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Validated All-in-One™ qPCR Primer for PXN(NM_002859.3) Search again
Product ID:
HQP054886
(click here to view gene annotation page)
Species:
Human
Symbol:
Alias:
-
Gene Description:
paxillin
Target Gene Accession:
NM_002859.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Gene References into function
- Binding of Paxillin to the alpha 9 Integrin Cytoplasmic Domain Inhibits Cell Spreading.
- expression in conventional renal cell carcinomas (RCCs), papillary RCCs, chromophobe RCCs, collecting duct carcinomas, oncocytomas; role in signal transductions as a focal adhesion between tumor cells and the ECM in tumors with collecting duct phenotypes
- Tyrosine phosphorylation of PXN regulates localization and downstream signaling with profound effects on cell movement.
- Binding of cytoskeletal paxillin to the C-terminal of Pyk2 in cultured human umbilical vein endothelial cells is phosphorylation-independent and is not affected by acute exposure to thrombin.
- Amino acid substitutions at relevant serine residues in urokinase prevents paxillin redistribution in MCF-7 cells.
- Paxillin binding to the alpha 4 integrin tail is required for both efficient communication between integrins alpha 4 beta 1 and alpha L beta 2 and for direct integrin alpha 4 beta 1-dependent T cell migration.
- Integrin alpha 4 beta 1-dependent T cell migration requires both phosphorylation and dephosphorylation of the alpha 4 cytoplasmic domain to regulate the reversible binding of this protein.
- phosphorylation of paxillin by JNK seems essential for maintaining the labile adhesions required for rapid cell migration
- interaction of bcl-2 with paxillin plays an important role during nephrogenesis
- Data show that phosphorylation of paxillin is involved in NGF-induced neurite extension of PC-12 cells, probably through regulating focal adhesion organization.
- RhoA/Rho-kinase pathway followed by tyrosine phosphorylation of FAK and paxillin leads to ATP release and actin reorganization in vascular endothelium
- Lysophosphatidic acid induces Rho activation and consequent tyrosine phosphorylation of paxillin in human corneal epithelial cellss. Likely contributes to promotion of corneal epithelial migration by this agent.
- early spreading responses to HGF may partly relate to increased paxillin availability for incorporation into, and turnover within, dynamic cytoskeletal/membrane complexes whose rapid and transient adhesion to the matrix drives migration.
- chemoattractant stimulation induces paxillin association with alpha4 integrins, particularly in leukocytes
- paxillin tyrosine 31 and 118 phosphorylation controls polarization and motility of lymphoid cells and is PMA-sensitive
- Myocilin impaired focal adhesion formation and specifically blocked the incorporation of paxillin, but not vinculin, into focal adhesions.
- Angiotensin II mediates an increase in focal adhesion kinase and paxillin phosphorylation and induces human umbilical vein endothelial cells migration through signal transduction pathways
- Expression of paxillin and syndecan-1 in hepatocellular carcinoma(HCC) may affect its invasive and metastatic ability. May be converse correlation between expression of paxillin and syndecan-1 protein in HCC.
- Caco-2 migration on collagen IV is regulated by both p130cas and paxillin but Src phosphorylation of p130cas is more important for this process
- overexpression of paxillin synergistically contribute to the high metastatic potential of human osteosarcoma through the hyperphosphorylation of paxillin
- p130Cas and paxillin function as effectors of GD3-mediated signaling, leading to such malignant properties as rapid cell growth and invasion in melanoma cells
- proteomic analysis of paxillin post-translational modifications and interacting proteins by mass spectrometry
- Alpha4beta1-dependent adhesion strengthening under mechanical strain is regulated by paxillin association with the alpha4-cytoplasmic domain
- Metastasizing squamous cancer cell adhesiveness may be increased by paxillin-overexpression or by paxillin activation by extracellular pressure during surgical manipulation or growth within a constraining compartment.
- Our results indicate that Src maintains fibronectin matrix at the cell surface through its effect on integrin activity and paxillin phosphorylation.
- Hic-5 and paxillin function as negative feedback regulators of Src family kinases in aggregated platelets
- study reports paxillin is phosphorylated in response to fibronectin-bound group A Streptococcus that express either M1 or PrtF1/SfbI protein; integrin-linked kinase activity is indispensable for M1-induced paxillin recruitment and phosphorylation
- analysis of paxillin and ponsin interaction in nascent costameres of muscle cells
- OxPAPC promoted novel interactions between focal adhesion and adherens junction complexes via paxillin and beta-catenin association, which was critically dependent on Rac and Cdc42 activities.
- These findings support a novel role for RACK1 as a key regulator of cell migration and adhesion dynamics through the regulation of Src activity, and the modulation of paxillin phosphorylation at early adhesions.
- Invadopodia ring expansion is controlled by paxillin phosphorylations on tyrosine 31 and 118, which allows invadopodia disassembly.
- Focal adhesion kinase as well as p130Cas and paxillin should be a crucial molecule undergoing stronger tyrosine phosphorylation in GD3-expressing melanoma cells.
- These results establish an important role for paxillin in lung cancer.
- Tissue factor pathway inhibitor prevented paxillin/focal adhesion kinase phosphorylation in endothelial cells to influence angiogenesis.
- No correlation occurs with clinocopathological parameters of esophageal squamous cell carcinoma,nor is paxilcillin an effective prognositic marker in these patients.
- Data show that genetic upregulation of matriptase-2 reduces the aggressiveness of prostate cancer cells in vitro and in vivo and affects FAK and paxillin localisation.
- the alpha-parvin CH2-paxillin LD1 complex has a role in for focal adhesion assembly
- analysis of PAFR activation and pleiotropic effects on tyrosine phospho-EGFR/Src/FAK/paxillin in ovarian cancer
- These data show a dual role of paxillin in the HGF- and VEGF-mediated endothelial barrier regulation and suggest essential paxillin role in the modulation of Rac-Rho crosstalk.
- PAK1-specific paxillin phosphorylation at Ser(273) is critically involved in the positive-feedback regulation of the Rac-PAK1 pathway.
- These results suggest that phosphorylation of paxillin on Ser 178 by JNK is required for the association of paxillin with FAK, and subsequent tyrosine phosphorylation of paxillin.
- paxillin is a critical downstream effector of Rac1 that may be involved in PMA-stimulated migration presumably by modulating the integrity of focal complex formation.
- analysis of JNK-mediated phosphorylation of paxillin in adhesion assembly and tension-induced cell death by the adenovirus death factor E4orf4
- An unusual degree of binding degeneracy in the paxillin/alpha-parvin system that may facilitate the assembly of dynamic signaling complexes in the cell.
- Expression of nuclear-localized paxillin LIM domains stimulate DNA synthesis and cell proliferation
- PGE2 greatly induced hepatocellular carcinoma cell adhesion, migration, and invasion by activating FAK/paxillin/Erk pathway.
- Data show that CXCL8 stimulation leads to paxillin phosphorylation in normal neutrophils, and that both CXCL8 receptors (CXCR1 and CXCR2) mediate CXCL8-induced paxillin phosphorylation.
