Volume 21, Issue 4 (4-2025)
lmj 2025, 21(4): 17-21 |
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Sarafrazi F, Nazemizadeh A, Hesaraki M, Habibi M, Fateh M, Rasouli H. Production of recombinant interleukin-2 protein on a laboratory scale using a microbial expression system. lmj 2025; 21 (4) :17-21
URL: http://icml.ir/article-1-664-en.html
URL: http://icml.ir/article-1-664-en.html
Fereshteh Sarafrazi 
, Armin Nazemizadeh , Mehdi Hesaraki , Masoud Habibi , Mohsen Fateh , Hassan Rasouli *
, Armin Nazemizadeh , Mehdi Hesaraki , Masoud Habibi , Mohsen Fateh , Hassan Rasouli *
Abstract: (612 Views)
Introduction: Interleukin-2 (IL-2), a cytokine that drives the expansion of T cells and their phenotypic development, plays a crucial role in wound healing. The most studied function of IL-2 is its influence on T-cell growth. However, other cell types, such as fibroblasts and skin cells responsible for wound repair, also express the IL-2 receptor and may respond to IL-2. Studies have indicated that IL-2 treatment can enhance the strength of healed skin, highlighting its significance in the wound-healing process.
Methods: In this study, a microbial expression vector containing the coding sequence for IL-2 was optimized and transferred to a bacterial strain. The expression of the recombinant protein was analyzed post-induction using SDS-PAGE and Western blotting with specific antibodies. For purification, affinity chromatography was employed. The biological activity of the produced protein was assessed by plotting the growth curve of NIH-3T3 cells.
Results: After establishing an appropriate expression pathway, 8.01 mg of IL-2 was purified per liter of bacterial culture in an Erlenmeyer flask. The purified IL-2 exhibited suitable structure and biological activity.
Conclusion: The bacterial strain can produce recombinant IL-2 with proper folding. The produced recombinant IL-2 has biological activity, and the production method was scalable and economically viable.
Methods: In this study, a microbial expression vector containing the coding sequence for IL-2 was optimized and transferred to a bacterial strain. The expression of the recombinant protein was analyzed post-induction using SDS-PAGE and Western blotting with specific antibodies. For purification, affinity chromatography was employed. The biological activity of the produced protein was assessed by plotting the growth curve of NIH-3T3 cells.
Results: After establishing an appropriate expression pathway, 8.01 mg of IL-2 was purified per liter of bacterial culture in an Erlenmeyer flask. The purified IL-2 exhibited suitable structure and biological activity.
Conclusion: The bacterial strain can produce recombinant IL-2 with proper folding. The produced recombinant IL-2 has biological activity, and the production method was scalable and economically viable.
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Received: 2025/05/4 | Accepted: 2025/04/30 | Published: 2025/06/30
Received: 2025/05/4 | Accepted: 2025/04/30 | Published: 2025/06/30
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