Lys-c (lysyl-endopeptidase), Active

3.4.21.50 ( BRENDA | IUBMB )

Recombinant tag-free Achromobacter lyticus Lys-c (lysyl-endopeptidase) (206-473aa) was expressed in E.coli cells.

Overview
Lysyl-endopeptidase (Lys-c) was isolated from the Gram-negative soil bacterium Achromobacter lyticus by Msaki 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.

This enzyme hydrolyzes amide and peptide ester bonds at the carboxylic side of lysine and S-aminoethylcysteine residues, at a catalytic pH range of 9.0-9.5, catalytic temperature range of 30-37 ℃.

The enzyme functions optimally between 30-37 ℃ and suffers from degradation when subjected to temperatures above 50 ℃. Lysyl-endopeptidase retains complete activity after incubation in 4M urea or in 0.1% SDS solution for up to 6 hours at 30 ℃.

Catalytic pH range 9.0-9.5. Catalytic temperature range 30-37 ℃.

For R&D only.

200

expressed in E. coli (206-473aa)

buffered aqueous glycerol solution

1 mg/mL

8.5

9.0 - 9.5 (catalytic)

P15636

dry ice

−20℃

1mg/ml in Plastic

Store product at -20℃ for up to one year. Avoid freeze/thaw cycles.

12 - Non Combustible Liquids

WGK 1