Expression of Porcine Interleukin-2 in Escherichia coli

Abstract

A mature form of porcine interleukin−2(IL−2)protein without signal peptides was expressed as glutathione S−transferase(GST)fusion proteins in Escherichia coli using pGEX vector.Since most of GST−IL−2 fusion protein was detected in an insoluble fraction on SDS−PAGE analysis, the insoluble fusion protein was solubilized by refolding procedure using urea.The recombinant IL−2(rIL−2)was purified by a batch method using Glutathione Sepharose 4B and factor Xa digestion and used for preparation of antisera in mice.The antisera reacted with rIL−2 expressed in baculovirus system on immunoblot analysis.In addition, the purified rIL−2 showed a high biological activity on CTLL−2 proliferative response.