| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Podoplanin; Aggrus; Glycoprotein 36; Gp36; PA2.26 antigen; T1-alpha; T1A; 29kDa cytosolic podoplanin intracellular domain; PICD; PDPN; GP36; PSEC0003, PSEC0025 |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | E.coli-derived mouse Podoplanin/gp36/Pdpn recombinant protein (Position: T24-P172). |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Target | |
| UniProt # |
Overview
Anti-Podoplanin/gp36/Pdpn Antibody Picoband® is an antibody for Pdpn detection raised in Rabbit (Polyclonal, Rabbit IgG), with reported reactivity: Mouse,Rat. Commonly used in WB, IHC, IF, ICC, Flow Cytometry, ELISA workflows.
Key elements and design rationale
- Target: Pdpn (podoplanin); UniProt: Q62011
- Antibody format: Rabbit, Polyclonal, Rabbit IgG
- Molecular weight: 37 kDa
- Applications: WB, IHC, IF, ICC, Flow Cytometry, ELISA
Vendor description (summary): Boster Bio Anti-Podoplanin/gp36/Pdpn Antibody Picoband® catalog # A01124-2.
Biological background
Biological context: Mediates effects on cell migration and adhesion through its different partners. During development plays a role in blood and lymphatic vessels separation by binding CLEC1B, triggering CLEC1B activation in platelets and leading to platelet activation and/or aggregation (PubMed:14522983, PubMed:15231832, PubMed:17616532, PubMed:18215137, PubMed:17222411). Interaction with CD9, on the contrary, attenuates platelet aggregation induced by PDPN (PubMed:18541721). Through MSN or EZR interaction promotes epithelial-mesenchymal transition (EMT) leading to ERZ phosphorylation and triggering RHOA activation leading to cell migration increase and invasiveness (PubMed:17046996, PubMed:21376833). Interaction with CD44 promotes ional cell migration in epithelial and tumor cells (PubMed:20962267). In lymph nodes (LNs), controls fibroblastic reticular cells (FRCs) adhesion to the extracellular matrix (ECM) and contraction of the actomyosin by maintaining ERM proteins (EZR; MSN and RDX) and MYL9 activation through association with unknown transmembrane proteins. Engagement of CLEC1B by PDPN promotes FRCs relaxation by blocking lateral membrane interactions leading to reduction of ERM proteins (EZR; MSN and RDX) and MYL9 activation (By similarity). Through binding with LGALS8 may participate to connection of the lymphatic endothelium to the surrounding extracellular matrix (PubMed:19268462). In keratinocytes, induces changes in cell morphology showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion (PubMed:15515019). Controls invadopodia stability and maturation leading to efficient degradation of the extracellular matrix (ECM) in tumor cells through modulation of RHOC activity in order to activate ROCK1/ROCK2 and LIMK1/LIMK2 and inactivation of CFL1 (PubMed:25486435). Required for normal lung cell proliferation and alveolus formation at birth (By similarity). Does not function as a water channel or as a regulator of aquaporin-type water channels (PubMed:9651190). Does not have any effect on folic acid or amino acid transport (By similarity).
Expression and localization notes: cellular localization: Cytoplasm., tissue context: Highly expressed in placenta, lung, skeletal muscle and brain. Weakly expressed in brain, kidney and liver. In placenta, expressed on the apical plasma membrane of endothelium. In lung, expressed in alveolar epithelium. Up-regulated in colorectal tumors and expressed in 25% of early oral squamous cell carcinomas..
Common research applications
- Western blotting (WB): Compare Pdpn levels across samples and conditions using appropriate loading and biological controls.
- Immunohistochemistry (IHC): Evaluate spatial distribution of Pdpn in tissue sections, considering fixation and antigen retrieval effects.
- Immunofluorescence / ICC: Assess subcellular localization patterns and co-localization with compartment markers in cultured cells.
- Flow cytometry: Quantify Pdpn-positive populations in single-cell suspensions with appropriate gating and controls.
- ELISA: Use antibody-based detection formats to assess antigen presence or binding in plate-based assays.
Notes for experimental interpretation
- Account for isoforms, post-translational modifications, and sample-specific processing that can shift apparent molecular weight or epitope accessibility.
- Use positive/negative biological controls where possible (e.g., known-expressing cells/tissues, knockdown/knockout models) and include appropriate secondary-only/isotype controls for imaging workflows.
Additional product notes (from provided fields)
- Background: Podoplanin (PDPN) 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 International radiation Hybrid mapping consortium mapped the T1A gene to chromosome 1. It has got 162 amino acid protein which is a typical type I membrane glycoprotein, with an N-terminal signal sequence, a signal sequence cleavage site, a C-terminal hydrophobic stretch, and a short cytoplasmic tail. Northern blot analysis detected a 1.2-kb T1A2 transcript only in lung. It has been described as a differentiation antigen and influenza-virus receptor, and a marker of lung injury.
- Cross reactivity: No cross-reactivity with other proteins.
- Cellular localization: Cytoplasm.
- Tissue details: Highly expressed in placenta, lung, skeletal muscle and brain. Weakly expressed in brain, kidney and liver. In placenta, expressed on the apical plasma membrane of endothelium. In lung, expressed in alveolar epithelium. Up-regulated in colorectal tumors and expressed in 25% of early oral squamous cell carcinomas.
- Research category: Cancer,Co-Activators/Co-Repressors,Energy Metabolism,Energy Transfer Pathways,Epigenetics and Nuclear Signaling,Metabolic Signaling Pathways,Metabolism,Neurology Process,Neuroscience,Nuclear Hormone Receptors,Nuclear Receptors,Nuclear Signaling,Nuclear Signaling Pathways,Pathways and Processes,Signal Transduction,Signaling Pathway
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