LYSC9001
Lys-c (lysyl-endopeptidase), Active
from Achromobacter lyticus, recombinant, expressed in E. coli (206-473aa), tag-free, powder
Synonym(s):
API, Lysyl endopeptidase, Protease I
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General description
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.
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.
Specificity
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 °C.
Application
The enzyme functions optimally between 30-37 °C and suffers from degradation when subjected to temperatures above 50 °C. Lysyl-endopeptidase retains complete activity after incubation in 4M urea or in 0.1% SDS solution for up to 6 hours at 30 °C.
Packaging
1mg/ml in Plastic
Preparation Note
Catalytic pH range 9.0-9.5. Catalytic temperature range 30-37 °C.
Reconstitution
Reconstitute in sterile water.
Storage and Stability
Store product at -20°C. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles once the protein has been resolubilized in sterile water.
Other Notes
For R&D only.
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Danger
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - Skin Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
Certificates of Analysis (COA)
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