Abstract: Objective：To explore the method which to express and purify the bioactive Grb7 SH2 domain.Methods：The fusion gene of GST-Grb7 SH2,which was constructed into the site between EcoRⅠ and XhoⅠ in the pEGX-4T-1,was induced by the 0.2 mmol/L IPTG to express in the BL 21 competent cells,at 25 ℃ for overnight,and the MALDI-TOF and Biacore3000 were used to identify the purity and bioactivity of the recombinant protein.Results：GST-Grb7 SH2 domain fusion protein(415 g) was purified from 500 ml LB bacterial liquid,and protein peaks were observed on the map of MALDI-TOF,and interactions between GST-Grb7 SH2 domain and phosphorylated peptide pY(1180) from the ErbB3,with concentrations of 10 nmol/L and 100 nmol/L,were measured by Biacore 3000.Conclusions：The recombinant GST-Grb7 SH2 domain can be obtained through a improved method,which may help to furtherly investigate the functions of Grb7 SH2 domain.