Enzymes in Recombinant Proteins

<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>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>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>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>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>Immobilized lipase is an advanced enzymatic product, which is derived from lipases, enzymes primarily sourced from microbial, plant, or animal origins. This product operates through a catalytic mechanism where the lipase is attached to a solid support, enhancing its stability and reusability in various reactions. This immobilization allows the enzyme to maintain activity over a wide range of conditions, including different pH levels and temperatures.</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 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>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>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>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.</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>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>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>

<p>Ultra nuclease (EC 3.1.30.2) is an enzyme that digests DNA and RNA in any form: single- and double-stranded, linear, circular and supercoiled. The ultimate reaction product is 5'-monophosphate oligonucleatides that are mostly three, four and five bases long. Please enquire for more information about Ultra nuclease, liquid, recombinant including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>Lipase Y 01 is an enzymatic catalyst, which is derived from microbial fermentation with a specific mode of action involving the hydrolysis of triglycerides into glycerol and free fatty acids. This enzyme operates by breaking ester bonds in fats, facilitating their breakdown and conversion into simpler molecules.</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>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.</p>

<p>Lipase 01 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7 and temp. optimum at 25-45°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 01 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (57 %), laurate (13 %), palmitate (9 %), stearate (6 %), arachidate (2 %) and behenate (0.1 %).</p>

<p>LacBuster® Settle Plates contain a general purpose growth medium (tryptone soya agar) supplemented with LacBuster®, a high-performing beta-lactamase to effectively neutralize beta-lactam antibiotics. The media plates are suitable for the cultivation of a wide variety of microorganisms in environmental monitoring within the pharmaceutical industry.</p>

<p>Cocarboxylase tetrahydrate is a coenzyme form of vitamin B1; cofactor for enzymes involved in carbohydrate catabolism</p>

<p>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.</p>

<p>A N-Acetyl Muramidase enzyme that cleaves N-acetylmuramyl-β(1-4)-N-acetylglucosamine linkage in peptidoglycan within the bacterial cell wall.</p>

<p>Dextranase (alternative names dextran hydrolase, endo-dextranase, endodextranase, dextranase DL 2, α-D-1,6-glucan-6-glucanohydrolase, 1,6-α-D-glucan 6-glucanohydrolase, EC 3.2.1.11) is dextran-degrading enzyme that hydrolyzes the α(1→6) glycosidic linkage of dextran, cutting it into progressively shorter fragments, ultimaly producing isomaltose (a disaccharide) and glucose. One unit of dextranase will cleave dextrane to yield 1.0 μmole of isomaltose per min at pH 6.0 and 37 °C.</p>

<p>A proprietary potent and stable alternative to chemical neutralizers such as pyruvate - for the utilization in environmental monitoring applications. Use of catalase as a supplement in media plates offers a more effective and reliable solution for safe and secure environmental monitoring of sterilization in clean rooms, isolators or production facilities by also removing remaining traces and spots of high concentration of H2O2. Currently, agar plates for monitoring disinfection or sterilization are supplemented with pyruvate, which is consumed during the neutralization of hydrogen peroxide. One of the main benefits of this catalase is its high stability in agar media at 50°C, which allows easy preparation of media and processing into plates. Due to the high stability no special storage conditions are needed and a shelf-life of &gt; 6 months at 4-25°C can be guaranteed.<br>Key features are:</p>

<p>Cell wall enzyme</p>

<p>Chloramphenicol acetyltransferase from escherichia coli (EC 2.3.1.28) detoxfies the antibiotic Chloramphenicol by attaching aceryl group. This renders chroramphenicol inactive, as it looses its ability to bind and inactivate ribosomes. One unit of Chloramphenicol acetyltransferase will convert 1 nmol of chloramphenicol and acetyl-CoA to chloramphenicol 3-acetate and CoA per min at pH 7.8 and 25 °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>Lipoxidase, from soybean</p>

<p>Pectin is an enzyme that breaks down pectin, a complex polysaccharide found in plant cell walls. It widely used in food and beverage, wine and brewing and textile and paper industries</p>

<p>PAIRED PRODUCTS AVAILABLE:</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>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>As a member of the family of hydrolases this enzyme acts on carbon-nitrogen bonds and may be used in the commercial production of semisynthetic penicillin.</p>

<p>Amidase is a hydrolase acting on carbon-nitrogen bonds in linear amides, and can be used in hydrolysis of amides to acids. Amidase 01 is of bacterial origin (P. aeruginosa) and has been produced in E.coli.</p>

