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Expression of human interleukin-2 receptor cDNA in E. coli
Biochemical and Biophysical Research Communications
|December 15, 1986
Summary
Researchers expressed the human interleukin-2 receptor (IL-2R) in E. coli. The resulting protein successfully binds to interleukin-2 (IL-2), demonstrating functional expression of the IL-2 receptor in bacteria.
Area of Science:
- Molecular Biology
- Immunology
- Biotechnology
Background:
- Human interleukin-2 receptor (IL-2R) cDNAs have been cloned and sequenced.
- Understanding IL-2R function requires methods for producing functional receptor proteins.
Purpose of the Study:
- To describe the expression of a human interleukin-2 receptor cDNA clone in E. coli.
- To demonstrate the functionality of the bacterially produced IL-2 receptor protein.
Main Methods:
- Utilized an "open reading frame" expression vector (pMR100) for E. coli expression.
- Constructed a tripartite fusion polypeptide: lambda cI protein - IL-2 receptor - beta-galactosidase.
- Analyzed the binding capability of the expressed protein to interleukin-2.
Main Results:
- Successfully expressed the human IL-2 receptor cDNA in E. coli transformants.
- The expressed fusion protein demonstrated the ability to bind to interleukin-2.
- Confirmed functional expression of the IL-2 receptor in a bacterial system.
Conclusions:
- Bacterial expression systems can produce functional human interleukin-2 receptor protein.
- This method provides a viable approach for studying IL-2 receptor interactions.