Recombinant Human ICAM-1-Fc Chimera (carrier-free)
Description
ICAM-1, intercellular adhesion molecule 1, is a member of the immunoglobulin superfamily. Structurely, ICAM-1 is characterized by heavy glycosylation with an extracellular domain composed of multiple loops created by disulfide bridges within the protein. The dominant secondary structure of the protein is the beta sheet, leading investigators to hypothesize the presence of dimerization domains within ICAM-1. This protein is constitutively expressed at low levels on the cell surface of leukocytes, endothelial cells, macrophages, and lymphocytes. Upon cytokine activation, by cytokines such as IL-1 and TNFα, the concentration of ICAM-1 on the cell surface greatly increases. The ligand of ICAM-1 is LFA-1 (leukocyte function associated antigen 1), which is found on all T cells. LFA-1/ICAM-1 interaction has been shown to be important for T cell-T cell interactions, which leads to further T cell differentiation. ICAM-1 was found to play a role in infectious diseases, as it was identified as the binding target for entry of the major group of human rhinoviruses into various cell types and is also known for its affinity for Plasmodium falciparum-infected erythrocytes. These findings indicate that ICAM-1 may participate in the pathogenesis of several infectious agents.