Endoglin is a 90 kDa protein that forms a disulfide-linked homodimer on the cell surface . It associates with TGF-β type I receptors, including the endothelial cell-specific ALK1 (activin receptor-like kinase 1) and the ubiquitous ALK5, as well as the TGF-β type II receptor . This association is essential for the regulation of angiogenesis and vascular development.
Mutations in the endoglin gene are responsible for Hereditary Hemorrhagic Telangiectasia (HHT) type 1, a vascular disorder characterized by defective angiogenesis, arteriovenous malformations, telangiectasia, and frequent nosebleeds (epistaxis) . Additionally, endoglin is implicated in preeclampsia, a pregnancy-related condition characterized by high blood pressure and damage to other organ systems .
Recombinant human endoglin is produced using a mouse myeloma cell line, NS0-derived human endoglin/CD105 protein . It is typically used in research to study its role in angiogenesis and related diseases. The recombinant protein is purified to a high degree, with a purity greater than 90% as determined by SDS-PAGE . It is also tested for endotoxin levels to ensure it is suitable for use in various biological assays .
Recombinant human endoglin is used in various research applications, including: