Mouse JAM-B/VE-JAM Biotinylated Antibody

The family of juctional adhesion molecules (JAM), comprising at least three members, are type I transmembrane receptors belonging to the immunoglobulin (Ig) superfamily (1, 2). These proteins are localized in the tight junctions between endothelial cells or epithelial cells. Some family members are also found on blood leukocytes and platelets. JAM-B, alternatively named vascular endothelial JAM (VE-JAM), is expressed prominently on high endothelial venules of lymphoid organs where it is localized to the intercellular boundaries of high endothelial cells. It is also expressed on the endothelium of a variety of non-lymphoid organs, especially the heart and placenta (2, 3, 5). Mouse JAM-B/VE-JAM cDNA predicts a 298 amino acid (aa) residue precursor protein with a putative 28 aa signal peptide, a 209 aa extracellular region containing two Ig domains, a 23 aa transmembrane domain, and a 38 aa cytoplasmic domain containing a PDZ-binding motif and a PKC phosphorylation site (2, 3). Mouse JAM-B shares approximately 79% aa sequence homology with its human homologue. It also shares approximately 35% aa sequence homology with mouse JAM-A or JAM-C. JAM-B exhibits homotypic interactions, as well as heterotypic interactions with JAM-C, but not JAM-A (4, 5, 7). It is also a ligand for the integrin alpha4beta1. However, the JAM-B/alpha4beta1 interaction is facilitated only after prior adhesion of JAM-B to JAM-C (6). Through its heterotypic interactions with JAM-C, JAM-B is an adhesive ligand for T, NK, and dendritic cells, and may play a role in regulating leukocyte transmigration (5).