Podoplanin, Human, clone LpMab12
Monoclonal antibody LpMab12 recognizes Podoplanin. Podoplanin (PDPN), also known under the name Aggrus, is highly expressed in various tumors (such as oral, lung, esophageal, brain) and in normal cells as lymphatic endothelial cells and podocytes. PDPN is a small type-I membrane glycoprotein with a large number of O-glycoside chains and therefore it belongs to mucin-type proteins. It can be found on the surface of many types of normal cells originating from various germ layers. It is present primarily on the endothelium of lymphatic vessels, type I pneumocytes and glomerular podocytes. Increased levels of podoplanin or its neo-expression have been found in numerous types of human carcinomas, but it is especially common in squamous cell carcinomas, such as cervical, larynx, oral cavity, skin and lung cancer. This small sialomucin is also seen on the surface of cancer-associated fibroblasts (CAFs) in lung adenocarcinomas, as well as in breast and pancreatic tumors. In most cancers, a high level of podoplanin expression, both in cancer cells, as well as in CAFs, is correlated with an increased incidence of metastasis to lymph nodes and shorter survival time of patients. Little is known about the biological role of podoplanin, however research carried out on mice with a knock-out gene of this glycoprotein shows that the presence of podoplanin determines normal development of lungs, the lymphatic system and heart. Podoplanin on cancer cells and CAFs seems to play an important role in the development and progression of various cancers. Podoplanin possesses in its N-terminal extracellular region 3 tandem repeats of platelet aggregation-stimulating domains (PLAGs). The O-glycosylation on Thr52 of human PDPN (hPDPN) is critical for the interaction of hPDPN with C-type lectin-like receptor-2 (CLEC-2), resulting in platelet aggregation. LpMab12 detects sialylated O-Glycan on Thr52 in PLAG. It detects endogenous hPDPN by flow cytometry. The minimal epitope of LpMab12 is identified as Asp49-Pro53 of hPDPN. LpMAB-12 did recognize the glycosylated hPDPN synthetic peptide 38-54, but not the non-sialylated peptide. LpMab12 could serve as a diagnostic tool for determining whether hPDPN possesses sialylation on Thr52 or not.
. FC: HM2376 can be used both intra- and extracellular.
W: reduced and non-reduced conditions were used. The expected band sizes are ~40 kDa.
Calculate your ELISA data easily
With the ELISA calculator you can easily calculate ELISA data. Assayfit Pro helps to perform curve fitting. The calculator generates advanced reports, fit graph, fit parameters and goodness of fit are shown.
Latest Hycult Biotech news
- New Human Complement Pathway AssaysWe are very proud of our newly developed human classical and alternative complement pathway assays. They are produced in response to a growing demand for quantitative investigation of complement inhibitors or regulators at lower sample dilutions. This development aims to address the issue of false negative results, enabling more accurate and reliable analysis of complement… Read more: New Human Complement Pathway Assays
- Navigating the pitfalls in complement analysisOur colleague Erik Toonen shared his experience on how to analyze complement at the Complement-based Drug Development Summit in Boston in September 11-13th, 2023. He showed valuable insights on analyzing complements. For accurate complement analysis, it is important that not only the correct technique is used but also that pre-analytical sample handling is performed in… Read more: Navigating the pitfalls in complement analysis
- NEW Human C3d ELISAWe are happy to introduce our new ELISA (cat.# HK3017) designed to detect human C3d. What sets this assay apart is its utilization of a distinctive neo-epitope capture antibody that selectively targets a specific C3d region of the alpha chain, which is not available in other C3 variants. This way it specifically distinguishes C3d from native C3… Read more: NEW Human C3d ELISA