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Validated All-in-One™ qPCR Primer for P2RX7(NM_002562.5) Search again
Product ID:
HQP012100
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
P2X7
Gene Description:
purinergic receptor P2X 7
Target Gene Accession:
NM_002562.5(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:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel and is responsible for ATP-dependent lysis of macrophages through the formation of membrane pores permeable to large molecules. Activation of this nuclear receptor by ATP in the cytoplasm may be a mechanism by which cellular activity can be coupled to changes in gene expression. Multiple alternatively spliced variants which would encode different isoforms have been identified although some fit nonsense-mediated decay (NMD) criteria. [provided by RefSeq].
Gene References into function
- First description of the expression of functional P2X7 receptors in a subpopulation of osteoblasts, activation of which can result in ATP-mediated apoptosis.
- K193 and K311 are essential residues in ATP binding in the hP2X(7)R.
- loss-of-function polymorphic mutation has anti-apoptotic effect, resulting in increase in B-cell numbers in CLL (chronic lymphocytic leukemia)
- signaling through P2X7 receptor in human T cells involves p56lck, MAP kinases, and transcription factors AP-1 and NF-kappa B
- The data show that monocyte-derived DC express the P2X7 receptor whose activation opens a cation-selective channel, and which leads to rapid and near complete shedding of CD23
- a loss-of-function polymorphism within the P2X(7) receptor: Ile-568 is critical to the trafficking domain, which is between residues 551 and 581.
- detection of nonfunctional receptors in HEK293 cells and B-lymphocytes
- P2X7R activation signals distinct, novel plasma membrane blebbing events (dependent on RhoA activation and Rho-effector kinase activity) and simultaneously initiates release of IL-1 beta.
- Different purinergic receptors have different functional roles in human epidermis with P2Y1 and P2Y2 receptors controlling proliferation, while P2X5 and P2X7 receptors control early differentiation, terminal differentiation and death of keratinocytes.
- The data presented are supportive of a model wherein residues Arg578 and Lys579 within the distal C-terminal lipid interaction domain of P2X7 are required for normal trafficking of the receptor as well as ligand binding and channel gating.
- Blockade of the pore-forming P2X7 receptor inhibits formation of multinucleated human osteoclasts in vitro.
- Non-melanoma skin cancers express functional purinergic receptors and that P2X7 receptor agonists significantly reduce cell numbers in vitro.
- the influenceof P2X7 genotype on susceptibility to chronic lymphocytic leukaemia or clinical outcome is small
- A single nucleotide polymorphism (1513A-->C) in the P2X7 gene allows survival of mycobacteria within infected host cells.
- Activation of P2X(7) ionotropic receptors is necessary and sufficient to increase 2-arabinoylglycerol production in microglial cells.
- ATP-induced release of IL-1 beta is slower in monocytes from subjects homozygous for the Glu496Ala loss-of-function polymorphism in the P2X7 receptor, and this reduced rate of IL-1 beta release is associated with a lower ATP-induced potassium ion efflux.
- Our data do not support a role of the P2X7 genotype as a prognostic marker in B-cell CLL.
- P2X7 alleles modulate LPS-stimulated cytokine production, and may serve as an amplification loop of innate immunity.
- Arg(307) polymorphism abolishes the binding of ATP to the extracellular domain of P2X7.
- Fibroblasts from type 2 diabetes patients are characterized by a hyperactive purinergic loop based either on a higher level of ATP release or on increased P2X7 reactivity.
- the reversible permeabilization of erythrocytes by extracellular ATP is mediated by the P2X7 receptor
- signaling via the P2X7R may modulate the astrocytic response to inflammation in the human central nervous system.
- investigated P2X7 expression in 11 human hematopoietic cell lines, representing different lineages, as well as bone marrow mononuclear cells (BMMC) samples from 87 leukemia and 10 myelodysplastic syndrome (MDS) patients
- P2X7/Ca2+ influx is modulated by estrogen in human ectocervical epithelial cells
- A mechanism for P2X(7) receptor action, where activation involves a GRK-3-, beta-arrestin-2-, and dynamin-dependent internalization of the receptor into clathrin domains, followed in part by receptor degradation and recycling into the plasma membrane.
- the P2X(7) receptor, via regulation of mature IL-1beta production, plays a common upstream transductional role in the development of pain of neuropathic and inflammatory origin.
- the ability of P2X(7) polymorphisms to regulate the LPS-induced TNF-alpha to IL-10 ratio
- A 5' intronic splice site polymorphism leads to a null allele of P2X7.
- We report the identification of seven variants of human P2X7 which result from alternative splicing.
- Current mapping suggests that murine P2RX7 receptor gene lies within lupus susceptibility locus SLEB4; P2RX7 receptor gene encodes a product with functional characteristics consistent with a role in systemic lupus erythematosus.
- activation of the P2X7 ATP receptor elevates mitochondrial calcium and potential, increases cellular ATP levels, and promotes serum-independent growth
- novel regulation of P2X7R outward and inward permeability to large molecules by Cl-(o) and Na+(o), respectively
- The effect of polymorphisms in the P2X7 gene on the capacity of macrophages to kill mycobacteria is reported.
- increased ATP-dependent activation of the P2X(7) 489T mutant with respect to the wild type receptor
- findings have shown, for the first time, that functional P2X7 receptors are present in human melanomas and that their activation causes a decrease in cell number by apoptosis
- Human Langerhans cells express functional P2X7 receptors, which play a role in the skin immune system.
