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Increased expression of twist/podoplanin in ductal breast carcinoma was associated with shorter patient survival.
Study showed that podoplanin increases the motility of fibroblasts and facilitates their interaction with endothelial cells. This, respectively, favors movement of fibroblasts into the breast tumor stroma and affects tumor angiogenesis, what creates a favorable microenvironment for breast cancer progression.
Data suggest that podoplanin (PDPN) might be a pathogenetic determinant of malignant pleural mesothelioma (MPM) dissemination and aggressive growth and may thus be an ideal therapeutic target.
high podoplanin expression in primary brain tumors induces platelet aggregation, correlates with hypercoagulability, and is associated with increased risk of VTE
This article provides evidence supporting the implication of podoplanin expression as a marker of bad prognosis of cutaneous squamous cell carcinoma
A possible crosstalk between epithelial and stromal tumor cells in hepatocellular carcinoma tumor microenvironment may be mediated by podoplanin
interest, LpMab-17 did not bind to monkey PDPN, whereas the homology is 94% between human PDPN and monkey PDPN, indicating that the epitope of LpMab-17 is unique compared with the other anti-PDPN mAbs. The combination of different epitope-possessing mAbs could be advantageous for the PDPN-targeting diagnosis or therapy
podoplanin expression is significantly associated with malignant transformation of chronic lip discoid lupus erythematosus into lip squamous cell carcinoma
the epitope of PMab-21 was identified as Leu44-Glu48, which is corresponding to platelet aggregation-stimulating (PLAG) domain, indicating that Ser61-Ala68 of rabbit PDPN is a more appropriate epitope for immunohistochemistry compared with PLAG domain. PMab-32 could be useful for uncovering the function of rabbit PDPN
NZ-1 inhibits the hPDPN-CLEC-2 (show CLEC1B Proteins) interaction and is also useful for anti-PA tag MAb.The minimum epitope of LpMab-13 was identified as Ala42-Asp49 of hPDPN using Western blot and flow cytometry. The combination of different epitope-possessing MAbs could be advantageous for the hPDPN-targeting diagnosis and therapy
Describe a bone-specific conditional Pdpn hypomorphic knockout mouse and confirm a role for Pdpn in the attainment of fully elongated osteocyte dendrites.
In podoplanin conditional knockout mice (Wnt1 (show WNT1 Proteins)-Cre;PdpnDelta/Deltamice), the tooth and alveolar bone showed no morphological abnormalities and grow normally, indicating that podoplanin is not critical in the development of the tooth and bone.
Podoplanin expressed by lymphatic vessels prevents postnatal blood filling of the lymphatic vascular system and contributes to efficient dendritic cell migration to the lymph nodes.
Study provides evidence that podoplanin as a novel component of the neuronal machinery underlying neuritogenesis, synaptic plasticity, and hippocampus-dependent memory functions.
This study suggests that ppGalNAc-T13 (show GALNT13 Proteins) contributes to neuronal differentiation through glycosylating and stabilizing PDPN, which provides insights into the regulatory roles of O-glycosylation in mammalian neural development.
Data show that E11/glycoprotein 38(GP38) was up-regulated upon SEMA3A (show SEMA3A Proteins) stimulation, and cyclin-dependent kinase 6 (CDK6 (show CDK6 Proteins)) was down-regulated in a time-dependent manner.
this study uncovers a unique molecular mechanism of lymphangiogenesis in which galectin-8 (show LGALS8 Proteins)-dependent crosstalk among VEGF-C (show VEGFC Proteins), podoplanin and integrin pathways plays a key role.
A reciprocal interaction between CLEC-2 (show CLEC1B Proteins) on megakaryocytes and PDPN on Bone marrow (BM) Fibroblastic reticular cell-like cells contributes to the periarteriolar megakaryopoietic microenvironment in mouse BM.
Data indicate that a mechanism reliant upon blockade of proteasome-mediated E11 destabilization contributes to osteocytogenesis and that this may involve downstream targeting of RhoA (show RHOA Proteins).
it is likely that PDPN, while being dispensable during re-epithelialization, has a crucial role in migration and invasion of transformed keratinocytes.
These results indicated that PDPN gene plays a significant role in the proliferation and maturation of bovine Sertoli cells.
This gene encodes a type-I integral membrane glycoprotein with diverse distribution in human tissues. The physiological function of this protein may be related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor. The specific function of this protein has not been determined but it has been proposed as a marker of lung injury. Alternatively spliced transcript variants encoding different isoforms have been identified.
, PA2.26 antigen
, glycoprotein 36
, glycoprotein, 36-KD
, lung type I cell membrane associated glycoprotein
, lung type-I cell membrane-associated glycoprotein (T1A-2)
, glycoprotein 38
, transmembrane glycoprotein E11
, E11 antigen epitope
, epithelial cell surface transmembrane protein antigen
, pulmonary type I alveolar epithelial cell transmembrane differentiation marker
, type I cell 40 kDa protein
, mucin-type membrane protein gp40