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>   首页   >   产品   >   一抗   >   心血管   >   Podoplanin / GP36 / T1A-2 Antibody (N-term)   

Podoplanin / GP36 / T1A-2 Antibody (N-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - Podoplanin / GP36 / T1A-2 Antibody (N-term) AP2016b
    Western blot analysis of anti-T1A-2 Pab (Cat. #AP2016b) in NCI-H460 cell lysate. T1A-2 (Arrow) was detected using purified Pab. Secondary HRP-anti-rabbit was used for signal visualization with chemiluminescence.
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession Q86YL7
Other Accession NP_006465
Reactivity Human
Host Rabbit
Clonality Polyclonal
Isotype Rabbit Ig
Calculated MW 16698 Da
Additional info
Gene ID 10630
Other Names Podoplanin, Aggrus, Glycoprotein 36, Gp36, PA226 antigen, T1-alpha, T1A, PDPN {ECO:0000312|EMBL:AAH146682}
Target/Specificity This Podoplanin / GP36 / T1A-2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 33-63 amino acids from the N-terminal region of human Podoplanin / GP36 / T1A-2.
Dilution WB~~1:1000
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsPodoplanin / GP36 / T1A-2 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name PDPN {ECO:0000312|EMBL:AAH14668.2}
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: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 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 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).
Cellular Location Podoplanin: Membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q62011}. Cell projection, lamellipodium membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q62011}. Cell projection, filopodium membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q62011}. Cell projection, microvillus membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q62011}. Cell projection, ruffle membrane; Single- pass type I membrane protein {ECO:0000250|UniProtKB:Q62011} Membrane raft. Apical cell membrane. Basolateral cell membrane. Cell projection, invadopodium. Note=Localized to actin-rich microvilli and plasma membrane projections such as filopodia, lamellipodia and ruffles (By similarity). Association to the lipid rafts is required for PDPN-induced epithelial to mesenchymal transition (EMT) (PubMed:21376833). Colocalizes with CD9 in tetraspanin microdomains (PubMed:18541721). Localized at invadopodium adhesion rings in tumor cell. Association to the lipid rafts is essential for PDPN recruitment to invadopodia and ECM degradation (PubMed:25486435). {ECO:0000250|UniProtKB:Q62011, ECO:0000269|PubMed:18541721, ECO:0000269|PubMed:21376833, ECO:0000269|PubMed:25486435}
Tissue Location 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 Areas

BACKGROUND

T1A-2 is 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.

REFERENCES

Kato, Y., et al., J. Biol. Chem. 278(51):51599-51605 (2003).
Ma, T., et al., Am. J. Respir. Cell Mol. Biol. 19(1):143-149 (1998).
Zimmer, G., et al., Biochem. J. 341 (Pt 2), 277-284 (1999).

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