- P2X7 has a role in preventing apoptosis of human primary osteoclasts
- P2X7 with a Thr357 to Ser polymorphism has absent or reduced function and impaired ATP-induced mycobacterial killing by macrophages
- neuroblastoma cells seem to have molded P2X(7) function to their advantage in two ways (i.e., by silencing P2X(7) proapoptotic activity and by coupling P2X(7) stimulation to release of locally acting trophic factors)
- a novel role for P2X(7) as a pro-inflammatory receptor involved in rapid MMP-9 release and leukocyte recruitment.
- a novel P2X7 variant has apoptosis-inhibitory actions; the truncated variant has a the ability to antagonize its full-length counterpart through hetero-oligomerization
- The strongest association was observed in bipolar families at the non-synonymous SNP P2RX7-E13A, which results from an over-transmission of the mutant G-allele to affected offspring.
- shedding of CD21 and CD62L is mediated via the P2X7R.
- P2RX7 polymorphism might play a causal role in the development of depression.
- Single amino acid differences between species can account for large changes in agonist effectiveness and differentiate between the two widely used agonists at P2X7 receptors.
- pannexin-1 is required for processing of caspase-1 and release of mature IL-1beta induced by P2X(7) receptor activation.
- There is an association between expression of pro-apoptotic P2X(7) receptor and glomerulonephritis in rodent models, and in one form of human glomerulonephritis, the underlying relationship and its functional significance remain to be explored.
- in polarized epithelial cells under steady-state conditions the P2X7-R is located in the apical membrane, and activation of the receptor induces formation of P2X7-R pores preferentially in the apical membrane
- analysis of expression of a truncated naturally occurring variant of the human purinergic receptor P2X7 (P2X7-R) in human cancer cervical cells
- Our results indicate a possible role for novel PKC isoforms in the regulation of P2X(7)-mediated PLD activity.
- a novel mechanism of IL-1beta release from activated microglia (brain macrophages) that occurred independently of P2X(7) ATP receptor activation
- a prominent association found between severity of panic- and agoraphobia symptoms and an exonic SNP (rs3817190) in the CaMKKb gene and a trend for association with an exonic SNP in P2RX7 (rs1718119) with severity scores in the panic- and agoraphobia scal
- The analysed intragenetic variants of the P2X(7) receptor may not be a susceptibility factor for CD.
- P2X(7) activation by extracellular ATP can induce phosphatidylserine exposure in erythrocytes.
- monocyte-derived human dendritic cells stimulated with a P2X7 receptor (P2X7R) agonist undergo a large release of microparticles containing the membrane-bound form of tissue factor
- Levels of P2X(7) protein and mRNA were significantly lower in vivo, in tissues of complex hyperplasia with atypia or endometrial adenocarcinoma, than in tissues of normal endometrium, simple hyperplasia or complex hyperplasia tissues.
- Human transfected P2X(7) receptor-induced depolarization and associated pottassium efflux may reduce sodium occupancy of the regulatory sodium binding site.
- The A1513C polymorphism in the P2X7R gene is related to the occurrence of infections and survival after allogeneic stem cell transplantation.
- P2X7 Glu496Ala and the Ile568Asn single nucleotide polymorphisms are associated with 10-year fracture risk in postmenopausal women and response to hormone replacement therapy treatment.
- 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.
- Our results indicate that ADP-ribosylation of R125 positions this common chemical framework to fit into the nucleotide-binding site of P2X7 and thereby gates the channel.
- An enhanced P2X(7)R function might be a feature of human thyroid cancer.
- A significant up-regulation of P2X(7) receptor expression on mononuclear cells was observed after overnight incubation with ATP without any significant differences between rheumatoid arthritis patients and normals.
- Describe negative modulators of P2X-7 receptor.
- a novel P2X7 purinoceptor inflammatory pathway may be involved in the release of interleukin-1 beta, which may be linked to the onset of labor.
- ROS-mediated activation of the ASK1-p38 MAPK pathway downstream of P2X(7) receptor is required for ATP-induced apoptosis in macrophages.
- Analysis of the P2X(7) receptor gene in the Russian Slavic population showed that the 1513C allele is a possible risk factor for clinical TB, whereas the -762 P2RX7 polymorphism did not appear to be associated with human susceptibility to TB
- Signaling via NADPH oxidase activity is fundamental for the processing of mature IL-1 beta induced in monocytes by ATP receptor P2X7R and caspase-1 activation.
- human RA type B synoviocytes, express the P2X7 receptor which may modulate IL-6 release but not inducing changes in cell membrane permeability.
- Explored the pharmacological action of compounds known to block gap junctions on Panx1 channels activated by the P2X(7)R and the mechanisms involved in the interaction between these two proteins.
- the P2X7 carboxyl tail is a regulatory module of P2X7 receptor channel activity
- increased expression of miR-186 and miR-150 in cancer epithelial cells decreases P2X7 mRNA by activation of miR-186 and miR-150 instability target sites located at the 3'-UTR-P2X7
- P2X(7) is involved in the proliferative cell response to LL-37 and that the structural/aggregational properties of LL-37 determine its capacity to modulate the activation state of P2X(7).
- There is significant evidence of association between the single nucleotide polymorphism rs591874 in the first intron of the P2X7 gene and blood pressure.
- Analysis of P2X7 showed that the 1513A-->C and -762T-->C polymorphisms did not appear to be associated with the susceptibility of the Chinese Han population to tuberculosis.
- PIP(2) as a critical regulator of the function of the extracellular ligand-gated P2X receptor/channels and provide a novel way to control ATP-mediated cell death.
- a segment composed of residues from part of the M2 domain and part of the putative TM2 segment of P2X(7)R may be partially folded in a beta-sheet conformation: may play an important role in channel/pore formation associated with P2X7R activation
- P2X7 is a cation channel expressed by leukocytes and airway epithelial cells that is important to pathogen control and concomitant cellular inflammation