rLys-C, Mass Spec Grade

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 ...

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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.

Features - Benefits

• Competitive Performance: Matches cleavage specificity of a native Lys-C. Proteolytic activity is similar.
• Purity: No contaminating peptides are identified with reverse-phase HPLC.
• Application-Qualified: Each lot is qualified by mass spectrometry.
• Tolerance to Protein Denaturing Conditions: Retains activity in 8M urea.
• Cost-Effective: Severalfold price reduction as compared to a native Lys-C.

Applications

• Peptide mapping.
• Protein identification.

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