<p>Beta-lactamase solution targeting beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. According to US Pharmacopeia (USP &lt;71&gt;) and EP, LacBusterTM-L is suitable for sterility testing methods such as membrane filtration and direct inoculation.</p>

<p>Alpha Amylase (Amylase, α-Amylase, 1,4-α-D-glucan glucanohydrolase, glycogenase, PPA; systematic name 4-α-D-glucan glucanohydrolase; EC 3.2.1.1, CAS Number [9000-90-2]) is an enzyme that catalyzes hydrolysis of large polysaccharides 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. Porcine pancreatic Alpha Amylase is supplied as lyophilized, off-white to white powder, lyophilized from tris chloride and mannitol, pH 7.2. Activity is ≥70U/mL, specific activity ≥100 U/mg protein. Store at -20°C on arrival.</p>

<p>Protein kinase LATS2 is a serine/threonine kinase, which is a crucial component sourced intrinsically from cellular kinase cascades involved in cell regulation. This protein kinase is pivotal in the Hippo signaling pathway, which regulates cell growth, apoptosis, and stem cell renewal. LATS2 is part of the core kinase cascade that, upon activation, phosphorylates and inhibits the activity of the transcriptional co-activators YAP and TAZ, thereby controlling their transcriptional activity. This inhibition is key to maintaining proper cell proliferation and preventing uncontrolled cell growth that could lead to tumorigenesis.</p>

<p>A general purpose growth medium supplemented with LacBuster™ to effectively neutralize beta-lactam antibiotics. This product is suitable for the cultivation of a wide variety of microorganisms for environmental monitoring within the pharmaceutical industry and for high performance monitoring of your isolators and clean rooms during beta lactam manufacture</p>

<p>Cymit Quimica’s econoLuciferase™ (econoLuc Cymit Quimica Cat. No. L-8090) is a recombinant luciferase from the firefly Luciola lateralis that has been expressed as a luciferase-GFP fusion protein in E. coli.The luciferase enzyme has been optimized for increased thermo-stability by genetic modification to be stable for one hour at 37°C and up to two days at room temperature.Stabilized econoLuciferase™ thus overcomes the disadvantages and limitations of wild-type Luciferase, notably its short active life, outperforming enzyme from the Photinus pyralis firefly for both performance and stability.This optimized luciferase is the perfect enzyme for ATP detection assays in hygiene control, microbial tests using caged luciferins and it is the luciferase of choice for biochemical tests measuring ATP consumption and production in diverse enzymatic reactions.The product L-8090 is available on a large scale and is intended for use in the chemical, diagnostic, pharmaceutical and related industries.</p>

<p>Alpha Amylase, powder, is an enzyme preparation that acts as a catalyst for the hydrolysis of starch, breaking it down into simpler sugars like maltose and glucose. This enzyme is derived from microbial or fungal sources, commonly via fermentation processes using strains of bacteria or fungi specifically optimized for enzyme production.</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 an enzyme from the family of carbohydrolases acting specifically on α-1,6-glucosidic branch linkages in polysaccharides such as amylopectin or glycogen, but rarely hydrolyzes such bonds in pullulan. Isoamylase has been obtained from P. amyloderamosa and has a temperature optimum in the 30 – 40 °C range and pH optimum between pH 3 and 4.</p>

<p>Cholesterol dehydrogenase (EC 1.1.1.840) is NADP+-dependant oxidoreductase, that catalyses the following reaction:cholesterol + NADP+ + H2O → cholest-4-en-3-one + NADPH + H+This is achieved by oxidizing alcohol hydroxy-group into ketone. One unit of cholesterol dehydrogenase will produce 1.0 μmole of cholest-4-en-3-one per minute at pH 8.5 and 25 °C.</p>

<p>ApStar Taq DNA Polymerase is a thermostable DNA polymerase, originally derived from the thermophilic bacterium Thermus aquaticus. It operates by synthesizing new strands of DNA through the extension of primers in the 5' to 3' direction, utilizing a DNA template. This enzyme is specifically engineered to withstand high temperatures, making it ideal for the denaturation phases of PCR.</p>

<p>Catalyst for signal development in immunoassays</p>

<p>A general purpose growth medium supplemented with LacBuster™ to effectively neutralize beta-lactam antibiotics. This product is suitable for the cultivation of a wide variety of microorganisms for environmental monitoring within the pharmaceutical industry and for high performance monitoring of your isolators and clean rooms during beta lactam manufacture</p>