Anti-Podoplanin/gp36/PDPN Antibody Picoband® Fluoro647 Conjugated

PDPN (Podoplanin), also called T1A, T1A2, GP36, OTS8 or AGGRUS, is a protein that in humans is encoded by the PDPN gene. This gene encodes a type-I integral membrane glycoprotein with diverse distribution in human tissues. The PDPN gene is mapped to chromosome 1 by the International radiation Hybrid mapping consortium. The physiological function of PDPN may be related to its mucin-type character. The specific function of this protein has not been determined but it has been proposed as a marker of lung injury. Immunohistochemical analysis of PDPN in placenta, kidney, lung, and nasal polyps showed expression at the apical plasma membrane of vascular endothelial cells and in alveolar epithelial cells. Overexpression of rat PDPN in human and rodent endothelial cells promoted formation of elongated cell extensions and significantly increased endothelial cell adhesion, migration, and tube formation. Inhibition of PDPN expression by small interfering RNAs decreased cell adhesion in cultured human dermal lymphatic endothelial cells.

In adult kidney, expressed on the urinary surface and foot processes of podocytes and in parietal epithelial cells of Bowman's capsule where it is localized to luminal surfaces. In lung, expressed exclusively on luminal surfaces of type I alveolar epithelial cells and pleural mesothelial cells. Not expressed in type II alveolar cells. In bone, expressed in osteocytes and osteoblasts. In spleen, liver, stomach and intestine, expressed in mesoepithelium. Also expressed in thymic epithelial cells, choroid plexus and leptomeninges. .

May be involved in cell migration and/or actin cytoskeleton organization. When expressed in keratinocytes, induces changes in cell morphology with transfected cells showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion. Required for normal lung cell proliferation and alveolus formation at birth. Induces platelet aggregation. Does not have any effect on folic acid or amino acid transport. Does not function as a water channel or as a regulator of aquaporin-type water channels (By similarity) . .

1. Kato, Y., Fujita, N., Kunita, A., Sato, S., Kaneko, M., Osawa, M., Tsuruo, T. Molecular identification of Aggrus/T1-alpha as a platelet aggregation-inducing factor expressed in colorectal tumors. J. Biol. Chem. 278: 51599-51605, 2003. 2. Ma, T., Yang, B., Matthay, M. A., Verkman, A. S. Evidence against a role of mouse, rat, and two cloned human T1-alpha isoforms as a water channel or a regulator of aquaporin-type water channels. Am. J. Resp. Cell Molec. Biol. 19: 143-149, 1998. 3. Schacht, V., Ramirez, M. I., Hong, Y.-K., Hirakawa, S., Feng, D., Harvey, N., Williams, M., Dvorak, A. M., Dvorak, H. F., Oliver, G., Detmar, M. T1-alpha/podoplanin deficiency disrupts normal lymphatic vasculature formation and causes lymphedema. EMBO J. 22: 3546-3556, 2003.

Membrane ; Single-pass type I membrane protein . Cell projection, lamellipodium membrane ; Single-pass type I membrane protein . Cell projection, filopodium membrane ; Single-pass type I membrane protein . Cell projection, microvillus membrane ; Single-pass type I membrane protein . Cell projection, ruffle membrane ; Single-pass type I membrane protein . Localized to actin-rich microvilli and plasma membrane projections such as filopodia, lamellipodia and ruffles.