Trypsin Protease

The field of proteomics is continually looking for new ways to investigate protein dynamics within complex biological samples. Recently, many researchers have begun to use RNA interference (RNAi) as a method of manipulating protein levels within their samples, but the ability to accurately determine these protein amounts remains a challenge. Fortunately, over the past decade, the field of proteomics has witnessed significant advances in the area of mass spectrometry. These advances, both in instrumentation and methodology, are providing researchers with sensitive assays for both identification and quantification of proteins within complex samples. This discussion will highlight some of these methodologies, namely the use of Multiple Reaction Monitoring (MRM) and Protein-AQUA.

Get better detection and quantification of proteases with this high-sensitivity red protease detection assay.

Evaluation of Recombinant, Chemically Treated Trypsin in Proteomics and Protein Characterization Assays

Pretreatment with Mucinase StcE increases glycopeptide identification from mucin samples, enhancing sample preparation efficiency for glycopeptide analysis.

Continuous spectrophotometric rate determination method using BAEE substrate measures trypsin activity, essential for enzyme characterization.

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