Sign In to View Organizational & Contract Pricing.
Select a Size
20 μG
$442.00
100 μG
$1,540.00
$442.00
Ships within 2 weeks. (Orders outside of US and Europe, please allow an additional 1-2 weeks for delivery)
Skip To
1 of 4
This Item | |||
|---|---|---|---|
| grade Proteomics Grade | grade Proteomics Grade | grade protein sequencing grade | grade Proteomics Grade |
| biological source Achromobacter lyticus | biological source Achromobacter lyticus | biological source bacterial (Lysobacter enzymogenes) | biological source - |
| form lyophilized powder | form ready-to-use solution | form lyophilized | form lyophilized |
| recombinant expressed in E. coli (206-473aa) | recombinant expressed in E. coli (206-473aa) | recombinant - | recombinant - |
| storage temp. −20°C | storage temp. −20°C | storage temp. 2-8°C | storage temp. 2-8°C |
| UniProt accession no. | UniProt accession no. | UniProt accession no. | UniProt accession no. - |
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.
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.
Biochem/physiol Actions
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.
Packaging
1mg/ml in Plastic
Preparation Note
Catalytic pH range 9.0-9.5. Catalytic temperature range 30-37 °C.
Reconstitute in sterile water.
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.
signalword
Danger
Storage Class
11 - Combustible Solids
wgk
WGK 3
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Active Filters
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service



