Trypsin Recombinant Rabbit mAb (SDT-2433-32)

Trypsin is a serine protease commonly found in the vertebrate digestive system that hydrolyzes proteins. Active trypsin specifically hydrolyzes peptide bonds on the carboxyl side of lysine or arginine residues, provided the next residue is not proline. This specificity makes trypsin indispensable for the initial digestion of dietary proteins into smaller peptides, which are then further degraded by other proteases. Trypsin consists of two subunits, the alpha subunit (with 2 polypeptide chains forming it) and the beta subunit (with 1 polypeptide chain forming it). Trypsin, Mass Spectrometry Grade was subjected to reductive methylation, producing a highly active, stable molecule that strongly prevented its autolytic activity and reduced interference from excess peptide fragments generated by self-hydrolysis. It can be widely applied in laboratory proteomics analyses such as protein and peptide sequencing identification and HPLC peptide-map analysis. In biopharmaceutical and vaccine production, trypsin is used to detach adherent cells during culture. However, residual trypsin must be rigorously detected and controlled because it can degrade protein-based products, compromise drug efficacy and stability, and potentially cause adverse immune reactions in patients. Therefore, testing by Trypsin ELISA Kit (composed of pair trypsin antibodies) ensures final product safety, quality, and compliance with regulatory standards.