Abstract
Western blotting enables the detection and characterization of proteins of low abundance. Sodium dodecyl sulfate (SDS) polyacrylamide gel-separated proteins are normally transferred electrophoretically to nitrocellulose or polyvinylidene difluoride membranes. Here we describe the transfer proteins [Ro 60 (or SSA) autoantigen, 220 and 240 kDa spectrin antigens, and prestained molecular weight standards] by diffusion from SDS polyacrylamide gels at 37 °C. Up to 12 immunoblots can be obtained from a single gel by this method.
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Kurien, B. T., & Hal Scofield, R. (2015). Multiple immunoblots by passive diffusion of proteins from a single SDS-PAGE gel. In Western Blotting: Methods and Protocols (pp. 77–86). Springer New York. https://doi.org/10.1007/978-1-4939-2694-7_11
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