BD, 612120, Purified Mouse Anti-JAM-1 43/JAM-1

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.

The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography. Store undiluted at -20°C.
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.