Format
lyophilized powder
Additional information
The trypsin inhibitor is soluble in water and phosphate buffers at 10 mg/mL. It is soluble in balanced salt solutions at 1 mg/mL and in serum-free media. Concentrated solutions greater than 10 mg/mL may be hazy and have a yellow to amber color. After trypsinizing cells, resuspend in 1 mL trypsin inhibitor solution at 1 mg/mL for every mL of trypsin solution used for dissociation. The cell suspension should then be centrifuged at 1000 rpm, forming a cell pellet.
Solution
H2O: >10 mg/mL
phosphate buffer: >10 mg/mL (hazy above 10 mg/ml)
soluble
Application
Trypsin has been used in a study to assess the potential application in animal cell culture of an alkaline protease from a non-toxigenic mangrove isolate of Vibrio sp. V26. [1] Trypsin has also been used in a study to improve the detection of fungi in eosinophilic mucin.
Description
This inhibitor has less effect on trypsin, chymotrypsin and plasminase. It also inhibits proteases by a mechanism similar to trypsin, plasma kalase, and clotting factor x. Trypsin inhibitors do not act on metalloproteinases, tissue-based potassiases, acid proteases, or thiophenases. This inhibitor acts by forming a 1:1 chemical complex with the protease active site, and then cutting an arginine-isoleucine bond on the inhibitor. This inhibition is reversible and pH dependent.