Podoplanin is a transmembrane glycoprotein that has roles in development, immunology, and cancer.{64186,64187} It is composed of a glycosylated extracellular domain, which is critical for podoplanin-induced platelet activation, a single transmembrane region that associates with CD9 and CD44, and a short cytoplasmic tail that interacts with the ezrin-radixin-moesin (ERM) family of proteins to promote rearrangement of the actin cytoskeleton, as well as the epithelial-to-mesenchymal transition (EMT) during embryonic development.{64187} Podoplanin is expressed in various tissues during murine embryonic development but is predominantly restricted to stromal, lymphatic endothelial, and immune cells, lymphoid organs, and the heart and choroid plexus in the adult mouse.{64186,64187} Its expression is upregulated by various pro-inflammatory cytokines, including IL-22, IL-6, IFN-?, and TGF-?, and is increased in T cells, fibroblasts, and macrophages during inflammation. It localizes to the cell surface within lipid rafts where it interacts with numerous proteins to modulate cell adhesion and motility.{64186} Podoplanin binds to C-type lectin receptor 2 (CLEC-2), which is expressed on platelets, to induce platelet aggregation and activation, an effect that is inhibited by the interaction of podoplanin with CD9. Mice implanted with MCF-7 cells overexpressing podoplanin exhibit reduced primary tumor growth but enhanced tumor lymphangiogenesis and lymph node metastasis.{64188} Tumor podoplanin expression is associated with reduced overall survival in patients with oral squamous cell carcinoma (OSCC).{64189} Cayman’s Podoplanin Monoclonal Antibody (Clone pmab-1) can be used for flow cytometry (FC) and Western blot (WB) applications. The antibody recognizes podoplanin at ~42 kDa from mouse samples.