The typical use for this product is in removing adherent cells from a culture surface. The concentration of trypsin necessary to dislodge cells from their substrate is dependent primarily on the cell type and the age of the culture. Trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestions. Additional applications include assessing crystallization by membrane-based techniques and in a study to determine that protein folding rates and yields can be limited by the presence of kinetic traps. Trypsin Powder, Porcine 1:250 is used to release adherent cells from tissue culture plates for passaging. It was used in the isolation and culture of human endothelial cells.

Trypsin is a serine protease found in the digestive system of many vertebrates, where it hydrolyses proteins. It is produced in the pancreas as the inactive proenzyme trypsinogen. It cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. Trypsin is composed of two subunits, a-trypsin and b-trypsin. α-Trypsin is composed of two peptide chains and β-trypsin is composed of one chain. Trypsin is inhibited by organophosphorus compounds such as diisopropyl fluorophosphate and natural trypsin inhibitors from pancreas, soybean, lima bean and egg white. Silver ions are also potent inhibitors. Specific inhibitors are AEBSF, antipain, aprotinin, DFP, leupeptin, PMSF, TLCK, and Trypsin Inhibitor.

The activity causing a change in absorbance of 0.003/minute at 253 nm.