Anti-Podoplanin Antibody, clone LpMab-17 clone LpMab-17, 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-17 is reported to bind to non-PLAG domain and detects endogenous podoplanin in cancer cells and normal cells. It recognizes glycan-deficient podoplanin indicating that its interaction with podoplanin is independent of its glycosylation. The minimum epitope of LpMab-17 is identified as Gly77-Asp82. Although human and monkey podoplanin exhibit 94% homology, this clone does not recognize monkey podoplanin. (Ref.: Kato, Y., et al. (2016). Monoclon. Antib. immunodiag. Immunother. 35(2); 109-116).