T9003
Trypsin inhibitor from Glycine max (soybean)
lyophilized powder
Synonym(s):
SBTI
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About This Item
Recommended Products
biological source
Glycine max (soybean)
Quality Level
form
lyophilized powder
mol wt
20.1 kDa
solubility
H2O: >10 mg/mL
phosphate buffer: >10 mg/mL (hazy above 10 mg/ml)
soluble
application(s)
diagnostic assay manufacturing
storage temp.
2-8°C
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Application
Trypsin has been used in a study to assess the potential application in animal cell culture of an alkaline protease from a non-toxigenic mangrove isolate of Vibrio sp. V26. Trypsin has also been used in a study to improve the detection of fungi in eosinophilic mucin.
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.
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 1.0-3.0 mg trypsin of activity ~10,000 BAEE units per mg protein.
Signal Word
Danger
Hazard Statements
Precautionary Statements
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)
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Alkaline protease from a non-toxigenic mangrove isolate of Vibrio sp. V26 with potential application in animal cell culture
Manjusha, K., et al.
Cytotechnology, DOI: 10-DOI: 10 (2012)
Frank Helle et al.
American journal of physiology. Renal physiology, 298(5), F1170-F1177 (2010-03-12)
Inhibition of nitric oxide synthesis (NOS) induces hypertension and heavy proteinuria. Renal structure and function have shown striking improvement after interventions targeting ANG II or endothelin (ET) receptors in rats recovering after long-term NOS inhibition. To search for mechanisms underlying
Hermann Bultmann et al.
Antimicrobial agents and chemotherapy, 54(10), 4275-4289 (2010-07-21)
The linear cationic amphiphilic EB peptide, derived from the FGF4 signal sequence, was previously shown to be virucidal and to block herpes simplex type I (HSV-1) entry (H. Bultmann, J. S. Busse, and C. R. Brandt, J. Virol. 75:2634-2645, 2001).
Joelle M-J Romac et al.
Nature communications, 9(1), 1715-1715 (2018-05-02)
Merely touching the pancreas can lead to premature zymogen activation and pancreatitis but the mechanism is not completely understood. Here we demonstrate that pancreatic acinar cells express the mechanoreceptor Piezo1 and application of pressure within the gland produces pancreatitis. To
Joshua K Endow et al.
PloS one, 11(12), e0167802-e0167802 (2016-12-10)
PolyGly is present in many proteins in various organisms. One example is found in a transmembrane β-barrel protein, translocon at the outer-envelope-membrane of chloroplasts 75 (Toc75). Toc75 requires its N-terminal extension (t75) for proper localization. t75 comprises signals for chloroplast
Protocols
Enzymatic Assay of Trypsin Inhibitor
Chromatograms
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