ICAM-2 Fc

Intracellular adhesion molecule‐2 (ICAM‐2), also known as CD102, is a member of the Ig superfamily of calcium‐ independent transmembrane glycoproteins. ICAM‐2 is a ligand for the β2‐integrins, lymphocyte function‐ associated antigen‐1 (LFA‐1) and Mac‐1. Constitutively expressed on all vascular endothelial cells and at endothelial cell junctions, it is also expressed at low levels on most leukocytes. As a cell surface adhesion molecule, it is involved in leukocyte recruitment and mediates leukocyte binding. Through interaction with LFA‐1, ICAM‐2 activates the PI3K/AKT pathway which leads to inhibition of TNF‐α and Fas‐mediated apoptosis. ICAM‐2 is highly expressed in lymphomas and it is postulated to be involved in lymphocyte recirculation and trafficking. T cell crawling and diapedesis across the blood‐brain barrier has been shown to be regulated by ICAM‐2 via ligation of LFA‐1 as well as neutrophil crawling and IL‐1ß‐stimulated extravasation through ligation of Mac‐1. ICAM‐2 has been shown to suppress neuroblastoma cell motility by binding with the cytoskeletal linker protein α‐actinin which, in turn, regulates metastasis. Additionally, it has been found to enhance the immune response in colon carcinoma cells and induce an antitumor immune response in pancreatic carcinogenesis. The CHO‐derived Recombinant Human ICAM‐2 Fc is a glycosylated, disulfide‐linked homodimer of 435 amino‐acid‐residues whose monomer consists of the 202‐amino‐acid extracellular portion of ICAM‐2 fused to the 231 amino‐acid length Fc portion of human IgG by two glycine residues. The calculated molecular weight of monomeric CHO cell‐derived Recombinant Human ICAM‐2 Fc is 48.5 kDa; however, due to glycosylation, it migrates at an apparent molecular weight of approximately 70‐80 kDa by SDS‐PAGE analysis under reducing conditions.