Trypsin is commonly used in proteomics for biological research experiments to precipitate proteins into peptides for mass spectrometry analysis or in order to concentrate proteins and purify them from various contaminants. Trypsin preferentially hydrolyzes bonds whose carboxyl groups are contributed by lysine (Lys) or arginine (Arg).
Trypsin has application in diagnosis of disease for its activity in production of polyclonal antibodies that are ideally suited for use in sandwich assays as second stage antigen detectors.
Trypsin is used to re-suspend cells adherent to the cell culture dish wall during the process of harvesting cells. Some cell types have a tendency to “stick” – or adhere – to the sides and bottom of a dish when cultivated in vitro. Trypsin is used to cleave proteins bonding the culture to the dish, so that the cells can be suspended in fresh solution and transferred to new dishes. Trypsin can also be used to dissociate dissected cells.
Raw materials are sourced from government-certified facilities. All extraction and refining is done under cGMP guidelines for active pharmaceutical ingredients (API). Preparations are available in lyophilized (freeze-dried) powder and range in colour from an off white to light beige. These preparations comply with the recommended purity requirements for food grade enzymes provided by the Joint FAO/WHO Expert Committee on Food Additives (JECFA), the Food Chemical Codex (FCC), as well as specific requirements stipulated in the most recent edition of the U.S. Pharmacopoeia.