Multiplexed MRM-based quantitation of candidate cancer biomarker proteins in undepleted and non-enriched human plasma
Version of Record online: 6 JUN 2013
© 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Volume 13, Issue 14, pages 2202–2215, July 2013
How to Cite
Percy, A. J., Chambers, A. G., Yang, J. and Borchers, C. H. (2013), Multiplexed MRM-based quantitation of candidate cancer biomarker proteins in undepleted and non-enriched human plasma. Proteomics, 13: 2202–2215. doi: 10.1002/pmic.201200316
- Issue online: 18 JUL 2013
- Version of Record online: 6 JUN 2013
- Accepted manuscript online: 16 APR 2013 01:42PM EST
- Manuscript Accepted: 26 MAR 2013
- Manuscript Revised: 6 FEB 2013
- Manuscript Received: 24 JUL 2012
- Genome Canada, Genome BC, and the Western Economic Diversification of Canada
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Table S1. Interference screening results for the 60 interference-free peptides targeting 27 cancer-related plasma proteins analysed on Agilent's standard-flow LC-MRM/MS platform. Data are displayed as average relative ratios between SIS in buffer, SIS in plasma, and NAT in plasma for 3 transitions per peptide (%CVs indicated in paranthesis). Each peptide's transitions are ranked according to their average relative ratios, variability, and NAT vs. SIS peak symmetry comparisons.
Table S2. Optimized MRM parameters for 60 peptides representing 27 cancer-related plasma proteins (masses and m/z values listed are for the natural (NAT) peptide forms).
Table S3. Analytical reproducibility, linearity, sensitivity, plasma protein concentration, and quantitation accuracy for a 57-peptide panel (representing 27 plasma proteins) obtained from per-peptide calibration curves (n = 5 for each of the 8 concentration levels)
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