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A DNA sequence encoding the signal peptide, pro-peptide and extracellular domain of human L-Selectin (aa 1-343) was fused to the Fc region of human IgG1 (aa 93-330). The chimeric protein was expressed in modified human 293 cells.

L-Selectin (CD62L) is a type I membrane protein expressed on the surface of T cells, B cells, monocytes, neutrophils, macrophages, eosinophils and NK cells. L-Selectin mediates entry of lymphocytes into secondary lymphoid tissue by adherence to endothelial cells of high endothelial venules (HEV). Recruitment of leukocytes to sites of inflammation also involves L-Selectin dependent adhesion to the endothelium. L-Selectin has been considered as a suitable target for treatment or prevention of inflammatory diseases such as asthma, rheumatoid arthritis, inflammatory bowel disease, allergies and atherosclerosis. L-Selectin is a glycoprotein composed of a C-type lectin family domain at the amino terminus, an EGF-like domain, two Sushi consensus domains, a transmembrane domain and a short cytoplasmic tail. L-Selectin is extensively glycosylated and different glycoforms exist on different leukocyte subsets. Moreover, different L-Selectin glycosylation patterns influence the binding activity to various ligands on the endothelium. L-Selectin contains 7 potential N-linked glycosylation sites. For a recent review of L-Selectin adhesion, signaling and role in inflammation please refer to Barkhausen T, et al. (2005) Exp Toxicol Pathol. 57(1): 39-52.