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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:
EC Number:
MDL number:
NACRES:
NA.77

biological source

Glycine max (soybean)

Quality Level

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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1 of 4

This Item
T9767T9128T6522
form

powder

form

powder

form

lyophilized powder

form

powder

mol wt

20,100 Da

mol wt

20,000 Da

mol wt

20,100 Da

mol wt

20.1 kDa

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

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

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

solubility

balanced salt solution: 1 mg/mL, serum-free medium: soluble

shipped in

ambient

shipped in

ambient

shipped in

ambient

shipped in

ambient

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°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.

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.

Certificates of Analysis (COA)

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The Journal of clinical investigation, 118(7), 2574-2582 (2008-06-24)
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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
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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

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.

Chromatograms

application for HPLC

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