Human GLP-1 was produced and correctly refolded from recombinant E. coli, establishing bacterial expression as a manufacturing platform for this important diabetes drug peptide.
Key findingHuman GLP-1 was produced and correctly refolded from recombinant E. coli, establishing bacterial expression as a manufacturing platform for this impor
What the researchers found
Human GLP-1 was produced and correctly refolded from recombinant E. coli, establishing bacterial expression as a manufacturing platform for this important diabetes drug peptide.
Why it matters
Relevant for peptide research.
How the study worked
research study.
What this study cannot tell us
See abstract.
How to read the evidence
emerging evidence.
When this study was published
Published in 2011.
The bigger picture
Advances peptide research.
Questions still open
- Further research needed.
Common questions
What was studied?
What was found?
Read the original research
Production and solid-phase refolding of human glucagon-like peptide-1 using recombinant Escherichia coli.
Protein expression and purification, 78(2), 197-203
Citation
Kim, Sung-Gun; Shin, So-Yeon; Park, Yong-Cheol; Shin, Chul-Soo; Seo, Jin-Ho. (2011). Production and solid-phase refolding of human glucagon-like peptide-1 using recombinant Escherichia coli.. Protein expression and purification, 78(2), 197-203. https://doi.org/10.1016/j.pep.2011.03.008