Identification and evaluation of proteins in the extracellular matrix (ECM) has proved challenging due to the insolubility of the bulk of ECM proteins in traditional proteomic extraction buffers. Multiple ECM-focused proteomic workflows have been developed over the past 10 years. These methods rely on decellularization followed by chaotrope extraction and ultimately enzymatic or chemical digestion. To date, there has not been a side-by-side comparison of all current methods on uniform, complex tissue samples. Herein, we present an evaluation of ECM-specific methods alongside several single-shot methods for tissue analysis. We provide recommendations for method selection based on ECM protein identification and sequence coverage as well as the ease and precision of the given methods.
[doi:10.25345/C52N2F]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: extracellular matrix ; proteomics ; sample preparation methods ; collagen ; glycoprotein ; proteoglycan ; matrisome
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Kirk Hansen, University of Colorado Anschutz Medical Campus, United States |
Submitting User: | maxwellmccabe |
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