Ultra-LEAF™ Purified anti-human BMP9 (GDF2) Antibody anti-BMP9 - A16035H,BioLegend,611703

BMP9 was initially isolated from fetal mouse liver cDNA libraries. The human and mouse proteins share 84% identity. They are part of the bone morphogenetic protein (BMP) family of proteins, which are members of the TGF-β superfamily and play a key role in skeletal development, bone formation, and stem cell differentiation. BMP9 is one of the most osteogenic factors of the family. It is sinthetized by hepatocytes and intrahepatic biliary epithelial cells and circulates in plasma as an unprocessed inactive form that can be further activated by furin, and as a mature and fully active form as a complex associated to its prodomain. BMPs signal through heterotetrameric complex receptors, which include four type I receptors (ALK1, ALK2, ALK3 and ALK6) and three type II receptors (BMPRII, ActRIIA and ActRIIB). BMP9 and -10 bind to ALK1 (mainly expressed in endothelial cells). BMP9 inhibits the proliferation of endothelial cells induced by basic FGF and the VEGF-stimulated angiogenesis by its binding to ALK1. BMP9 also binds to ALK2 in primary myeloma cells, and this binding can be inhibited by membranal or soluble endoglin (accessory receptor for the TGFβ family). BMP9 activity is inhibited by crossveinless2 (CV2), a member of the chordin family and extracellular regulator. BMP9 induces CV2 expression in endothelial cells and in a negative feedback loop inhibits its own activity by the binding of CV2 to BMP9, and consequently inhibits its binding to ALK1. BMP9 and -10 possess tumor suppressing activity in breast and prostate cancer; BMP9 as well induces apoptosis in primary myeloma cells. In contrast, autocrine BMP9 signaling induces proliferation of ovarian and liver cancer cells.