Anti-Podoplanin antibody produced in rabbit

Podoplanin (PDPN) is a transmembrane sialoglycoprotein. It consists of 162 amino acids and is part of the type-1 transmembrane sialomucin-like glycoprotein family. The protein is expressed in various tissues. The PDPN gene is localized on human chromosome 1p36.21.

Podoplanin is an integral membrane mucoprotein present on the surface of podocytes in kidney glomeruli and the parietal cells of the glomerular Bowman′s capsule. It is a single membrane-spanning protein composed of a heavily glycosylated extracellular domain and a short intracytoplasmic tail. Podoplanin, also named E11 antigen, is present in normal, inflammatory and neoplastic lymphatic capillary endothelium. It is expressed selectively by dermal microvascular lymphatic endothelial cells but not by blood vascular endothelial cells.

synthetic peptide corresponding to amino acids 24-40 of human podoplanin with an N-terminal added cysteine, conjugated to KLH.

Anti-Podoplanin antibody produced in rabbit has been used in immunoblotting.

Anti-Podoplanin antibody produced in rabbit has been used in immunohistochemistry.

Podoplanin (PDPN) is expressed in many cancers. In cancerous cells, it induces platelet aggregation and epithelial-mesenchymal transition. The protein is an immunohistochemical marker of lymphatic vessels. Podoplanin also has a role in embryonic development.

Podoplanin appears to play an important role in the maintenance of podocyte foot processes, and hence, glomerular permeability. It is detectable in human angiosarcomas, lymphangiomas and in Kaposi′s sarcomas. Experiments involving depletion of T1a/podoplanin in mice indicate a critical regulatory role for it in formation of the lymphatic vasculature.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide and 1% bovine serum albumin.

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