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Rat (Rattus) Arrestin 3 ELISA Kit for Sandwich ELISA - ABIN810989
Oda, Tadokoro, Takase, Kanahara, Watanabe, Shirayama, Hashimoto, Iyo: G protein-coupled receptor kinase 6/?-arrestin 2 system in a rat model of dopamine supersensitivity psychosis. in Journal of psychopharmacology (Oxford, England) 2015
Lowering the level of cellular FLNA caused an elevation in RalA activity and resulted in selective interference with the normal intracellular trafficking and signaling of D3R through beta-arrestins.
This study reveals contrasting abilities of IGF-1R (show IGF1R ELISA Kits) to interact with each b-arrestin (show SAG ELISA Kits) isoform, depending on the presence of the ligand and demonstrates the antagonism between the two b-arrestin (show SAG ELISA Kits) isoforms in controlling IGF-1R (show IGF1R ELISA Kits) expression and function, which could be developed into a practical anti-IGF-1R (show IGF1R ELISA Kits) strategy for cancer therapy.
Results demonstrate that GPR3 (show GPR3 ELISA Kits) signals at the plasma membrane and can be silenced by GRK2 (show ADRBK1 ELISA Kits)/beta-arrestin overexpression. These results also strongly implicate the serine and/or threonine residues in the third intracellular loop in the regulation of GPR3 (show GPR3 ELISA Kits) activity.
EPCR (show PROCR ELISA Kits) occupancy recruits G-protein coupled receptor kinase 5 (show GRK5 ELISA Kits), thereby inducing beta-arrestin-2 biased PAR1 (show MARK2 ELISA Kits) signaling by both APC (show APC ELISA Kits) and thrombin (show F2 ELISA Kits). In
CCR5 is highly expressed in active inflammatory bowel disease, and it has positive correlation with lymphocyte grade and negative correlation with expression of beta-arrestin2.
Data suggest that PAR4 (show PAWR ELISA Kits) and P2Y12 (show P2RY12 ELISA Kits) heterodimer internalization/endocytosis is required for beta-arrestin-2 recruitment to endosomes and up-regulation of Akt (show AKT1 ELISA Kits) signaling; activation of PAR4 (show PAWR ELISA Kits) but not of P2Y12 (show P2RY12 ELISA Kits) drives internalization of the PAR4 (show PAWR ELISA Kits)-P2Y12 (show P2RY12 ELISA Kits) heterodimer. (PAR4 (show PAWR ELISA Kits) = protease-activated receptor 4 (show F2RL3 ELISA Kits); P2Y12 (show P2RY12 ELISA Kits) = purinergic receptor P2Y (show P2RY1 ELISA Kits), G-protein coupled, 12 protein; Akt (show AKT1 ELISA Kits) = proto-oncogene (show RAB1A ELISA Kits) protein c (show PROC ELISA Kits)-akt (show AKT1 ELISA Kits))
Analyzing the functional relevance of individual sites using phosphosite-deficient receptor mutants we found phosphorylation of the ADRB1 (show ADRB1 ELISA Kits) at Ser461/Ser462 in the distal part of the C-terminus to determine beta-arrestin2 recruitment and receptor internalization
Heterodimerization of the kappa opioid receptor (show OPRK1 ELISA Kits) and neurotensin receptor 1 contributes to a novel beta-arrestin-2-signaling pathway.
These results were consistent with those seen for beta2-AR. Thus, both beta-arrs negatively control AM1 receptor internalization, which depends on the C-tail of CLR (show DCLK3 ELISA Kits).
The downregulation of beta-arrestins 1/2 in saphenous vein endothelial cells (SVECs) prevented the shear stress-induced rise in levels of phosphorylation of Akt (show AKT1 ELISA Kits) and endothelial nitric oxide synthase (eNOS (show NOS3 ELISA Kits), Serine 1177).
The fraction of arrestin2 molecules found in clusters larger than 100nm correlates with the magnitude of ligand-induced CCR5 internalization.
K2A mutations in arrestin-1 (show SAG ELISA Kits), -2, and -3 significantly reduced their binding to active phosphorhodopsin.
Results reveal that multiple intramolecular interactions coordinately regulate arrestin2 interaction with clathrin, highlighting this interaction as a critical step in regulating receptor trafficking.
selective inactivation of the GPCR (show GPBAR1 ELISA Kits)-associated protein beta-arrestin 2 in hepatocytes of adult mice results in greatly increased hepatic GCGR (show GCGR ELISA Kits) signaling, leading to striking deficits in glucose homeostasis
AT1R (show AGTRAP ELISA Kits)-beta-arrestin-2 pathway signaling plays an important role in renal fibrosis.
These data suggest that one allele of arrestin-2 (show ARRB1 ELISA Kits) is unable to support normal locomotor behavior due to signaling and/or developmental defects.
Beta-arrestin-2 with beta-arrestin-1 shared common mechanisms to suppress podocyte autophagy by negative regulation of ATG12-ATG5 conjugation.
[beta]-arrestin2 regulates intestinal mucosal inflammation under both homeostatic and colitic conditions. Its mode of action involves negative regulation of T-cell activation and its requirement for induction of regulatory T cells.
Results suggest that the antipruritic effects of kappa opioid receptor (show OPRK1 ELISA Kits) agonists may not require betaarrestin2
that pro- and anti-inflammatory activities of beta-arrestin2 are determined by beta-arrestin2 ubiquitination and that changes in USP20 (show USP20 ELISA Kits) expression and/or activity can therefore regulate inflammatory responses
This shows that mood stabilizers lamotrigine, lithium and valproate can exert behavioral effects in mice by disrupting the beta-arrestin 2-mediated regulation of Akt (show AKT1 ELISA Kits)/GSK3 (show GSK3b ELISA Kits) signaling by D2 dopamine receptors.
findings show for the first time that Ang II (show AGT ELISA Kits) receptor signaling to beta-arrestin regulates ARF6 (show ARF6 ELISA Kits) activation. These proteins together control receptor endocytosis and ultimately cell migration.
These results reveal that the protective effect of deficiency of Arrb2 is due to loss of negative regulation of Akt (show AKT1 ELISA Kits).
Arrb2 physically interacts with the beta subunit (show POLG ELISA Kits) of trimeric G-proteins and Dishevelled (show DVL2 ELISA Kits), the interaction between arrb2 and Dishevelled (show DVL2 ELISA Kits) is promoted by the beta/gamma subunits of trimeric G-proteins.
results suggest that a functional interaction between beta-arrestin 2 and Smoothened may be critical to regulate hedgehog (show SHH ELISA Kits) signaling in zebrafish development
Members of arrestin/beta-arrestin protein family are thought to participate in agonist-mediated desensitization of G-protein-coupled receptors and cause specific dampening of cellular responses to stimuli such as hormones, neurotransmitters, or sensory signals. Arrestin beta 2, like arrestin beta 1, was shown to inhibit beta-adrenergic receptor function in vitro. It is expressed at high levels in the central nervous system and may play a role in the regulation of synaptic receptors. Besides the brain, a cDNA for arrestin beta 2 was isolated from thyroid gland, and thus it may also be involved in hormone-specific desensitization of TSH receptors. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.
arrestin beta 2
, arrestin, beta 2
, arrestin 2
, beta-Arrestin 2
, arrestin beta-2
, arrestin 3
, beta arr2
, beta-arrestin 2