SDS
CofA
Description
Trypsin is a serine protease enzyme that plays a role in digestion by hydrolyzing proteins. Specifically, trypsin cleaves peptide bonds located on the carboxyl side of the amino acids arginine and lysine. It was once believed that trypsin was synthesized exclusively in the pancreas. However, it has been demonstrated that endothelial cells in many non-pancreatic tissues express trypsin in both mice and humans. Trypsin is a single-chain polypeptide consisting of 223 amino acid residues.
One of the most common uses of trypsin in the laboratory is in the digestion of proteins resistant to other proteolytic agents. It is also used extensively for the dissociation and culturing of cells in studies attempting to isolate and research individual cell types. Recent research has also indicated that trypsin derived from cod may be effective in combating certain pathogenic viruses and promoting the healing of wounds.
Applications
• 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
Specifications
• Trypsin Content: >2,500 U/mg
• pH range of 7-9 will allow for optimal trypsin activity
• EC Number: 3.4.21.4
| GHS PICTOGRAMS |   |
|---|---|
| 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. |
