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Human bone morphogenetic protein-2 (hBMP-2) is a potent growth and differentiation factor for bone induction and regeneration. Recombinant hBMP-2 (rhBMP-2) was cloned and expressed as a soluble protein using E. coli-based expression system. A full-length gene encoding mature hBMP-2 was amplified by RT-PCR, cloned into an expression vector and expressed using SHuffle E. coli cells. The rhBMP-2 was successfully expressed as a soluble protein under the control of the lacUV5 and protein A promoters by IPTG induction. The rhBMP-2 fused with ZZ domain at its N-terminus was successively purified with a single step by using IgG Sepharose 6 fast flow affinity chromatography. Analysis of the purified protein on SDS-PAGE, Western blot analysis and LC-MS/MS, verified that the purified protein was rhBMP-2. The biological activity testing on hFOB 1.19 showed that rhBMP-2 had the ability to significantly induce cell proliferation in a dose dependent manner. ALP staining and activity assay also increased after rhBMP-2

Porcine placenta extract (PPE) is an effective pharmaceutical and cosmetic ingredient, despite its high bioavailability. Despite this, only a few studies on the extract's effect on human osteoblast cellular behavior have been conducted. This study used hFOB 1.19 cells to demonstrate the mechanism by which a novel potent osteogenic compound that was discovered by stimulating the growth, alkaline phosphatase secretion, mineralization, and osteogenesis markers of human osteoblast hFOB 1.19 cells resulted in significant increases in extracellular signal-regulated kinase (ERK)1/2, Akt, and c-Jun N-terminal kinase (JNK) phosphorylation. In addition, PPE was discovered to significantly increase in vitro bone formation that may provide the beneficial potential for osteoporosis prevention and treatment.