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anti-Mouse (Murine) RIC8A Antikörper:
anti-Rat (Rattus) RIC8A Antikörper:
anti-Human RIC8A Antikörper:
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Human Polyclonal RIC8A Primary Antibody für ELISA, WB - ABIN250313
Klattenhoff, Montecino, Soto, Guzmán, Romo, García, Mellstrom, Naranjo, Hinrichs, Olate: Human brain synembryn interacts with Gsalpha and Gqalpha and is translocated to the plasma membrane in response to isoproterenol and carbachol. in Journal of cellular physiology 2003
the small molecule stabilizes a mobile C-terminal helix inside a hydrophobic crevice of NCS-1 (zeige NCS1 Antikörper) to impede Ric8a interaction.
Data indicate that Ric-8 binds to Galpha12 (zeige GNA12 Antikörper)/13 subunit, Concertina (Cta (zeige PCYT1A Antikörper)) through an interface of conserved residues.
Ric-8, which belongs to a family of guanine nucleotide-exchange factors for Galphai, regulates cortical localization of the subunits Galphai and Gbeta13F.
both receptor-dependent and receptor-independent G-protein functions are executed at the plasma membrane and require the Ric-8 protein.
Ric-8 homologue is required for asymmetric division of both NBs (zeige NLRP2 Antikörper) and pl cells.Ric-8 is necessary for membrane targeting of Galphai, Pins and Gbeta13F
New studies show that targeting of G-protein subunits to membrane requires Ric-8, pointing to possible novel roles for this protein in both receptor-dependent and independent pathways.
Data suggest that Ric-8A plays essential roles during the migration of cranial neural crest (NC) cells, possibly by regulating cell adhesion and spreading.
Genetic epistasis experiments show that activator of G protein signaling (AGS-3 (zeige GPSM1 Antikörper)) and guanine nucleotide exchange factor (zeige ARHGEF12 Antikörper) RIC-8 act during food deprivation in a mutually dependent fashion to activate G protein Galpha(o (zeige GNAO1 Antikörper)).
Data suggest a mechanism in which RIC-8 favors generation of Galpha (zeige SUCLG1 Antikörper) free from Gbetagamma and enables GPR-1/2 to mediate asymmetric cell division.
ric-8 (synembryn) paralysis can be rescued by neuronal G alpha(s (zeige GNAS Antikörper)) pathway activation.
Analysis of a ric-8 mutant suggests that it is required to maintain both the G alpha(q) vesicle priming pathway and the neuronal G alpha(s (zeige GNAS Antikörper)) pathway in a functional state.
RIC-8 directly modulates Galpha (zeige SUCLG1 Antikörper) activity and that Galpha (zeige SUCLG1 Antikörper)-GTP (zeige AK3 Antikörper) is the signaling molecule regulating spindle positioning in the early embryo
requirement toward GPA-16 is distinct from the known function of RIC-8 in enabling interaction between Galpha (zeige SUCLG1 Antikörper) proteins and GPR-1/2
found that RIC8A plays an important role in the organisation and remodelling of actin cytoskeleton and cell-extracellular matrix association
Results suggest that RIC8A has an essential role in the development of mammalian nervous system by maintaining the integrity of pial basement membrane and modulating cell division
Data show that the localization of maternally expressed RIC8 protein is highly dynamic and is dependent on the stage of folliculogenesis, oogenesis and cleavage, and imply that it may have a regulatory function in mammalian gametogenesis.
Data show that disrupting resistance to inhibitors of cholinesterase 8A (Ric-8A) expression in hematopoietic cells results in a loss of GTP-binding protein (zeige DRG1 Antikörper) alpha subunits Galphai2 (zeige GNAI2 Antikörper), Galphai3 (zeige GNAI3 Antikörper), and Galphaq (zeige GNAQ Antikörper).
The activity of RIC8A in neurons is essential for survival and its deficiency causes a severe neuromuscular phenotype.
Ric-8 proteins support G protein levels by serving as molecular chaperones that promote Galpha (zeige SUCLG1 Antikörper) subunit biosynthesis
These data indicate a dynamic interaction between GPR (zeige ALDH18A1 Antikörper) proteins, Galpha (zeige SUCLG1 Antikörper)(i1) and Ric-8A, in the cell that influences subcellular localization of the three proteins and regulates complex formation.
The results of this study revealed a novel role of Ric-8a in modulating Bergmann glia-basement membrane adhesion during foliation.
NCAM180 regulates Ric8A membrane localization and potentiates beta-adrenergic response
data suggest that Ric-8 proteins are molecular chaperones required for the initial association of nascent Galpha (zeige SUCLG1 Antikörper) subunits with cellular membranes
Human NCS-1 (zeige NCS1 Antikörper) and Ric8a reproduce the binding and maintain the structural requirements at these key positions. Drosophila Ric8a and Galphas (zeige GNAS Antikörper) regulate synapse number and neurotransmitter release, and both are functionally linked to Frq2.
Results confirmed that Ric-8A can directly bind to AGS3S but failed to facilitate Galpha (zeige SUCLG1 Antikörper)(i)-induced suppression of adenylyl cyclase, suggesting that it may not serve as a guanine exchange factor for AGS3 (zeige GPSM1 Antikörper)/Galpha (zeige SUCLG1 Antikörper)(i/o)-GDP complex in a cellular environment.
Ric-8A co-localized with Vps34 (zeige PIK3C3 Antikörper) at the midbody.
The ubiquitination of Galphai2 (zeige GNAI2 Antikörper) and Galphaq (zeige GNAQ Antikörper) is suppressed by expression of Ric-8A. The suppression likely requires Ric-8A interaction with these Galpha (zeige SUCLG1 Antikörper) proteins; the C-terminal truncation of Galphaq (zeige GNAQ Antikörper) and Galphai2 (zeige GNAI2 Antikörper) completely abrogates their interaction with Ric-8A.
RGS14 (zeige RGS14 Antikörper) can form complexes with GPCRs in cells that are dependent on Galpha (zeige SUCLG1 Antikörper)(i/o) and these RGS14 (zeige RGS14 Antikörper).Galpha (zeige SUCLG1 Antikörper)(i1).GPCR (zeige NMUR1 Antikörper) complexes may be substrates for other signaling partners such as Ric-8A
Ric-8A is critical for growth factor receptor-induced actin cytoskeletal reorganization
Ric-8A signaling leads to assembly of a cortical signaling complex that functions to orient the mitotic spindle.
Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex (By similarity). Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation.
, resistance to inhibitors of cholinesterase 8 homolog A
, resistance to inhibitors of cholinesterase 8 homolog A a
, resistance to inhibitors of cholinesterase 8 homolog A (C. elegans)
, heterotrimeric G protein guanine nucleotide exchange factor Ric-8A
, resistance to inhibitors of cholinesterase 8A
, likely ortholog of mouse synembryn
, synembryn A
, Protein Ric-8A
, resistance to inhibitors of cholinesterase 8 homolog A b