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Protein Expression and Purification Core

Welcome

The protein production core facility helps to produce highly purified recombinant proteins for functional and structural studies. At this point, we mainly use bacteria as the expression host. In the future, other systems such as yeast, insect and mammalian cells shall also be available.

For protein production in E. coli, different conditions (e.g., induction temperature, IPTG concentration and incubation time) will be tested and various strategies will be used to achieve optimal expression and keep the target protein in the soluble portion. The expressed target protein will be first purified using affinity chromatography. Other purification methods (e.g., ion exchange and size exclusion chromatography) will be applied if deemed necessary. Protein is normally expressed in 1-5 L scale and milligrams of final purified protein can be expected.

 
Department of Biochemistry | Graduate School of Biomedical Sciences | UTHSCSA

UTHSCSA | Graduate School of Biomedical Sciences | Department of Biochemistry | CTRC | Research

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Updated: 02/18/2011
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