L-Selectin/CD62L Extracellular Domain (human, recombinant)

L-Selectin/CD62L Extracellular Domain (human, recombinant)

CAT N°: 35509
Price:

505.00 429.25

L-Selectin, also known as CD62L, is a glycoprotein and cell adhesion molecule that is encoded by the SELL gene in humans.{60879,60892} 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.{60893} It also exists as a soluble form that results from alternative splicing of SELL pre-mRNA or by ectodomain shedding via proteolytic cleavage.{60892} L-selectin facilitates leukocyte rolling on activated vascular endothelium and lymphocyte homing to high endothelial venules of lymph nodes.{60894} 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).{60879} Human, but not mouse, L-selectin also binds to E-selectin from human, pig, rat, and mouse neutrophils.{60914} 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.{60894} Serum levels of soluble L-selectin are lower in patients with sepsis and associated with higher mortality.{60895} 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.

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