Proteomics

Dataset Information

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Protein aggregation capture on microparticles enables multi-purpose proteomics sample preparation


ABSTRACT: Universal proteomics sample preparation is challenging due to the high heterogeneity of biological samples. Here we describe a novel mechanism that exploits the inherent instability of denatured proteins for non-specific immobilization on microparticles by protein aggregation capture. To demonstrate the general applicability of this mechanism, we analyzed phosphoproteomes, tissue proteomes, and interaction proteomes as well as dilute secretomes. The findings presents a practical, sensitive and cost-effective proteomics sample preparation method.

INSTRUMENT(S): Orbitrap Fusion Lumos, Q Exactive HF-X

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

TISSUE(S): Skeletal Muscle, Cell Culture, Hela Cell

SUBMITTER: Tanveer Batth  

LAB HEAD: Jesper Velgaard Olsen

PROVIDER: PXD011677 | Pride | 2019-03-05

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
AP-MSanalysis-IngelvsPAC.zip Other
Digestionanalysis-insolvsPAC.zip Other
MaxQuantsearchfiles.zip Other
Phosphoanalysis-GndhclvsPAC.zip Other
Secretomeanalysis.zip Other
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Publications

Protein Aggregation Capture on Microparticles Enables Multipurpose Proteomics Sample Preparation.

Batth Tanveer S TS   Tollenaere MaximA X MX   Rüther Patrick P   Gonzalez-Franquesa Alba A   Prabhakar Bhargav S BS   Bekker-Jensen Simon S   Deshmukh Atul S AS   Olsen Jesper V JV  

Molecular & cellular proteomics : MCP 20190304 5


Universal proteomics sample preparation is challenging because of the high heterogeneity of biological samples. Here we describe a novel mechanism that exploits the inherent instability of denatured proteins for nonspecific immobilization on microparticles by protein aggregation capture. To demonstrate the general applicability of this mechanism, we analyzed phosphoproteomes, tissue proteomes, and interaction proteomes as well as dilute secretomes. The findings present a practical, sensitive and  ...[more]

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