【Aim】 We prepared mouse anti-Helicoverpa armigera cytochrome P450 (CYP6AE17 and CYP6AE19) polyclonal antibodies by cloning and expressing CYP6AE17 and CYP6AE19 of H. armigera, aiming to lay a foundation for further research on the function of cytochrome P450 inH. armigera and provide a theoretical basis for the green control of H. armigera. 【Method】 The recombinant plasmid pET32a-CYP6AE was constructed, and the recombinant protein was induced to be expressed, purified, and used as an antigen to immunize mice for the preparation of polyclonal antibodies. The titer and specificity of the prepared polyclonal antibodies were determined by ELISA and Western blot, respectively. 【Result】 The coding sequences of CYP6AE17 and CYP6AE19 were 1 572 and 1 587 bp in length, encoding 523 and 528 amino acid residues, respectively. The results of SDS-PAGE showed that the CYP6AE17 and CYP6AE19 could be efficiently induced to be expressed in the prokaryotic expression system ofEscherichia coli, and the recombinant proteins mainly existed in the form of inclusion bodies. ELISA results showed that the mouse anti-H. armigera cytochrome P450 (CYP6AE17 and CYP6AE19) polyclonal antibodies were prepared with titers of 1∶102 400 0 and 1∶512 000, respectively. Both of them could specifically recognize the natural P450 protein in H. armigera. 【Conclusion】 The results of this study laid a material foundation for further in-depth research on the functions of H. armigera cytochrome P450 and provided a theoretical basis for the development of new targets for controllingH. armigera.