ICAM-1/CD54 Extracellular Domain (human, recombinant)

Intercellular adhesion molecule-1 (ICAM-1), also known as CD54, is a cell surface glycoprotein and member of the Ig superfamily. It is composed of five extracellular Ig domains, which can vary in number through alternative splicing, a transmembrane domain, and a short C-terminal cytoplasmic domain. ICAM-1 is basally expressed at low levels but cytokines, such as NF-kappaB, TNF-alpha, and IL-1alpha, increase ICAM-1 levels in endothelial, epithelial, and immune cells. It binds integrins, such as lymphocyte function-associated antigen-1 (LFA-1) and complement 3 receptor (C3R), and directs lymphocytes or other immune cells to locally inflamed areas, among other roles in forming epithelial and endothelial barriers, regulating cell migration, and immune signaling. ICAM-1 can be cleaved from the cell membrane by cathepsin G or neutrophil elastase and promote or antagonize inflammation in a context-dependent manner and induce wound healing. Blood levels of soluble ICAM-1 are increased in patients with cancer, and serum levels of soluble ICAM-1 are increased in patients with acute ischemic stroke. Cayman's ICAM-1/CD54 Extracellular Domain (human, recombinant) protein consists of 459 amino acids and has a calculated molecular weight of 50. kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 71. kDa due to glycosylation.