• Human Podoplanin/PDPN protein (Recombinant) (C-hFc&His) (STJP000980)
  • Human Podoplanin/PDPN protein (Recombinant) (C-hFc&His) (STJP000980)
  • Human Podoplanin/PDPN protein (Recombinant) (C-hFc&His) (STJP000980)
  • Human Podoplanin/PDPN protein (Recombinant) (C-hFc&His) (STJP000980)

Human Podoplanin/PDPN protein (Recombinant) (C-hFc&His) (STJP000980)

SKU:
STJP000980

Current Stock:
Host: HEK293 cells
Reactivity: Human
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Recombinant-Human Podoplanin/PDPN-C-hFc&His protein was developed from hek293 cells and has a target region of C-hFc&His. For use in research applications.
Formulation: Lyophilized from a 0.22 Mu m filtered solution of PBS, pH 7.4. Contact us for customized product form or formulation.
Immunoreactivity: Measured by its binding ability in a functional ELISA. Immobilized Human CLEC-2 Protein at 5 Mu g/mL (100 Mu L/well) can bind Human Podoplanin with a linear range of 0.98-46 ng/mL.
Gene Symbol: PDPN
Gene ID: 10630
Uniprot ID: PDPN_HUMAN
Immunogen: Recombinant Human Podoplanin/PDPN Protein is produced by HEK293 cells expression system. The target protein is expressed with sequence (Glu97–Lys199) of human PDPN/Podoplanin (Accession #NP_006465.3) fused with an Fc, 6×His tag at the C-terminus.
Tissue Specificity 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.
Post Translational Modifications Extensively O-glycosylated. Contains sialic acid residues. O-glycosylation is necessary for platelet aggregation activity. Disialylated at Thr-52.sialic acid is critical for platelet-aggregating activity and for CLEC1B interaction. The N-terminus is blocked. Cleaved by a metalloprotease within its extracellular (EC) domain, generating a membrane-bound C-terminal fragment (PCTF33) and an extracellular fragment. The resulting membrane-bound C-terminal fragment (PCTF33) is further processed between Val-150 and Val-151 by PSEN1/gamma-secretase generating the intracellular domain of podoplanin (PICD).
Function 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. Interaction with CD9, on the contrary, attenuates platelet aggregation induced by PDPN. 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. Interaction with CD44 promotes directional cell migration in epithelial and tumor cells. 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. Through binding with LGALS8 may participate in connection of the lymphatic endothelium to the surrounding extracellular matrix. 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. 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. Required for normal lung cell proliferation and alveolus formation at birth. Does not function as a water channel or as a regulator of aquaporin-type water channels. Does not have any effect on folic acid or amino acid transport.
Protein Name Podoplanin
Aggrus
Glycoprotein 36
Gp36
Pa2.26 Antigen
T1-Alpha
T1a Cleaved Into - 29kda Cytosolic Podoplanin Intracellular Domain
Picd
Database Links Reactome: R-HSA-114604
Reactome: R-HSA-9827857
Cellular Localisation Podoplanin: Membrane
Single-Pass Type I Membrane Protein
Cell Projection
Lamellipodium Membrane
Filopodium Membrane
Microvillus Membrane
Ruffle Membrane
Membrane Raft
Apical Cell Membrane
Basolateral Cell Membrane
Invadopodium
Localized To Actin-Rich Microvilli And Plasma Membrane Projections Such As Filopodia
Lamellipodia And Ruffles
Association To The Lipid Rafts Is Required For Pdpn-Induced Epithelial To Mesenchymal Transition (Emt)
Colocalizes With Cd9 In Tetraspanin Microdomains
Localized At Invadopodium Adhesion Rings In Tumor Cell
Association To The Lipid Rafts Is Essential For Pdpn Recruitment To Invadopodia And Ecm Degradation
29kda Cytosolic Podoplanin Intracellular Domain: Cytoplasm
Cytosol
Alternative Protein Names Podoplanin protein
Aggrus protein
Glycoprotein 36 protein
Gp36 protein
Pa2.26 Antigen protein
T1-Alpha protein
T1a Cleaved Into - 29kda Cytosolic Podoplanin Intracellular Domain protein
Picd protein
PDPN protein
GP36 protein
PSEC0003 protein
PSEC0025 protein

Information sourced from Uniprot.org

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