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How does electro blotting and Western blotting differ?

Electro blotting is a method in molecular biology, biochemistry and immunogenetics that is used to transfer proteins or nucleic acids onto a membrane such as PVDF or nitrocellulose, after gel electrophoresis. The resulting blot can be further used for different types of analysis.

Western blotting, also knows as protein immunoblotting, is a method in molecular biology, biochemistry and immunogenetics that is used to transfer proteins onto a membrane such as a PVDF or nitrocellulose, after gel electrophoresis. The membrane is stained or developed to visualize the protein band(s) of interest using antibodies. Often a secondary antibody conjugated to a dye or horseradish peroxidase is used for the development of the color.

As one can see “electro blotting” is a partial step of “western blotting”. However, for western blotting one would need an antibody that recognizes the target protein. If this is not available, the protein band can be cut out and used for Edman based protein sequencing. Alternatively, a gel band containing the protein of interest can be cut out, digested enzymatically or chemically and identified using tandem mass spectrometry approaches.