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A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells
Published on: July 31, 2012
Availability of dihydrofolate reductase affinity handle in expressing human prolactin as a soluble fusion protein
1National Institute of Bioscience and Human-Technology, Ibaraki, Japan.
Bioscience, Biotechnology, and Biochemistry
|November 1, 1993
Abstract:
Human prolactin (PRL) cDNA was successfully expressed in Escherichia coli cells with the aid of a dihydrofolate reductase (DHFR) affinity handle. The formed DHFR-PRL fusion protein was accumulated in E. coli cells as a soluble protein with DHFR activity at 30 degrees C. The fusion protein was highly purified with monitored the DHFR activity by methotrexate-bound affinity chromatography, suggesting the usefulness of the handle even in expressing a large polypeptide as a fusion protein.

