CAS · 9002-07-7
Product Overview
Trypsin is a high-purity biochemical-reagents supplied for industrial and specialty chemical applications. Contact our team for specifications, packaging options and lead times.
Product Specifications
| Grade | USP42 |
|---|---|
| Appearance | White or almost white lyophilized powder |
| Solubility | 500,000 USP Trypsin Units soluble in 10 mL water and 10 mL saline TS |
| Loss on drying | 5.0% max |
| Residue on ignition | 2.5% max |
| Limit of chymotrypsin | 50 USP Units per 2500 USP Trypsin Units/mg max |
| Assay | 1000 USP Units/mg min (calculated on dried basis) |
| Pseudomonas aeruginosa | Negative |
| Salmonella | Negative |
| Staphylococcus aureus | Negative |
| E. coli | 1000 CFU/g max |
| TAMC | 1000 CFU/g max |
| TYMC | 100 CFU/g max |
Applications
Trypsin is a widely used proteolytic enzyme applied in pharmaceuticals, biotechnology, and research laboratories. In cell culture, it is commonly employed to detach adherent cells from culture vessels for passaging, subculturing, or analysis. In protein chemistry and biochemistry, trypsin is used for controlled digestion of proteins into peptides, facilitating mass spectrometry, proteomic studies, and peptide mapping. It is also applied in the preparation of bioactive peptide fragments, enzyme assays, and in the study of enzymatic kinetics. In industrial and pharmaceutical contexts, trypsin can be incorporated into wound debridement formulations and digestive enzyme supplements. Additionally, it is used in research for studying enzyme-substrate interactions, protein processing, and cellular signaling pathways.
Benefits
The benefits of trypsin stem from its high specificity, efficiency, and stability under controlled conditions. Its ability to selectively cleave peptide bonds at the carboxyl side of lysine and arginine residues allows precise protein digestion and reproducible experimental results. Trypsin is highly effective in detaching cells without causing significant damage when properly used, improving consistency in cell culture workflows. Its enzymatic activity facilitates rapid and predictable peptide generation for proteomics and analytical studies. Furthermore, its availability in purified, stabilized forms enhances ease of handling, storage, and reproducibility across research and industrial applications, supporting consistent performance in protein processing and analytical experiments.
Conclusion
Trypsin is a versatile proteolytic enzyme extensively used in cell culture, protein analysis, and pharmaceutical formulations. Its specificity, efficiency, and stability make it a key tool for protein digestion, peptide mapping, enzymatic studies, and cell culture applications. These properties ensure its continued importance in laboratory research, industrial processes, and biotechnological applications.
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