Thermo Scientific Lys-C Protease, MS Grade, is a highly purified native endoproteinase validated for maximum activity and stability in proteomic applications.
This Lys-C is a mass spectrometry (MS)-grade serine protease isolated from Lysobacter enzymogenes. Lys-C has high activity and specificity for lysine residues resulting in larger peptides and less sample complexity than trypsin (i.e. fewer peptides). Unlike trypsin, Lys-C can cleave lysines followed by prolines, making it ideal for sequential protein digestion followed by trypsin to decrease missed cleavages. These unique Lys-C properties ensure high digestion efficiency when used alone or followed by tryptic digestion. Additionally, Lys-C prototypic peptides typically have higher charge states, making it an enzyme of choice for use with ETD fragmentation. Lys-C is commonly in phosphopeptide enrichment workflows because it generates peptides with primary amines at both the N-and C-terminus allowing the fragments to be double-labeled with amine-reactive isobaric tags. This results in enhanced peptide ionization and improved limits of quantitation since more fragment ions can be re-isolated during MS3 acquisition. This enzyme can be used for in-solution or in-gel digestion workflows to produce peptides for LC-MS/MS protein identification. This Lys-C enzyme is packaged lyophilized (20µg).
- Enhanced digestion – use in tandem with trypsin to decrease tryptic missed cleavages
- Increased sequence coverage – better protein characterization results from overlapping peptides with complementary chromatographic, ionization and fragmentation properties
- Versatile – effective enzyme activity under highly denaturing conditions (e.g., 8M urea)
- C-terminal lysine cleavage specificity – at least 90% for a complex protein sample
- Stable – provided in a lyophilized format
- Improved sequence coverage of protein digests
- De novo sequencing
- Epigenetic studies
- In-gel and in-solution digestion of proteins
The endoproteinase LysC specifically hydrolyzes proteins at the carboxyl side of lysine. Efficient protein digestion can be completed in 2 hours at 37°C. LysC remains active in highly denaturing conditions such as 8M urea, 2M guanidine•HCl, 1% SDS, 2% CHAPS and 40% acetonitrile and functions well within pH 7-9 (maximal activity at pH 8). This lyophilized enzyme has a mass of 30 kDa and is stable for 1 year when stored at -20°C.
- Simpson, Richard. (2003) Proteins and Proteomics, A Laboratory Manual, Cold Spring Harbor Press.
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