Abstract
Identification of proteins separated by gel electrophoresis or electricfocusing is often compounded by the small pore size of the gel, which limits penetration by macromolecular probes. Overcoming this problem can be achieved by blotting the proteins onto an adsorbent porous membrane (usually nitrocellulose or diazotized paper), which gives a mirror image of the gel (1). A variety of reagents can be incubated with the membrane specifically to detect and analyze the protein of interest. Antibodies are widely used as detecting reagents, and the procedure is sometimes called Western blotting. However, protein blotting or immunoblotting is the most descriptive.
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References
Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350–4354.
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© 1996 Humana Press Inc., Totowa, NJ
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Page, M., Thorpe, R. (1996). Protein Blotting by Electroblotting. In: Walker, J.M. (eds) The Protein Protocols Handbook. Springer Protocols Handbooks. Humana Press. https://doi.org/10.1007/978-1-60327-259-9_37
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DOI: https://doi.org/10.1007/978-1-60327-259-9_37
Publisher Name: Humana Press
Print ISBN: 978-0-89603-338-2
Online ISBN: 978-1-60327-259-9
eBook Packages: Springer Book Archive