Purity ~95% (SDS-PAGE, HPLC). Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex. The protein consists of a homodimer of 180kD with disulfide links. It has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Endoglin has been found to be part of the TGF-beta1 receptor complex. It thus may be involved in the binding of TGF-beta1, TGF-beta3, Activin-A, BMP-2, and BMP-7. It has been postulated that Endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Its expression is regulated during heart development. CD105 Human Recombinant extracellular domain produced in baculovirus is a homodimeric, glycosylated, polypeptide containing 586aa and having a molecular mass of 61kD but as a result of glycosylation, migrates at 90kD under reducing conditions in SDS-PA