BRD7 gene is a good candidate tumor suppression gene associated with NPC. In order to construct prokaryotic expression vector of BRD7 and express BRD7 in E.coli, The coding region with SalⅠ and NotⅠ restriction sites of BRD7 was obtained from pGEM-T Easy/BRD7 plasmid by PCR. PCR product and plasmid PGEX-4T-2 were digested by corresponding restrict endonucleases respectively. The fragments were ligated by T4 DNA ligase to gain recombinant expression vector. Endonuclease digesting and DNA sequencing confirmed that the coding region of BRD7 gene was correctly inserted into the vector. The recombinant plasmid PGEX-4T-2/BRD7 was transferred into competent Jm105 strain. The GST/BRD7 fusion protein was expressed in the bacteria under induction of IPTG. After induction, a new protein band of 90 ku appeared on SDS-PAGE. The result was confirmed by Western blot. The recombinant protein of 90 ku amounted to 28.48% of the total bacterial protein after inducing with IPTG for 4 h at 37℃. It existed not only in supernatant but also in precipitation of broken bacteria. The successes in construction of expression vector of BRD7 and expression of BRD7 in E.coli make it possible to study further on its biological function and antibody preparation.