Anti-Podoplanin Antibody, clone 8.1.1 clone 8.1.1, from hamster(Syrian)

Podoplanin (UniProt: Q62011; also known as Glycoprotein 38, Gp38, OTS-8, PA2.26 antigen, T1-alpha, T1A, Transmembrane glycoprotein E11) I encoded by the Pdpn (also known as Gp38) gene (Gene ID: 14726) in murine species. Podoplanin serves as the endogenous ligand of C-type lectin-like receptor-2 (CLEC-2) and is highly expressed in various tumors and in some normal cells, such as lymphatic endothelial cells and podocytes. Podoplanin is detected at high levels in lung and brain, at lower levels in kidney, stomach, liver, spleen and esophagus, and not detected in skin and small intestine. It is expressed in epithelial cells of choroid plexus, ependyma, glomerulus and alveolus, in mesothelial cells and in endothelia of lymphatic vessels. It is also expressed in stromal cells of peripheral lymphoid tissue and thymic epithelial cells and is detected in carcinoma cell lines and cultured fibroblasts. High expression of Podoplanin is observed in colon carcinomas. It may be involved in cell migration and/or actin cytoskeleton organization. Podoplanin is localized to actin-rich microvilli and plasma membrane projections, such as filopodia, lamellipodia, and ruffles. Extensively O-glycosylated. Contains sialic acid residues. O-glycosylation is necessary for platelet aggregation activity. Podoplanin levels are down-regulated by treatment with puromycin aminonucleoside. Mice lacking or with defective podoplanin die at birth of respiratory failure due to a low number of attenuated type I cells, narrow and irregular air spaces, and defective formation of alveolar saccules. Administration of PMab-1 antibody is shown to reduce lymphangiogenesis in the corneal suture and ear wound healing murine models. It suppresses thioglycollate-induced macrophages infiltration at the site of wound healing. (Ref.: Maruyama, Y et al (2014). Invest.Ophthal. Visual Sci. 55(8); 4813-4822).