Abstract: In order to obtain in vitro-induced MGF360-13 L protein of African swine fever virus（ASFV）, in the experiment, primers were designed according to the MGF360-13 L gene sequences reported in GenBank, the His tag was introduced, and the full sequence of ASFV was used as the template to amplify the target fragment. The target gene was cloned into the prokaryotic expression vector pGEX-6 p-1, which was transformed into BL21（DE3） Escherichia coli（E.coli） competent cells to induce expression in vitro, and the expression of the protein was analyzed by polyacrylamide gel electrophoresis（SDS-PAGE）. The recombinant protein was purified by Ni Sepharose column affinity chromatography, and the activity of the protein was analyzed by Western-blot. The results showed that the length of the cloned MGF360-13 L gene fragment was 1 060 bp; the obtained recombinant protein was expressed in the form of inclusion bodies in the precipitation, and the molecular weight was about 60 ku. After purification, a higher purity MGF360-13 L could be obtained; the highest concentration determined by BCA method was 2.73 mg/mL. Western-blot detection results showed an obvious specific band at 60 ku. The results suggested that MGF360-13 L protein could be expressed in BL21（DE3） E. coli competent cells and was purified, and MGF360-13 L with higher purity could be obtained after purification, and had good reactogenicity.