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T9128 Sigma

Trypsin inhibitor from Glycine max (soybean)

lyophilized powder

Synonym: SBTI

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Description

Frequently Asked Questions

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Components

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

Analysis Note

One mg of trypsin inhibitor will inhibit a minimum of 1.0 mg Trypsin of activity ~10,000 BAEE units/mg trypsin.

Caution

A solution at 10 mg/mL should be stored for greater than 3 years at 2-8°C retained activity. Solutions are stable in frozen aliquots at -20°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.

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.

One trypsin unit will produce a ΔA253 of 0.001 per min with BAEE as substrate at pH 7.6 at 25 °C; reaction volume 3.2 ml, 1 cm light path.

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.

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Trypsin inhibitor from <I>Glycine max</I> (soybean)

Type I-S, lyophilized powder

Trypsin inhibitor from <I>Glycine max</I> (soybean)

powder, BioReagent, suitable for cell culture

Trypsin inhibitor from <I>Glycine max</I> (soybean)

solution, 1 ×, sterile-filtered, BioReagent, suitable for cell culture

Safety & Documentation

Safety Information

Symbol 
GHS08  GHS08
Signal word 
Danger
Hazard statements 
Precautionary statements 
Hazard Codes (Europe) 
Xn
Risk Statements (Europe) 
Safety Statements (Europe) 
22-36/37-45
WGK Germany 
3

Documents

Certificate of Analysis

Certificate of Origin

Protocols & Articles

Protocols

Enzymatic Assay of Trypsin Inhibitor

2. SCOPE This procedure applies to all products that have a specification for Trypsin Inhibition at Sigma-Aldrich, St. Louis.

Peer-Reviewed Papers

References

Set your institution to view full text papers.

Transdermal delivery of timolol by electroporation through human skin. Denet AR and Préat V J. Control. Release 88(2), 253-62, (2003)

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Protease-activated receptor 2, dipeptidyl peptidase I, and proteases mediate Clostridium difficile toxin A enteritis. Cottrell GS, Amadesi S, Pikios S, et al. Gastroenterology 132(7), 2422-37, (2007)

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Effect of purified lipopolysaccharides from strains of Helicobacter pylori and Helicobacter felis on acid secretion in mouse gastric glands in vitro. Padol IT, Moran AP, and Hunt RH Infect. Immun. 69(6), 3891-6, (2001)

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In vitro culture of embryonic disc cells from porcine blastocysts. Hochereau-de Reviers MT and Perreau C Reprod. Nutr. Dev. 33(5), 475-83, (1993)

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Primary structure of cathepsin D inhibitor from potatoes and its structure relationship to soybean trypsin inhibitor family Mares, M., et al. FEBS Lett. 25, 94-98, (1989)

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An in vitro system to study Sertoli cell blood-testis barrier dynamics. Mruk DD and Cheng CY Methods Mol. Biol. 763, 237-52, (2011)

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VE-PTP maintains the endothelial barrier via plakoglobin and becomes dissociated from VE-cadherin by leukocytes and by VEGF. Nottebaum AF, Cagna G, Winderlich M, et al. J. Exp. Med. 205(12), 2929-45, (2008)

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A 1-megadalton translocation complex containing Tic20 and Tic21 mediates chloroplast protein import at the inner envelope membrane. Kikuchi S, Oishi M, Hirabayashi Y, et al. Plant Cell 21(6), 1781-97, (2009)

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Subjective food hypersensitivity: assessment of enterochromaffin cell markers in blood and gut lavage fluid. Kine Gregersen et al Int. J. Gen. Med. 4, 555-60, (2011)

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Cigarette smoke–induced neurogenic inflammation is mediated by α,β-unsaturated aldehydes and the TRPA1 receptor in rodents. Andrè, E., et al. Clin. Invest. Med. 118, 2574-2582, (2008)

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Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. Shorter J EMBO J. 27(20), 2712-24, (2008)

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Isolation and characterization of a trypsin inhibitor from the seeds of kohlrabi (Brassica napus var. rapifera) belonging to the napin family of storage proteins. Svendsen IB, Nicolova D, Goshev I, et al. Carlsberg Res. Commun. 54(6), 231-9, (1989)

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The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding. Chen BJ J. Virol. 82(20), 10059-70, (2008)

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Role of kallikrein-kininogen system in insulin-stimulated glucose transport after muscle contractions. Dumke CL, Kim J, Arias EB, et al. J. Appl. Physiol. 92(2), 657-64, (2002)

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NADPH oxidase expression and production of superoxide by human corneal stromal cells. O'Brien WJ Mol. Vis. 15, 2535-43, (2009)

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Calpain inhibition reduces ataxin-3 cleavage alleviating neuropathology and motor impairments in mouse models of Machado-Joseph disease. Simões AT, Gonçalves N, Nobre RJ, et al. Hum. Mol. Genet. 23(18), 4932-44, (2014)

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Protein minimization: characterization of the synthetic cyclic dodecapeptide corresponding to the reactive site region of the oil rape trypsin inhibitor type-III. Trovato M, Casavola EC, Maras B, et al. Biochem. Biophys. Res. Commun. 302(2), 311-5, (2003)

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