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anti-Mouse (Murine) GNB1 Antibodies:
anti-Human GNB1 Antibodies:
anti-Rat (Rattus) GNB1 Antibodies:
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Cow (Bovine) Polyclonal GNB1 Primary Antibody for WB - ABIN2785813
Ueda, Nagae, Kozawa, Morishita, Kimura, Nagase, Ohara, Yoshida, Asano: Heterotrimeric G protein betagamma subunits stimulate FLJ00018, a guanine nucleotide exchange factor for Rac1 and Cdc42. in The Journal of biological chemistry 2008
Human Polyclonal GNB1 Primary Antibody for FACS, WB - ABIN651226
Ahmed, Daulat, Meunier, Angers: G protein betagamma subunits regulate cell adhesion through Rap1a and its effector Radil. in The Journal of biological chemistry 2010
Show all 4 Pubmed References
Human Polyclonal GNB1 Primary Antibody for WB - ABIN4890642
Stockton, Gomes, Liu, Moraje, Hipólito, Jones, Maayan, Morón, Li, Devi: Morphine Regulated Synaptic Networks Revealed by Integrated Proteomics and Network Analysis. in Molecular & cellular proteomics : MCP 2015
Data, including data from studies using transgenic/knockout mice, suggest that Ppp1ca (show PPP1CA Antibodies) and Gnb1 interact in quiescent platelets; then, Ppp1ca (show PPP1CA Antibodies) and Plcb3 (show PLCB3 Antibodies) interact during platelet aggregation; thus, Gnb1 enlists Ppp1ca (show PPP1CA Antibodies) to modulate G protein-coupled receptor (show GPR34 Antibodies) signaling. (Ppp1ca (show PPP1CA Antibodies) = protein phosphatase 1 (show PPP1CB Antibodies), catalytic subunit alpha; Gnb1 = guanine nucleotide-binding protein (show TRIM23 Antibodies), subunit beta-1; Plcb3 (show PLCB3 Antibodies) = phospholipase C (show PLC Antibodies), subunit beta-3)
It was concluded that GIRK2 (show KCNJ6 Antibodies), through its dual responsiveness to G protein beta (show GNB3 Antibodies)-gamma and Na+, mediates a form of neuronal inhibition that is amplifiable in the setting of excess electrical activity.
During corticogenesis, a cilium-transduced, noncanonical IGF-1R (show IGF1R Antibodies)-Gbetagamma-phospho(T94)Tctex-1 (show DYNLT1 Antibodies) signaling pathway promotes the proliferation of neural progenitors through modulation of ciliary resorption and G1 length.
ectopically expressed cTalpha (show PCYT1A Antibodies) 1) forms a heterotrimeric complex with rod Gbeta (show SUCLG2 Antibodies)(1)gamma(1), and substitutes equally for rTalpha in generating photoresponses initiated by either rhodopsin (show RHO Antibodies) or S-cone opsin (show RHO Antibodies)
Results suggest a model in which the Gbetagamma dimer that is released as a result of the dissociation from Galpha(o (show GNAO1 Antibodies)) upon activation of mGluR6 (show GRM6 Antibodies) closes the TRPM1 (show TRPM1 Antibodies) channel, perhaps via a direct interaction.
WDR26 (show WDR26 Antibodies) is a novel Gbetagamma-binding protein that is required for the efficacy of Gbetagamma signaling and leukocyte migration
Our data suggest that the G-protein beta(1)gamma(2) dimer may play an important regulatory role in skeletal muscle excitation-contraction coupling.
G protein subunits beta1 and beta2 have different roles in neutrophil function, as revealed by gene expression silencing in primary mouse neutrophils
G betagamma binds HDAC5 (show HDAC5 Antibodies) and inhibits its transcriptional co-repression activity
G protein betagamma subunits stimulate type V and VI adenylyl cyclases
Through analysis of the genomic and proteomic profiles of resistant cells, we identified an acquired mutation in the GNB1 gene, K89M, as the most likely cause of the resistance
Germline De Novo Mutations in GNB1 Cause Severe Neurodevelopmental Disability, Hypotonia, and Seizures.
we demonstrate a pathogenic role of de novo and autosomal dominant mutations in GNB1 as a cause of Global developmental delay and provide insights how perturbation in heterotrimeric G protein function contributes to the disease
PhLP1 binding stabilizes the Gbeta (show SUCLG2 Antibodies) fold, disrupting interactions with CCT (show FLVCR2 Antibodies) and releasing a PhLP1-Gbeta (show SUCLG2 Antibodies) dimer for assembly with Ggamma.
GNB1 and GNB2 alterations confer transformed and resistance phenotypes across a range of human tumors and may be targetable with inhibitors of G protein signaling.
Data indicate that endogenous mTOR (show FRAP1 Antibodies) interacts with Gbetagamma.
GNB1 plays an important role in the mTOR (show FRAP1 Antibodies)-related anti-apoptosis pathway and can potentially be targeted in the treatment of human breast cancer.
Findings suggest a wide-ranging mechanism by which direct interaction of Gbetagamma with specific chromatin bound transcription factors regulates functional gene networks in response to GPCR (show NMUR1 Antibodies) activation in cells including the angiotensin II type 1 receptor (show AGTR1 Antibodies).
This study provided evidence that GNB1 gene polymorphisms are related to rapid virological response in HCV-1 and HCV-2 (show BMPER Antibodies) infected patients. GNB1 may play an important role in activating the antiviral response prior to treatment.
Gbeta1gamma2-mediated epithelial sodium channel (ENaC (show SCNN1A Antibodies)) inhibition involves activation of phospholipase C-beta (show PLCb4 Antibodies) and its enzymatic products that induce protein kinase C (show PKC Antibodies) and ERK1/2 (show MAPK1/3 Antibodies) signaling pathways.
Data suggest that a hetero-multimer complex forms between light-activated rhodopsin (show RHO Antibodies) and light-activated heterotrimeric transducin (show GNAT1 Antibodies) (T-alpha-1, Gnb1, Gngt1 (show GNGT1 Antibodies)); the stoichiometry is 1:1 rhodopsin:transducin. The complex appears to form on native rod outer segment membranes upon light activation.
The PIP2-induced orientation of the GRK2 (show ADRBK1 Antibodies)-Gbeta1gamma2 complex is therefore most likely caused by specific interactions between PIP2 and the GRK2 (show ADRBK1 Antibodies) PH domain.
determined the crystallographic structure of GRK2 in complex with G protein beta1gamma2 subunits
conclude that GNB1 constitutes over 99% of the GNbeta expressed in bovine rod outer segments and displays structural heterogeneity that is due to post-translational modification, some of which is due to phosphorylation of GNB1.
Heterotrimeric guanine nucleotide-binding proteins (G proteins), which integrate signals between receptors and effector proteins, are composed of an alpha, a beta, and a gamma subunit. These subunits are encoded by families of related genes. This gene encodes a beta subunit. Beta subunits are important regulators of alpha subunits, as well as of certain signal transduction receptors and effectors. This gene uses alternative polyadenylation signals.
guanine nucleotide binding protein, beta 1
, guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
, transducin beta chain 1
, G protein, beta-1 subunit
, beta subunit, signal-transducing proteins GS/GI
, guanine nucleotide-binding protein G(I)/G(S)/G(T) beta subunit 1
, Guanine nucleotide-binding protein beta 1
, guanine nucleotide binding protein (G protein), beta 1
, guanine nucleotide-binding protein, beta-1 subunit
, rod transducin
, beta 1 subunit of heterotrimeric GTP-binding protein