Lysyl-endopeptidase (Lys-c) was isolated from the Gram-negative soil bacterium Achromobacter lyticus by Masaki et al. The protein hydrolyzes amide and peptide ester bonds at the carboxylic side of lysine and S-aminoethylcysteine residues making it an important tool for enzymatic protein sequencing and Lys-X compound synthesis. The enzyme functions optimally between 30 – 37oC and suffers from degradation when subjected to temperatures above 50oC. Lysyl-endopeptidase retains complete activity after incubation in 4M urea or in 0.1% SDS solution for up to 6 hours at 30oC. Conversely, the enzyme is inhibited by DFP, PMSF, TLCK. Lysyl-endopeptidase is involved during the production of recombinant insulin and in proteomics research.
Immobilized Lysyl-Endopeptidase is covalently cross-linked to an agarose matrix circumventing the need for enzyme removal after cleavage. The resin can be reused 10-20 times after regenerating when proper storage conditions are followed.
API, Protease I, Lysyl endopeptidase
Average Particle Size:
1 mg protein / ml matrix
Maximum Flow Rate, Pressure:
100 cm/h, 0.3 bar
Enzyme Commission Number:
Storage, Stability, and Shipping:
Store product at 2 - 4oC for up to 6 months.
Catalytic pH range: 8.0 ~ 9.5
Catalytic temperature range:
15 ~ 37oC
Substrate ratio: 1:200 ~1:2,000
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