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LysargiNase mirrors trypsin for protein C-terminal and methylation-site identification.

Nature methods (2014-11-25)
Pitter F Huesgen, Philipp F Lange, Lindsay D Rogers, Nestor Solis, Ulrich Eckhard, Oded Kleifeld, Theodoros Goulas, F Xavier Gomis-Rüth, Christopher M Overall

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 ion-dominated spectra. This improved protein C terminal-peptide identification and several arginine-rich phosphosite assignments. Notably, cleavage also occurred at methylated or dimethylated lysine and arginine, facilitating detection of these epigenetic modifications.

Product Number
Product Description

LysargiNase, suitable for peptide or protein digestion insolution or in gel
Endoproteinase Arg-C from mouse submaxillary gland, suitable for protein sequencing, lyophilized powder

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