rLys-C, Mass Spec Grade, is a recombinant Lys-C expressed in E. coli. Sequence origin of rLys-C is Protease IV from Pseudomonas aeruginosa. Similar to a native Lys-C, rLys-C cleaves at the carboxyl side of lysine residues with exceptional specificity. rLys-C retains proteolytic activity under protein denaturing conditions such as 8M urea, which is used to improve digestion of proteolytically resistant proteins. rLys-C activity is optimal in the pH range of 8–9. The protease is supplied in a lyophilized form along with a Reconstitution Buffer, which is formulated to increase stability of rLys-C solution. Frozen rLys-C solution can be stored for a month at –20ºC without detectable loss of activity. rLys-C is recommended for digestion of single proteins and complex protein mixtures in-solution and in-gel.
rLys-C has been shown to be free of contaminating peptides by reverse-phase HPLC. This recombinant product is severalfold less expensive than, yet retains the activity of native rLys-C.
- Peptide mapping
- Protein identification