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Published April 1, 2015 | public
Journal Article Open

Protein Purification Using PDZ Affinity Chromatography


PDZ domains function in nature as protein-binding domains within scaffold and membrane-associated proteins. They comprise approximately 90 residues and undergo specific, high-affinity interactions with complementary C-terminal peptide sequences, other PDZ domains, and/or phospholipids. We have previously shown that the specific, strong interactions of PDZ domains with their ligands make them well suited for use in affinity chromatography. This unit provides protocols for the PDZ affinity chromatography procedure that are applicable for the purification of proteins that contain PDZ domains or PDZ domain-binding ligands, either naturally or introduced by genetic engineering. We detail the preparation of affinity resins composed of PDZ domains or PDZ domain peptide ligands coupled to solid supports. These resins can be used to purify proteins containing endogenous or genetically introduced PDZ domains or ligands, eluting the proteins with free PDZ domain peptide ligands.

Additional Information

© 2015 John Wiley & Sons, Inc. Published Online: 1 Apr. 2015. This work was supported by grants from the Gordon and Betty Moore Foundation, the Hicks Foundation for Alzheimer's Research, the Allen and Lenabelle Davis Foundation; National Institutes of Health Grant MH095095 to M.B.K. WGWIV was supported by the National Science Foundation Postdoctoral Research Fellowship in Biology (DBI1306188). We would like to thank Dr.'s Kathryn Ivanetich and Jost Vielmetter for careful editing of the manuscript and technical discussions.

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Accepted Version - nihms-678283.pdf


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August 22, 2023
August 22, 2023