E-Selectin/CD62E Fc Chimera Protein, Human

E-Selectin (Endothelial Leukocyte Adhesion Molecule-1, ELAM-1, CD62E), a member of the Selectin family, is a 107 - 115 kDa cell surface glycoprotein. E-selectin is a cell adhesion molecule that is critical for inflammation and neovascularization in areas of wound healing and ischemia. In response to tissue injury, release of cytokines/chemokines, including stromal cell-derived factor 1α (SDF-1α), induces local endothelial expression of membrane-bound E-selectin and systemic reciprocal E-selectin ligand expression on endothelial progenitor cells (EPCs) in the bone marrow via C-X-C motif chemokine receptor 4 (CXCR4). It is transiently expressed on vascular endothelial cells in response to IL-1 beta and TNF-alpha, and demonstrates peak expression at 4 hours, and decay at 24 hours, in response to activation. It is a cell surface glycoprotein that plays a role in immune adhesion. By interacting with SELPLG/PSGL1, it mediates the adhesion of blood neutrophils in the endothelium activated by cytokines. May play a role in capillary morphogenesis. E-Selectin mediates the attachment of flowing leukocytes to the blood vessel wall during inflammation by binding to E-Selectin ligands on leukocytes.  These interactions are labile and permit leukocytes to roll along the vascular endothelium in the direction of blood flow.  This initial interaction is followed by a stronger interaction involving ICAM-1 and VCAM-1 that leads eventually to extravasation of the white blood cell through the blood vessel wall into the extracellular matrix tissue.