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"Recombinant Lys-C for proteomics"

Owing to efficient proteolysis and particular advantages of trypsin-generated peptides for mass spectrometry analysis, trypsin is the most widely used proteomic protease.  Recently, however, LysC has been increasingly used as either a trypsin alternate or as supplement.   Its increasing favor is largely due to its ability to perform proteolytic digestion under protein denaturing conditions, an attribute that can greatly extend the observable proteome. Lys-C is found in number of bacterial hosts with Lysobacter enzymogenes being used as a most popular source of commercially available Lys-C preparations. Recently, we have developed a recombinant form of Lys-C from Pseudomonas aeruginosa. Similarly to Lysobacter Lys-C, the recombinant Pseudomonas Lys-C showed high cleavage specificity to lysine residues and tolerated denaturing conditions up to 8M urea. In our model study with use of yeast total protein extract the recombinant Lys-C efficiently digested yeast total protein and provided a similar number of identified peptides and proteins as compared to Lysobacter Lys-C. Recombinant Lys-C performed equally well in in-gel protein digestion. Reduced price and competitive performance make recombinant Lys-C a good fit for use in proteomic analysis.


This webinar is presented by Sergei Saveliev, Ph.D., R&D scientist of Promega

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