Trypsin specifically cleaves peptide bonds on the C-terminal side of lysine and arginine residues (hydrolysis is slowed by adjacent acidic residues and blocked entirely by a following proline), giving it high substrate specificity valuable for controlled protein digestion. In cell culture, this same proteolytic activity is exploited to cleave adhesion proteins anchoring cells to culture surfaces, enabling gentle, reproducible cell harvesting. The enzyme exists as two subunits (a-trypsin and ß-trypsin) and is commonly formulated with EDTA, which chelates calcium/magnesium ions that would otherwise mask trypsin's target peptide bonds, enhancing dissociation efficiency.
Trypsin (1:250) is a porcine pancreas-derived serine protease enzyme widely used for cell dissociation, tissue disaggregation, and protein digestion in proteomics research. The "1:250" designation reflects standardized activity testing, indicating that one part trypsin digests 250 parts casein under defined USP assay conditions.
| Chemical Name | Trypsin (1:250), Porcine Pancreas |
| CAS Number | 9002-07-7 |
| IUPAC Name | Porcine Pancreatic Trypsin (EC 3.4.21.4) |
| Molecular Formula | C₃₅H₄₇N₇O₁₀ |
| Molecular Weight | ~23.2 – 23.3 kDa (or about 23,200 to 24,000 g/mol) g/mol |
| Boiling Point | na |
| Density | na |
| Refractive Index | na |
| Flash Point | na |
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