Proteomics

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ITRAQ labeling is superior to mTRAQ for quantitative global proteomics and phosphoproteomics

ABSTRACT: Mertins P, Udeshi ND, Clauser KR, Mani DR, Patel J, Ong, SE, Jaffe JD, Carr SA. Mol Cell Proteomics 2012, mcp.M111.014423. doi:10.1074/mcp.M111.014423. Tranche_hash:5cHw5Rj36vYNshNpy8k4nojtPyW27N/FHcImna3+zw4QV6KIlLOg3i6zesWBdWkEX608MEgdxWuVyKvvdOgB9BAanesAAAAAAACEzw==

PROVIDER: MSV000078495 | MassIVE | Wed Nov 20 13:53:00 GMT 2013

REPOSITORIES: MassIVE

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iTRAQ labeling is superior to mTRAQ for quantitative global proteomics and phosphoproteomics.

Mertins Philipp P   Udeshi Namrata D ND   Clauser Karl R KR   Mani D R DR   Patel Jinal J   Ong Shao-en SE   Jaffe Jacob D JD   Carr Steven A SA  

Molecular & cellular proteomics : MCP 20111230 6

Labeling of primary amines on peptides with reagents containing stable isotopes is a commonly used technique in quantitative mass spectrometry. Isobaric labeling techniques such as iTRAQ™ or TMT™ allow for relative quantification of peptides based on ratios of reporter ions in the low m/z region of spectra produced by precursor ion fragmentation. In contrast, nonisobaric labeling with mTRAQ™ yields precursors with different masses that can be directly quantified in MS1 spectra. In this study, we  ...[more]

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