Recombinant Bovine Trypsin

Biomolecules

Trypsin is a serine protease that hydrolyses proteins and is found in the digestive system of numerous vertebrates. Trypsin is produced as the inactive proenzyme trypsinogen in the pancreas. Trypsin cleaves peptide chains at the carboxyl side of the amino acids lysine and arginine, except when either is followed by proline. Trypsin is secreted into the duodenum, where it acts to hydrolyses peptides into amino acids. The optimal pH for Trypsins is about pH 8 at 37C. In cystic fibrosis disease, there is a deficiency in transport of trypsin and other digestive enzymes from the pancreas. Trypsin is widely used in various biotechnological processes since it’s available in high quantity in the pancreas and can be easily purified. Recombinant Bovine Trypsin is free from any animal and human sources.

It is recommended to reconstitute the lyophilized Bovine Trypsin in sterile distilled water at not less than 100 ug/ml, which can then be further diluted to other aqueous solutions.