Trypsin is a serine protease found in the digestive system of many vertebrates where it hydrolyzes proteins. Through trypsinisation, it cleaves peptides at the carboxyl side of arginine and lysine, unless they are followed by a proline.
Trypsin has an optimal operating pH of about 7.5-8.5 and optimal operating temperature of about 37°C. Unlike chymotrypsin, the activity of trypsin is not affected by the inhibitor tosyl phenylalanyl chloromethyl ketone (TPCK).
Trypsin 1:250 indicates that one part trypsin will digest 250 parts casein in the USP activity assay.
from Porcine pancreas
TISSUE CULTURE GRADE
Storage/Handling: Store at -20°C.
|Grade||TISSUE CULTURE GRADE|
|Storage/Handling||Store at -20°C.|
High Throughput Bioluminescence Resonance Energy Transfer (BRET) Method using Rluc and Coelenterazine by SW Gersting, et al. (2012)
Sample Certificate of Analysis - Trypsin 1:250
COA for example only. Actual tests may differ.