Trypsin inhibitor from Glycine max (soybean), lyophilized powder, approx. 10000 U/mg

Stock Code: 3577587
Manufacturer Part No: 93620-1G
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Biochem/physiol Actions


This inhibitor acts against trypsin, and chymotrypsin and plasmin to a lesser extent. It will also inhibit proteases with mechanisms similar to trypsin, plasma kallikrein and coagulation Factor X. The trypsin inhibitor will not act against metalloproteases, tissue-baseed kallikrein, acid proteases, or thio proteases. This inhibitor acts by forming a 1:1 stoichiometric complex with the protease active site, and then cleaving a single arginine-isoleucine bond on the inhibitor. The inhibition is both reversible and pH dependent.


Other Notes


For the inhibition of proteolytic activity; Use in affinity chromatography for the purification of trypsin; Prepared by the method of M. Kunitz.


Preparation Note


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. Solutions can retain activity when stored short-term at 2-8° C. Solutions are stable in frozen aliquots at -20°C.


Unit Definition


1 U corresponds to the amount of inhibitor which reduces the trypsin activity by 1 BAEE-U. (1 BAEE-U is the amount of enzyme which increases the absorbance at 253 nm by 0.001 per minute at pH 7.6 and 25 °C; BAEE, Cat. No. 12880, as substrate).


One trypsin unit = A253 of 0.001 per minute with N-alpha-benzoyl-L-arginine ethyl ester (BAEE) as substrate at pH 7.6 at 25 °C.

Quality Level100
ManufacturerSIGMA-ALDRICH
Storage Temp.−20°C
Solubility0.1 M phosphate pH 7.6: 5 mg/mL, clear, colorless to almost colorless
Formlyophilized powder

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