93620
Trypsin inhibitor from Glycine max (soybean)
lyophilized powder, ~10000 U/mg
Synonym(s):
SBTI
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
Recommended Products
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
Looking for similar products? Visit Product Comparison Guide
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)
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
S. Katoh et al.
Polymer Preprints (American Chemical Society, Division of Polymer Chemistry), 21, 94-94 (1980)
The reactive site of trypsin inhibitors.
K Ozawa et al.
The Journal of biological chemistry, 241(17), 3955-3961 (1966-09-10)
Trypsin and chymotrypsin inhibitors from soybeans.
Y Birk
Methods in enzymology, 45, 700-707 (1976-01-01)
CRYSTALLINE SOYBEAN TRYPSIN INHIBITOR.
M Kunitz
The Journal of general physiology, 29(3), 149-154 (1946-01-20)
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
Chromatograms
application for HPLCOur team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service