Abstract
The analysis of the cell surface accessible proteome provides invaluable information about cellular identity, cellular functions, and interactions. Cell surface labeling in combination with quantitative proteomics enables the unbiased identification and quantification of cell surface proteins. We describe a fast, efficient, and robust protocol for the enrichment of the N-linked plasma membrane glycoproteome and subsequent analysis by mass spectrometry. Precise and multiplexed quantification of relative changes of cell surface protein presentation is enabled by an isobaric labeling strategy.
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We would like to thank all our colleagues at Cellzome for support and fruitful discussions.
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Kalxdorf, M., Eberl, H.C., Bantscheff, M. (2017). Monitoring Dynamic Changes of the Cell Surface Glycoproteome by Quantitative Proteomics. In: Lazar, I., Kontoyianni, M., Lazar, A. (eds) Proteomics for Drug Discovery. Methods in Molecular Biology, vol 1647. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7201-2_3
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DOI: https://doi.org/10.1007/978-1-4939-7201-2_3
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