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Immobilized Lys-c, Silica

Recombinant tag-free Lys-c (Lysyl-Endopeptidase) was expressed in E. coli cells.

Matrix: cross-linked silica Average Particle Size: 200 μm Ligand Density: 5 mg protein / ml matrix Maximum Flow Rate, Pressure: 300 cm/h, 2 bar
Catalog No. L585-31SN

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Silica immobilized proteases are amenable to large-scale proteolysis processes. 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 a silica matrix circumventing the need for enzyme removal after cleavage. The resin can be reused ~20 times after regenerating when proper storage conditions are followed.

Gene Aliases:

API, Protease I, Lysyl endopeptidase

Sample Data:

Enzyme Commission Number:


Storage, Stability, and Shipping:

Store product at 2 - 4oC for up to 6 months.

Digestion Conditions:

Catalytic pH Range: 8.0 ~ 9.5
Catalytic Temperature Range: 15 ~ 37oC
Enzyme : Substrate Ratio: 1:200 ~ 1:2,000

Product Datasheets

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