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Development of the Fc-III tagged protein expression system for protein purification and detection.

ABSTRACT: In the present work, we developed the Fc-III tagged protein expression system for protein purification and detection. The Fc-III sequence encodes for a 13 residue peptide and this peptide is cyclized by disulfide bond formation when the fusion protein is expressed. The Fc-III-fusion proteins selectively bind to immunoglobulin Fc domains (IgG-Fc) expressed from E. coli. We showed the efficient purification of Fc-III tagged proteins by immobilized non-native IgG-Fc and the detection of the cellular locations of fusion proteins by fluorescent-conjugated IgG-Fc. Our results prove that Fc-III tagged protein expression system is a simple and efficient tool for protein purification and detection and is a useful addition to the biochemistry and proteomics toolbox.

SUBMITTER: Feng S

PROVIDER: S-EPMC3430635 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature

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Development of the Fc-III tagged protein expression system for protein purification and detection.

Feng Shan S Tian Enbing E Zhang Lei L Wang Qingtao Q Deng Haiteng H

PloS one 20120829 8

In the present work, we developed the Fc-III tagged protein expression system for protein purification and detection. The Fc-III sequence encodes for a 13 residue peptide and this peptide is cyclized by disulfide bond formation when the fusion protein is expressed. The Fc-III-fusion proteins selectively bind to immunoglobulin Fc domains (IgG-Fc) expressed from E. coli. We showed the efficient purification of Fc-III tagged proteins by immobilized non-native IgG-Fc and the detection of the cellula ...[more]

PMID: 22952929

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