Related Experiment Video
Updated: Dec 29, 2025
Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain
Published on: October 24, 2017
05SAR-PAGE: Separation of protein dimerization and modification using a gel with 0.05% sarkosyl
Liqun Huang1, Xinhui Kou2, Wenwen Zheng2
1Key Laboratory of Magnetic Resonance in Biological System, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Center for Magnetic Resonance, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, China; University of Chinese Academy of Sciences, Beijing, 100049, China.
Abstract:
A protein gel electrophoresis procedure using 0.05% w/v sarkosyl, is reported. The method called 05SAR-PAGE can be used to identify the native masses, dimeric states and modification states of proteins, and also be suitable for pursuing native electroblotting and immunodetection. It has been demonstrated by NMR spectroscopy that 0.05% w/v SAR is much milder than SDS, so it has subtle effects on the native structure of proteins. Therefore, the non-covalent dimerization of PhoBN and PhoRcp can be identified by 05SAR-PAGE which cannot be observed by SDS-PAGE. It has also been demonstrated that 05SAR-PAGE can be used to identify the phosphorylated or methylated proteins. Besides, 05SAR-PAGE shows the advantages of simple operation and low cost, and can be easily adapted to diverse applications.
