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• W2014464905 abstract "Mass spectrometry (MS) coupled to affinity purification is a powerful approach for identifying protein−protein interactions and for mapping post-translational modifications. Prior to MS analysis, affinity-purified proteins are typically separated by gel electrophoresis, visualized with a protein stain, excised, and subjected to in-gel digestion. An inherent limitation of this series of steps is the loss of protein sample that occurs during gel processing. Although methods employing in-solution digestion have been reported, they generally suffer from poor reaction kinetics. In the present study, we demonstrate an application of a microfluidic processing device, termed the Proteomic Reactor, for enzymatic digestion of affinity-purified proteins for liquid chromatography tandem mass spectrometry (LC-MS/MS) analysis. Use of the Proteomic Reactor enabled the identification of numerous ubiquitinated proteins in a human cell line expressing reduced amounts of the ubiquitin-dependent chaperone, valosin-containing protein (VCP). The Proteomic Reactor is a novel technology that facilitates the analysis of affinity-purified proteins and has the potential to aid future biological studies. Keywords: Proteomic reactor • affinity purification • mass spectrometry • ubiquitination • H1299 cells • VCP" @default.
• W2014464905 created "2016-06-24" @default.
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• W2014464905 date "2006-12-14" @default.
• W2014464905 modified "2023-09-27" @default.
• W2014464905 title "The Proteomic Reactor Facilitates the Analysis of Affinity-Purified Proteins by Mass Spectrometry: Application for Identifying Ubiquitinated Proteins in Human Cells" @default.
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• W2014464905 doi "https://doi.org/10.1021/pr060438j" @default.
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