Component VI of Rackis. Does not inhibit chymotrypsin activity.
Inactivates trypsin on an equal molar basis. To ensure complete inhibition of trypsin activity, a working concentration of soybean trypsin inhibitor should exceed that of trypsin by a factor of at least 2.
Biochem/physiol Actions
Cell permeable: no
Primary Target Trypsin
Product does not compete with ATP.
Reversible: no
Warning
Toxicity: Standard Handling (A)
Unit Definition
One unit is defined as the amount of protein that will inhibit 1 unit of trypsin activity using BAEE as a substrate at 25°C, pH 7.6.
Reconstitution
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Other Notes
Uchino, T., et al. 1993. J. Biol. Chem.268, 527.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
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Cellular and molecular gastroenterology and hepatology, 13(2), 483-500 (2021-09-26)
Pancreatitis is characterized by acinar cell death and persistent inflammation. Ferroptosis is a type of lipid peroxidation-dependent necrosis, which is negatively regulated by glutathione peroxidase 4. We studied how trypsin, a serine protease secreted by pancreatic acinar cells, affects the
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