[Objectives]  To clarify the relationship between Apis cerana cerana heat shock protein 70 (HSP70) and Chinese sacbrood virus (CSBV). [Methods]  A specific pair of primers were developed for HSP70 based on the complete A. cerana cerana genome listed in NCBI (NO.MH122655.1). The HSP70 gene was amplified from 1-3 day old A. cerana cerana by RT-PCR using extracted total RNA as the template, then analyzed with bioinformatics tools. The resultant HSP70 was cloned into the prokaryotic expression vector pET-32a, then transformed into Escherichia coli BL21(DE3) for protein expression. The resultant recombinant protein was purified by affinity chromatography and the purified, recombinant, fusion protein was then injected into mice to create polyclonal antibodies as primary antibodies. Changes in the expression of HSP70 in larvae before, and after, CSBV infection of A.cerana cerana were detected using the Western-blot method. [Results]  A 1 833 bp HSP70 gene was successfully cloned, and a recombinant plasmid (pET-32a-HSP70) correctly constructed. Bioinformatics analysis revealed seven epitopes in the protein. Using a prokaryotic expression system, we obtained a recombinant fusion protein of HSP70 with a size of about 87 ku, which was purified and injected into mice to obtain polyclonal antibodies. Western-blot analysis indicated specific reactions with the tag protein. HSP70 expression significantly increased after CSBV infection. [Conclusion]  The HSP70 gene and HSP70 polyclonal antibody were successfully expressed through a prokaryotic expression system. HSP70 protein expression in the Chinese honeybee is affected by CSBV infection, a finding that promotes further research on the function of HSP70.