Cat No:PDE-0018
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.
Specifications | 25 mg, 100 mg, 250 mg, 500 mg, 1 g, 5 g |
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. |
Material Source | Glycine Max (Soybean) |
Appearance | Lyophilized powder |
Solution | H2O: >10 mg/mL; phosphate buffer: >10 mg/mL (hazy above 10 mg/mL) |
MW | 20.1 kDa |
Storage | 2-8°C |
Add | 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. |
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