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Merck

LYSC9000

Sigma-Aldrich

Lys-c (lysyl-endopeptidase), Active

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

Sinónimos:

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

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About This Item

Comisión internacional de enzimas:
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

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

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Artículos

Pretreatment with Mucinase StcE increases glycopeptide identification from mucin samples, enhancing sample preparation efficiency for glycopeptide analysis.

Pretreatment with Mucinase StcE increases glycopeptide identification from mucin samples, enhancing sample preparation efficiency for glycopeptide analysis.

Pretreatment with Mucinase StcE increases glycopeptide identification from mucin samples, enhancing sample preparation efficiency for glycopeptide analysis.

Pretreatment with Mucinase StcE increases glycopeptide identification from mucin samples, enhancing sample preparation efficiency for glycopeptide analysis.

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