Bone morphogenetic protein-2 (BMP-2) plays a decisive role during bone regeneration and repair as well as during various stages of embryonal development. The complete cDNA of human bone morphogenetic protein-2 (hBMP-2) is 1587bp long, and the 1188bp open reading frame encodes a 396aa protein which consists of a signal peptide, a pro-peptide and a 114 aa mature peptide. The recombinant hBMP-2 was expressed in COS, CHO and insect cells as a functional active form. Liu xin ping, Lu zifan, Zhao ming and Lin song et al expressed varied C-terminal peptides of hBMP-2 in E.coli respectively, and after purification and renaturation the rBMPs was prepared as a functional active form. In this paper, the cDNA encoding the mature peptide of hBMP-2 was cloned and expressed in E.coli.The cDNA fragment encoding the mature peptide of hBMP-2m was amplified with PCR and inserted into two heat-inducible expression vectors pDHEX and pDHEEX in which foreign gene is controlled by P_RP_L promoters. E.coli DH5α transformed with...
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