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Expression, purification and characterization of recombinant interleukin-21
Carol M Y Lee1, Helen McGuire, Antony Basten
1Garvan Institute of Medical Research, Darlinghurst/Sydney, Australia.
Journal of Immunological Methods
|August 31, 2010
Summary
Researchers developed a new method to produce pure and active Interleukin-21 (IL-21) protein. This breakthrough overcomes previous limitations, enabling further studies of this crucial immune system regulator.
Area of Science:
- Immunology
- Protein Biochemistry
- Recombinant Protein Expression
Background:
- Interleukin-21 (IL-21) is a critical immune system regulator.
- Previous research on IL-21 has been limited by the scarcity of recombinant protein preparations.
Purpose of the Study:
- To establish an efficient method for producing high-purity, active recombinant human and murine IL-21.
- To overcome the limitations posed by the limited availability of IL-21 protein for scientific research.
Main Methods:
- Refolding of inclusion bodies from E. coli expressed proteins via rapid dilution.
- Purification using affinity chromatography and gel-filtration.
- Assessment of protein purity and activity through endotoxin and cell proliferation assays.
Main Results:
- Successful production of pure and highly active human and murine IL-21 proteins.
- Milligram quantities of recombinant IL-21 are now available.
- The produced protein facilitated the generation of monoclonal antibody fragments against IL-21.
Conclusions:
- The described refolding and purification method provides a reliable source of active IL-21.
- This advancement will significantly support further structural, biochemical, and physiological investigations of IL-21.
- The availability of IL-21 protein aids in developing novel immunomodulatory strategies.
