The genome information combined with data derived from modern mass spectrometry enables us to determine the identity of a protein once it is isolated from a complex mixture. Two-dimensional gel electrophoresis established more than three decades ago serves as a powerful protocol to isolate many proteins at once for such protein analysis. In the first two decades, the original procedure to use a glass tube-based isoelectric focusing (IEF) had been commonly used. Since an IEF in glass tubes is rather difficult to maneuver, a new method to use an IEF on a thin agarose slab backed by a plastic film (IPG Dry Strip) has been invented and is now widely used. In this chapter, we describe the original protocol that uses a glass tube-based IEF because, the capacity of protein loading and resolving power of this type of classic two-dimensional gel is still indispensible. © 2012 Springer Science+Business Media, LLC.
CITATION STYLE
Matsumoto, H., Haniu, H., Kurien, B. T., & Komori, N. (2012). Two-dimensional gel electrophoresis: Glass tube-based IEF followed by SDS-PAGE. Methods in Molecular Biology, 869, 267–273. https://doi.org/10.1007/978-1-61779-821-4_22
Mendeley helps you to discover research relevant for your work.