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Date Published: 15/05/2024
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DOI: https://doi.org/10.51298/vmj.v538i3.9613
Issue
Vol. 538 No. 3 (2024)
Section
Các bài báo
How to Cite
Nguyễn, Q. T., Nguyễn, K. H., Tôn, T. V., & Vũ, T. T. (2024). EXPRESSION AND PURIFICATION OF HUMAN INTERLEUKIN-33 FUSED WITH SUMO IN ESCHERICHIA COLI. Vietnam Medical Journal, 538(3). https://doi.org/10.51298/vmj.v538i3.9613

EXPRESSION AND PURIFICATION OF HUMAN INTERLEUKIN-33 FUSED WITH SUMO IN ESCHERICHIA COLI

Quốc Thái Nguyễn, Kim Hưng Nguyễn, Thảo Vy Tôn, Thanh Thảo Vũ

Main Article Content

Abstract

Background: Interleukin (IL)-33 is a new member of the IL-1 superfamily that plays crucial roles in human immune responses via interaction with its ST2 receptor. IL-33 thus appears an attractive target for the drug development against IL-33 related disorders. Our research group has successfully transformed Escherichia coli with plasmid bearing human il33 gene fused with SUMO tag. Objectives: This study aims to examine the culture conditions and the purification process to obtain the recombinant IL-33. Methods: Expression conditions for optimal soluble recombinant IL-33 were examined, including culture medium (LB, TB, ZYP-5052); temperature (25°C and 37℃). The recombinant IL-33 fused with SUMO tag was purified by immobilized metal affinity chromatography method (IMAC). Results: The transformed E. coli BL21(DE3) can express soluble SUMO-IL-33 with high yield in autoinduction medium ZYP-5052 at 25°C. From 50 mL of bacterial culture, we obtained approximately 20 mg of purified protein by Ni Sepharose column. Conclusion: In this study, we have examined the culture and the purification conditions suitable to obtain soluble SUMO-IL-33 with high yield.

Article Details

Keywords

recombinant human interleukin-33, IMAC, pET-SUMO, E. coli

References

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