Enzymes in Recombinant Proteins

<p>Multi-copper oxidase from the family of polyphenol oxidades. It can be also found in many plants and bacteria. Laccase catalyses the oxidation of phenolic compounds such as lignin. It can oxidase non phenolic groups too with the use of mediators, chemical agents involved in the transfer of the electrons during the reaction. In some cases, laccase can also oxidise halogenated compounds. This enzyme is used for enzymatic assays, lignol screening tests and for waste water treatment to remove biodegrdable pollutants.</p>

<p>Peroxidase 12 recombinantly expressed in P. pastoria comes in a freeze-dried formulation. It has its pH optimum at 5-8 and temp. optimum at 20-40°C. 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. Peroxidase 12 was shown to act on styrene, veratryl alcohol, vanillyl alcohol, n-methyl anthranilate and thioanisole.</p>

<p>Phospholipase D 040, concentrated (100 U/mg), spray-dried, recombinant, of prokaryotic origin, is an enzyme preparation designed for advanced biochemical applications. This enzyme is derived from a prokaryotic source through recombinant DNA technology, allowing for high purity and activity. Phospholipase D functions by catalyzing the hydrolysis of phospholipids to produce phosphatidic acid and free head groups, which is a crucial reaction in both lipid signaling and membrane dynamics.</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>A catalase product which neutralizes hydrogen peroxide at much higher concentrations (&gt;10 %) compared to pyruvate, which is only capable of completely neutralizing hydrogen peroxide at the lowest concentration tested (2 %). Catalase (EC 1.11.1.6) catalyzes the following reaction:2H2O2 → 2H2O + O21 unit of catalase will decompose 1.0 μmole of H2O2 per min at pH 7.0 and 25 °C.</p>

<p>Phospholipases D belong to the family of esterases and act on phosphatidylcholine in the plasma membrane to release phosphatidic acid (PA) and choline. Phospholipases D can be used as versatile tools in hydrolysis and transphosphatidylation reactions for industrial, chemical and food applications.</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>Glucosyltransferase227-freeze dried is an enzyme-derived product, originating from microbial sources known for its role in catalyzing the transfer of glucose moieties from a donor molecule to specific acceptor molecules. The enzyme operates by facilitating covalent bond formation between glucose and target substrates, displaying specificity that can be exploited in various biochemical pathways.</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>A proteolytic enzyme; degrades protein contaminants in nucleic acid preparations</p>

<p>ALPK1 Protein, Human, Recombinant (His &amp; Myc) is expressed in Baculovirus.</p>

<p>Glucosyltransferase (GTase) is the enzyme that transfers glucose to another organic molecule (aglycon), establishing glycosidic linkage. UDP-glucose dependent GTases are part of the enzyme family of glucosyltransferases, they are versatile tools in glucosylation reactions. Different GTases have different substrate specificities. For the specificity of GT206 Glucosyltransferase, please see Table 1 that lists the available GTases with GT206 highlighted.Color: beigeForm: lyophilisateProtein content: 0.5 mg/mgThe glucosyltransferase was tested in a glucosylation reaction of a preferred substrate. High conversion after up to 24 h reaction time was observed.<br>Not sure which GTase to choose? Consider our Glucosyltransferase kit, which contains all 8 Glucosyltransferases.</p>

<p>The kit contains 8 different Glucosyltransferases (GTases), which are enzymes that transfer glucose to another organic molecule (aglycon), establishing glycosidic linkage. UDP-glucose dependent GTases are part of the enzyme family of glucosyltransferases, they are versatile tools in glucosylation reactions. Different GTases have different substrate specificities, as shown on Table 1. The kit is especially designed for screening and finding the most well-suited GTase for your specific process. All GTases in the kit are also available individually for bulk purchase.</p>

<p>Nitrile hydratase 21 recombinantly expressed in E. coli comes in a freeze-dried formulation. Nitrile hydratases can be utilized to convert nitriles into their corresponding amides, e.g. to produce acrylamide from acrylonitrile. Additional applications include the removal of nitriles from industrial wastewater. Our nitrile hydratases have been tested for hydrolysis of the following substrates:cyclohexanecarbonitrile, cinnamonitrile, benzonitrile, methacrylonitrile, pivalonitrile.</p>

<p>A pyridoxal phosphate-containing enzyme that converts L-methionine to α-ketobutyrate, ammonia and methyl mercaptan. Recombinant from e.coli source.  <br>EC 4.4.1.11</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 immobilized Lipase kit contains 7 different lipases, immobilised on a hydrophobic carrier either by adsorption or covalent linkage. Immobilized lipases can be utilized in various reaction types, and are optimal for all reactions in organic solvents or solvent-free systems.</p>

<p>A protease enzyme from bacillus subtilis which catalyzed proteolysis, a process that breaks down proteins and peptides to small polypeptides or amino acids</p>