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T9767 Sigma

Trypsin inhibitor from Glycine max (soybean)

BioReagent, For use as a marker in SDS-PAGE

Synonym: SBTI

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Properties

Related Categories Biochemicals and Reagents, Enzyme Inhibitors, Enzyme Inhibitors by Type, Enzymes, Inhibitors, and Substrates, Molecular Biology,
product line   BioReagent
mol wt   mol wt 20,000 Da
packaging   vial of 5 mg
storage temp.   2-8°C

Description

Frequently Asked Questions

Frequently Asked Questions are available for this Product.

Components

The soybean trypsin inhibitor is a monomeric protein containing 181 amino acid residues in a single polypeptide chain crosslinked by two disulfide bridges.

Application

This product has been tested for cell culture applications. Trypsin has been used in a study to assess the potential application in animal cell culture of an alkaline protease from a ton-toxigenic mangrove isolate of Vibri sp. V26. Trypsin has also been used in a study to improve the detection of fungi in eosinophilic mucin.

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

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.

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.

Price and Availability


Amicon Pro Purification System
Safety & Documentation

Safety Information

Symbol 
GHS08  GHS08
Signal word 
Danger
Hazard statements 
Precautionary statements 
RIDADR 
NONH for all modes of transport
WGK Germany 
3

Documents

Certificate of Analysis

Certificate of Origin

Protocols & Articles
Peer-Reviewed Papers
15

References

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