Monokine induced by interferon-γ (MIG, CXCL9) is a CXC chemokine which chemoattracts lymphocytes or neutrophils. Recent studies suggest that some members of CXC family, such as PF-4 and IL-8, CRG-2 and MIG also possess angiogenic or angiostatic properties. Recombinant mouse MIG protein were produced and purified and test its biological effects on endothelial cells. Mouse MIG cDNA was PCR amplified from mouse brain and cloned into pFASTBAC 1 vector in Bac-To-Bac baculovirus expression system. The recombinant mouse MIG Bacmid was introduced into High-Five (Tn-5B1-4) insect cells. After 48~72 h of incubation, the supernatant was collected and the MIG protein was purified by S-Sepharose. The yield of MIG was 10 mg/L and the purity is 90%. The MIG protein migrated as several bands on SDS-PAGE with the main band at 14.4 ku and was further confirmed by Western blot analysis. Functional assays demonstrated that purified mouse MIG protein not only elicited influx of calcium in mouse cytotoxic T cell lines but also inhibited both mouse endothelial cell migration and proliferation in a dose dependent manner. Thus, mouse MIG protein is not only a potent chemoattrant for lymphocytes but also an anti-angiogenic factor, which has important implications for angiogenesis-related diseases, such as tumor. It is the highest yield of recombinant mouse protein production described in the literature so far. The availability of large amount of purified active mouse MIG protein produced from baculovirus expression system has paved the way for the further studies of its in vivo angiostatic functions in mice.