Immobilized Trypsin is TPCK Treated Trypsinimmobilized on 4% agarose that eliminates the contamination
of protein digests by the trypsin. The immobilized trypsin is readily removed by separating the agarose from
the digestion solution.
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
Immobilzed Trypsin is supplied as a 50% slurry containing glycerol and sodium azide as a preservative.
• Eliminate contamination with trypsin
• Source: Bovine
• Activity: ≥200 TAME units/ml resin (1 unit= 1µmole TAME (p-toluenesulfonyl-L-arginine methyl ester)
hydrolyzed/min at pH8.2, 25°C)
• Support: 4% Cross-linked Agarose
Instruction sheet (PDF)