Use your antibodies-online credentials, if available.
Il n’y a pas de produits dans votre liste de comparaison.
Votre panier est vide.
Afficher toutes les espèces
Afficher tous les synonymes
Sélectionnez vos espèces et l'application
anti-Human Arrestin 3 Anticorps:
anti-Rat (Rattus) Arrestin 3 Anticorps:
anti-Mouse (Murine) Arrestin 3 Anticorps:
Vous arrivez à notre recherche pré-filtrée.
Human Polyclonal Arrestin 3 Primary Antibody pour ELISA, WB - ABIN185395
Lefkowitz, Shenoy: Transduction of receptor signals by beta-arrestins. dans Science (New York, N.Y.) 2005
Show all 3 Pubmed References
Human Polyclonal Arrestin 3 Primary Antibody pour IHC (p), IP - ABIN250385
Zakrzewicz, Krasteva, Wilhelm, Dietrich, Wilker, Padberg, Wygrecka, Grau: Reduced expression of arrestin beta 2 by graft monocytes during acute rejection of rat kidneys. dans Immunobiology 2011
Show all 2 Pubmed References
Human Polyclonal Arrestin 3 Primary Antibody pour ELISA, IHC - ABIN450082
Krishnamurthy, Galet, Ascoli: The association of arrestin-3 with the follitropin receptor depends on receptor activation and phosphorylation. dans Molecular and cellular endocrinology 2003
Show all 2 Pubmed References
Cow (Bovine) Polyclonal Arrestin 3 Primary Antibody pour IP, WB - ABIN152742
Chen, Rusnak, Lombroso, Sidhu: Dopamine promotes striatal neuronal apoptotic death via ERK signaling cascades. dans The European journal of neuroscience 2009
Human Polyclonal Arrestin 3 Primary Antibody pour ELISA, IF - ABIN4281708
Felemban, Dorgau, Hunt, Hallam, Zerti, Bauer, Ding, Collin, Steel, Krasnogor, Al-Aama, Lindsay, Mellough, Lako et al.: Extracellular matrix component expression in human pluripotent stem cell-derived retinal organoids recapitulates retinogenesis in vivo and reveals an important role for IMPG1 and CD44 in the ... dans Acta biomaterialia 2018
Beta-arrestin interacting with unphosphorylated ADRB2 fails to activate mitogen-activated protein kinase (MAPK) signaling and prolonged interaction of beta-arrestin with ADRB2 promoted the sorting of ADRB2 to lysosomes.
Pre-treatment with beta-arrestin2 agonists was shown to inhibit the AMPK/mTOR signaling pathway, and to inhibit autophagy by restoring the levels of beta-arrestin2 in BEAS-2B cells. These changes were reversed with the knockdown of beta-arrestin2, indicating that beta-arrestin2 suppressed autophagy through the AMPK-mTOR signaling pathway.
Extracellular alpha-synuclein induces sphingosine S1P1R uncoupled from inhibitory G-protein leaving beta-arrestin signal intact.
Results showed that significantly higher expression of betaarrestin2 was observed in colorectal cancer tissues compared with normal colon tissues.
These results show that b-arrestin1 and b-arrestin2 exert differential actions on PAC1R internalization and PAC1R-dependent ERK1/2 activation, and suggest that the two b-arrestin isoforms may be involved in fine and precise tuning of the PAC1R signaling pathways.
overexpression of beta-arrestin2 can inhibit the growth of renal cell carcinoma (RCC) cells in vitro, and beta-arrestin2 acts as a tumor suppressor gene in RCC; the main mechanism may directly suppress the phosphorylation of IkBa and indirectly suppress NFkB
Study investigated the association between five ARRB2 single nucleotide polymorphisms (SNPs): rs1045280, rs2036657, rs4790694, rs3786047 and rs452246, and response to antidepressant treatment in a sample of 569 patients with a major depressive episode treated for 6months: GG/GT patients for rs4522461 and AA/AC patients for rs4790694 had a lower response.
Itch/beta-arrestin2 complex binds SuFu and induces its Lys63-linked polyubiquitylation without affecting its stability.
These data highlight a novel arrestin-mediated modulation of CREB signalling, suggesting a reciprocal relationship between arrestin2 and arrestin3, wherein recruitment of arrestin3 restricts the ability of beta2AR to activate prolonged CREB phosphorylation by precluding recruitment of an arrestin2/Src/p38 complex.
A novel regulatory role of GRK2 was proposed for the ubiquitination of beta-arrestin in the context of the PKC-mediated heterologous regulation of GPCRs.
