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The product of P2RY2 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. Additionally we are shipping P2RY2 Antibodies (64) and P2RY2 Kits (4) and many more products for this protein.
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expression of P2Y (show P2RY1 Proteins)(2) receptor in peripheral sensory neurons that innervate the injured tissue and the activation of P2Y (show P2RY1 Proteins) 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.
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 (show RBP3 Proteins)
P2Y2 and Gq/G11 (show STK19 Proteins) are required for basal endothelial NO formation, vascular tone, and blood pressure.
The data suggest that the P2Y2/4 receptor activation elicits blood pressure responses via distinct mechanisms involving KCa3.1 (show KCNN4 Proteins) and Cx37 (show GJA4 Proteins).
P2Y2-mediated increase of cytoplasmic Ca(2 (show CA2 Proteins)+) concentration down-regulates the expression of NCC (show SLC12A3 Proteins).
P2Y2 receptors play important roles in bone marrow cell differentiation and mineralization as well as in bone cell mechanotransduction, leading to an osteopenic phenotype in P2Y2 knockout mice.
P2Y2R has a role in the skin wound-healing process in mouse models
P2Y2 receptor fails to repress IL-6 (show IL6 Proteins) expression by valve interstitial cells through Akt (show AKT1 Proteins) in calcific aortic valve disease.
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 (show FPR2 Proteins)), and ATP is turned into an activating agonist through a receptor cross-talk mechanism that involves both FPR2 (show FPR2 Proteins) 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 (show EPHB2 Proteins) and PKC (show PRRT2 Proteins) pathways are involved in the P2Y2R-mediated invasion of breast cancer cells.
P2Y2R may play an important role in cancer metastasis via modulation of the crosstalk between cancer cells and endothelial cells.
These results demonstrate that P2Y2R plays an important role in activation of the HIF-1alpha (show HIF1A Proteins)-LOX (show LOX Proteins) axis, the induction of collagen crosslinking and the recruitment of CD11b (show ITGAM Proteins)+ hematopoietic bone marrow-derived cells.
Data indicate that ATP-evoked Hoechst 33258 uptake was dependent on activation of P2Y (show P2RY1 Proteins) receptors P2Y1 (show P2RY1 Proteins) and P2Y2.
ATP increased P2Y (show P2RY1 Proteins)-mediated upregulation of MUC8 expression; however, IL-1alpha significantly decreased the extent to which ATP/P2Y (show P2RY1 Proteins) upregulated MUC8 expression.
the effect of ATP on Na+-ATPase activity could be involved in antinatriuresis induced by P2Y4 receptor (show P2RY4 Proteins) 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