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AB87357

Recombinant Human Podoplanin protein

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Recombinant Human Podoplanin protein is a Human Fragment protein, in the 99 to 207 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.

View Alternative Names

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

1 Images
SDS-PAGE - Recombinant Human Podoplanin protein (AB87357)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Podoplanin protein (AB87357)

3ug by SDS-PAGE under reducing condition and visualized by coomassie blue stain.

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q86YL7

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 0.58% Sodium chloride, 0.242% Tris

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMASTGQPEDDTETTGLEGGVAMPGAEDDVVTPGTSEDRYKSGLTTLVATSVNSVTGIRIEDLPTSESTVHAQEQSPSATASNVATSHSTEKVDGDTQTTVEKDGLSTVTL","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":207,"aminoAcidStart":99,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q86YL7","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Podoplanin also known as gp36 and PDPN is a small transmembrane protein weighing approximately 36 kDa. It mainly expresses in lymphatic endothelial cells podocytes and various other tissues like the lung and kidney. It functions as a marker in mesothelial cells and is noticeable in histochemical studies such as mesothelioma using podoplanin staining in immunohistochemistry (IHC). Podoplanin emerges as an important tool in identifying lymphatic vessels and has significant roles in the development of certain tissues.
Biological function summary

The protein participates in maintaining the integrity of cell structures and lymphangiogenesis. This protein does not form part of a larger complex but actively interacts with different molecules. In lymphoid tissues podoplanin contributes to the proper formation of lymphatic channels and assists in platelet aggregation. These actions are pivotal in wound healing and protecting the epithelial cell layers in multiple organs.

Pathways

Podoplanin impacts the platelet activation pathway and the Lymphatic Vessel Development pathway. Its interaction with CLEC-2 (C-type lectin-like receptor 2) triggers downstream signaling leading to changes in platelet morphology and actin cytoskeleton reorganization. Podoplanin’s activation of these pathways links it to key processes that include cell migration and tissue homeostasis TGF-beta interaction also represents a significant relationship within these pathways.

Podoplanin has correlations with conditions like cancer specifically mesothelioma and squamous cell carcinoma. Dysregulation of podoplanin and its pathways may contribute to tumor progression and metastasis. In mesothelioma podoplanin interacts with other proteins like E-cadherin influencing cancer cell migration and adhesion. Its role in disease states highlights the importance of podoplanin IHC as a diagnostic tool aiding in the better understanding and identification of disease pathology.

Specifications

Form

Liquid

Additional notes

ab87357 is purified using conventional chromatography techniques.

General info

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 (PubMed : 14522983, PubMed : 15231832, PubMed : 17222411, PubMed : 17616532, PubMed : 18215137). 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 directional 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 in 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).

Sequence similarities

Belongs to the podoplanin family.

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 (PubMed:17222411, PubMed:25458834).. 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).

Product protocols

Target data

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 : 17222411, PubMed : 17616532, PubMed : 18215137). 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 directional 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 in 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).
See full target information PDPN

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