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Validated All-in-One™ qPCR Primer for P2RX4(NM_002560.2) Search again
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:
Summary
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 have been identified for this gene although their full-length natures have not been determined. [provided by RefSeq].
Gene References into function
- Results show that P2X4 and P2X6 receptors are associated with VE-cadherin at HUVEC adherens junctions.
- shear stress stimulates pulmonary artery endothelial cells to release ATP, which activates Ca2+ influx via P2X4 receptors.
- We have identified a distinct subpopulation of P2X4-positive macrophages infiltrating the dystrophic fibres. These cells were absent from normal muscle and rarely present in the dystrophic muscle taken before and after the onset of degeneration.
- Increased contractility likely underlies survival benefit from P2X4 receptor overexpression.
- in human parotid acinar cells, in addition to modulation of Ca(2+) release, Ca(2+) influx through P2X(4)R may constitute a further locus for the synergistic effects of Ca(2+) and PKA activation.
- wild-type desensitization properties requires an aromatic moiety at position 374 and an amino rather than a guanidino group at position 373
- P2X4 receptor-specific residues contribute to the ivermectin effects on channel deactivation
- Main role for P2X(4) receptor in nucleotide-induced apoptosis in human mesangial cells, indicating a relevant role for purinergic signaling in regulating death rate in these cells.
- This review discusses the need to reinterpret the assumed "go-it alone" function of the P2X7 receptor in light of convincing biochemical and electrophysiological evidence for the existence of P2X4/P2X7 heteromeric receptors.
- support a common site of ATP action at P2X receptors and suggest that non-conserved residues also play a regulatory role in agonist action
- analysis of molecular shape, architecture, and size of P2X4 receptors
- INF-gamma selectively increases P2X4-receptor gene expression, leading to an up-regulation of purinergic signaling in vascular endothelial cells.
