93620
Trypsin inhibitor from Glycine max (soybean)
lyophilized powder, ~10000 U/mg
Synonym(s):
SBTI
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About This Item
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biological source
Glycine max (soybean)
form
lyophilized powder
specific activity
~10000 U/mg
mol wt
Mr ~20000
solubility
0.1 M phosphate pH 7.6: 5 mg/mL, clear, colorless to almost colorless
shipped in
wet ice
storage temp.
−20°C
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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.
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.
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.
Solutions can retain activity when stored short-term at 2-8° C. Solutions are stable in frozen aliquots at -20°C.
Other Notes
For the inhibition of proteolytic activity; Use in affinity chromatography for the purification of trypsin; Prepared by the method of M. Kunitz.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Find documentation for the products that you have recently purchased in the Document Library.
The reactive site of trypsin inhibitors.
K Ozawa et al.
The Journal of biological chemistry, 241(17), 3955-3961 (1966-09-10)
CRYSTALLINE SOYBEAN TRYPSIN INHIBITOR.
M Kunitz
The Journal of general physiology, 29(3), 149-154 (1946-01-20)
Trypsin and chymotrypsin inhibitors from soybeans.
Y Birk
Methods in enzymology, 45, 700-707 (1976-01-01)
S. Katoh et al.
Polymer Preprints (American Chemical Society, Division of Polymer Chemistry), 21, 94-94 (1980)
Yangyang Hu et al.
Journal of cellular physiology, 234(12), 21988-21998 (2019-05-07)
The severity of acute pancreatitis (AP) is greatly attributed to the pancreatic acinar cell (PAC) death response. It has been established that the apoptosis-inducing therapy can protect against experimental pancreatitis and have great clinical therapeutic potential. However, current pharmacologic agents
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