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LYSC9000

Sigma-Aldrich

Lys-c (lysyl-endopeptidase), Active

from Achromobacter lyticus, recombinant, expressed in E. coli (206-473aa), tag-free, solution

Synonym(s):

Lys-c (lysyl-endopeptidase), Active, API, Lysyl endopeptidase, Protease I

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About This Item

Enzyme Commission number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Achromobacter lyticus

Quality Level

recombinant

expressed in E. coli (206-473aa)

grade

Proteomics Grade

form

ready-to-use solution

concentration

1 mg/mL

optimum pH

8.5

pH range

9.0-9.5(catalytic)

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

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.

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


Certificates of Analysis (COA)

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