Expression and purification of the SNX1/SNX6 complex
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Updated: Feb 8, 2026

Tandem Affinity Purification of Protein Complexes from Eukaryotic Cells
Published on: January 26, 2017
Xin Yong1, Wenfeng Hu1, Xue Zhou1
1Key Laboratory of Birth Defects and Related Diseases of Women and Children, Department of Paediatrics, Drug Clinical Trial Institute, West China Second University Hospital, Sichuan University, Chengdu 610041, China.
Abstract:
The sorting nexin (SNX) family proteins play an essential role in vesicular transport, cell signaling, and membrane remodeling. The SNX members SNX1/2 and SNX5/6 form dimers, and mediate endosome-to-trans Golgi network (TGN) transport through coordinating cargo selection and membrane remodeling. It is well-known how a SNX-BAR protein forms a homodimer; however, it is less clear how a heterodimer is formed. Here a detailed expression and purification protocol of the SNX1/SNX6 complex, from both worm and human, is described. Keys to the successful protein production include co-expression of both genes, and inclusion of glycerol in the protein buffer. Solution studies suggest that SNX1 and SNX6 form a 1:1 heterodimer. The production of a large amount, high quality of the SNX1/SNX6 complex provides a basis for future biochemical and structural studies of the complex, and in vitro reconstitution of SNX1/SNX6-mediated transport.
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