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anti-Mouse (Murine) P2RY2 Antibodies:
anti-Human P2RY2 Antibodies:
anti-Rat (Rattus) P2RY2 Antibodies:
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Human Polyclonal P2RY2 Primary Antibody for ELISA, WB - ABIN549506
Guns, Van Assche, Fransen, Robaye, Boeynaems, Bult: Endothelium-dependent relaxation evoked by ATP and UTP in the aorta of P2Y2-deficient mice. in British journal of pharmacology 2006
Show all 3 Pubmed References
Human Polyclonal P2RY2 Primary Antibody for IF (p), IHC (p) - ABIN755008
Liu, Kong, Jin, Gao, Qu, Zheng: Expression of the P2Y2 receptor in the terminal rectum of fetal rats with anorectal malformation. in International journal of clinical and experimental medicine 2015
Human Polyclonal P2RY2 Primary Antibody for IHC (p), IHC - ABIN239034
Zaika, Zhang, Shapiro: Functional role of M-type (KCNQ) K⁺ channels in adrenergic control of cardiomyocyte contraction rate by sympathetic neurons. in The Journal of physiology 2011
interfering with somatic P2Y2 signalling prevents excessive immune cell deposition in diet-induced obesity (DIO), both attenuating adipose tissue inflammation and ameliorating the metabolic phenotype.
results suggest that LPS induces unbalanced proteostasis in astrocytes by blocking P2Y2R. Finally, our findings point to the design of selective P2Y2R agonist drugs as a new therapeutic approach to treat the neuroinflammatory status.
We conclude that P2Y2 receptors on myeloid cells are important in mediating acute inflammation but are dispensable for the development of whole body insulin resistance in diet-induced obese mice
The P2Y2R enhances Ubiquitin-Proteasome System activity by increasing the subunits expression beta 5 and beta 1.
The results of this study suggest that P2Y2Rs contribute to the development of salivary gland inflammation in IL-14alphaTG mice and may also contribute to autoimmune sialadenitis in humans.
Our results clearly demonstrate the involvement of P2Y2R subtypes in the pathogenesis of fibrotic lung diseases in humans and mice and hence support the development of selective P2Y2R antagonists for the treatment of IPF.
both LRP1 and LDLR expression and agLDL uptake are regulated by P2Y2R in vascular smooth muscle cells, and agLDL uptake due to P2Y2R activation is dependent upon cytoskeletal reorganization mediated by P2Y2R binding to FLN-A
knockdown of P2Y2R retarded cyst expansion in vitro and prevented ATP- and HIF-1alpha-dependent cyst growth. In conclusion, P2Y2R mediates ATP-dependent cyst growth and is transcriptionally regulated by HIF-1alpha.
P2Y2R is an inhibitor of arterial intimal calcification, regulating the osteoblastic trans-differentiation of smooth muscle cells through P2Y2R-mediated Runx2 antagonism.
These findings are consistent with the notion that the primary action of P2Y2 receptor signalling in bone is to regulate extracellular ATP levels.
Results demonstrate that P2Y2 contributes to response properties of cutaneous afferents, as P2Y2 deletion reduces responsiveness of conventional unmyelinated polymodal afferents to heat and appears to result in the acquisition of mechanical responsiveness in a subset of TRPV1-expressing afferents.
This study suggests that P2Y2 may participate in cardiomyopathy in mdx mice.
Extracellular ATP induces vascular inflammation and atherosclerosis via activation of P2Y2.
Endothelial cell-specific P2Y2R deficiency reduces atherosclerotic burden and promotes plaque stability in ApoE(-/-) mice through impaired macrophage infiltration acting together with reduced matrix metalloproteinase-2 activity and increased smooth muscle cell migration.
Calcium-mediated purinergic receptors regulate the migration and phagocytic ability of microglia during post-natal brain development.
expression of P2Y(2) receptor in peripheral sensory neurons that innervate the injured tissue and the activation of P2Y receptors contributes to mechanical allodynia following inflammation
In P2Y1R (-/-) mice, the expression of P2Y2 receptor in muscle was reduced by over 50 %, as compared to P2Y1R (+/+) mice.
gene deficiency restricted to hematopoietic tissues results in longer survivak after GvHD
P2Y2R deficiency does not alter baseline collateral vessel formation but does significantly impair collateral maturation, with resultant persistent limb ischemia despite enhanced angiogenesis.
