Increasing evidence suggests that RGS proteins play an integral role in G-protein signaling. To date, however, information regarding the functional roles of RGS proteins is limited primarily to in vitro biochemical assays and heterologous overexpression experiments. Thus, the role played by natively expressed RGS proteins in G-protein signaling remains unclear. A reason for this void in our knowledge is the lack of experimental tools for uncoupling endogenous RGS proteins from G-protein signaling pathways. Thus, the development of the better tools represents a major challenge for understanding the physiological roles subserved by RGS proteins. In this regard, several potential strategies are apparent. First, genetically ablating specific RGS proteins, either acutely (e.g., antisense techniques) or stably (e.g., knock-out mice), might lend insight into endogenous RGS protein functions. However, ,20 mammalian RGS proteins have been identified so far, and it is likely that even single cells contain ...
The effect of endogenous RGS proteins on receptor-mediated signaling has been studied in various systems by expressing RGS-insensitive or -sensitive Gαo (Jeong and Ikeda, 2000; Boutet-Robinet et al., 2003; Clark et al., 2003). Insensitivity of Gαo to endogenous RGS proteins increases receptor signaling to some, but not all, pathways that have been studied. In this work we have expressed RGS-insensitive and -sensitive Gαo in C6 glioma cells expressing the rat μ-opioid receptor. This allowed us to test two hypotheses, namely, that coupling of the μ-opioid receptor to Gαo can provide for adenylyl supersensitization and that RGS proteins decrease the degree of supersensitization because of their effect in shortening the lifetime of the active signaling molecule Gαo-GTP and its Gβγ counterpart. The results show the presence of active Gαo alone allows for the development of μ-opioid agonist-mediated adenylyl cyclase supersensitization and that this effect is greatly enhanced when Gαo is ...
Regulator of G-protein signaling 13 is a protein that in humans is encoded by the RGS13 gene.[5][6] RGS 13 is a member of R4 subfamily of RGS (Regulators of G Protein Signaling) proteins which have only short peptide sequences flanking the RGS domain. RGS 13 suppresses the immunoglobulin E- mediated allergic responses.[7] The protein encoded by this gene is a member of the regulator of G protein signaling (RGS) family. RGS family members share similarity with S. cerevisiae SST2 and C. elegans egl-10 proteins, which contain a characteristic conserved RGS domain. RGS proteins accelerate GTPase activity of G protein alpha-subunits, thereby driving G protein into their inactive GDP-bound form, thus negatively regulating G protein signaling. RGS proteins have been implicated in the fine tuning of a variety of cellular events in response to G protein-coupled receptor activation. The biological function of this gene, however, is unknown. Two transcript variants encoding the same isoform exist.[6] ...
Opioids are potent analgesic drugs prescribed to treat pain that ranges from moderate to severe. They have unwanted side effects, can lead to tolerance and dependence, and display addictive properties. Opioids function by acting on mu opioid receptors (MORs) located throughout the CNS. MOR is coupled to inhibitory heterotrimeric G proteins of the Gαi/o family, which have many downstream signaling effects, including inhibition of adenylyl cyclase. Regulators of G protein signaling (RGS) proteins negatively modulate this receptor-mediated G protein signaling. One of the remaining questions regarding the effects of RGS proteins on MOR signaling is which, if any, Gαi/o protein subtype serves as the site of action for RGS protein inhibition of opioid signaling. To evaluate the role of one Gα subunit, Gαo, in the effects of RGS proteins on opioid signaling, MOR-mediated biochemistry was evaluated in mice that express an RGS- insensitive (RGSi), mutant Gαo protein (Gαo -RGSi). In particular, MOR ...
The regulators of heterotrimeric guanosine triphosphate (GTP)-binding protein (G protein) signaling (RGS proteins) were named for their ability to act as GTP-activating proteins (GAPs) for G proteins and, thus, limit the signal generated by G protein-coupled receptors (GPCRs). In addition to this characteristic biochemical trait, RGS proteins constitute a large family of structurally diverse proteins with variable sequence motifs that permit additional specific interactions. RGS proteins may also serve as a bridge from GPCRs to receptor tyrosine kinases or transmembrane channels, allowing signals from GPCRs to regulate signaling through other types of receptors, and vice versa.. ...
