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Sample Preparation Solutions for Cellular Protein Fractionation Poster, Rev A

T Slyker, B Gillece-Castro, M Nguyen, L Sapp, MG Brubacher, and WB Strong


Presented by the Authors at The Association of Biomolecular Resource Facilities (ABRF)

February 1013, 2003
Denver, Colorado

Abstract
2-D gel electrophoresis (2DE) is a widely used, proven method for proteome analysis. The quality and value of the information obtained from a 2DE experiment is highly dependent upon the initial sample preparation. In order to identify the most complete array of cellular proteins it is often necessary to reduce the complexity of the protein sample. A strategy for reduction in sample complexity is especially important when analysis of low-abundance and membrane proteins is the goal. Ideally the method(s) employed should be simple, reproducible, general to a wide variety of cell types, and result in a low conductivity protein sample that is free of substances that interfere with 2DE. With these aims in mind, we will present several solutions for convenient and efficient extraction of cellular proteins into discrete, more easily manageable fractions that are enriched in certain classes of proteins such as cytosolic, nuclear, membrane, and signaling. The majority of these procedures are intended to provide tools that simplify the preparation of membrane proteins that are generally considered difficult to isolate. These proteins are of considerable interest due to their roles in signal transduction and cell-to-cell interactions among other functions. 2DE and MALDI peptide mass fingerprinting data will be presented to illustrate the effective application of these techniques to improved sample prefractionation and protein identification.
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