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.
API, Protease I, Lysyl endopeptidase
Sample Purity Data. For specific information on a given lot, see related technical data sheet.
Enzyme Commission Number:
Storage, Stability, and Shipping:
Store product at –20oC for up to 1 year. Aliquot enzymes to avoid freeze / thaw cycles.
Catalytic pH range: 9.0 ~ 9.5; catalytic temperature range: 30 ~ 37oC
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