Related Experiment Video
Updated: Aug 14, 2026

Protein Complex Affinity Capture from Cryomilled Mammalian Cells
Published on: December 9, 2016
A method for the rapid and efficient elution of native affinity-purified protein A tagged complexes
Caterina Strambio-de-Castillia1, Jaclyn Tetenbaum-Novatt, Brian S Imai
1Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, NY 10021-6399, USA.
Abstract:
A problem faced in proteomics studies is the recovery of tagged protein complexes in their native and active form. Here we describe a peptide, Bio-Ox, that mimics the immunoglobulin G (IgG) binding interface of Staphylococcus aureus Protein A, and competitively displaces affinity-purified Protein A fusion proteins and protein complexes from IgG-Sepharose. We show that Bio-Ox elution is a robust method for the efficient and rapid recovery of native tagged proteins, and can be applied to a variety of structural genomics and proteomics studies.
Related Concept Videos
Immunoprecipitation
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...
Tagging and Fusion Proteins
Affinity Chromatography

