The purity and absence of contaminating protease activity are crucial for the data quality of peptide mapping and bottom-up proteomics experiments. Trypsin is typically derived from animal sources, e.g., porcine pancreas. Other digestive proteases, such as chymotrypsin, are often co-purified along with trypsin.
Trypsin-ultra™, Mass Spectrometry Grade (Recombinant) is inherently free of contamination. Moreover, because it is engineered to reduce autolysis, trypsin-derived peptides are absent from the spectra.
Together, its purity and autolysis resistance result in specific proteolysis, reduced spectra complexity, and more confident protein identification and quantification, thereby improving data analysis and reporting in a regulated environment.
