| Description | Laccase (Denilite IIS) is a multi-copper oxidase (MCOs), which widely exists in microorganisms, plants and fungi, and can catalyze the oxidation of one electron of various phenolic compounds. Laccase can promote the oxidative coupling of single lignin, which plays an important role in the formation Laccase (Denilite IIS) is a multi-copper oxidase (MCOs), which widely exists in microorganisms, plants and fungi, and can catalyze the oxidation of one electron of various phenolic compounds. Laccase can promote the oxidative coupling of single lignin, which plays an important role in the formation and biodegradation of lignin, and also has the potential to cross-link food polymers. Note:Enzyme is a protein. Inhalation of dust or aerosols may cause sensitization and may cause allergic reactions in sensitized individuals. Some enzymes irritate the skin, eyes and mucous membranes after prolonged exposure... Read More | Purity>95% (SDS-PAGE&HPLC) Endotoxin level<1.0 EU/µgFunctionBifunctional growth-modulating glycoprotein. Inhibits growth of several human carcinoma cells in culture and stimulates proliferation of human fibroblasts and certain other tumor cells | Purity>95% (SDS-PAGE) Endotoxin level<1.0 EU/µgFunctionMay play some important roles in inflammatory responses. Up-regulates IL-6 and TNF-alpha and induces apoptosis | Purity>95% SDS-PAGE.FunctionProbable cell adhesion protein | Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA. Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA. Recombinant Human Trypsin is a genetically engineered protein expressed in E.coli and purified by high pressure liquid chromatography. There are no contaminating enzyme activities such as carboxypeptidase A and chymotrypsin. No protease inhibitors such as PMSF are contained in the preparation.Animal origin free:The use of recombinant Human Trypsin eliminates the risk of virus presence, and of any other potential adventitious agents found in animal pancreas-derived trypsin. Recombinant human trypsin:The amino acid sequence is the same as the Human Trypsin 2.Stable:A sterile recombinant human trypsin lyophilized eliminates the contamination risks and decreases the chance of activity loss in the process of transport and storage.High purity:(1) Recombinant human trypsin provides increased specificity and eliminates contaminating activities found in lower purity enzymes.(2) No other contaminating proteases such as chymotrypsin or carboxypeptidase A... Read More |