Anti-Podoplanin Antibody, clone PMab-2 clone PMab-2, from mouse

Podoplanin (UniProt: Q64294; also known as E11 antigen epitope, Glycoprotein 38, Gp38, OTS-8, RTI140, T1-alpha, T1A, Type I cell 40 kDa protein) is encoded by the Pdpn (also known as Gp38, Ots8) gene (Gene ID: 54320) in rat. 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. 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. 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 23-135), a helical domain (aa 136-156) and a cytoplasmic region (aa 157-166). Podoplanin is extensively O-glycosylated and contains sialic acid residues. O-glycosylation is believed to be essential for its platelet aggregation activity. Clone PMab2 exhibits high affinity for podoplanin (Kd = 0.59 nM). (Ref.: Oki, H et al. (2015). Monoclon. Antib. Immunodiagn. Immunother. 34(6); 396-403).