Recombinant trypsin is a serinease that specifically cleaves peptide bonds at the C-terminal of lysine and arginine residues. Recombinant pancreatic trypsin is widely used various biotechnological processes. For example, protein hydrolysis to produce peptides; cell isolation of various tissues; enzymatic hydrolysis, sequencing of proteins; of recombinant insulin, etc.
Recombinant pancreatic trypsin also has many other functions, such as protein digestion, recombinant tryps can specifically cleave the carboxyl terminal peptide bonds of arginine (Arg) and lysine (Lys) residues, breaking down proteins into small pept segments. Cell separation, in cell culture, recombinant pancreatic trypsin is often used to dissociate adherent cells, by degrading extracellular matrix intercellular junction proteins, to detach cells from the surface of the culture dish, for easy subculture or experimental operation. Or recombinant protein production, in the pharmaceutical industry recombinant pancreatic trypsin is used to activate zymogens or precursor proteins, converting them into active forms, etc.
