biological source
bacterial (Lysobacter enzymogenes)
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.
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.
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.
Biochem/physiol Actions
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.
Heat inactivation: Enzyme can be denatured using heat (5 min at 100 °C) or by TCA.
Preparation Note
Storage conditions (working solution): +2 to +8 °C
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.
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
Regulatory Information
常规特殊物品
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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)
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
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
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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