Recombinant Trypsin (MS Grade), Lyophilized

DESCRIPTION

Trypsin is a serine endopeptidase that specifically cleaves peptide bonds at the carboxyl side of lysine (Lys) and arginine (Arg) residues in proteins. This recombinant MS grade trypsin is expressed in Pichia pastoris and produced under GMP-compliant conditions, ensuring high purity, batch-to-batch consistency, and reproducible digestion performance.

Unlike animal-derived trypsin, this recombinant product is free from animal-origin components and devoid of animal viral contaminants such as swine influenza virus or porcine parvovirus, making it suitable for high-sensitivity analytical workflows. It contains no chymotrypsin activity, which ensures clean and specific cleavage for protein mass spectrometry applications.

The enzymatic activity can be inhibited by serine protease inhibitors (e.g., PMSF, TLCK) and metal ion chelators (e.g., EDTA). Each USP unit is defined as a 0.003 increase in absorbance at 253 nm per minute during enzymatic digestion of BAEE in a 3.2 mL reaction system at 25 °C, pH 7.6. The lyophilized enzyme can be easily reconstituted with 1 mM HCl, aliquoted, and stored at −20 °C for long-term stability.

This recombinant trypsin is ideally suited for protein mass spectrometry, peptide mapping, sequencing, and proteomic analysis. Its high specificity and purity make it a reliable tool for researchers requiring reproducible and contamination-free protein digestion.