Recombinant Human L-Selectin (CD62L)-Fc Chimera (carrier-free)
Description
L-selectin, belonging to the selectin/LECAM family, is a type I transmembrane protein, consisted of one C-type lectin domain and EGF-like repeats, followed by a transmembrane region and a short cytoplasmic tail of 17 amino acids. L-selectin gene encodes a protein with a predicted size of 42 kD, but the actual molecular weight is around 70 kD to 120 kD, due to N-linked glycosylation. L-selectin is constitutively expressed on leukocytes. As a homing receptor, L-selectin mediates adhesion and rolling of leukocytes on endothelial cells, in turn leukocytes enter peripheral lymphoid organs via high endothelial venules (HEV). L-selectin also directs leukocytes to inflammation sites. Circulating leukocytes can also tether on adherent leukocytes through the interaction between L-selectin and P-selectin glycoprotein ligand-1 (PSGL-1). L-selectin also interacts with mucins, such as CD34, glycosylated cell adhesion molecule-1 (GlyCAM-1) and podocalyxin. Ligand-induced clustering of L-selectin enhances leukocyte tethering and causes signaling cascade, promoting activation of integrin and mobilizing chemokine receptor on cell surface. To negatively regulate leukocyte recruitment and migration, L-selectin is cleaved by ADAM17, released from cell surface (ectodomain shedding) with functional activity. High level of soluble L-selectin can be detected in human plasma.