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Updated: Apr 20, 2026

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
Solubilization and refolding of inclusion body proteins
Anupam Singh1, Vaibhav Upadhyay, Amulya K Panda
1Product Development Cell, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi, 110067, India.
Abstract:
High-level expression of recombinant proteins in Escherichia coli often results in accumulation of protein molecules into aggregates known as inclusion bodies (IBs). Isolation of properly folded, bioactive protein from IBs is a cumbersome task and most of the times results in poor recovery. The process of recovering bioactive proteins from IBs consists of solubilization of IB aggregates using denaturants, followed by refolding of the solubilized protein. Here, we describe a simple protocol for screening of buffers for solubilization of IB proteins. Various IB aggregate solubilization methods including organic solvents have been described.
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