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anti-Mouse (Murine) P2RX4 Antibodies:
anti-Rat (Rattus) P2RX4 Antibodies:
anti-Human P2RX4 Antibodies:
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Human Polyclonal P2RX4 Primary Antibody for ELISA, WB - ABIN314244
Yeung, Kharidia, Brown, Górecki: Enhanced expression of the P2X4 receptor in Duchenne muscular dystrophy correlates with macrophage invasion. in Neurobiology of disease 2004
Show all 2 Pubmed References
Human Polyclonal P2RX4 Primary Antibody for ELISA, WB - ABIN334455
Yuan, Zhu, Zhou, Chen, Zhu, Ma, He, Tian, Shi: Role of mast cell activation in inducing microglial cells to release neurotrophin. in Journal of neuroscience research 2010
Show all 3 Pubmed References
Human Polyclonal P2RX4 Primary Antibody for FACS, WB - ABIN518564
Bornø, Ploug, Bune, Rosenmeier, Thaning: Purinergic receptors expressed in human skeletal muscle fibres. in Purinergic signalling 2012
Human Polyclonal P2RX4 Primary Antibody for ELISA, WB - ABIN4342619
Freeman, Bowman, Zetter: Regenerative protein thymosin beta-4 is a novel regulator of purinergic signaling. in FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2011
Study demonstrates that microglia-derived ATP differentially modulates synaptic transmission and short-term plasticity at hippocampal mossy fibre synapses by acting, respectively, on presynaptic P2X4 receptors and on adenosine A1 receptors after conversion of extracellular ATP to adenosine.
These data support that P2X7 (show P2RX7 Antibodies) and P2X4 receptor activation has a protective effect during severe Escherichia coli infection.
This study provides a molecular mechanism for lysosomal ATP transport mediated by SLC17A9 (show SLC17A9 Antibodies) and also suggests a regulatory mechanism of lysosomal P2X4 by SLC17A9 (show SLC17A9 Antibodies)
IRF5 (show IRF5 Antibodies) expression in microglia is regulated by IRF8 (show IRF8 Antibodies). IRF5 (show IRF5 Antibodies) directly upregulates P2rX4 expression on microglia in peripheral nerve injury, and may play a role in neuropathic pain.
Specific localization of the P2X4 receptor subunit was evaluated in mouse, rat and cat retinae using fluorescence immunohistochemistry and pre-embedding immuno-electron microscopy
P2X4 receptors contribute to ethanol intake and indicate that there is a complex interaction between P2X4 receptors and ethanol.
Loss of P2X4 expression is associated with exaggerated renal fibrosis following unilateral ureteric obstruction.
There is a protective role for endogenous cardiac myocyte P2X4R in heart failure. It is demonstrated in a physical interaction between the myocyte receptor and eNOS (show NOS3 Antibodies).
Our previous and current findings, combined with our preliminary evidence of increased ethanol consumption in P2X4R knockout mice, suggest that the ethanol and IVM action pocket in P2X4Rs formed by positions 42, 46, 331, and 336.
The hippocampus was partially protected from status epilepticus-induced neuronal death in P2X4R-deficient mice compared with wild-type animals.
the intersubunit physical couplings among the DF and two lower body domains fostered by the LF domain at the open state act as an integrated structural element that is stringently required for the channel gating of P2X4 receptors.
These findings provide new insights in understanding the contribution of the salt bridge between Asp (show ASIP Antibodies)-85 and Arg-309 and its structurally coupled beta2,3-sheet to the function of P2X4 receptors.
The results suggest a role of PrP(C (show PRNP Antibodies)) in proteostasis, dysfunctions of which may be involved in the pathogenesis of neurodegenerative diseases such as TSE and Alzheimer's Disease.
Fndings support role for P2X7 (show P2RX7 Antibodies) and P2X4 coupled to induction of inflammatory molecules in modulating high glucose and palmitate-induced endothelial cell activation and dysfunction.
These data suggest that vascular smooth muscle cells from human gastro-omental arteries express P2X1 (show P2RX1 Antibodies) and P2X4 receptor subunits
This study demonstrates a major physiological finding that the shear-induced effects on endothelial KLF2 (show KLF2 Antibodies) axis are in part dependent on ATP release and P2X4, a previously unidentified mechanism.
Using pHluorin, P2X4 was found to be expressed on the plasma membrane and within subcellular compartments in hippocampus.
It appears to mediate the cells' response to extracellular ATP. Although Ca2thorn influx via P2X1 receptor is necessary for alpha-synuclein accumulation.
P2X4 and calmodulin form a complex at endolysosomal membrane where P2X4 activation recruits calmodulin to promote fusion and vacuolation in a Ca(2 (show CA2 Antibodies)+)-dependent fashion.
the lysosome-localized P2X4 may play specific roles in membrane trafficking of acidic organelles in mammalian cells.
The renal epithelial Na channel is stimulated by P2Xreceptor activation; the stimulation is dependent on increases in intracellular Ca(2 (show CA2 Antibodies)) and phosphatidylinositol 3-kinase activation.
A point mutation in ectodomain-transmembrane 2 of P2X4 receptor significantly reduces ethanol's inhibitory effects.
ATP-recognition of P2X4 receptors
a property that is essential for purinergic sensory signaling. Apo (show C9orf3 Antibodies) and ATP-bound X-ray structures of the detergent-solubilized zebrafish P2X4 receptor provide a blueprint for receptor mechanisms
crystal structure of the zebrafish P2X4 receptor in complex with ATP and a new structure of the apo (show C9orf3 Antibodies) receptor
Cloning and characterization of zebrafish P2X4 and P2X5 (show P2RX5 Antibodies).
Comparison of the acid-sensing ion channel (show ACCN2 Antibodies) structure with the ATP-gated P2X(4) receptor reveals similarity in pore architecture and aqueous vestibules
The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel with high calcium permeability. The main pharmacological distinction between the members of the purinoceptor family is the relative sensitivity to the antagonists suramin and PPADS. The product of this gene has the lowest sensitivity for these antagonists. Multiple alternatively spliced transcript variants, some protein-coding and some not protein-coding, have been found for this gene.
purinergic receptor P2X4
, purinergic receptor P2X, ligand-gated ion channel, 4
, p2X purinoceptor 4-like
, ATP receptor
, P2X purinoceptor 4
, ionotropic purinergic receptor
, ATP-gated cation channel protein
, P2X receptor, subunit 4
, purinoceptor P2X4
, P2X4 purinoceptor
, ATP-gated ion channel subunit P2X4