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Key Documents

T9767

Sigma-Aldrich

Trypsin inhibitor from Glycine max (soybean)

For use as a marker in SDS-PAGE, BioReagent

Synonym(s):

SBTI

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About This Item

CAS Number:
9035-81-8
EC Number:
232-906-9
MDL number:
MFCD00082103
UNSPSC Code:
12352200
NACRES:
NA.77

biological source

Glycine max (soybean)

Quality Level

200

product line

BioReagent

form

powder

mol wt

20,000 Da

packaging

vial of 5 mg

technique(s)

electrophoresis: suitable

solubility

balanced salt solution: 1 mg/mL
concentrate: >10 mg/mL, hazy, amber-yellow
phosphate buffer: 10 mg/mL
water: 10 mg/mL
serum-free medium: soluble

shipped in

ambient

storage temp.

2-8°C

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Application

Trypsin inhibitor from Glycine max (soybean) has been used as a standard molecular weight marker in electrophoresis.

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.

Components

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

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 = 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.

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H317 - H334

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’.

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Endosymbiotic and host proteases in the digestive tract of the invasive snail Pomacea canaliculata: diversity, origin and characterization
Godoy MS, et al.
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Selective enrichment of albumin in biological samples by CE using segmental filling with sodium octyl sulfate in the background electrolyte
Lin Chin-Yu and Tseng Wei-Lung
Electrophoresis, 30(3), 532-539 (2009)
Quantification of tear proteins by SDS-PAGE with an internal standard protein: a new method with special reference to small volume tears
Li K, et al.
Graefe'S Archive For Clinical and Experimental Ophthalmology = Albrecht Von Graefes Archiv Fur Klinische Und Experimentelle Ophthalmologie, 248(6), 853-862 (2010)
Isabelle Le Potier et al.
Methods in molecular biology (Clifton, N.J.), 1466, 1-10 (2016-07-31)
Capillary electrophoresis (CE) coupled to fluorescence detection is an invaluable technique for the quantitative analysis of proteins of interest in the field of clinical diagnosis and quality control of novel biotechnology products. The various chemical and instrumental approaches that have
Martín S Godoy et al.
PloS one, 8(6), e66689-e66689 (2013-07-03)
Digestive proteases of the digestive tract of the apple snail Pomacea canaliculata were studied. Luminal protease activity was found in the crop, the style sac and the coiled gut and was significantly higher in the coiled gut. Several protease bands
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Protocols

Trypsin Inhibitors

Natural trypsin Inhibitors also known as serine protease inhibitors (serpins) are the largest and most diverse family of protease inhibitors. Serpins control the activation and catabolism of proteins by the inhibition of serine proteases in vivo.

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