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The Basics of Western Blotting

The western (note that in this context ‘‘western’’ should be spelt with a lower-case ‘‘w’’) blot is commonly used to identify, quantify, and determine the size of specific proteins. Western blotting evolved from Southern blotting, which is used to detect specific DNA sequences among DNA fragments separated by gel electrophoresis, and northern blotting, which is used to detect and quantify RNA and to determine its size, and also involves gel electrophoresis to separate RNA. In the late 1970s, Towbin et al. (1979) enabled proteins to be electrophoretically separated using polyacrylamide–urea gels and transferred onto a nitrocellulose membrane. Burnette (1981) later employed the more widely used sodium dodecyl sulfate-polyacrylamide gels (SDS-PAGE), which eventually led to this method being termed western blotting. It is also called protein blotting or immunoblotting and has rapidly become a powerful tool for studying proteins. Basically, gel electrophoresis is used to separate native or denatured proteins. The proteins are then transferred to a membrane for detection using antibodies specific to the target protein. The technique has continued to evolve, and there are many reports on troubleshooting and improving the technique (Kurien and Scofield, 2009).