Trypsin(bovine pancreas) (USP,1:2500;2500USPu/mg(BAEE 10000u/mg))

Trypsin(bovine pancreas) (USP,1:2500;2500USPu/mg(BAEE 10000u/mg)), specifically hydrolyzes the carboxyl-terminal peptide bonds or ester bonds of lysine or arginine ^[2]. The optimal pH range of Trypsin is 8.0-8.8 and Calcium ions can stabilize the activity of Trypsin^[2]. When the temperature rises, the hydrophobic part of Trypsin becomes exposed and undergoes irreversible aggregation^[3]. Trypsin is used for the detachment of adherent cells to digest the adhesion molecules by which the cells are attached to the surface of the culture flask^[4]. Trypsin is commonly used in activity assays and inhibitor screening^[5].

References:
[1] Soreide K, Janssen E A, Körner H, et al. Trypsin in colorectal cancer: molecular biological mechanisms of proliferation, invasion, and metastasis[J]. The Journal of Pathology: A Journal of the Pathological Society of Great Britain and Ireland, 2006, 209(2): 147-156.
[2] Woodard S L, Mayor J M, Bailey M R, et al. Maize (Zea mays)‐derived bovine trypsin: characterization of the first large‐scale, commercial protein product from transgenic plants[J]. Biotechnology and applied biochemistry, 2003, 38(2): 123-130.
[3] Trampari S, Papagiannopoulos A, Pispas S. Temperature-induced aggregation behavior in bovine pancreas trypsin solutions[J]. Biochemical and Biophysical Research Communications, 2019, 515(2): 282-288.
[4] Mótyán J A, Tóth F, Tőzsér J. Research applications of proteolytic enzymes in molecular biology[J]. Biomolecules, 2013, 3(4): 923-942.
[5] Vlasova I, Krüsselmann P, Kostenko Y, et al. The assessment of chemical composition and biological activity of faba bean pods as a potential feed additive utilized in piglets nutrition[J]. Scientific Reports, 2025, 15(1): 1234.