LYSC9000
Lys-c (lysyl-endopeptidase), Active
from Achromobacter lyticus, recombinant, expressed in E. coli (206-473aa), tag-free, solution
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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.
Storage and Stability
Store product at -20°C for up to one year. Avoid freeze/thaw cycles.
Other Notes
For R&D only.
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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Articles
Pretreatment with Mucinase StcE increases glycopeptide identification from mucin samples, enhancing sample preparation efficiency for glycopeptide analysis.
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