USP33 may indirectly regulate the degradation and recycling of CXCR4 through deubiquitinating beta-arrestin2, promoting colorectal tumor cell metastasis.
Antihistamines displayed similar kinetic signatures on antagonizing histamine-induced beta-arrestin2 recruitment as compared to displacing radioligand binding from the H1R.
the internalization motif for the human neuropeptide Y4 receptor, which regulates arrestin-3 recruitment and receptor endocytosis, was identified.
Collectively, these data show that beta-arrestin2 phosphorylation at Thr(383) underlies beta-arrestin-dependent Erk1/2 activation by G protein-coupled receptors.
Data indicate that a constitutively monomeric CXCL12 variant reproduced the G protein-dependent and beta-arrestin-dependent responses that are associated with normal CXCR4 signaling and lead to cell migration.
This work demonstrates that the expression of FSHR and LHCGR can be induced in hGL5 cells but that the FSHR-dependent cAMP/PKA pathway is constitutively silenced, possibly to protect cells from FSHR-cAMP-PKA-induced apoptosis.
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 to interact with each b-arrestin isoform, depending on the presence of the ligand and demonstrates the antagonism between the two b-arrestin isoforms in controlling IGF-1R expression and function, which could be developed into a practical anti-IGF-1R strategy for cancer therapy.
Results demonstrate that GPR3 signals at the plasma membrane and can be silenced by GRK2/beta-arrestin overexpression. These results also strongly implicate the serine and/or threonine residues in the third intracellular loop in the regulation of GPR3 activity.
EPCR occupancy recruits G-protein coupled receptor kinase 5, thereby inducing beta-arrestin-2 biased PAR1 signaling by both APC and thrombin. In
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, -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.
These data suggest that inhibition of GABAergic inhibitory postsynaptic currents by morphine involves a beta-arr2/c-Src mediated mechanism.
Knockout of Arrb2 in the infralimbic prefrontal cortex, specifically in excitatory neurons, impaired extinction learning of cocaine-conditioned place preference.
Data show that inactivation of the beta-arrestin-2 gene, barr2, in beta-cells of adult mice greatly impairs insulin release and glucose tolerance .
GPCR-arrestin complex initiates non-desensitized signalling at the plasma membrane by coupling with ion channels.
Spinal Arrb2 may serve as an intracellular gate for acute to chronic pain transition via desensitization of NMDAR.
Knockout of mice beta-arrestin2, but not beta-arrestin1, results in deficits in plasticity mediated by mGlu1 receptors in CA3 pyramidal neurons and by mGlu5 receptors in CA1 pyramidal neurons.
beta-arrestin 2 can protect liver tissue from LPS-induced injury via inhibition of TLR4/NF-kappaB signaling pathway-mediated inflammation.
Non-visual arrestins regulate the focal adhesion formation via small GTPases RhoA and Rac1 independently of G-protein-coupled receptors.
Arrb2 induces cardiomyocyte death by interacting with the p85 subunit of PI3K, and negatively regulating the formation of p85-PI3K/CaV3 survival complex, thus blocking activation of PI3K-Akt-GSK3beta cell survival signalling pathway in cardiac ischemia-reperfusion.
these results suggest that beta-arrestin2 down-regulation increases hepatocellular carcinoma cell migration and invasion ability
beta-Arrestin2 increases the Itch-mediated ubiquitylation of SuFu
Our data reveal beta-arrestin 1, beta-arrestin 2, and AT1R as key regulatory molecules in the Frank-Starling mechanism, which involves length-dependent enhancement of cardiac myofilament Ca(2+) sensitivity.
Arrestin beta2 deficiency-mediated intestinal progenitor/stem cell radioprotection relied on protracted NF-kappaB activation and subsequent suppression of PUMA induction.
GIP stimulation induces a switch in GIPR recycling from a rapid endosomal to a slow trans-Golgi network (TGN) pathway. GPCR kinases and b-arrestin2 are required for this switch in recycling.
beta-arrestin2-biased negative modulators of mGlu5 offer significant advantages over first-generation inhibitors for the treatment of fragile X and related disorders.
selective inactivation of the GPCR-associated protein beta-arrestin 2 in hepatocytes of adult mice results in greatly increased hepatic GCGR signaling, leading to striking deficits in glucose homeostasis
AT1R-beta-arrestin-2 pathway signaling plays an important role in renal fibrosis.
These data suggest that one allele of arrestin-2 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.
Arrb2 physically interacts with the beta subunit of trimeric G-proteins and Dishevelled, the interaction between arrb2 and Dishevelled 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 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