assay
≥90% (SDS-PAGE)
form
lyophilized solid
specific activity
≥7,000 units/mg protein
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze, desiccated
color
white
solubility
67 mM potassium phosphate buffer, pH 7.6: 5 mg/mL
shipped in
ambient
storage temp.
−20°C
Quality Level
General description
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
Trypsin
Product does not compete with ATP.
Reversible: no
Preparation Note
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Other Notes
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.
Uchino, T., et al. 1993. J. Biol. Chem.268, 527.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Standard Handling (A)
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Storage Class
11 - Combustible Solids
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Ke Liu et al.
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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