EMCN Human

Endomucin is a membrane-bound glycoprotein expressed luminally by endothelial cells that line postcapillary venules, which are primary sites of leukocyte recruitment during inflammation . The human recombinant form of Endomucin is produced in E. coli and is a single, non-glycosylated polypeptide chain containing 197 amino acids with a molecular mass of 20.5 kDa . It is often fused to a His-tag at the N-terminus for purification purposes .

Endomucin interferes with the assembly of focal adhesion complexes and inhibits interactions between cells and the extracellular matrix . It is essential for vascular endothelial growth factor (VEGF)-induced clathrin-mediated endocytosis and signaling of VEGF receptor 2 (VEGFR2) . This process is crucial for angiogenesis, the formation of new blood vessels from pre-existing ones, which is necessary for various homeostatic and pathological processes such as embryonic development, wound healing, and tumor growth .

Endomucin interacts with the AP2 complex, which is essential for clathrin-mediated endocytosis . It does not affect clathrin recruitment to the AP2 complex following VEGF stimulation but is necessary for the interaction between VEGFR2 and the AP2 complex during endocytosis . This specificity is highlighted by the fact that Endomucin does not inhibit VEGFR1 and FGFR1 internalization or their downstream activities .

Human recombinant Endomucin is used in various research applications, including blocking assays and control experiments . It is also studied for its role in preventing leukocyte-endothelial cell adhesion, which has implications for inflammatory responses .