Arg-C, also known as clostripain, is a heterodimeric cysteine endopeptidase derived from Hathewaya histolytica (Clostridium histolyticum). It specifically cleaves peptide bonds at the C-terminus of arginine residues, including those followed by proline, making it a valuable tool in proteomics research. Additionally, Arg-C can cleave lysine residues, albeit at a lower rate. This enzyme is activated by sulfhydryl reagents and requires calcium ions for optimal activity. Its unique specificity complements trypsin digestion, enhancing protein identification and post-translational modification analysis in mass spectrometry applications.
The use of Arg-C offers several advantages in protein analysis. It provides an alternative to trypsin, which can sometimes produce large peptides difficult to analyze by mass spectrometry. By generating a different set of peptides, Arg-C can improve the coverage of protein sequences and help identify specific modifications or mutations. This enzyme is particularly useful in studies requiring detailed structural information or when analyzing proteins with complex post-translational modifications. Overall, Arg-C is a versatile enzyme that expands the capabilities of proteomic research by offering complementary digestion strategies.
Additional information for Arg-C, His-Tag, C-terminal
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SDS-PAGE/Coll. Coomassie
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Histogram of marked lane in gel picture
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Additional information for Arg-C, His-Tag, N-terminal
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SDS-PAGE/Coll. Coomassie
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Histogram of marked lane in gel picture
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