P2Y2-/- mice are less susceptible to mount an autoimmune response against IRBP
Signal crosstalk between purinergic receptor P2Y2 (P2Y2R) and bradykinin B2 receptor (B2R) occurs in lipid rafts.
Study demonstrates that radiotherapy-resistant breast cancer cells, particularly RT-R-MDA-MB-231 cells, release higher levels of ATP than do breast cancer cells, and extracellular ATP promotes invasion and tumor growth through the activation of P2Y2R.
Study demonstrated that the P2Y2 receptor was highly expressed in MCF7 and Hs578T breast cancer cells and indicated that the P2Y2 receptor promoted cell migration and invasion in breast cancer cells via EMT-related genes Snail and E-cadherin.
Proliferation and migration of functionally impaired cardiac progenitor cells are enhanced by P2Y2R-mediated YAP activation, revealing a novel link between extracellular nucleotides released during injury/stress and Hippo signaling-a central regulator of cardiac regeneration.
nterleukin-8 release after purinergic stimulation in ALI-cultured HEECs is mediated through P2Y2 receptor activation.
Human umbilical vein endothelial cells exposed to either P2Y2 receptor antagonists or siRNA showed impaired fluid shear stress-induced cell alignment, and actin stress fiber formation as early as 6 h.
There is increased expression of P2Y2 receptors in the rectosigmoid mucosa of diarrhea-predominant irritable bowel syndrome patients. P2Y2 correlated with abdominal pain.
A novel SNP-systemic lupus erythematosus association was identified between FCHSD2 and P2RY2, peaking at rs11235667 on a 33-kb haplotype upstream of ATG16L2.
Hypoxia and upregulated HIF-1a both upregulated the P2Y2 levels in hepatocellular carcinoma cells and increased their survival.
Results show that purinergic receptor P2Y2 (P2Y2R) requires N-glycosylation for expression on the cell surface.
Data indicate that knockdown of caveolin-1 (Cav-1) expression causes redistribution of the P2Y2 nucleotide receptor (P2Y2R) from membrane rafts.
The P2RY2 receptor induces carcinoma cell migration and epithelial-mesenchymal transition through cross-talk with EGFR.
Activation of P2Y2R increased TF promoter activity and mRNA expression in coronary artery endothelial cells.
Data show that the purinergic receptor P2Y2 (P2Y2R) pepducin activates neutrophils through formyl peptide receptor 2 (FPR2), and ATP is turned into an activating agonist through a receptor cross-talk mechanism that involves both FPR2 and P2Y2R.
P2Y2 receptor and EGFR cooperate to promote prostate cancer cell invasion via ERK1/2 pathway.
These results indicate that B2R couples with P2Y2R and that these G-protein-coupled receptors act together to fine-tune cellular responsiveness.
These results suggest that over-activated ERK and PKC pathways are involved in the P2Y2R-mediated invasion of breast cancer cells.
P2Y2 and Gq/G11 are required for basal endothelial NO formation, vascular tone, and blood pressure.
P2Y2R may play an important role in cancer metastasis via modulation of the crosstalk between cancer cells and endothelial cells.
the effect of ATP on Na+-ATPase activity could be involved in antinatriuresis induced by P2Y4 receptor or a mechanism to counterbalance the natriuretic effect of P2Y2 receptor, promoting fine control of sodium reabsorption in proximal tubule cells.
The product of this gene belongs to the family of P2 receptors, which is activated by extracellular nucleotides and subdivided into P2X ligand-gated ion channels and P2Y G-protein coupled receptors. This family has several receptor subtypes with different pharmacological selectivity, which overlaps in some cases, for various adenosine and uridine nucleotides. This receptor, found on many cell types, is activated by ATP and UTP and is reported to be overexpressed on some cancer cell types. It is involved in many cellular functions, such as proliferation, apoptosis and inflammation. Three transcript variants encoding the same protein have been identified for this gene.
P2Y purinoceptor 2
, ATP receptor
, P2U purinoceptor 1
, P2U nucleotide receptor
, P2U receptor 1
, purinergic receptor P2Y2
, purinoceptor P2Y2
, P2Y ATP receptor 2
, P2Y2 nucleotide receptor