COPENHAGEN, Denmark, November 18, 2024 – KPL ApS is proud to announce the launch of our latest product Arg-C Zero, a high performance sequencing-grade arginyl endopeptidase. Recombinantly produced in Escherichia coli, Arg-C Zero (KPL0146) enables unparalleled efficiency in the C-terminus cleavage of Arginine residues within proteins and peptides. It is the perfect protease for many proteomic applications and we are excited to expand our portfolio with such a high quality product.
Next-generation performance
Originally identified as a virulence factor from Porphyromonas gingivalis, Arg-C Zero delivers highly specific and efficient hydrolysis of peptide bonds at the C-terminus of Arginine residues. It is an excellent enzyme for many bottom-up proteomic applications such as peptide mapping and analysis of different protein post-translational modifications. A must have in the toolkit for every proteomic scientist.
Key Benefits of Arg-C Zero KPL0146
Highly specific for Arginine residues: Arg-C Zero specifically cleaves at Arginine residues, providing high specificity for various peptide mapping and bottom-up proteomic applications.
High cleavage efficiency: High-performance enzyme that can achieve close to 100% cleavage efficiency in the hydrolysis of peptide bonds at the C-terminus of Arginine residues.
Reduce sample complexity: High cleavage efficiency results in less complex data, whether it is UV spectra or a mass spectrometer spectra. This also increases the reproducibility in your experiments, important factors for any proteomic analysis.
Learn more and order:
To learn more and order Arg-C Zero KPL0146, visit https://kplbio.com/product/arg-c/ .