The protein encoded by this gene is a member of the regulator of G protein signaling (RGS) family. RGS family members share similarity with S. cerevisiae SST2 and C. elegans egl-10 proteins, which contain a characteristic conserved RGS domain. RGS proteins accelerate GTPase activity of G protein alpha-subunits, thereby driving G protein into their inactive GDP-bound form, thus negatively regulating G protein signaling. RGS proteins have been implicated in the fine tuning of a variety of cellular events in response to G protein-coupled receptor activation. The biological function of this gene, however, is unknown. Two transcript variants encoding the same isoform exist. [provided by RefSeq, Jul 2008 ...
Regulator of G protein signaling (RGS) proteins accelerate GTP hydrolysis by Gα subunits and thus facilitate termination of signaling initiated by G protein-coupled receptors (GPCRs). RGS proteins hold great promise as disease intervention points, given their signature role as negative regulators of GPCRs-receptors to which the largest fraction of approved medications are currently directed. RGS proteins share a hallmark RGS domain that interacts most avidly with Gα when in its transition state for GTP hydrolysis; by binding and stabilizing switch regions I and II of Gα, RGS domain binding consequently accelerates Gα-mediated GTP hydrolysis. The human genome encodes more than three dozen RGS domain-containing proteins with varied Gα substrate specificities. To facilitate their exploitation as drug-discovery targets, we have taken a systematic structural biology approach toward cataloging the structural diversity present among RGS domains and identifying molecular determinants of their ...
We identified the transcription factor E2F8 in the course of a screen for novel activators of heterotrimeric G proteins. In S. cerevisiae, E2F8 was able to activate a G protein/MAP kinase reporter pathway; this activity was specific for particular G protein isoforms, mapped epistatically to the level of heterotrimers, and was antagonized by a GTPase-accelerating protein. The amino-terminus of the protein appeared to be most important for G protein activation. The most parsimonious interpretation of these results is that E2F8 stimulates nucleotide exchange on the α subunit of heterotrimeric G proteins. Since E2F8 did not reduce the maximal receptor-mediated signal (Figure 2), but rather caused a left-shift in the receptors dose-response curve, E2F8 does not compete with receptors for G proteins. Instead, E2F8 and receptors may be complementary to one another in their mode of action, using different molecular mechanisms to activate Gα.. G protein activation would be a novel function for an E2F ...
When membrane potential is depolarized, intracellular Ca2+ beneath the plasma membrane of cardiac myocytes increases. Ca2+ binds to CaM and Ca2+/CaM complex leads to the facilitation of RGS action to accelerate hydrolysis of GKα-GTP to GKα-GDP. GKα-GDP binds free Gβγ to form trimeric G proteins, which therefore decreases the number of free Gβγ and thus the number of available KG channels at depolarized potentials. The time-dependent increase in KG current on hyperpolarization can then be interpreted as the reflection of the reverse reactions of these events, ie, less Ca2+ influx, less Ca2+/CaM, lesser activity of RGS, and more available Gβγ.. There still remain, however, two major questions in this reaction scheme. The first one is how Ca2+/CaM facilitates RGS action. It was reported that Ca2+/CaM binds RGS but does not change its GTPase accelerating activity in vitro.14 Therefore, some mechanisms other than direct facilitating action of Ca2+/CaM on the GTPase-accelerating function of ...
