Forming active recombinant enterokinase expressed in Escherichia coli

Advances and challenges in recombinant protein expression in Escherichia coli

PURIFICATION AND CHARACTERIZATION OF THE CLONED HUMAN GM-CSF GENE EXPRESSED IN ESCHERICHIA COLI

The human granulocyte-macrophage colony stimulation factor (hGM-CSF) gene was cloned in the pET 23a( +) expression vector under the control of strong bacteriophage T7 transcription and translation signals. The hGM-CSF gene was transferred into E. coli strainBL21 (DE3)pLysS andIPTG was used for induction of GM-CSF gene. Production of the target protein was obtained as revealed by ELISA and ...

In Vitro Activation and Inhibition of Recombinant EGFR Tyrosine Kinase Expressed in Escherichia coli

The present work concerns the heterologous expression of the intracellular domain harbouring the tyrosine kinase activity of the epidermal growth factor receptor (EGFR). Protein expression was improved thanks to the deletion of a 13-amino acid peptide of the juxtamembrane region (JM). The recombinant proteins were produced as a glutathione S-transferase (GST) fusion in Escherichia coli, and the...

Translocation of -Synuclein Expressed in Escherichia coli

Translocation of -Synuclein Expressed in Escherichia coli Guoping Ren,† Xi Wang,† Shufeng Hao, Hongyu Hu, and Chih-chen Wang* National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China, and Graduate School of the Chinese Academy of Sciences, Beijing 100049, China, and Institute of Biochemistry and Cell Biology, Chinese Academy of Scienc...

Recombinant protein expression in Escherichia coli.

Escherichia coli is one of the most widely used hosts for the production of heterologous proteins and its genetics are far better characterized than those of any other microorganism. Recent progress in the fundamental understanding of transcription, translation, and protein folding in E. coli, together with serendipitous discoveries and the availability of improved genetic tools are making this...