Endoglin Human, His
Description
Product Specs
Product Science Overview
Endoglin is characterized by a large, disulfide-linked extracellular region and a short, constitutively phosphorylated cytoplasmic tail . It contains an RGD tripeptide, which is a key recognition structure in cellular adhesion, suggesting a critical role in the binding of endothelial cells to integrins and/or other RGD receptors .
As an accessory receptor for the TGF-β superfamily ligands, endoglin binds TGF-β1 and TGF-β3 with high affinity, not by itself but by associating with the TGF-β type II receptor (TβRII), thereby activating downstream signaling pathways . In human umbilical vein endothelial cells, ALK-1 is also a receptor kinase for endoglin threonine phosphorylation .
Mutations in the endoglin gene can result in hereditary hemorrhagic telangiectasia (HHT), an autosomal-dominant vascular dysplasia . This condition is characterized by abnormal blood vessel formation and can lead to serious complications such as nosebleeds, gastrointestinal bleeding, and arteriovenous malformations.
Recombinant human endoglin (His-Tag) is a form of endoglin that has been genetically engineered to include a polyhistidine tag at the C-terminal. This tag facilitates the purification and detection of the protein in various experimental settings . The recombinant protein is typically expressed in HEK293 cells and consists of 572 amino acids after the removal of the signal peptide, predicting a molecular mass of 62.3 kDa . Due to glycosylation, it migrates as an approximately 80-90 kDa protein in SDS-PAGE under reducing conditions .
Recombinant human endoglin is used in various research applications, including studies on angiogenesis, TGF-β signaling, and vascular diseases. It is provided as a lyophilized powder and is stable for up to twelve months when stored at -20°C to -80°C under sterile conditions .
