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Updated: Jun 24, 2026

Fluorescent Silver Staining of Proteins in Polyacrylamide Gels
Published on: April 21, 2019
Application of SYPRO Ruby- and Flamingo-stained polyacrylamide gels to Western blot analysis
Makoto Hagiwara1, Ken-Ichi Kobayashi, Tadahiro Tadokoro
1Department of Agricultural Chemistry, Graduate School of Agriculture, Tokyo University of Agriculture, Setagaya-ku, Tokyo 156-8502, Japan.
Abstract:
Western blot analysis has been a useful method for analysis of expression levels of specific proteins and is conducted after sodium dodecyl sulfate (SDS) or native polyacrylamide gel electrophoresis without staining the gel. However, when it is necessary to analyze the gel, duplicate polyacrylamide gels usually must be prepared, one of which is stained, leading to the consumption of precious sample. Thus, we developed a convenient and efficient Western blotting method using a stained gel. This simple modification should be beneficial for analyzing samples that are limited in quantity and/or samples for which the stained gel serves as the loading control.
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Western Blotting
The technique begins with separating proteins from the sample using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by protein transfer, immunoblotting, and finally, protein detection.
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A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...
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Denatured DNA fragments must be transferred onto a carrier membrane from the gel to make it accessible to a probe - a small ssDNA fragment complementary to the target DNA...

