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Updated: Jul 1, 2026
The Multifaceted Benefits of Protein Co-expression in Escherichia coli
Published on: February 5, 2015
Soluble protein expression in E. coli cells using IgG-binding domain of protein A as a solubilizing partner in the
1Yokohama Research Center, Chisso Corporation, 5-1 Okawa, Kanazawa-ku, Yokohama 236-8605, Japan. sinouye@chisso.co.jp
Abstract:
We constructed a cold induced expression vector in Escherichia coli cells that consists of a histidine tag sequence for nickel chelate affinity purification, IgG-binding domain of protein A (ZZ-domain) and the multiple cloning sites. The role of ZZ-domain as a solubilizing partner at 15 degrees C was demonstrated by expressing the imidazopyrazinone-type luciferases of Renilla, Oplophorus, Gaussia, and Vargula (Cypridina) as well as the calcium-binding photoproteins and firefly luciferase. The fused protein with ZZ-domain was expressed efficiently as a soluble form in the cytoplasm of E. coli cells at low temperature.
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