Abstract:The basic helix-loop-helix（bHLH）transcription factor family is one of the largest families of transcription factors in eukaryotes.In the present study，an Agaricus bisporus bHLH（AbbHLH）transcription factor was，for the first time，cloned in the A.bisporus，and the prokaryotic expression vector pET-28a（+）-AbbHLH was constructed and transferred into the E.coli BL21（DE3）competent cells to induce the expression of recombinant protein.The recombinant 6×His-AbbHLH protein was obtained mainly in the form of inclusion bodies，followed by purification and renaturation to produce the antigen protein with a purity higher than 80%.Polyclonal antibody was prepared by immunizing New Zealand white rabbits with the above prepared antigen protein，and the immunity serum titer reached 102 400 detected by indirect enzyme-linked immunosorbent assay（ELISA）.After successive purification of the antibody serum by Protein A and CNBr，the antibody specificity was detected by Western blot，showing the specific recognition of the purified antibody to AbbHLH protein in A.bisporus.