"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.
is presented by
Sergei Saveliev, Ph.D., R&D scientist of Promega
Thank you for your request for the Promega @cademy
Recording / Presentation. To download the recording, please fill out and submit the following form. You will receive an email with the URL where you can download the
recording and the presentation.