Human E-Selectin / CD62E Protein, His Tag

E-Selectin is also known as CD62 antigen-like family member E (CD62E), endothelial-leukocyte adhesion molecule 1 (ELAM-1), or leukocyte-endothelial cell adhesion molecule 2 (LECAM2), a member of the Selectin family, is a 107-115 kDa cell surface glycoprotein. It is transiently expressed on vascular endothelial cells in response to IL-1β and TNFα. E selectin has a cassette structure: an N-terminal, C-type lectin domain, an EGF (epidermal-growth-factor) -like domain, 6 Sushi domain (SCR repeat) units, a transmembrane domain (TM) and an intracellular cytoplasmic tail (cyto) . During inflammation, E-selectin plays an important part in recruiting leukocytes to the site of injury. The local release of cytokines IL-1 and TNF-α by damaged cells induces the over-expression of E-selectin on endothelial cells of nearby blood vessels. E-selectin mediates the adhesion of tumor cells to endothelial cells, by binding to E-selectin ligands expressed by neutrophils, monocytes, eosinophils, memory-effector T-like lymphocytes, natural killer cells or cancer cells. Furthermore, a number of studies have reported that levels of E-Selectin may be elevated in subjects with a variety of pathological conditions.

This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 59.5 kDa. The protein migrates as 67-96 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

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