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ENDOLYSS-RO

Roche

Endoproteinase Lys-C Sequencing Grade

from Lysobacter enzymogenes

Synonym(s):

lys-c, lysyl endopeptidase, protease

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About This Item

Enzyme Commission number:
3.4.21.50 (BRENDA, IUBMB)
UNSPSC Code:
12352204

biological source

bacterial (Lysobacter enzymogenes)

grade

protein sequencing grade

form

lyophilized

specific activity

≥200 units/mg protein (at 25 °C, with Chromozym PL)

mol wt

33 kDa by SDS-PAGE (reducing)

purified by

electrophoresis

packaging

pkg of 3 × 5 μg (11047825001)
pkg of 5 μg (11420429001)

manufacturer/tradename

Roche

storage condition

(Keep container tightly closed in a dry and well-ventilated place.)

technique(s)

activity assay: suitable

color

white

optimum pH

8.5-8.8

pH range

5-12

solubility

water: soluble

suitability

suitable for enzyme test

UniProt accession no.

Q7M135

storage temp.

2-8°C

Related Categories

General description

Endoproteinase Lys-C Sequencing Grade is isolated from Lysobacter enzymogenes as a highly purified and specific protease. Endoproteinase Lys-C from Lysobacter enzymogenes is a member of the peptidase S1 family. It is mostly used for the initial fragmentation of polypeptide chains in protein sequence analysis.

Specificity

This enzyme is a serine protease that specifically hydrolyzes amide, ester, and peptide bonds at the carboxylic side of Lys (in Tris-HCl buffer, pH 7.0 to 9.0).
Heat inactivation: Enzyme can be denatured using heat (5 min at 100 °C) or by TCA.

Application

Use Endoproteinase Lys-C Sequencing Grade  for protein structure analysis and for sequence analysis. It is suitable to digest proteins in solution, in polyacrylamide gels or on blotting membranes.

Preparation Note

Storage conditions (working solution): +2 to +8 °C

Reconstitution

Lyophilized Endoproteinase Lys-C sequencing grade is reconstituted in 50 μl double-dist. water. This results in a buffer concentration of 50 mM Hepes, pH 8.0, 10 mM EDTA and 5 mg/ml raffinose. To avoid autolysis, the incubation temperature should not exceed 37 °C.
Stable in 4 M urea.

Other Notes

For life science research only. Not for use in diagnostic procedures.

Storage Class Code

11 - Combustible Solids

WGK

WGK 2

Flash Point(F)

does not flash

Flash Point(C)

does not flash

Certificates of Analysis (COA)

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H Alexander Ebhardt et al.
Rapid communications in mass spectrometry : RCM, 28(24), 2735-2743 (2014-11-08)
Tandem mass (MS/MS) spectra generated by collision-induced dissociation (CID) typically lack redundant peptide sequence information in the form of e.g. b- and y-ion series due to frequent use of sequence-specific endopeptidases cleaving C- or N-terminal to Arg or Lys residues.
Heterologous expression and pro-peptide supported refolding of the high specific endopeptidase Lys-C
Stressler T, et al.
Protein Expression and Purification, 118, 31-38 (2016)
Tao Xu et al.
Nature protocols, 4(3), 325-332 (2009-02-21)
This protocol outlines the essential steps of mass spectrometry-based analysis of protein samples that can be used to identify post-translational arginylation. We describe special considerations for sample preparation and digestion, mass spectrometry analysis using high-precision instruments, database searching for the
Jung Hun Oh et al.
Journal of proteome research, 10(3), 1406-1415 (2011-01-14)
Many efforts have been made to discover novel bio-markers for early disease detection in oncology. However, the lack of efficient computational strategies impedes the discovery of disease-specific biomarkers for better understanding and management of treatment outcomes. In this study, we
Jason A Wall et al.
American journal of physiology. Heart and circulatory physiology, 291(5), H2462-H2472 (2006-06-13)
Ischemia-reperfusion (I/R) has critical consequences in the heart. Recent studies on the functions of I/R-activated kinases, such as p38 mitogen-activated protein kinase (MAPK), showed that I/R injury is reduced in the hearts of transgenic mice that overexpress the p38 MAPK

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