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anti-Human P2RX4 Antikörper:
anti-Mouse (Murine) P2RX4 Antikörper:
anti-Rat (Rattus) P2RX4 Antikörper:
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Human Polyclonal P2RX4 Primary Antibody für 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
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Human Polyclonal P2RX4 Primary Antibody für 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
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Human Polyclonal P2RX4 Primary Antibody für 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 für 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
Authors conclude that P2X4 receptor expression was significant in the presence of HCV HCC. This may confirms the potential role of P2X4 receptor in the presence of virus in liver pathology.
Three single nucleotide polymorphisms (SNPs) within P2X4R and two SNPs within CAMKK2 influenced concentrations of TNFalpha in peripheral blood mononuclear cells, but these SNP did not associate with risk for HIV-associated sensory neuropathy in South Africans.
the data reveals a role for P2X4 in determining the duration of ATP-evoked Ca(2+) responses and CXCL5 secretion in human primary macrophage.
the data provides evidence that P2X4 is functionally expressed in THP-1 differentiated macrophages as reflected from their contribution towards ATP-evoked Ca2+ response, but their functional evidence in THP-1 monocyte is lacking.
Our study nominates rare genetic variants in P2RX4 and P2RX7 as major genetic contributors to disease, further supporting a role for these purinergic receptors in MS and the disruption of transmembrane cation channels leading to impairment of phagocytosis as the pathological mechanisms of disease
Overexpressing P2X4Rs on microglia are a central player in evoking neuropathic pain. (review)
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-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) 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 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 and P2X4 receptor subunits
This study demonstrates a major physiological finding that the shear-induced effects on endothelial KLF2 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+)-dependent fashion.
the lysosome-localized P2X4 may play specific roles in membrane trafficking of acidic organelles in mammalian cells.
P2X4 assembles with P2X7 and pannexin-1 in gingival epithelial cells and modulates ATP-induced reactive oxygen species production and inflammasome activation during P. gingivalis infection.
Data indicate that MgATP2- activates P2X1 and P2X3, but not P2X2 and P2X4 receptors.
Results suggest that ATP-P2X4 signaling mediates high glucose-induced activation of the NLRP3 inflammasome.
These findings highlight Rab5 GTPase as a key regulator of P2X4 receptor cell surface expression and internalisation
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
Specific deletion of P2X4 receptors in sensory neurons markedly decreases behavioral and primary afferent mechanical sensitivity, thus positioning keratinocyte-released ATP to sensory neuron P2X4 signaling as a critical component of baseline mammalian tactile sensation.
Study shows that P2X4R deletion protects against stroke acutely but predisposes to depression-like behavior chronically after stroke.
the newly developed P2X4R antagonist NP-1815-PX produces anti-allodynic effects in chronic pain models without altering acute pain sensitivity, suggesting that microglial P2X4R could be an attractive target for treating chronic pain.
Data found that P2RX4, which is abundantly expressed in vascular endothelial cells, is required for ischemic tolerance following middle artery occlusion in mice, and demonstrate a novel mechanism whereby vascular endothelial cells are involved in ischemic tolerance.
P2RX4-signaling contributes to allergen induces airway inflammation pathogenesis by regulating dendritic cell mediated Th2 cell priming via modulating IL-1ss secretion.
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 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 and also suggests a regulatory mechanism of lysosomal P2X4 by SLC17A9
The results suggested that ATPP2X4R signaling may not only contribute to airway inflammation, but it may also contribute to airway remodeling in allergic asthma in mice.
IRF5 expression in microglia is regulated by IRF8. IRF5 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.
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.
findings highlight a putative role of P2X4Rs in the regulation of perceptual and sociocommunicative functions.
The hippocampus was partially protected from status epilepticus-induced neuronal death in P2X4R-deficient mice compared with wild-type animals.
Data suggest that P2X4 is expressed in majority of myenteric neurons, contributes to membrane currents activated by ATP, and plays important role in cell signaling as subunit of purinergic P2X receptor/channel.
co-expression of P2X4 receptor with P2X7 receptor in dendritic cells leads to enhancement of inflammation through facilitation of P2X7-dependent release of pro-inflammatory cytokines.
Our NMR analyses also revealed that the transmembrane region adopts the open conformation in the state bound to the inhibitor trinitrophenyl-ATP, and thus the antagonism is due to the closure of ion pathways, except for the pore in the transmembrane region: i.e., the lateral cation access in the extracellular region.
ATP-recognition of P2X4 receptors
a property that is essential for purinergic sensory signaling. Apo 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 receptor
These computational studies produced the first complete model, supported by experimental data, for how ATP binding triggers activation of a P2X receptor.
Cloning and characterization of zebrafish P2X4 and P2X5.
Comparison of the acid-sensing ion channel structure with the ATP-gated P2X(4) receptor reveals similarity in pore architecture and aqueous vestibules
crystal structures of the zebrafish P2X(4) receptor in its closed, resting state
The renal epithelial Na channel is stimulated by P2Xreceptor activation; the stimulation is dependent on increases in intracellular Ca(2) and phosphatidylinositol 3-kinase activation.
A point mutation in ectodomain-transmembrane 2 of P2X4 receptor significantly reduces ethanol's inhibitory effects.
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.
, ATP-gated cation channel protein
, P2X purinoceptor 4
, P2X receptor, subunit 4
, purinergic receptor P2X4
, purinoceptor P2X4
, P2X4 purinoceptor
, purinergic receptor P2X, ligand-gated ion channel, 4
, p2X purinoceptor 4-like
, ionotropic purinergic receptor
, ATP-gated ion channel subunit P2X4
, purinergic receptor P2X4 subunit variant 1
, purinergic receptor P2X4 subunit variant 2
, purinergic receptor P2X4b