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Explore how neutrophils shape the immune response in health and disease. This poster highlights neutrophil pathogen defense mechanisms, including phagocytosis, degranulation, and NETosis, as well as neutrophil roles in inflammation and NET-associated pathologies.
DOWNLOAD NOWL-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-sLeX) epitope, including P-selectin glycoprotein ligand-1 (PSGL-1) and glycosylation-dependent cell adhesion molecule-1 (GlyCAM-1).1 Human, but not mouse, L-selectin also binds to E-selectin from human, pig, rat, and mouse neutrophils.5 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.6 Cayman’s L-Selectin (human, recombinant) protein consists of 315 amino acids, has a calculated molecular weight of 35.6 kDa, and a predicted N-terminus of Asp29 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 50 kDa due to glycosylation.
WARNING This product is not for human or veterinary use.
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2. L-
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4. Lymphocyte homing and leukocyte rolling and migration are impaired in L-
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6. Soluble L-