Cayman L-Selectin/Cd62l Extracellular Domain (Mouse, Recombinant)

L-Selectin, also known as CD62L, is a glycoprotein and cell adhesion molecule that is encoded by the SELL gene in humans.^1,2 It is composed of an N-terminal calcium-dependent lectin domain that recognizes glycoproteins, an EGF-like domain, two consensus repeats, a transmembrane domain, and an intracellular C-terminal tail. L-selectin is expressed in leukocytes and localizes to the plasma membrane.³ It also exists as a soluble form that results from alternative splicing of SELL pre-mRNA or by ectodomain shedding via proteolytic cleavage.² L-selectin facilitates leukocyte rolling on activated vascular endothelium and lymphocyte homing to high endothelial venules of lymph nodes.⁴ It binds to several glycoproteins containing the sulfated sialyl Lewis X (6-sulfo-sLe^X) epitope, including P-selectin glycoprotein ligand-1 (PSGL-1) and glycosylation-dependent cell adhesion molecule-1 (GlyCAM-1).¹ Sell^-/- mice exhibit a reduction in the lymphocyte count in peripheral lymph nodes, as well as a decrease in neutrophil recruitment in a model of peritonitis induced by thioglycolate.⁴ Serum levels of soluble L-selectin are lower in patients with sepsis and associated with higher mortality.⁵ Cayman’s L-Selectin/CD62L Extracellular Domain (mouse, recombinant) protein can be used for cell-based assays. This protein is a disulfide-linked homodimer. The reduced monomer, composed of L-selectin (amino acids 1-332) fused to His-tagged human IgG1 at its C-terminus, consists of 542 amino acids, has a calculated molecular weight of 61 kDa, and a predicted N-terminus of Trp39 after signal peptide cleavage. As a result of glycosylation, the monomer migrates at approximately 100-110 kDa by SDS-PAGE under reducing conditions.

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