Circulating free fatty acids are a reflection of the balance between lipogenesis and lipolysis that takes place mainly in adipose tissue. We found that mice deficient for regulator of G protein signaling (RGS)-4 have increased circulating catecholami
Materials. Sulfated [Thr28,Nle31]-CCK25-33 (CCK9s) was synthesized as described previously (Moroder et al., 1981). 125I-Na (2000 Ci/mmol) was from GE Healthcare (Les Ulis, France). Sulfated [Thr28,Nle31]-CCK25-33 was conjugated with Bolton-Hunter reagent, purified, and radioiodinated as described previously and is referred as 125I-CCK9s (Fourmy et al., 1989).. Site-Directed Mutagenesis and Transfection of COS-7 Cells. All mutant receptor cDNAs were constructed by oligonucleotide-directed mutagenesis (Quik Change site-directed mutagenesis kit; Stratagene, Strasbourg, France) using the human CCK2R cDNAs with HA or Myc epitope tag at the amino terminus cloned into pRFENeo vector as template. Truncated receptors at the C terminus were obtained by introducing a stop codon (TGA) at position 410 (CCK2[1-409]), 430 (CCK2[1-429]), or 440 (CCK2[1-439]). The cDNA for mouse RGS2 with an HA epitope tag at the amino terminus subcloned into pCR3.1 was a gift from Luc De Vries (Institut de Recherche Pierre ...
Signal transduction by G protein coupled receptors (GPCRs) in the cardiovascular, nervous and visual systems is the focus of our research. GPCRs are the largest and most important class of receptors in humans because they are the targets of more than half of all therapeutic agents, as well as many drugs of abuse.. Our research focuses on RGS proteins, a large family we discovered that function as novel regulators, effectors and integrators in GPCR signaling pathways. Indeed, RGS proteins have important roles in hypertension, heart failure, anxiety, schizophrenia, vision and drug addiction. Accordingly, RGS proteins provide a promising new class of drug targets.. Currently our goals are to elucidate the mechanistic and physiological functions of RGS proteins in the cardiovascular, nervous and visual systems through biochemical, cell biological, genetic and physiologic studies of knockout and transgenic mice. We are working to: 1) determine the mechanisms whereby RGS proteins participate in ...
We evidenced a differential regulation of these RGS in the lumbar spinal cord of animals undergoing SNI. In particular, RGS3 appeared upregulated at early stages after the lesion whereas expression of RGS2 and RGS4 was decreased at later stages. Decrease in RGS7 expression was already observed after 3 days and outlasted until 21 days after the lesion. In cultured astrocytes, we observed that changes in the culture conditions distinctly influenced the constitutive expression of these RGS. Also, brief exposures (4 to 8 h) to either interleukin-1β, interleukin-6, or tumor necrosis factor α caused rapid changes in the mRNA levels of the RGS, which however did not strictly recapitulate the regulations observed in the spinal cord of lesioned animals. Longer exposure (48 h) to inflammatory cytokines barely influenced RGS expression, confirming the rapid but transient regulation of these cell signaling modulators.. CONCLUSION ...
Summary is not available for the mouse gene. This summary is for the human ortholog.] Regulator of G protein signaling (RGS) family members are regulatory molecules that act as GTPase activating proteins (GAPs) for G alpha subunits of heterotrimeric G proteins. RGS proteins are able to deactivate G protein subunits of the Gi alpha, Go alpha and Gq alpha subtypes. They drive G proteins into their inactive GDP-bound forms. Regulator of G protein signaling 4 belongs to this family. All RGS proteins share a conserved 120-amino acid sequence termed the RGS domain. Regulator of G protein signaling 4 protein is 37% identical to RGS1 and 97% identical to rat Rgs4. This protein negatively regulate signaling upstream or at the level of the heterotrimeric G protein and is localized in the cytoplasm. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jul 2008 ...
Regulator of G protein signaling (RGS) family members are regulatory molecules that act as GTPase activating proteins (GAPs) for G alpha subunits of heterotrimeric G proteins. RGS proteins are able to deactivate G protein subunits of the Gi alpha, Go alpha and Gq alpha subtypes. They drive G proteins into their inactive GDP-bound forms. Regulator of G protein signaling 4 belongs to this family. All RGS proteins share a conserved 120-amino acid sequence termed the RGS domain. Regulator of G protein signaling 4 protein is 37% identical to RGS1 and 97% identical to rat Rgs4. This protein negatively regulate signaling upstream or at the level of the heterotrimeric G protein and is localized in the cytoplasm. Alternatively spliced transcript variants have been found for this gene ...
