Podoplanin (LpMab-12) Mouse mAb #26981
- IHC
- F
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | |
| Source/Isotype | Mouse IgG1 |
Application Key:
- IHC-Immunohistochemistry
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Immunohistochemistry (Paraffin) | 1:250 |
| Flow Cytometry (Fixed/Permeabilized) | 1:800 |
| Flow Cytometry (Live) | 1:800 |
Storage
Protocol
Specificity / Sensitivity
Podoplanin (LpMab-12) Mouse mAb recognizes endogenous levels of human podoplanin. The antibody specifically recognizes podoplanin that is sialylated on Thr52 in the third platelet aggregation domain (PLAG3) of human podoplanin (10).
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with LN-229 glioma cells expressing human podoplanin.
Background
Podoplanin (aggrus, glycoprotein 36) is a single-pass transmembrane protein belonging to the type-1 family of sialomucin-like glycoproteins. Podoplanin was first described in the rat as a surface glycoprotein that regulated podocyte morphology (1). It is now commonly used as a marker of lymphatic endothelial cells, where its expression is associated with the process of lymphangiogenesis (2). Its role in this regard is presumably due to its putative involvement in regulating actin cytoskeleton dynamics (3). Research studies have shown that podoplanin expression is upregulated in a number of tumor types including colorectal cancers (4), oral squamous cell carcinomas (5), and germ cell tumors (6), with higher expression levels often associated with more aggressive tumors (7). Research studies have suggested a functional role for podoplanin in the stromal microenvironment of tumors. For example, it has been reported that podoplanin expression in cancer-associated fibroblasts (CAFs) is positively associated with a stromal environment that promotes cancer progression (8,9).
Podoplanin is O-glycosylated at multiple sites in the extracellular domain, including disialylation at Thr52 in the third platelet-aggregation (PLAG3) domain (10). Research studies have shown that glycoylation at this site is required for tumor cell-induced platelet aggregation activity (11).
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- Feng, J.Q. et al. (2012) Oral Oncol 48, 848-852.
- Mishima, K. et al. (2006) Acta Neuropathol 111, 563-8.
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- Schoppmann, S.F. et al. (2012) Breast Cancer Res Treat 134, 237-44.
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- Kato, Y. et al. (2016) PLoS One 11, e0152912.
- Kaneko, M.K. et al. (2007) FEBS Lett 581, 331-6.
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