Abstract: In order to express Porcine parvovirus type 7（PPV7） VP2 protein（encoded by Cap gene） and prepare its polyclonal antibody, in the experiment, PPV7 Cap gene sequences from GenBank database were downloaded and the high frequency sequences of different strains were selected as the target gene sequences; T4 DNA ligase was used to connect the target gene with pET-32a expression vector and the ligated product was transformed into DH5α competent cells; the recombinant bacteria were induced by IPTG, and the expressed recombinant protein was analyzed for solubility and purification, and the immunogenicity of the recombinant protein was detemined by Western-blot; the purified recombinant protein was used to immunize New Zealand White rabbits for the preparation of polyclonal antibody; the titer of the polyclonal antibody and the reactivity with the recombinant protein were detected by indirect ELISA and Western-blot, respectively. The results showed that the recombinant bacteria showed obvious bands at 56 ku after induction, and the recombinant protein was mainly expressed in the form of inclusion bodies; the purified recombinant protein was a single band with a mass concentration of 0.46 mg/mL, which could bind specifically to the His-tag antibody; the titer of the prepared polyclonal antibody was 1∶51 200. Polyclonal antibody could bind specifically to the recombinant protein. The results suggested that PPV7 VP2 protein was successfully expressed, which had good reactivity and immunogenicity, and the prepared polyclonal antibody had high titer.