SELE Antibody / E-selectin, 100ug

SELE antibody, also known as E-selectin antibody, recognizes E-selectin, a type I transmembrane adhesion molecule encoded by the SELE gene and commonly referred to as CD62E and endothelial-leukocyte adhesion molecule 1. E-selectin is primarily localized to the plasma membrane of activated endothelial cells and is a member of the selectin family of calcium-dependent lectins. Under basal conditions, SELE expression is low or absent; however, it is rapidly induced in endothelial cells in response to inflammatory cytokines such as interleukin-1 and tumor necrosis factor alpha, linking vascular activation to immune cell recruitment.<br><br>SELE antibody detects a glycoprotein composed of an N-terminal C-type lectin domain, an epidermal growth factor-like domain, multiple short consensus repeat units, a single transmembrane region, and a short cytoplasmic tail. The lectin domain mediates binding to sialylated carbohydrate ligands, including sialyl Lewis x structures on neutrophils, monocytes, and subsets of lymphocytes. Through these interactions, E-selectin supports leukocyte tethering and rolling along the vascular endothelium under shear flow conditions, representing a critical early step in extravasation during inflammation.<br><br>Functionally, E-selectin plays a central role in acute and chronic inflammatory responses by regulating leukocyte trafficking into tissues. Because its expression is tightly controlled and transient following cytokine stimulation, SELE is widely used as a marker of endothelial activation in experimental models of vascular inflammation. Elevated E-selectin levels have been associated with atherosclerosis, cardiovascular disease, autoimmune disorders, and other inflammatory conditions. In oncology research, endothelial E-selectin can contribute to adhesion of circulating tumor cells, implicating SELE in metastatic dissemination and tumor-vascular interactions.<br><br>The SELE gene is located on chromosome 1 and is transcriptionally regulated by inflammatory signaling pathways, including those downstream of nuclear factor kappa B activation. The endothelial-restricted and inducible nature of E-selectin expression makes detection of this protein valuable for studying cytokine signaling, vascular biology, and immune-endothelial interactions.<br><br>This recombinant monoclonal SELE antibody (clone r16G4) targets E-selectin protein in research applications. SELE antibody supports investigation of endothelial activation, leukocyte recruitment mechanisms, and disease-associated inflammatory signaling.

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