Objective:To express and identify immunoreactivity of recombinant Tp0965(r Tp0965) protein of Treponema pallidum(Tp), provid a basis for further investigation of its significance in syphilis serodiagnosis and vaccine.Method:The prokaryotic expression recombinant p ET-28a(+)/Tp0965 was constructed and induced to express recombinant proteins which then were purified with Ni-NTA affinity chromatography. Western blot was used to identify immunoreactivity of r Tp0965.Result:The recombinant p ET-28a(+)/Tp0965 was constructed successfully and a soluble recombinant protein with approximate 43 KDa molecular weight was expressed efficiently in E.coli with more than 95% of purity. Western blot indicated that purified proteins were able to be recognized specially by pooled sera from syphilis patients.Conclusion:The recombinant protein Tp0965 is expressed efficiently in E.coli and has good immunoreactivity.