Buy our Recombinant Human RGS21 protein. Ab116158 is a full length protein produced in Escherichia coli and has been validated in SDS-PAGE. Abcam provides free…
Regulator of G protein signaling 2 (RGS2), a Gq-specific GTPase activator protein (GAP), is strongly implicated in cardiovascular function. RGS2-/- mice are hypertensive and prone to heart failure and several rare human mutations that speed RGS2 degradation have been identified in hypertensive patients. Consequently, pharmacological up-regulation of RGS2 protein levels could be beneficial. We utilized a β-galactosidase complementation method to screen several thousand compounds with known pharmacological function for those that increase RGS2 protein levels. Several cardiotonic steroids (CTS), including ouabain and digoxin increase RGS2 but not RGS4 protein levels. CTS increase RGS2 protein levels through a posttranscriptional mechanism by slowing protein degradation. RGS2 mRNA levels in primary vascular smooth muscle cells are unaffected by CTS treatment while protein levels are increased 2-3 fold. Na/K-ATPase is required for the increase in RGS2 protein levels as the effect is lost in ...
Previous studies showed that RGS4 mRNA is expressed in atrial11,12,27 and ventricular12,29 myocytes; however, its expression in the murine SAN has not been examined previously. Using 2 approaches (ie, LacZ reporter/HCN4 immunostaining colocalization and real-time RT-PCR), our results demonstrate that RGS4 is more highly expressed in SAN myocytes compared to myocytes in the RAA. Because RGS4 is known to attenuate Gαi/o but not Gαs activation, we anticipated that its loss would cause selective increases in the response to parasympathetic stimulation in the SAN. Basal HRs in conscious RGS4-deficient mice were not different from wild-type controls, potentially because of the dominant effect of sympathetic versus parasympathetic tone on HR control in mice. However, consistent with a role for RGS4 in the regulation of HR under conditions of increased parasympathetic tone, conscious RGS4-deficient mice showed enhanced bradycardic responses to CCh and anesthetized RGS4-deficient animals showed lower ...
The etiology of hypertension in most cases is idiopathic. Current dogma states that all forms of hypertension arise from renal abnormalities of sodium handling. We have hypothesized that a primary abnormality of vascular smooth muscle cell (SMC) contraction can cause hypertension. To directly test this hypothesis we created and characterized inducible, SMC-specific RGS2 knockout mice (RGS2-SMC-KO) harboring a SMC-specific deletion of the PKGIα target the GTPase activating protein Regulator of G-protein Signaling 2. In these studies, SMC-specific deletion of RGS2 was induced at 7 weeks of age and Cre-negative mice treated identically as the RGS2-SMC-KO were used as controls. Telemetric blood pressure (BP) studies in ambulatory mice demonstrated that BP was significantly higher in RGS2-SMC-KO vs. control mice (135 ± 5 vs. 122 ± 7 mmHg, respectively. P,0.01), with no change in heart rate. Ex vivo aortic rings of RGS2-SMC-KO mice were hypercontractile in response to phenylephrine (PE) (138 ± 6 ...
1996 by the National Academy of Sciences Contributed by Melvin I. Simon, September 26, 1996 Data deposition: The sequence reported in this paper has been deposited in the GenBank data base (accession no. U72881). C.-K.C. and T.W. contributed equally to this work. We thank Dr. Wolfgang Baehr for mouse retinal cDNA library and members of the Simon lab and, in particular, Bo Yu for stimulating discussion. This work was supported from the National Institute on Aging (AG 12288). T.W. is the recipient of a fellowship from the Deutsche Forschungsgemeinschaft. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact ...
