Abstract: This work aims to explore the soluble expression and biological activity of interleukin-2; recombinant fusion protein MBP-rhIL2 was successfully expressed into soluble form in E.coli BL21 (DE3). The purification of MBP-rhIL2 was conducted through amylose resin. The rhIL-2 was efficiently released by the cleavage of protease Factor Xa from the fusion protein. Bioactivity analysis showed the biological activity of purified rhIL-2 is 4.4 ×106 IU/mg.

Key words: Interleukin-2, soluble expression, protein purification