Anti-Podoplanin Antibody, clone LpMab-12 clone LpMab-12, 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-12 specifically detects sialylated O-Glycan on Thr52 of platelet aggregation-stimulating domain of human podoplanin. It also reacts with the synthetic glycopeptide of hPDPN, corresponding to 38 54 amino acids that carries 2-6 sialylated N-acetyl-D-galactosamine (GalNAc) on Thr52. The minimal epitope of LpMab-12 is identified as Asp49 Pro53 of hPDPN. (Ref.: Kato, Y et al. (2016). PLoS ONE 11(3): e0152912).