EMS0008
LysargiNase Protease
Cleaves before lysine and arginine, suitable for mass spectrometry and complimentary to trypsin, recombinant, expressed in E. coli
Synonym(s):
LysargiNase mirrors trypsin for protein C-terminal and methylation-site identification
Skip To
Product Name
LysargiNase, suitable for peptide or protein digestion insolution or in gel
recombinant
expressed in E. coli
form
solid
shipped in
ambient
Quality Level
Related Categories
1 of 4
This Item | TRYPSEQ-RO | EMS0007 | EMS0006 |
|---|---|---|---|
| recombinant expressed in E. coli | recombinant - | recombinant expressed in Pichia pastoris | recombinant expressed in Pichia pastoris |
| form solid | form lyophilized (salt-free) | form lyophilized powder | form lyophilized powder |
| shipped in ambient | shipped in - | shipped in wet ice | shipped in wet ice |
| Quality Level 100 | Quality Level 100 | Quality Level 200 | Quality Level 200 |
Application
LysargiNase is suitable for peptide or protein digestion in solution or in gel.
LysargiNase is suitable for peptide or protein digestion in solution or in gel. It is active under a variety of solvent conditions including 5 mM TCEP, 5% methanol, 5% acetonitrile, 0.8 M urea, 0.1% RapiGest, 1% deoxycholate, 0.2% SDS and 1% NP-40. It is active up to 55°C at pH 6 – 9. LysargiNase is reversibly inhibited by 1, 10-phenanthroline, EDTA and other calcium and zinc chelating agents. For peptide or protein digestion, a ratio of between 1:100 to 1:20 (w/w) enzyme:substrate is recommended.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
LysargiNase is a metalloproteinase found in the thermophilic archaea Methanosarcina acetivorans. It specifically cleaves before lysine and arginine residues in proteins. This cleavage results in peptides with molecular weights similar to tryptic peptides, but with N-terminal lysine or arginine residues that can be fragmented with b ion-dominated spectra. This can improve protein C-terminal peptide identification and several arginine rich phosphosite assignments. Unlike with trypsin, LysargiNase cleavage also occurs at methylated lysine and arginine, allowing detection of these epigenetic modifications.
LysargiNase is suitable for peptide or protein digestion in solution or in gel.
Other Notes
Concentration: Please refer to lot specific datasheet.
Each vial contains 20 µg LysargiNase, prepared by recombinant expression in E. coli and lyophilized from buffer.
Physical form
Each vial contains 20 µg LysargiNase, prepared by recombinant expression in E. coli and lyophilized from buffer. Upon reconstitution in 20 µL water, the enzyme is in 50 mM HEPES, 5 mM CaCl2, pH 7.5.
Preparation Note
Store the lyophilized product at -20°C for up to 2 years. After reconstitution, the unused material can be stored in the freezer in aliquots. Avoid repeated freeze thaw cycles.
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 1
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Le Zhang et al.
ACS chemical biology, 16(11), 2595-2603 (2021-11-05)
Methods for the selective labeling of biogenic functional groups on peptides are being developed and used in the workflow of both current and emerging proteomics technologies, such as single-molecule fluorosequencing. To achieve successful labeling with any one method requires that
Cynthia Tallant et al.
The Journal of biological chemistry, 281(26), 17920-17928 (2006-04-22)
The metzincin clan encompasses several families of zinc-dependent metalloproteases with proven function both in physiology and pathology. They act either as broad spectrum protein degraders or as sheddases, operating through limited proteolysis. Among the structurally uncharacterized metzincin families are the
Liana Tsiatsiani et al.
The FEBS journal, 282(14), 2612-2626 (2015-04-01)
Peptide-centered shotgun analysis of proteins has been the core technology in mass spectrometry based proteomics and has enabled numerous biological discoveries, such as the large-scale charting of protein-protein interaction networks, the quantitative analysis of protein post-translational modifications and even the
Kazuya Tsumagari et al.
STAR protocols, 2(3), 100682-100682 (2021-08-12)
Characterization of protein termini is essential for understanding how the proteome is generated through biological processes such as post-translational proteolytic events. Here, we introduce a practical protocol for terminomics to achieve simple and sensitive N- and C-terminal peptide enrichment. We
Pitter F Huesgen et al.
Nature methods, 12(1), 55-58 (2014-11-25)
To improve proteome coverage and protein C-terminal identification, we characterized the Methanosarcina acetivorans thermophilic proteinase LysargiNase, which cleaves before lysine and arginine up to 55 °C. Unlike trypsin, LysargiNase-generated peptides had N-terminal lysine or arginine residues and fragmented with b
Related Content
Active Filters
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service