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RGS7BP encodes a protein that binds to all members of the R7 subfamily of regulators of G protein signaling and regulates their translocation between the nucleus and the plasma membrane. Additionally we are shipping and many more products for this protein.
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The results of this study indicated that R7bp is a key regulator of itch sensation and suggest the potential targeting of R7bp-dependent GTPase activating protein activity as a novel therapeutic strategy for pathological itch
R7-binding protein had a strong inhibitory effect on homo-oligomerization of RGS7.
R7BP-dependent regulation of R7-RGS proteins shapes specific aspects of light-evoked and spontaneous activity of retinal ganglion cells in mature and developing retina.
GIRK modulation occurs by channel assembly with R7-RGS/Gbeta5 complexes under allosteric control of R7 RGS-binding protein (R7BP).
R7BP is a negative modulator of the analgesic and locomotor activating actions of morphine that contributes to the development of morphine tolerance.
regulator of G-protein signalling 7 binding protein contributes significantly to the nuclear localization of endogenous G beta(5)/R7-RGS complex in brain
These results indicate that dopamine signaling in the striatum is controlled by concerted interplay between two RGS proteins, RGS7 and RGS9-2, which are balanced by a common subunit, R7BP.
All four R7 RGS proteins co-precipitate with R7BP from brain extracts and recombinant R7 proteins bind recombinant R7BP with high efficiency
Review. R7BP transduces signals directly from receptors and G proteins at the plasma membrane to the nucleus, and this plasma membrane-nuclear shuttling is controlled by reversible palmitoylation of R7BP.
R7BP controls expression of regulator of G-protein signaling (RGS)9-2 expression at the posttranslational level.
R7-Gbeta5-R7BP complexes in the mouse could regulate signaling by modulatory Gi/o-coupled GPCRs in the developing and adult nervous systems.
Delivery of RGS7/Gbeta5 to dendrites of ON-bipolar cells occurs independently of its association with R7BP. These findings provide a new mechanism for adapter-independent targeting of RGS/Gbeta5 complexes.
Gbeta5 and R7BP in striatum undergo remodeling upon changes in neuronal activity.
Data (including data from studies using transgenic mice) suggest that R7BP-RGS7 heterotrimers interact with Galpha13 to augment signaling pathways in neurons that regulate neurite morphogenesis. (R7BP = RGS7 family binding protein; RGS7 = regulator of G-protein signaling 7 protein; Galpha13 = GTP-binding protein alpha subunit 13)
BL3-ht2 of RGS7BP may be an important genetic variant associated with AERD. The haplotype of block 3 may play a protective role against aspirin hypersensitivity in asthma, perhaps by altering the responsiveness of muscarinic receptors.
cytoplasmic RGS7*Gbeta5*R7BP heterotrimers and RGS7*Gbeta5 heterodimers are equivalently inefficient regulators of G protein-coupled receptor signaling relative to plasma membrane-bound heterotrimers bearing palmitoylated R7BP.
the successful purification of functionally intact Gbeta5-free recombinant RGS11 was reported that differentially interact with R7BP and Galpha(oa).
This gene encodes a protein that binds to all members of the R7 subfamily of regulators of G protein signaling and regulates their translocation between the nucleus and the plasma membrane. The encoded protein could be regulated by reversible palmitoylation, which anchors it to the plasma membrane. Depalmitoylation localizes the protein to the nucleus. Polymorphisms in this gene may be associated with risk of aspirin-exacerbated respiratory disease. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
R7 binding protein
, R7 family-binding protein
, regulator of G-protein signaling 7-binding protein
, R7 family-binding protein A
, regulator of G-protein signaling 7-binding protein A