Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex. Endoglin consists of a homodimer of 180 kDa 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 586 amino acids and having a molecular mass of 61 kDa, but as a result of glycosylation, migrates at 90 kDa under reducing conditions in SDS-PAGE. The CD105 is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.