Description
General description
Soybean trypsin inhibitor was first isolated by Kunitz. Several other related inhibitors are also found in soybeans. Trypsin inhibitor from soybeans is a monomeric protein containing 181 amino acid residues in a single polypeptide chain crosslinked by two disulfide bridges. Soybean trypsin inhibitor inhibits trypsin, and to a lesser extent chymotrypsin and plasmin.
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.
Features and Benefits
Features: Qualified Raw Materials: Products that meet the stringent requirements of the Elevated Assurance Program, ensuring compliance with regulatory standards.
Comprehensive Documentation: Includes essential documents such as certificates, impurity profiles, and declarations to support audits and risk assessments.
M-Clarity™ Quality Attributes: Products are classified within the MQ300 quality segment or higher, demonstrating superior quality assurance. M-Clarity™ Program
Confirmed Process Controls: Established processes that ensure consistency and reliability in manufacturing.
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Freely Available Dossiers: Access to robust, ready-to-present product dossiers that include:Site quality assessment
ISO 9001 certificate
Detailed product specifications
Relevant declarations/statements (e.g., animal origin content, BSE/TSE, nitrosamine)
Benefits:Regulatory Compliance: Helps you meet compliance standards effectively, reducing the risk of regulatory issues.
Audit Readiness: Instills confidence during audits with comprehensive documentation and confirmed process controls, demonstrating your commitment to high-quality products.
Operational Transparency: Supports supply chain transparency, allowing you to track and verify the quality of raw materials.
Enhanced Support: Provides exceptional quality-related information and tailored assistance to meet your specific needs.
Risk Mitigation: Facilitates thorough risk assessments with detailed documentation, helping you manage potential compliance challenges.
Informed Decision-Making: Access to clear and comprehensive product information enables better decision-making and enhances operational efficiency.
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.
Other Notes
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.
The soybean trypsin inhibitor is a monomeric protein containing 181 amino acid residues in a single polypeptide chain crosslinked by two disulfide bridges.
Legal Information
M-CLARITY is a trademark of Merck KGaA, Darmstadt, Germany
