its primary mode of action involves the hydrolysis of penicillin G, catalyzing the cleavage of the side chain amide bond to produce 6-aminopenicillanic acid (6-APA), a core building block for the synthesis of a variety of semi-synthetic penicillins.</p>

<p>Alpha Amylase 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. Systematic name of alpha-amylase is 4-α-D-glucan glucanohydrolase, EC 3.2.1.1. One unit of Alpha Amylase will produce 1.0 mg of maltose from starch in 1 minute at pH 4.9 and 40 °C.</p>

<p>Beta-lactamase enzymes demonstrate 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.</p>

<p>Lipase 14 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 30-40°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 14 was shown to hydrolyze p-Nitrophenyl esters of butyrate (74 % activity compared to octanoate), octanoate (100 %), laurate (8 %), palmitate (5 %), stearate (4 %), arachidate (1 %) and behenate (0.6 %).</p>

<p>Beta-lactamase enzyme targeting beta-lactam antibiotics</p>

<p>Lipase 17 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-8. 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 17 was shown to hydrolyze p-Nitrophenyl esters of butyrate (2 % activity compared to octanoate), octanoate (100 %), laurate (20 %), palmitate (3 %), stearate (1 %), arachidate (1 %) and behenate (1 %).</p>

<p>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.</p>

<p>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 %).</p>

<p>3-Oxo-5β-steroid Δ4-dehydrogenase is an enzyme crucial in the metabolic pathway of steroid hormones, facilitating the conversion of androgens and estrogens. It is predominantly found in the liver, but also in other tissues where steroid biosynthesis occurs. This enzyme catalyzes the dehydrogenation at the Δ4 position of 3-oxo-5β-steroids, playing a significant role in the modulation and regulation of steroid hormone levels within cells.</p>

<p>Hydrolytic enzyme; biocatalyst in production of beta-lactam antibiotics</p>

<p>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 solid</p>

<p>Phosphorylase is an enzyme that plays a crucial role in carbohydrate metabolism, primarily sourced from various biological organisms, including humans, plants, and bacteria. Its mode of action involves catalyzing the breakdown of glycogen into glucose-1-phosphate by adding an inorganic phosphate group. This process is critical in regulating energy release and storage within cells.</p>

<p>Porcine Pancreatic Alpha Amylase 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. Systematic name of alpha-amylase is 4-α-D-glucan glucanohydrolase, EC 3.2.1.1. One unit of Alpha Amylase will produce 1.0 mg of maltose from starch in 1 minute at pH 4.9 and 40 °C. Please enquire for more information about Alpha Amylase, Porcine Pancreatic including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>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.</p>

<p>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.</p>

<p>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.</p>

<p>Alpha-L-iduronidase is a glycoside hydrolase enzyme that cleaves the non-reducing, terminal alpha-L-iduronic acid residues from polysaccharides and oligosaccharides. Alpha-L-iduronidase is involved in the lysosomal degradation of glycosaminoglycans and its deficiency leads to the accumulation of dermatan sulphate and heparan sulphate in tissues, a condition known as mucopolysaccharidosis I (MPS I). Alpha-L-iduronidase activity can be detected and quantified in an assay using a fluorogenic substrate 4MU-alpha-L-idopyranosiduronic acid. Alpha-L-iduronidase is also used in a 2-step assay for Hunter syndrome (MPS II) testing in combination with 4-MU-alpha-L-idopyranosiduronic acid 2-sulphate.<br>This enzyme is supplied as a 2 mg/mL aqueous solution in 25 mM sodium acetate, 150 mM NaCl, 50% glycerol, pH 5.0 from a bacterial source, recombinantly expressed in Escherichia coli (see application notes for more details). Alpha-L-iduronidase is also available as lyophilisate (FA181881)</p>

<p>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 &lt;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 %).</p>

<p>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 %).</p>

<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.</p>

<p>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.</p>

<p>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.</p>

<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. Immobilized lipases can be utilized in various reaction types, and are optimal for all reactions in organic solvents or solvent-free systems.</p>

<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 lipase from the yeast Y. lipolytica has a temperature optimum in the 30 - 40 °C range and pH optimum between pH 7 and 8.</p>

<p>Mannitol dehydrogenase (MDH, mannitol 2-dehydrogenase, EC 1.1.1.67) is an enzyme that catalyzes the following reaction:  D-mannitol + NAD+ ⇌ D-fructose + NADH + H+  One unit of mannitol dehydrogenase will generate 1.0 μmole of D-fructose per min in the presence of NAD+ at pH 8.6 and 40°C. NAD+ is available here and NADH is available here, depending on whether you require the reaction to proceed from left to right or from righ to left, respectively.</p>

<p>Collagenase is an enzymes that is responsible for breaking peptide bonds in collagen</p>

<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.</p>

<p>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.</p>

<p>Peroxidases can be utilized as enzymes catalyzing e.g. aromatic ring hydroxylation, epoxidation, halogenation, N- or S-oxidation, ether cleavage and alcohol/aldehyde oxidation reactions.</p>

<p>α-Glucosidase (EC 3.2.1.20) is a glycoside hydrolase enzyme that hydrolyzes α-1,4-linked D-glucose residues to produce α-D-glucose. This enzyme has been isolated from Bacillus stearothermophilus and is used as an industrial catalyst in the production of glucose syrups.  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 under optimum conditions.</p>

<p>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.</p>

<p>Lipase 64 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7 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 64 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (0.5 %) and laurate (0.1 %).</p>

<p>Cell wall enzyme</p>

<p>Enzyme involved in the reduction of hydrogen peroxide to water and oxygen. This is a highly important reaction as it protects the cell from oxidative damage.</p>

<p>Tyrosinase (EC 1.14.18.1) is an enzyme that oxydises phenol derivatives (e.g. tyrosine, dopamine). One unit of tyrosinase dissolved in 3mL reaction mixture will cause the absorbance at 280nm to increase by 0.001 in the presence of L-tyrosine at pH 6.5 and 25 °C. L-tyrosine is available here.Lyophilized, from mushroom. Activity ≥1000 unit/mg</p>

<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.</p>

<p>In a single vial and in a single step, the X-ShiningTM all-in-one ATP Assay provides an optimized reaction solution for the specific bioluminescent detection of ATP.  Simply reconstitute, and the X-ShiningTM all-in-one ATP Assay solution can be directly applied to samples for ATP measurement in a 1:1 ratio for an immediate bioluminescent read-out. The measurement of ATP levels is crucial to study cell cultures, cell viability, cell response, biochemical processes, to monitor environmental sample activity levels, to assess water quality, to test for biological contamination and to assess biocide efficacy. The X-ShiningTM all-in-one ATP Assay provides sufficient reagent solution to perform 50-to-100 measurements in a 96-well plate and can be easily adapted to measurements in tubes. Find out more about our innovative X-ShiningTM range here X-Shining | Innovation | Cymit Quimica .</p>

<p>Elastase (EC 3.4. 21.36) is a serine protease that breaks down elastin fibers. One unit of Elastase release 1 nmol of p-nitrophenol per sec from BOC-L-alanine p-nitrophenyl ester at pH 6.5 and 37°C</p>

<p>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.</p>

<p>Fructose-6-phosphate kinase (Phosphofructokinase, PFK, EC 2.7.1.11) is an enzyme that catalyzes the following reaction:  F6P + ATP ⇌ F1,6BP + ATP  One unit of PFK will convert 1.0 μmole of fructose 6-phosphate and ATP to fructose 1,6-diphosphate and ADP per minute at pH 9.0 at 30 °C.</p>