Comparison of recombinant trypsin and traditional trypsin digestion
Trypsin is a serine proteolytic enzyme. Its precursor is a biologically active trypsinogen, which is produced in the pancreas. When the pancreatic juice is secreted into the small intestine and activated by the intestinal peptidase in the small intestine, the protein can be decomposed into polypeptides and decomposed into amino acids. The site of the cleavage of the peptide chain is mainly located at the carboxy terminus of lysine or arginine. Therefore, in in vitro cell culture, trypsin is used to digest adherent cells to obtain individual cells that are separated from each other.
Traditionally used trypsin, obtained from the pancreas of cattle, pigs or sheep, is obtained by post-purification crystallization. Animal sources and production processes have innately determined that traditional trypsin has a high possibility of foreign virus contamination and hybrid enzyme contamination, and cannot be applied to clinical fields such as biopharmaceuticals and cell therapy. And need to save at -20 °C.
The recombinant trypsin is produced by recombinant E. coli expression, and the amino acid sequence is completely consistent with the porcine pancreas-derived cationic trypsin. The enzyme digestion specificity is the same. The molecular weight is 24 kD and the optimum pH is 7-10. In addition to the function of the traditional natural trypsin to digest and cleave the peptide chain (intercellular protein digestion), since it is not derived from the pancreas of pigs, cattle or sheep, the product does not contain any animal-derived components, Due to the unique nature of the product produced by recombinant protein, in addition to trypsin, there are no components such as chymotrypsin which are inevitable in traditional trypsin. In addition, the unique non-patented secret production process design for recombinant protein methylation modification greatly improves the temperature stability of the recombinant protein, and the product can be stably stored in the environment of 2-8 °C. No need to save at -20 °C.
Characteristics of recombinant recombinant trypsin:
1. Higher purity, less impurities, no animal source components.
2. Store at 2-8 ° C, no need to save at -20 ° C, ready to use, no waiting.
3. Strong digestion and mild effect.
Traditionally used trypsin, obtained from the pancreas of cattle, pigs or sheep, is obtained by post-purification crystallization. Animal sources and production processes have innately determined that traditional trypsin has a high possibility of foreign virus contamination and hybrid enzyme contamination, and cannot be applied to clinical fields such as biopharmaceuticals and cell therapy. And need to save at -20 °C.
The recombinant trypsin is produced by recombinant E. coli expression, and the amino acid sequence is completely consistent with the porcine pancreas-derived cationic trypsin. The enzyme digestion specificity is the same. The molecular weight is 24 kD and the optimum pH is 7-10. In addition to the function of the traditional natural trypsin to digest and cleave the peptide chain (intercellular protein digestion), since it is not derived from the pancreas of pigs, cattle or sheep, the product does not contain any animal-derived components, Due to the unique nature of the product produced by recombinant protein, in addition to trypsin, there are no components such as chymotrypsin which are inevitable in traditional trypsin. In addition, the unique non-patented secret production process design for recombinant protein methylation modification greatly improves the temperature stability of the recombinant protein, and the product can be stably stored in the environment of 2-8 °C. No need to save at -20 °C.
Characteristics of recombinant recombinant trypsin:
1. Higher purity, less impurities, no animal source components.
2. Store at 2-8 ° C, no need to save at -20 ° C, ready to use, no waiting.
3. Strong digestion and mild effect.
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