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Sample Preparation Solutions for Cellular Protein Fractionation Poster, Rev A


Introduction
High-resolution 2DE is the most widely used separation method for global proteome analysis. Continuous improvements in the technique are expanding the capabilities of gel separations and removing limits on the types of proteins that can be resolved. Here, we describe new sample preparation kits that enhance the detection capabilities of 2-D gels.

These protocols address two key issues in applying 2-D gels to proteomics analysis of complex samples. One issue is how to handle both the enormous chemical diversity and the wide dynamic range of proteins in a biological sample so that lowabundance and housekeeping proteins can be monitored and identified. We have developed a number of protocols to quickly prepare highly enriched protein fractions based on protein solubility. One protocol separates a complex sample into enriched fractions of nuclear and cytoplasmic proteins. A second protocol enriches for membrane-associated signaling proteins. Other protocols enrich for membrane proteins. All protocols enhance the capability to monitor and identify proteins of biological interest.

The other issue is how to solubilize these hydrophobic proteins so they can be separated in 2-D gels. A number of new detergents and more stringent chaotropic agents have been incorporated into a complete protein solubilization buffer (PSB), which efficiently solubilizes hydrophobic proteins for immediate application to a 2-D gel. Using both the simplified enrichment and enhanced solubilization protocols, we significantly expanded the capabilities of applying 2-D gels for proteome analysis of complex cellular extracts.


Methods
Sample Preparation
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