GingisREX™
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GingisREX (RgpB) is an arginine-specific protease that digests proteins C-terminally of arginine residues, including Arg-Pro linkages that are difficult to digest with other enzymes.

SmartEnzymes™
GingisREX can be used in peptide mapping, de novo peptide sequencing and analysis of post-translational modifications.
Digests any peptide or protein containing arginine, including Arg-Pro motifs
60 min reaction
Active in 6 M urea and 0.1% SDS
Digests C-terminally of arginine residues


GingisREX is a cysteine protease that specifically digests peptide bonds C-terminally to arginine residues, including arginine linked to proline. Cysteine is required for enzymatic activity.
Longer peptides are generated, as compared to trypsin digestion, which can be resolved and identified by high-resolution MS. This offers more options in sample preparation for bottom-up approaches, to achieve alternative digestion profiles and increased sequence coverage. GingisREX does not have activity at lysines, as commonly observed using Arg-C. The enzyme is active at a broad pH range of 5.0 – 9.0, it requires cysteine and is inhibited by guanidine hydrochloride.
The enzyme is purified from Porphyromonas gingivalis.
Arginine-specific peptide mapping with improved perfomance over Arg-C, generates larger peptides complementary to trypsin.
Highly specific arginine-specific protease with limited off-target digestion, enabling clean peptide maps and high-confidence LC-MS data analysis.
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Download Scientific Poster

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No, GingisREX is inhibited by GdHCl even in low concentrations. This chaotrope should be avoided.
Yes, cysteine is required for both activity and specificity of the GingisREX enzyme.
The digestion time is affected by many factors like the enzyme to sample ratio, pH of the digestion reaction, and the sample characteristics. The reaction time needs to be optimized for each specific case.
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