Podoplanin is present on the surface of podocytes in kidney glomeruli and the parietal cells of the glomerular Bowman′s capsule. It is also named E11 antigen and has been described to be present in normal, inflammatory, and neoplastic lymphatic capillary endothelium. Podoplanin is expressed selectively by dermal microvascular lymphatic endothelial cells but not by blood vascular endothelial cells. It is composed of heavily glycosylated extracellular domain and a short intracytoplasmic tail.
Podoplanin is part of the type-1 transmembrane sialomucin-like glycoprotein family. The gene encoding this 43kDa protein is localized on rat chromosome 5.
synthetic peptide of rat podoplanin (amino acids 111-129) with N-terminal cysteine, conjugated to KLH. The sequence in mouse differs by one residue.
Anti-Podoplanin (HG-19) antibody produced in rabbit has been used in immunostaining, immunoblotting and immunofluorescence staining.
200 μL in poly bottle
Podoplanin is a marker of lymphatic endothelial cells. It may have a role in tumor cell invasion and migration.
Podoplanin expression is regulated by the lymphatic-specific homeobox gene Prox-1. Podoplanin appears to play an important role in the maintenance of podocyte foot processes, and hence, glomerular permeability. It has a critical regulatory role in the formation of the lymphatic vasculature. Podoplanin does not seem to be upregulated in tumor angiogenesis. It is detectable in human angiosarcomas, lymphangiomas, and in Kaposi′s sarcomas.
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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