Improving Protein Production with SUMO Tag
Author Information
Author(s): Kong Bo Guo, Grace L. Cotterill
Primary Institution: University of Kansas Medical Center
Hypothesis
Can the SUMO fusion tag improve the solubility and refolding of recombinant Fgf15 protein expressed in E. coli?
Conclusion
The study successfully developed a method to express functional Fgf15 protein in prokaryotic cells using a SUMO fusion tag.
Supporting Evidence
- Fgf15 protein was expressed in E. coli but was found in inclusion bodies.
- The SUMO tag did not improve the solubility of Fgf15 but assisted in its refolding.
- Both SUMOtFgf15 and tFgf15 proteins suppressed hepatic Cyp7a1 mRNA levels in mice.
Takeaway
The researchers found a way to make a protein called Fgf15 work better by using a special tag that helps it fold correctly after being made in bacteria.
Methodology
The study involved expressing Fgf15 in E. coli with a SUMO tag, purifying it, and then refolding it in vitro.
Limitations
The study did not explore the effects of other potential fusion tags on Fgf15 solubility.
Participant Demographics
10–16 week old male mice were used for in vivo experiments.
Statistical Information
P-Value
<0.05
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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