| Description | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 6.34 | Laccase is an enzyme, produced by ericoid mycorrhiza and ectomycorrhiza fungi. It belongs to the group of polyphenol oxidases. Laccase is also present in plants and bacteria.Laccase from Trametes versicolor has been used: to assess the use of four laccase-producing strains in waste water treatment Laccase is an enzyme, produced by ericoid mycorrhiza and ectomycorrhiza fungi. It belongs to the group of polyphenol oxidases. Laccase is also present in plants and bacteria.Laccase from Trametes versicolor has been used: to assess the use of four laccase-producing strains in waste water treatment in laccase assay in screening the lignolsSome of the enzymatic actions of laccase are associated with sporulation, detoxification, morphogenesis, melanin polymerization and it offers protection to spore coat. Laccase can catalyse a number of substrates including medicinal drugs and halogenated pesticides. It utilizes oxygen for its catalysis. For these reasons, it might be useful in the biological degradation of micropollutants in wastewater treatment. Laccase catalyzes the oxidation of phenol containing compounds, including lignin, through the reduction of oxygen to water. The presence of mediators will allow the oxidation of non-phenlic compounds as well. The primary function of laccase is to degrade lignin in fungi... Read More | Store at +4°C. Store under desiccating conditions. The product can be stored for up to 12 months | Purified pectinase is a multi-component preparation highly effective in depolymerizing plant pectins with varying degrees of esterification. The product contains substantial hemicellulase, cellulase, pectinesterase and xylanase activities which together with pectin lyase and polygalacturonase work Purified pectinase is a multi-component preparation highly effective in depolymerizing plant pectins with varying degrees of esterification. The product contains substantial hemicellulase, cellulase, pectinesterase and xylanase activities which together with pectin lyase and polygalacturonase work synergistically to digest plant cell wall tissues. When used with Worthington purified cellulase, purified pectinase has been found to be highly successful for generating good yields of viable protoplasts in several plant systems, e.g., corn, soybean, red beet, sunflower, tomato and citrus. In general, a concentration range of 0.1% to 0.5% pectinase (with accompanying 0.5% to 1.5% cellulase) used at 24°C to 37°C for periods of 1 to 16 hours will yield good results... Read More | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description: DCX (doublecortin, N-GST chimera)contains 2 doublecortin domains and belongs to the doublecortin family. It is highly expressed in neuronal cells of fetal brain, but not expressed in other fetal tissues. In the Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description: DCX (doublecortin, N-GST chimera)contains 2 doublecortin domains and belongs to the doublecortin family. It is highly expressed in neuronal cells of fetal brain, but not expressed in other fetal tissues. In the adult, it is highly expressed in the brain frontal lobe, but very low expression in other regions of brain, and not detected in heart, placenta, lung, liver, skeletal muscles, kidney and pancreas. DCX is a microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. It may act by competing with the putative neuronal protein kinase DCAMKL1 in binding to a target protein. DCX may in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. It may be part with LIS-1 of a overlapping, but distinct, signaling pathways that promote neuronal migration. Defects in DCX are the cause of lissencephaly X-linked type 1 and subcortical band heterotopia X-linked... Read More |