Recombinant Mouse Podoplanin Fc Chimera Protein, CF

Podoplanin, also known as glycoprotein 38 (gp38), PA2.26 antigen, T1-alpha (T1A), and aggrus, is a 38 kDa type I transmembrane sialoglycoprotein and member of the podoplanin family (1, 2). Podoplanin is synthesized as a 172 amino acid (aa) precursor with a 22 aa signal sequence, a 119 aa extracellular domain (ECD), a 21 aa transmembrane region, and a short, 10 aa cytoplasmic tail (SwissProt #: Q62011). The ECD contains abundant Ser/Thr residues as potential sites for O-glycosylation, and the cytoplasmic region contains putative sites for kinase C and cAMP phosphorylation (2, 3). Mouse Podoplanin shares 77% and 46% aa sequence identity with rat and human Podoplanin, respectively. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells (4, 5), and on numerous tumors including colorectal tumors (3), squamous cell carcinomas (4, 6), testicular seminoma (7), and brain tumors (8-10). One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver (1). Podoplanin is the ligand for C-type lectin-like receptor 2 (CLEC-2) (2). Their association is dependent on sialic acid on O-glycans of Podoplanin (2). Through its association with CLEC-2, Podoplanin induces platelet aggregation and tumor metastasis (2). Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth (2).