CD62L (L-Selectin) is a type-I transmembrane glycoprotein and a member of the selectin family of adhesion molecules, constitutively expressed on most circulating leukocytes, including lymphocytes (except a substantial population of memory T cells), monocytes, and polymorphonuclear cells. It plays a crucial role in the immune response by mediating the rolling adhesion of leukocytes to endothelial cells, which is essential for lymphocyte homing to secondary lymphoid organs and for the migration of monocytes and neutrophils into inflamed tissues. Structurally, L-Selectin consists of an N-terminal C-type lectin domain, an epidermal growth factor (EGF)-like domain, two short consensus repeat (SCR) sequences, a transmembrane region, and a short cytoplasmic tail. The N-terminal lectin domain interacts with specific carbohydrate ligands such as sialyl Lewis X (sLex) to facilitate adhesion. Additionally, L-Selectin is involved in embryonic implantation by aiding the attachment of the blastocyst to the endometrial endothelium.
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