Construction and expression of ULBP3 extracellular domain chaperonin10 recombinant fusion protein

[Objective] To study the function of ULBP3 and express the ULBP3 extracellular domain recombinant fusion protein. [Methods] The extracellular domain of ULBP3 cDNA was cloned into the recombinant pET28a-chaperonin10 prokaryotic expression vector to construct a recombinant pET28a-chaperonin10-ULBP3 prokaryotic expression vector with ULBP3 cDNA fused to the hydroxy end of chaperonin10 gene. Then the recombinant plasmid was transduced into E.Coli. expression host BL21(DE3), the expression of fusion protein was induced by IPTG, and identified by Western blot. [Results] recombinant pET28a-chaperonin10-ULBP3 plasmid was constructed successfully and recombinant fusion protein chaperonin10-ULBP3 was identified by SDS-PAGE and Western blot. [Conclusion] The ULBP3 extracellular domain recombinant fusion protein was expressed in BL21(DE3) stably.