Lys-C Protease, MS Grade (CAT#: Glyco-075CL)

Lys-C Protease, MS Grade, is a highly purified native endoproteinase validated for maximum activity and stability in proteomic applications.


Specific Inquiry
  • Datasheet
  • MSDS
  • COA

Specifications

  • Product Size
  • 20 µg
    100 µg
  • Final Product
  • Peptide
  • Workflow Step
  • Protein Digestion
  • Detection Method
  • Mass Spectrometry
  • Starting Material
  • Cell Lysate, Protein samples
  • For Use With (Equipment)
  • Mass Spectrometer
  • Contents & storage
  • Store at -20°C in a nonfrost-free freezer.

Background

  • Description
  • 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 (20 µg or 100 µg quantities).

    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.

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For research use only. Not intended for any clinical use. No products from Creative Biolabs may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative Biolabs.

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