Immobilized Trypsin is TPCK Treated Trypsin immobilized on 4% agarose that eliminates the contamination of protein digests by the trypsin

Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, arginine and lysine residues and typically there is little or no cleavage at arginyl-proline and lysyl-proline bonds. The distribution of these residues in proteins allows trypsin digestion to produce peptides that are readily identified by mass spectrometry. Native trypsin is prone to autolysis that results in pseudotrypsin, which exhibits a broader proteolytic specificity (a chymotrypsin like activity) and trypsin fragments that interfere with sequence analysis.

The Trypsin is TPCK treated to inactive the interfering chymotrypsin activity and the resulting protein is affinity purified. Immobilzed Trypsin is supplied as a 50% slurry containing glycerol and sodium azide as a preservative.

The immobilized trypsin is readily removed by separating the agarose from the digestion solution.