Cloning, Expression and Characterization of the Recombinant Protein Component of the Ectodomin Receptor of Bone Morphogenetic Protein Receptor in the Host of Prokaryotic

Bone morphogenetic proteins (BMPs) belong to the superfamily transforming growth factor-beta. These molecules play a role in fetal development and differentiation of different cells. In this regard, two homodimer molecules BMP-2 and BMP-7 play an important role in the formation of ectopic bone So that two types of recombinant form are available for ectopic use. After binding of the homodimer BMP-2 to its receptor at the cell surface, the accumulation of homodimers of type I and II receptors results in a biological response within the cell. Despite the existence of recombinant types of BMP-2 and BMP-7 due to the dangers of their use, the strategy of using monoclonal antibodies to trap endogenous types is still a priority in research programs. Instead of using monoclonal antibodies, the alternative method is to use the natural receptors of the ligand in the body. In this regard, due to the proper Kd binding of the ectodomain component of the receptor II of the BMP molecule in this project, the expression and purification of this part were attempted to trap BMP-2 endogenous. The protein component of the type II receptor ectodomain was expressed and purified by the bacterial host, which, by evaluating CD, of this recombinant protein showed a similar structure to that of the natural type. Also, its binding to the BMP-2 ligand with ELISA was evaluated and then calculated as Kd. Based on the results, the type II receptor ectodomain can be connected to the BMP-2 with a suitable binding property at the nM concentration, and in subsequent studies, it can be used as an alternative to a monoclonal antibody to Trap endogenous BMP molecules.