Tandem affinity purification of protein complexes from arabidopsis cell cultures

Abstract

Tandem affinity purification (TAP) coupled to mass spectrometry has become a powerful approach to identify protein–protein interactions from different biological systems, including plants, in a proteome-wide manner. By using two sequential affinity purification steps, TAP allows for isolation of high-purity TAP-tagged proteins of interest and their associated proteins. Here we describe optimized procedures to use the GSRhino TAP technology for protein complex isolation from Arabidopsis cell suspension cultures.