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EnzymoPure™,suitable for mass spectrometry (MS),Recombinant,≥99%(HPLC),≥25 U/mg protein Recombinant,Suitable for mass spectrometry (MS),EnzymoPure™ for sensitive chromatographic and analytical workflows requiring minimal baseline interference.
Store at -20°C,Avoid repeated freezing and thawing Ships Ice chest + Ice pads Check lot-specific COA for exact specifications.
SDS, COA, datasheet, and spec sheet available for download. Lot-specific COA accessible via lot number lookup.
Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.
MS-grade Lys-C protease specifically cleaves peptide bonds at the C-terminus of lysine residues. It can improve the digestion of hard-to-hydrolyze proteins and is recommended for use in 6–8 M urea solutions. Reconstitution Solution: Reconstitute Lys-C protease in 50 mM acetic acid buffer. pH Range: rLys-C exhibits optimal activity at pH 8–9. Application: Lys-C protease specifically cleaves lysine (K) residues in denatured proteins that are resistant to proteolysis. It is recommended for use in combination with trypsin. Recommended SOP for Mixed Protease Digestion: A. General In-Solution Digestion Use a mixture of 100 μg trypsin and 20 μg Lys-C at a protein-to-protease ratio (w/w) of 25:1. Incubate overnight at 37°C for 13–16 hours. Tip: Urea concentration should be <1 M; use 50 mM Tris-HCl buffer (pH 8). B. 1+1 Step In-Solution Digestion 1. Use a mixture of 100 μg trypsin and 20 μg Lys-C at a protein-to-protease ratio (w/w) of 25:1. Incubate at 37°C for 2–4 hours. Tip: Urea concentration should be 6–8 M; use 50 mM Tris-HCl buffer (pH 8). 2. Dilute the solution 6-fold and incubate overnight at 37°C for 13–16 hours. Tip: Urea concentration should be <1 M; use 50 mM Tris-HCl buffer (pH 8).
Comprehensive hazard, handling, storage, and regulatory compliance document.
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