JAM-1 Mouse anti-Human, Unlabeled, Clone: 43, BD

Description

• Tight junctions (zonulae occludens) are critical to the maintenance of cell polarity and intercellular barriers
• Protein components of the tight junctions include actin filaments, symplekin, occludin, ZO-1, ZO-2, and ZO-3
• Junctional adhesion molecules, JAM-1, -2, and -3, are a new subfamily in the immunoglobulin (Ig) superfamily that colocalize with these components of tight junctions
• JAM-1 was identified through a screen of antibodies that recognizes antigens located at cell-cell contacts
• The structure of JAM-1 includes two V-type Ig domains in the extracellular region, two N-glycosylation sites, and a small C-terminal cytoplasmic region
• JAM-1 protein is expressed at cell-cell junctions in endothelial and epithelial cells, and antibodies to JAM-1 inhibit spontaneous and chemokine-induced monocyte transmigration through an endothelial cell monolayer
• In addition, TNFα and IFN-γ cause redistribution of JAM-1 from intercellular junctions to the cytoplasm
• JAM-1 also is the receptor for the platelet membrane protein, F11 antigen, and activation of platelets leads to PKC phosphorylation of JAM-1
• Thus, JAM-1 is a junctional adhesion molecule that functions in endothelial, epithelial, and platelet adhesion
• Western Blotting