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Description
The monoclonal antibody BV16 recognizes the human junction adhesion molecule (JAM)-A. Together with JAM-C (JAM-2) and JAM-B (VE-JAM or JAM-3), JAM-A belongs to a family of adhesion proteins with a V-C2 immunoglobulin domain organization and their molecular weight is about 30-40 kDa. JAMs are important for a variety of cellular processes, including tight junction assembly, leukocyte transmigration, platelet activation, angiogenesis and virus binding. JAM-A is expressed by endothelial and epithelial cells, platelets, neutrophils, monocytes, lymphocytes and erythrocytes. Like all other JAMs, JAM-A plays an important role in tight junctions where it is involved in cell-to-cell adhesion through homophilic interaction. It codistributes with other tight junction components as ZO-1, 7H6 antigen, cingulin and occludin. JAM-A also plays an important role in leukocyte transmigration. Leukocyte transmigration can be blocked by antibodies and by soluble JAM-A/Fc fusion proteins. Homophilic JAM-A interactions between leukocytes and the endothelium but also heterophilic interactions of JAM-A with the beta2-integrin leukocyte function-associated antigen-1 (LFA-1) are considered to actively guide leukocytes during transmigration. Several studies imply a role for JAM-A in the initiation of atherosclerosis since JAM-A is upregulated on early atherosclerotic endothelium. The adhesion of activated platelets on the activated endothelium is mediated by homophilic interactions of JAM-A. PAM-1, JAM-1, JAMA, CD321, platelet F11 receptor Aliases Fusion protein consisting of the extracellular domain of human JAM and the Fc portion of human IgGs Immunogen Mouse IgG1