Trypsin is a pancreatic serine protease formed by removing trypsinogen’s amino-terminal hexapeptide, cleaved at the peptide bond of Lys-lle. It is a single-chain polypeptide consisting of 223 amino acid residues.
Trypsin cleaves peptides on the carboxyl-side of lysine and arginine residues unless either is followed by a proline residue. This protease is also capable of cleaving ester and amide links of amino acid synthetic-derivatives. A pH range of 7-9 will allow for optimal trypsin activity.
• Digestion of peptides, digestion of proteins for proteomics research, gel-digestions
• Cell culture: removal of adherent cells from a culture surface, re-suspension of cells in cell culture
• Tissue disassociation
• Protein sequencing
• Trypsin Content: >2,500 U/mg
• EC Number: 220.127.116.11
|Synonyms||Tryptar, Trypure, Trypsevas, Parenzyme, Parenzymol|
|Appearance||White crystalline powder|
|Handling||Use in a chemical fume hood, with air supplied by an independent system. Avoid inhalation, contact with eyes, skin and clothing. Avoid the formation of dust and aerosols. Use in a well-ventilated area. Keep away from sources of ignition. Avoid prolonged or repeated exposure. Store in cool, well-ventilated area. Keep away from direct sunlight. Keep container tightly sealed until ready for use. Recommended storage temperature -20 °C. Product is sensitive to light and moisture. Storage class (TRGS 510): Non Combustible Solids.|
|Certificate of Analysis 1||T-2763, H1211A.pdf|
|Certificate of Analysis 2||T-2763, H1211.pdf|
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