Anti-Human BMP-7 Antibody

Bone morphogenetic protein 7 (BMP7), also known as osteogenic protein 1 (OP1), is a widely expressed TGFβ superfamily member with important functions during embryogenesis, in the adult, and in disease. Human BMP7 is synthesized with a 29 amino acid (aa) signal sequence, a 263 aa propeptide, and a 139 aa growth factor domain. The growth factor domain of human BMP7 shares 98% aa sequence identity with mouse and rat BMP7. The BMP7 propeptide is cleaved intracellularly but often remains associated with the mature Cterminus. Based on in vivo and in vitro studies, BMP 7 has the potential to be secreted as a disulfidelinked mature homodimer, or particularly as a heteromeric complex that consists of two propeptides noncovalently associated with a mature disulfidelinked homodimer. The presence of the propeptides in BMP7 appears to stabilize the molecule and provide a docking mechanism for extracellular storage on molecules such as fibrillin 1 and 2 . The propeptides themselves do not impart latency to the complex. BMP7 binding to type II receptors rapidly displaces the prodomain:mature molecule interaction and has no effect on activity. But it is suggested that immobilized BMP7 (via prodomain:fibrillin) is inactive, allowing for possible longterm storage of the molecule. BMP 7 interacts with the type 2 receptors Activin RIIA, Activin RIIB, and BMPRII and the type 1 receptors Activin RIA, BMPRIA, and BMPRIB. BMP7 may also be processed into a disulfidelinked heterodimer with either BMP2 or BMP4. Such complexes may show increased potency and range of activity compared to BMP7 homodimers. BMP7 plays a role in a variety of organ systems. It promotes new bone formation and nephron development (10, 11), inhibits the branching of prostate epithelium (12), and antagonizes epithelialmesenchymal transition (EMT).