Anti-Podoplanin Antibody, clone LpMab-13 clone LpMab-13, from mouse

Podoplanin (UniProt: Q86YL7; also known as Aggrus, Glycoprotein 36, Gp36, PA2.26 antigen, T1-alpha, T1A) is encoded by the PDPN (also known as GP36) gene (Gene ID: 10630) in human. 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. 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. Six isoforms of podoplanin have been described that are produced by alternative splicing. It is synthesized with a signal peptide of 22 amino acids, which is cleaved to produce the mature form. Podoplanin contains an extracellular domain (aa 23-131), a helical domain (aa 132-152) and a cytoplasmic region (aa 153-162). Podoplanin possesses three tandem repeat of platelet aggregation-stimulating (PLAG) domains in its N-terminus. Among the PLAG domains, sialylated O-glycan on Thr52 of PLAG3 is essential for the binding to C-type lectin-like receptor-2 (CLEC-2). Interaction of human podoplanin with CLEC-2 mainly involves Glu47 and Asp48 in the platelet PLAG3. Clone LpMab-13 binds to PLAG2/3 domains and recognizes endogenous hPDPN of cancer cells, including glioblastoma, oral cancer, lung cancer, and malignant mesothelioma, and normal cells such as lymphatic endothelial cells and podocytes of kidney. The interaction between LpMab-13 and hPDPN is independent of its glycosylation. The minimum epitope of LpMab-13 is identified to be Ala42-Asp49 of hPDPN. ((Ref.: Ogasawara, S., et al. (2016). Monoclon. Antib. immunodiag. Immunother. 35(3); 155-163).