MilliporeSigma
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T1021

Sigma-Aldrich

Trypsin inhibitor from Glycine max (soybean)

Isoelectric focusing marker, pI 4.6

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Synonym(s):
SBTI
CAS Number:
9035-81-8
EC Number:
232-906-9
MDL number:
MFCD00082103
NACRES:
NA.77

Quality Level

200

biological source

Glycine max (soybean)

form

powder

mol wt

20,100 Da

technique(s)

isoelectric focusing (IEF): suitable

pI 

4.6

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.

−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.

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.

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.

Certificate of Analysis

Enter Lot Number to search for Certificate of Analysis (COA).

Certificate of Origin

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Product Information Sheet

Product Information Sheet - T1021

Quotes and Ordering

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  1. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

  2. How do I get lot-specific information or a Certificate of Analysis?

    The lot specific COA document can be found by entering the lot number above under the "Documents" section.

  3. How do I find price and availability?

    There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote.  USA customers:  1-800-325-3010 or view local office numbers.

  4. What is the Department of Transportation shipping information for this product?

    Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product. 

  5. What is the molecular weight and amino acid sequence of trypsin inhibitor from Glycine max (soybean)?   

    Soybean trypsin inhibitor is a mixture of the three types. We have not characterized our trypsin inhibitor products in terms of how much of each of the three types may be present. All three have a molecular weight of between 20,000 and 20,200 daltons, so one might use 20,100 daltons as an average.The three types vary in the amino acids at a few positions. The detailed summary of the three types (or variants) was published in the following linked reference:     J. Biochem. (Japan), 98, 435-448 (1985).Note that the authors use Tia, Tib and Tic to indicate the three variants.

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    Ask a Scientist here.

James Shorter et al.
The EMBO journal, 27(20), 2712-2724 (2008-10-04)
Self-templating amyloid forms of Sup35 constitute the yeast prion [PSI(+)]. How the protein-remodelling factor, Hsp104, collaborates with other chaperones to regulate [PSI(+)] inheritance remains poorly delineated. Here, we report how the Ssa and Ssb components of the Hsp70 chaperone system
Shingo Kikuchi et al.
The Plant cell, 21(6), 1781-1797 (2009-06-18)
Chloroplast protein import is mediated by two hetero-oligomeric protein complexes, the Tic and Toc translocons, which are located in the inner and outer envelope membranes. At the inner membrane, many Tic components have been identified and characterized, but it remains
Kine Gregersen et al.
International journal of general medicine, 4, 555-560 (2011-09-03)
Food hypersensitivity is commonly suspected, but seldom verified. Patients with subjective food hypersensitivity suffer from both intestinal and extraintestinal health complaints. Abnormalities of the enterochromaffin cells may play a role in the pathogenesis. The aim of this study was to
Astrid F Nottebaum et al.
The Journal of experimental medicine, 205(12), 2929-2945 (2008-11-19)
We have shown recently that vascular endothelial protein tyrosine phosphatase (VE-PTP), an endothelial-specific membrane protein, associates with vascular endothelial (VE)-cadherin and enhances VE-cadherin function in transfected cells (Nawroth, R., G. Poell, A. Ranft, U. Samulowitz, G. Fachinger, M. Golding, D.T.
I B Svendsen et al.
Carlsberg research communications, 54(6), 231-239 (1989-01-01)
A trypsin inhibitor with a Km of 5 x 10(-5) M has been isolated from kohlrabi (Brassica napus var. rapifera). Subtilisin DY is inhibited only weakly and chymotrypsin not at all. The inhibitor is closely related to napin as determined
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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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