P2X2, control peptide, 100 ug.
- Known as:
- P2X2, reference short protein sequence, 100 ug.
- Catalog number:
- P10109
- Product Quantity:
- 1
- Category:
- -
- Supplier:
- Neuromi
- Gene target:
- P2X2 control peptide 100 .
Related genes to: P2X2, control peptide, 100 ug.
- Gene:
- P2RX2 NIH gene
- Name:
- purinergic receptor P2X 2
- Previous symbol:
- DFNA41
- Synonyms:
- P2X2
- Chromosome:
- 12q24.33
- Locus Type:
- gene with protein product
- Date approved:
- 2001-03-30
- Date modifiied:
- 2016-02-05
Related products to: P2X2, control peptide, 100 ug.
Related articles to: P2X2, control peptide, 100 ug.
- Source: PubMed
- Extracellular adenosine 5'-triphosphate (ATP) activates P2X receptor channels (P2XRs) that serve important roles in the immune and nervous systems. Available structures of P2XRs in detergents reveal that ATP binding to the extracellular domain leads to severing of subunit interfaces within transmembrane regions as the pore opens. Here we report cryo-electron microscopy structures of the human P2X2R in lipid nanodiscs in an apo closed state, with ATP, Mg-ATP, and suramin bound. We find that a unique Arg residue interacts with the γ-PO of ATP in P2X2R and underlies the requirement of this subtype for ATP. Channel opening and desensitization occur when ATP binds, whereas the channel remains closed when Mg-ATP binds. A continuous belt of partially resolved lipids in the outer leaflet stabilizes the closed state, and the presence of lipids prevents the severing of subunit interfaces as the channel opens. These findings establish key mechanistic principles of gating for P2X2R in a membrane-like environment, providing a framework for future mechanistic studies and therapeutic development. - Source: PubMed
Publication date: 2026/05/27
Dhingra SurbhiMoog MaiaSwartz Kenton J - Fibromyalgia (FM) is a chronic pain syndrome characterized by central sensitization, in which glutamatergic and purinergic signaling pathways are thought to play critical roles. This study aimed to evaluate the diagnostic potential of serum glutamate ionotropic receptor N-methyl-D-aspartate type subunit 1 (GRIN1), purinergic receptor P2X 1 (P2RX1), and purinergic receptor P2Y 2 (P2RY2) levels in patients with FM. A total of 93 newly diagnosed FM patients and 93 age- and sex-matched healthy controls were included in the study. Serum levels of GRIN1, P2RX1, and P2RY2 were measured using enzyme-linked immunosorbent assay (ELISA). Receiver operating characteristic (ROC) curve analysis was performed to assess the diagnostic performance of these biomarkers. ROC analysis demonstrated good diagnostic accuracy for all three biomarkers. The area under the curve (AUC) values were 0.817 for GRIN1, 0.778 for P2RX1, and 0.842 for P2RY2 ( < 0.001 for all). At optimal cut-off values, GRIN1, P2RX1, and P2RY2 showed sensitivities of 91.4%, 78.5%, and 92.5%, and specificities of 72.00%, 75.3%, and 80.6%, respectively. Serum GRIN1, P2RX1, and P2RY2 levels exhibit strong diagnostic performance in FM and may serve as promising biomarkers reflecting altered glutamatergic and purinergic signaling in disease pathophysiology. - Source: PubMed
Publication date: 2026/03/31
Dogan Sevil CeyhanKaya Gülcihan CinarTuncbilek ZuhalAtas MertTas Ayca - The enrichment of immunosuppressive M2 macrophages, combined with diminished CD8 T cell infiltration, represents a key mechanism driving tumor progression and limiting immunotherapy efficacy in non-small cell lung cancer (NSCLC). Here, we provide evidence that the purinergic P2Y2 receptor (P2RY2) is a key regulator of M2 macrophage enrichment and contributes to the exclusion of CD8 T cells from the tumor microenvironment (TME). P2RY2 expression is significantly elevated in human NSCLC compared to non-malignant tissues and M2-like macrophages expressing P2RY2 are more prevalent in tumors with an advanced TNM (Tumor, Node, Metastasis) stage. Elevated P2RY2 mRNA levels are significantly associated with poorer overall survival in a NSCLC patients. Furthermore, we selectively inhibited P2RY2 in syngeneic or autochthonous mouse models of NSCLC driven by Kras or Egfr mutations. This resulted in a significant reduction of M2-like macrophages, enhanced CD8 T cell migration and tumor infiltration and a marked decrease in tumor burden. Similar results were evident following the genetic deletion of P2ry2, validating the impact on the TME. Importantly, macrophages are the predominant P2RY2-expressing cells within the TME. Moreover, tumor-educated macrophages (TEMs) isolated from P2ry2 tumor-bearing mice exhibited reduced proliferation compared with wild-type macrophages when co-cultured with LLC1 cells, revealing a potential mechanism underlying P2RY2-mediated pro-tumorigenic activity. Our study underscores the clinical significance of P2RY2 in NSCLC and provides evidence of its pivotal role in the regulation of M2 macrophage enrichment and the exclusion of CD8 T cells from the TME. Targeting P2RY2 may offer a novel immunotherapeutic intervention for NSCLC. - Source: PubMed
Publication date: 2026/03/24
El-Gazzar AhmedAschenbrenner BertramForsthuber AgnesKramer MarkusKargarpour ZahraMetekol SedaJohn LisaPapaporfyriou AnastasiaBereš MašaTrouvilliez SarahHomolya MonikaDöme BalázsMegyesfalvi ZsoltHorvath LillaLang ChristianHoda Mir AlirezaZeillinger RobertObermayr EvaGeleff SilvanaFrommlet FlorianLichtenberger Beate MGompelmann DanielaCasanova EmilioMoll Herwig PIdzko Marco - Activating mutations in the epidermal growth factor receptor () gene drive non-small cell lung cancer (NSCLC). Oncogenic EGFR mutants are ligand-independent and more stable, but the underlying mechanism remains unclear. We hypothesized that EGFR mutants selectively leverage cellular stabilizers to evade degradation. Genome-wide RNA interference screens identified genes (encoding for stabilizers) responsible for mutant EGFR stability, with P2Y2 receptor (P2Y2) emerging as a bona fide stabilizer. Mechanistically, high extracellular adenosine triphosphate (ATP) levels transactivate EGFR mutants via P2Y2 activation, previously shown to signal through Src kinase-dependent EGFR phosphorylation. Our study reveals that ATP-driven P2Y2 activation stabilizes EGFR mutants by forming a P2Y2-integrin β1-EGFR complex enriched in endosomes. Targeting this axis destabilizes EGFR mutants and offers a strategy against drug resistance. Elevated P2Y2 and integrin β1 expression in patients with NSCLC implies clinical relevance. Our results provide previously unidentified insight that EGFR mutants enhance extracellular ATP levels to activate P2Y2-integrin for enhanced stability of EGFR mutants to drive the oncogenic program. - Source: PubMed
Publication date: 2026/01/21
Du YafeiWang WenjingGoh Hui ChinVaiyapuri Thamil SelvanRaju AnandhkumarHsiao Yu-ChunWang Cheng ChunAgrawal VanishaMohideen Noorul FarzanaMohd Mazian Norhidayah BinteKaratekin FerideWang Wendy KehanLakshmanan ManikandanGupta KomalChang HanLe Guezennec XavierBard FredericTan Daniel S WTergaonkar VinayHung Mien-ChieLiu XiaogangHong WanjinBoopathy Gandhi T K