ABSTRACT
The Bombyx mori decapentaplegic gene is one of the conserved genes in vertebrate and invertebrates. The TGF-beta superfamily contains conserved polypeptide growth factors that play important roles in different cellular processes such as proliferation, apoptosis, differentiation and cell-fate determination. The B. mori dpp gene shares genetic homology with hBMPs and Drosophila dpp. Until now, only few studies have been conducted to examine the functions of B. mori dpp; and hence, its function is not yet well understood. In this study, the baculovirus expression vector system (BEVS) was used for expression of the recombinant B. mori dpp protein and in which the recombinant baculovirus is recovered in the host Sf9 cells. The selected pure recombinant baculovirus containing B. mori dpp gene (rBV-egfp-Bm dpp) was used to increase the effective protein purification by using His-tag extraction strategy. After selection of recombinant baculovirus, recombinant B. mori dpp proteins were extracted from the re-infected cells with pure rBV-egfp-Bm dpp. Herein, we summarize the efficient expression and purification of B. mori dpp proteins from the insect cells using the BEVS. This recombinant protein could be suitable for functional test and various application studies.