EASI-tag enables accurate multiplexed and interference-free MS2-based proteome 
quantification

Virreira Winter, Sebastian; Meier, Florian; Wichmann, Christoph; Cox, Juergen; Mann, Matthias; Meissner, Felix

doi:10.1038/s41592-018-0037-8

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EASI-tag enables accurate multiplexed and interference-free MS2-based proteome quantification

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Virreira Winter, Sebastian
Meissner, Felix / Experimental Systems Immunology, Max Planck Institute of Biochemistry, Max Planck Society;

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Meier, Florian
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

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Wichmann, Christoph
Cox, Jürgen / Computational Systems Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Cox, Juergen
Cox, Jürgen / Computational Systems Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Mann, Matthias
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

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Meissner, Felix
Meissner, Felix / Experimental Systems Immunology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Virreira Winter, S., Meier, F., Wichmann, C., Cox, J., Mann, M., & Meissner, F. (2018). EASI-tag enables accurate multiplexed and interference-free MS2-based proteome quantification. Nature methods, 15(7), 527-530. doi:10.1038/s41592-018-0037-8.

Cite as: https://hdl.handle.net/21.11116/0000-0002-0B49-1

Abstract

We developed EASI-tag (easily abstractable sulfoxide-based isobaric-tag), a new type of amine-derivatizing and sulfoxide- containing isobaric labeling reagents for highly accurate quantitative proteomics analysis using mass spectrometry. We observed that EASI-tag labels dissociate at low collision energy and generate peptide-coupled, interference-free reporter ions with high yield. Efficient isolation of C-12 precursors and quantification at the MS2 level allowed accurate determination of quantitative differences between up to six multiplexed samples.