2006Journal of Shantou UniversityRequires access

Solution and Purification of ECRG2 Recombinant Fusion Protein Inclusion Body

Shixin Lu

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Abstract

In this study,ORF of ECRG2 cDNA was cloned into the pEGX-4T-1 vector and expressed in Escherichia coli as a GST fusion protein.Inclusion body GST-ECRG2 was collected,dissolved in SKL,refolded in PBS and purified using GST affinity column.After optimization,purified protein has been obtained at high yield.

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What this paper is about

In this study,ORF of ECRG2 cDNA was cloned into the pEGX-4T-1 vector and expressed in Escherichia coli as a GST fusion protein.Inclusion body GST-ECRG2 was collected,dissolved in SKL,refolded in PBS and purified using GST affinity column.After optimization,purified protein has been obtained at high yield.

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Available abstract

In this study,ORF of ECRG2 cDNA was cloned into the pEGX-4T-1 vector and expressed in Escherichia coli as a GST fusion protein.Inclusion body GST-ECRG2 was collected,dissolved in SKL,refolded in PBS and purified using GST affinity column.After optimization,purified protein has been obtained at high yield.

Key concepts: Inclusion bodies, Recombinant DNA, Fusion protein, Escherichia coli, Complementary DNA, Affinity chromatography, Chemistry, Protein purification

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