Trypsin specifically hydrolyzes peptide bonds at the carboxylic sides of lysine and arginine residues. Unmodified trypsin is subject to autolysis, generating fragments that can interfere with protein sequencing, HPLC or mass spectrometry analysis of the peptides. In addition, autolysis can result in the generation of pseudotrypsin, which has been shown to exhibit an additional chymotrypsin-like specificity. Promega Trypsin has been modified by reductive methylation, rendering it extremely resistant to autolytic digestion. In functional stability tests, modified trypsin retains at least two times as much activity a...
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Trypsin specifically hydrolyzes peptide bonds at the carboxylic sides of lysine and arginine residues. Unmodified trypsin is subject to autolysis, generating fragments that can interfere with protein sequencing, HPLC or mass spectrometry analysis of the peptides. In addition, autolysis can result in the generation of pseudotrypsin, which has been shown to exhibit an additional chymotrypsin-like specificity. Promega Trypsin has been modified by reductive methylation, rendering it extremely resistant to autolytic digestion. In functional stability tests, modified trypsin retains at least two times as much activity as unmodified trypsin after a 3-hour incubation at 37°C.
The sequencing grade of modified trypsin has been further improved by TPCK treatment followed by affinity purification yielding a highly active and stable molecule. Sequencing grade modified trypsin is provided as a frozen liquid in convenient 20μg aliquots with a stability-optimized dilution buffer. A protease:protein ratio of 1:100 to 1:20 (w/w) is recommended for protein sequencing.
Recommended Reaction Buffer: 50mM NH4HCO3 (pH 7.8).
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Sequencing Grade Modified Trypsin, Frozen
Sequencing Grade Modified Trypsin, Porcine, Frozen (liquid 0.5mg/ml)
Trypsin Resuspension Dilution Buffer
Store at –70°C.
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V5113 For Laboratory Use. Outside of the United States, this product is intended for research use only unless otherwise stated.