Podoplanin Antibody (Rabbit mAb) [K11E7]

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IP1:30 IHC1:4000 FCM1:300

Application
WB, IP, IHC, FCM

Reactivity
Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
17 kDa 38 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
Podoplanin Antibody (Rabbit mAb) [K11E7] detects endogenous levels of total Podoplanin protein.

Clone
K11E7

Synonym(s)
GP36, PSEC0003, PSEC0025, PDPN, Podoplanin, Aggrus, Glycoprotein 36, PA2.26 antigen, T1-alpha, Gp36, T1A

Background
Podoplanin, also known as gp36, PA2.26, or T1alpha, is a mucin-type, type I transmembrane glycoprotein expressed on lymphatic endothelial cells, fibroblastic reticular cells within lymph nodes, kidney podocytes, type I lung alveolar epithelial cells, and choroid plexus epithelium, while notably absent from vascular blood endothelial cells, an expression boundary that is functionally central to its role. Podoplanin functions as the principal endogenous ligand for CLEC-2, a C-type lectin-like receptor expressed at high levels on platelets and megakaryocytes; engagement of CLEC-2 by podoplanin cross-links and clusters CLEC-2 dimers on the platelet surface, and this clustering recruits a single Syk kinase molecule to each pair of CLEC-2 receptors, triggering CLEC-2 and Syk phosphorylation that proceeds largely through Syk's own kinase activity rather than depending primarily on Src-family kinases, and this activated Syk subsequently phosphorylates the downstream LAT signalosome to drive platelet activation and aggregation. Correct surface expression of podoplanin on lymphatic endothelial cells requires transcriptional activation by the transcription factor Prox1 together with modification of the protein with core-1-derived O-glycans, and this glycosylation is functionally required for productive CLEC-2 engagement rather than a passive structural feature. Beyond its role as a CLEC-2 ligand, podoplanin engages in constitutive, cell-autonomous signaling through direct interaction with proteins of the ezrin/radixin/moesin family, providing a structural link between the podoplanin cytoplasmic tail and the underlying actin cytoskeleton that supports cell shape and migratory behavior independently of platelet engagement. During embryonic development, podoplanin-CLEC-2 signaling in lymphatic endothelial cells is required to initiate and maintain physical separation of the blood and lymphatic vasculatures as the lymph sac buds from the cardinal vein, and this same interaction stabilizes the integrity of high endothelial venules within lymph nodes in adult tissue; loss of either podoplanin or CLEC-2 produces blood-lymphatic vessel mixing and hemorrhage, directly linking this single receptor-ligand pair to vascular compartmentalization. Podoplanin additionally facilitates hematogenous tumor metastasis through CLEC-2-mediated platelet activation at the tumor cell surface, and podoplanin knockdown in lymphatic endothelial cells reduces RhoA activation, cell migration, and tube formation, while podoplanin overexpression in cancer cell lines activates RhoA and correlates with a migratory, epithelial-mesenchymal-transition-like phenotype, positioning the CLEC-2-podoplanin axis as a defined target relevant to both normal vascular development and tumor-associated thromboinflammation and metastasis.

Background

Podoplanin, also known as gp36, PA2.26, or T1alpha, is a mucin-type, type I transmembrane glycoprotein expressed on lymphatic endothelial cells, fibroblastic reticular cells within lymph nodes, kidney podocytes, type I lung alveolar epithelial cells, and choroid plexus epithelium, while notably absent from vascular blood endothelial cells, an expression boundary that is functionally central to its role. Podoplanin functions as the principal endogenous ligand for CLEC-2, a C-type lectin-like receptor expressed at high levels on platelets and megakaryocytes; engagement of CLEC-2 by podoplanin cross-links and clusters CLEC-2 dimers on the platelet surface, and this clustering recruits a single Syk kinase molecule to each pair of CLEC-2 receptors, triggering CLEC-2 and Syk phosphorylation that proceeds largely through Syk's own kinase activity rather than depending primarily on Src-family kinases, and this activated Syk subsequently phosphorylates the downstream LAT signalosome to drive platelet activation and aggregation. Correct surface expression of podoplanin on lymphatic endothelial cells requires transcriptional activation by the transcription factor Prox1 together with modification of the protein with core-1-derived O-glycans, and this glycosylation is functionally required for productive CLEC-2 engagement rather than a passive structural feature. Beyond its role as a CLEC-2 ligand, podoplanin engages in constitutive, cell-autonomous signaling through direct interaction with proteins of the ezrin/radixin/moesin family, providing a structural link between the podoplanin cytoplasmic tail and the underlying actin cytoskeleton that supports cell shape and migratory behavior independently of platelet engagement. During embryonic development, podoplanin-CLEC-2 signaling in lymphatic endothelial cells is required to initiate and maintain physical separation of the blood and lymphatic vasculatures as the lymph sac buds from the cardinal vein, and this same interaction stabilizes the integrity of high endothelial venules within lymph nodes in adult tissue; loss of either podoplanin or CLEC-2 produces blood-lymphatic vessel mixing and hemorrhage, directly linking this single receptor-ligand pair to vascular compartmentalization. Podoplanin additionally facilitates hematogenous tumor metastasis through CLEC-2-mediated platelet activation at the tumor cell surface, and podoplanin knockdown in lymphatic endothelial cells reduces RhoA activation, cell migration, and tube formation, while podoplanin overexpression in cancer cell lines activates RhoA and correlates with a migratory, epithelial-mesenchymal-transition-like phenotype, positioning the CLEC-2-podoplanin axis as a defined target relevant to both normal vascular development and tumor-associated thromboinflammation and metastasis.

References
https://pubmed.ncbi.nlm.nih.gov/26498027/ https://pubmed.ncbi.nlm.nih.gov/31778548/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%