Trypsin is a single chain polypeptide of 223 amino acid residues and is a member of the serine protease family. The active site amino acid residues of trypsin include HIs46 and Ser183. Trypsin is produced by removing the N-terminal hexapeptide from trypsinogen which is cleaved at the peptide bonds at Lys6 - lle7. This cleavage yields a single chain native form of trypsin called β-Trypsin. Ensuing autolysis of β-Trypsin results in α-Trypsin having two peptide chains bound by disulphide bonds. This enzyme predominantly cleaves peptide chains at the carboxyl side of Arginine and Lysine, with an exception when either one is followed by a Proline. or trypsin digestion of peptides, use a ratio of about 1:100 to 1:20 for trypsin:peptide. The typical use for this product is in removing adherent cells from a culture surface. The concentration of trypsin necessary to dislodge cells from their substrate is dependent primarily on the cell type and the age of the culture. Trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestionsns?. Additional applications include assessing crystallization by membrane-based techniques and in a study to determine that protein folding rates and yields can be limited by the presence of kinetic traps.
Names and Identifiers
WGK Germany
1
RTECS
YN5075000
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H2413505
