Usually proteins are separated by polyacrylamide gel electrophoresis (PAGE) in the presence of a detergent and under (heat-) denaturing and (non- or) reducing conditions. The most commonly used detergent is sodium dodecyl sulfate (SDS). The major function of SDS is to shield the respective charge of the proteins present in the mixture to be analyzed and to provide all proteins with a negative charge. As a consequence, the proteins will be separated according to their molecular weight. Electrophoresis of proteins can also be performed in the absence of SDS. Using such “native” conditions, the charge of each of the proteins, which will depend on the primary amino acid sequence of the protein (isoelectric point) and the pH during electrophoresis, will mainly influence the mobility of the respective protein during electrophoresis. Here we describe a starting protocol for “native” PAGE.
- “Native” polyacrylamide gels
- “Blue native” polyacrylamide gels
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Special thanks for excellent technical support to Christin Gräfe, Livia Schulze, und Barbara Uteß (Inst. Immunology, Dresden, Germany).
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Arndt, C., Koristka, S., Bartsch, H., Bachmann, M. (2012). Native Polyacrylamide Gels. 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_5
Publisher Name: Humana Press, Totowa, NJ
Print ISBN: 978-1-61779-820-7
Online ISBN: 978-1-61779-821-4
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