1. Product introduction
Trypsin is a serine protease that cleaves peptide bonds at the C-terminus of lysine and arginine. Trypsin is widely used in various biotechnological processes. Such as: protein enzymatic hydrolysis to produce polypeptides; cell separation of various tissues; protein enzymatic hydrolysis and sequencing; recombinant production and so on. Recombinant porcine trypsin is expressed and produced by recombinant E. coli, and its amino acid sequence is exactly the same as cationic trypsin derived from porcine pancreas. The specificity of restriction enzymes is the same. The molecular weight is 24kD, and the optimum pH is 7-10. The activity is inhibited by serine protease inhibitors such as PMSF, and metal ion chelating agents such as EDTA inhibit enzymatic activity.
2. Product advantages
No animal origin: recombinant production, no foreign virus contamination, such as swine flu virus, porcine parvovirus, etc. High purity: no other miscellaneous enzyme pollution
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