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Immunoelectrophoresis: A Method with Many Faces

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Protein Electrophoresis

Part of the book series: Methods in Molecular Biology ((MIMB,volume 869))

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Abstract

Immunoelectrophoresis (IEP) was the first practical method that combined electrophoresis and ­immunoprecipitation for identifying and characterizing proteins within complex mixtures. Over the years, IEP has been extended to include a variety of techniques and, as a general name, has been applied to virtually any technique that involves electrophoresis and antigen–antibody precipitin reaction for proteins. Because of the diversity in technical details of different IEP versions, the method described here deals only with classic IEP. Although it requires some manual expertise, IEP is versatile, relatively easy to customize, and economical with no need for expensive instrumentation. Further, it can discern identity, partial identity, and nonidentity of the proteins. Any low-viscosity body fluid specimen or, possibly, culture fluid and tissue extract could be tested with IEP if proper antibodies are available. With these attributes, classic IEP remains a valuable tool for clinical diagnostic testing, purity checking of biochemical and pharmaceutical products, and research.

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Acknowledgments

The author wishes to thank Dr. Rita Ellerbrook of the Helena Laboratories, Beaumont, TX, USA for kindly providing illustrations to this article.

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Correspondence to Gyorgy Csako .

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Csako, G. (2012). Immunoelectrophoresis: A Method with Many Faces. In: Kurien, B., Scofield, R. (eds) Protein Electrophoresis. Methods in Molecular Biology, vol 869. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-61779-821-4_28

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  • DOI: https://doi.org/10.1007/978-1-61779-821-4_28

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-61779-820-7

  • Online ISBN: 978-1-61779-821-4

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