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Radixin is a cytoskeletal protein that may be important in linking actin to the plasma membrane. Additionally we are shipping Radixin Kits (5) and Radixin Proteins (4) and many more products for this protein.
Showing 10 out of 111 products:
Human Monoclonal Radixin Primary Antibody for IF, ELISA - ABIN562623
Zhao, Williams, Shin, Brügger, Gillespie: Large membrane domains in hair bundles specify spatially constricted radixin activation. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2012
Show all 4 references for ABIN562623
Human Polyclonal Radixin Primary Antibody for WB - ABIN657949
Parisiadou, Xie, Cho, Lin, Gu, Long, Lobbestael, Baekelandt, Taymans, Sun, Cai: Phosphorylation of ezrin/radixin/moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2009
Show all 3 references for ABIN657949
Human Polyclonal Radixin Primary Antibody for ELISA, WB - ABIN251569
Ivetic, Florey, Deka, Haskard, Ager, Ridley: Mutagenesis of the ezrin-radixin-moesin binding domain of L-selectin tail affects shedding, microvillar positioning, and leukocyte tethering. in The Journal of biological chemistry 2004
Human Polyclonal Radixin Primary Antibody for WB - ABIN2786750
Kubo, Yoshii, Kamiyama, Tominaga, Tanaka, Sato, Yamamoto: Ezrin, Radixin, and Moesin (ERM) proteins function as pleiotropic regulators of human immunodeficiency virus type 1 infection. in Virology 2008
Human Polyclonal Radixin Primary Antibody for ELISA, WB - ABIN1535256
Wilgenbus, Milatovich, Francke, Furthmayr: Molecular cloning, cDNA sequence, and chromosomal assignment of the human radixin gene and two dispersed pseudogenes. in Genomics 1993
Phospho-Ezrin/Radixin/Moesin (ERM (show MSN Antibodies)) inhibit cell adhesion, and therefore, dephosphorylation of ERM (show ETV5 Antibodies) proteins is essential for cell adhesion.Phospho-ERM (show ETV5 Antibodies) induce formation and/or maintenance of spherical cell shape.
These studies identify Akt2 (show AKT2 Antibodies) as a critical kinase that regulates radixin phosphorylation and leads to Mrp-2 (show ABCC2 Antibodies) translocation and function.
Intracellular sphingosine kinase 2 (show SPHK2 Antibodies)-derived sphingosine-1-phosphate mediates epidermal growth factor (show EGF Antibodies)-induced ezrin-radixin-moesin (show MSN Antibodies) phosphorylation and cancer cell invasion.
High Radixin expression is associated with glioblastoma.
Ezrin (show EZR Antibodies), radixin and moesin (show MSN Antibodies) are unlikely targets for autoantibodies in demyelinating neuropathies.
Data show that silencing ezrin-radixin-moesin (ERM (show MSN Antibodies)) protein expression ablates deleted in colorectal carcinoma (show DCC Antibodies) protein (DCC (show DCC Antibodies))-protein kinase A (PKA) interaction and specifically blocks netrin-induced PKA activity and phosphorylation.
These data suggest an association between RDX polymorphisms and the clinical features of RA patients, particularly the ESR (show ESR1 Antibodies)
Radixin was identified as a target gene of miR (show MLXIP Antibodies)-196a/-196b. Elevated miR (show MLXIP Antibodies)-196a/-196b expression in GC cells led to reduced radixin protein levels and vice versa.
This study finding have implications concerning the importance of concomitant radixin upregulation in tumor progression and poor prognosis of patients with gliomas.
VIP (show Vip Antibodies) regulates CFTR (show CFTR Antibodies) membrane expression and function in Calu (show CALU Antibodies)-3 cells by increasing its interaction with NHERF1 (show SLC9A3R1 Antibodies) and P-ERM (show ETV5 Antibodies) in a VPAC1 (show VIPR1 Antibodies)- and PKCepsilon (show PRKCE Antibodies)-dependent manner.
These results indicate that radixin plays an important role in regulating P-glycoprotein localization and P-glycoprotein functional activity at the intestinal membrane.
The specific location of radixin-positive cells in the peri (show POSTN Antibodies)-infarct region and in microglia suggests a role for radixin in microglial activation after stroke.
A Pak1-PP2A-ERM signaling axis mediates F-actin rearrangement and degranulation in mast cells.
the extracellular matrix molecule VN and its neuronal receptor TLCN (show ICAM5 Antibodies) play a pivotal role in the phosphorylation of ezrin/radixin/moesin (show MSN Antibodies) proteins and the formation of phagocytic cup-like structures on neuronal dendrites
Ezrin/radixin/moesin (show MSN Antibodies) are required for the purinergic P2X7 receptor (P2X7R (show P2RX7 Antibodies))-dependent processing of the amyloid precursor protein (show APP Antibodies).
The ERM (ezrin, radixin, moesin) proteins are novel scaffolds at the level of SOS activity control, which is relevant for both normal Ras function and dysfunction known to occur in several human cancers.
Ezrin-radixin-moesin (ERM (show MSN Antibodies)) proteins are induced in activated microglia/macrophages, whereas ERM (show ETV5 Antibodies) molecules are only marginally expressed in quiescent microglia in the normal brain.
Ezrin (show EZR Antibodies), radixin, and moesin (show MSN Antibodies) are phosphorylated in response to 2-methoxyestradiol and modulate endothelial hyperpermeability.
Results show that while CD43 (show SPN Antibodies) binding to ezrin-radixin-moesin (show MSN Antibodies) proteins is crucial for S76 phosphorylation, CD43 (show SPN Antibodies) movement and regulation of T-cell migration can occur through an ERM (show ETV5 Antibodies)-independent, phosphorylation-dependent mechanism.
Radixin inactivation causes hyperbilirubinemia (likely due to a defect in the localization Multidrug resistance protein 2 (show ABCC2 Antibodies) in the bile canalicular membranes) and deafness due to progressive degeneration of cochlear stereocilia. (Review)
Radixin is a cytoskeletal protein that may be important in linking actin to the plasma membrane. It is highly similar in sequence to both ezrin and moesin. The radixin gene has been localized by fluorescence in situ hybridization to 11q23. A truncated version representing a pseudogene (RDXP2) was assigned to Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was mapped to 11p by Southern and PCR analyses. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.
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