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T9128

Sigma-Aldrich

Trypsin inhibitor from Glycine max (soybean)

lyophilized powder

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Synonym(s):
SBTI
CAS Number:
EC Number:
MDL number:
NACRES:
NA.77

biological source

Glycine max (soybean)

Quality Level

type

Type II-S

form

lyophilized powder

mol wt

20,100 Da

technique(s)

inhibition assay: 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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This Item
93620T6414SRE0044
Quality Level

300

Quality Level

-

Quality Level

100

Quality Level

400

form

lyophilized powder

form

lyophilized powder

form

solution

form

lyophilized powder

shipped in

ambient

shipped in

wet ice

shipped in

dry ice

shipped in

wet ice

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

solubility

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

solubility

0.1 M phosphate pH 7.6: 5 mg/mL, clear, colorless to almost colorless

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

0.067 M sodium phosphate buffer, pH 7.6: 1 mg/mL, clear, colorless to very faintly yellow

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 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.

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.

Analysis Note

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

pictograms

Health hazard

signalword

Danger

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Dolores D Mruk et al.
Methods in molecular biology (Clifton, N.J.), 763, 237-252 (2011-08-30)
The use of an in vitro system based on primary cultures of Sertoli cells isolated from rat testes has greatly facilitated the study of the blood-testis barrier in recent years. Herein, we summarize the detailed procedures on the isolation of
I T Padol et al.
Infection and immunity, 69(6), 3891-3896 (2001-05-12)
As a bacterial product, Helicobacter pylori lipopolysaccharide (LPS) can originate in close proximity to parietal cells, but the role of this uniquely structured endotoxin on acid secretion has not been fully investigated and remains unclear. The purpose of this study
Patrik Hollos et al.
eNeuro, 7(1) (2020-01-16)
In this study, we use an optogenetic inhibitor of c-Jun NH2-terminal kinase (JNK) in dendritic spine sub-compartments of rat hippocampal neurons. We show that JNK inhibition exerts rapid (within seconds) reorganization of actin in the spine-head. Using real-time Förster resonance
Ho Am Jang et al.
Developmental and comparative immunology, 67, 97-106 (2016-11-09)
Riptortus pedestris, a common pest in soybean fields, harbors a symbiont Burkholderia in a specialized posterior midgut region of insects. Every generation of second nymphs acquires new Burkholderia cells from the environment. We compared in vitro cultured Burkholderia with newly in vivo
Graeme S Cottrell et al.
Gastroenterology, 132(7), 2422-2437 (2007-06-16)
We studied the role of protease-activated receptor 2 (PAR(2)) and its activating enzymes, trypsins and tryptase, in Clostridium difficile toxin A (TxA)-induced enteritis. We injected TxA into ileal loops in PAR(2) or dipeptidyl peptidase I (DPPI) knockout mice or in

Protocols

This technical article described the Enzymatic Assay of Trypsin Inhibitor.

Chromatograms

application for HPLC

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