Our research is centered on G proteins and G protein-coupled receptors (GPCRs). GPCRs are the target of nearly half of all pharmaceuticals, as well as light, taste, odors, hormones and neurotransmitters. Generally speaking, persistent stimulation of G proteins lead to desensitization. Familiar examples include desensitization to light, odors and chemical stimulants such as caffeine.. Receptors, G proteins, and effector MAP kinases are conserved in evolution and are even found in the simplest eukaryotes such as yeast. We have been conducting large-scale genomic and proteomic analysis in yeast to identify mutants with altered signaling and desensitization properties. These mutants are then characterized biochemically in yeast as well as in animal cells using homologous components. This approach led to the identification in yeast of a family of desensitization factors called RGS proteins (Regulator of G protein signaling). RGS proteins inactivate G proteins by accelerating their intrinsic GTPase ...
Ahlers, K. E., Stewart, A., Yang, J., Koland, J. G. & Fisher, R. A. (2017). Molecular Cloning of a Novel 69 kDa Brain-Specific Isoform of Regulator of G Protein Signaling 6 (RGS6). (Vols. 31). (1), pp. Supplement 936.9. The FASEB Journal.. Perschbacher, K. J., Sandgren, J. A., Carrillo-Saenz, L., Witcher, P. C., Pearson, N. A., Santillan, D. A., Devor, E. J., Pierce, G. L., Santillan, M. K., Fisher, R. A., Gibson-Corley, K. N. & Grobe, J. L. (2017). Reduced Placental Regulator of G-Protein Signaling-2 (RGS2) and Preeclampsia. (Vols. 31). (1), pp. Supplement 692.3. The FASEB Journal.. Fisher, R. A. (2016). A High Throughput Screening Campaign for Inhibitors of RGS6 and RGS17. (Vols. 30). pp. 1190.11. FASEB J.. Chakravarti, B., Yang, J., Luo, Z. & Ahlers, K. E. (2016). Contribution of NADPH Oxidase (Nox)-derived Reactive Oxygen Species (ROS) to Doxorubicin-induced Cardiomyopathy Mediated by Regulator of G protein Signaling 6 (RGS6). (Vols. 30). pp. 939.3. FASEB J.. Luo, Z., Ahlers, K. E., Yang, ...
Regulator of G protein signaling 14 (RGS14) is a multifunctional signaling protein primarily expressed in mouse pyramidal neurons of hippocampal area CA2 where it regulates synaptic plasticity important for learning and memory. However, very little is known about RGS14 protein expression in the primate brain. Here, we validate the specificity of a new polyclonal RGS14 antibody that recognizes not only full-length RGS14 protein in primate, but also lower molecular weight forms of RGS14 protein matching previously predicted human splice variants. These putative RGS14 variants along with full-length RGS14 are expressed in the primate striatum. By contrast, only full-length RGS14 is expressed in hippocampus, and shorter variants are completely absent in rodent brain. We report that RGS14 protein immunoreactivity is found both pre- and postsynaptically in multiple neuron populations throughout hippocampal area CA1 and CA2, caudate nucleus, putamen, globus pallidus, substantia nigra, and amygdala in ...
Results. Cones of WT mice strongly express RGS9-1. Figure 1 presents images of WT and RGS9-1 -/- retinas stained to reveal the expression of RGS9-1. As reported previously, RGS9-1 antibody ("RGS9") binds strongly in the outer segment layer [4] in WT, but not in RGS9-1 -/- retinas. Peanut-agglutinin ("PNA") staining reveals cones at approximately the same density in normal and RGS9-1 null retinas: counts of 3 sections of 2 mice of each type yielded 2.5±0.5 (mean±s.d.) cones per 20 mm (RGS9-1 -/-) and 2.7±0.2 cones per per 20 mm (WT). Given that the sections are 15 mm thick, the cone density is estimated to be about 3 cones per (20 mm x 15 mm) = 300 mm2, or 1 cone per 100 mm2. Since the density of rods in rodent retinas is about 1 per 3 mm2, cones constitute about 3% of the photoreceptors in these retinas. The superposition of the images generated with the antibody and the peanut agglutinin ("PNA") confirms the strong expression of RGS9-1 in the cones of WT mice, as found previously in bovine ...
We performed medium-throughput calcium mobilization assays of agonist-stimulated muscarinic acetylcholine and protease-activated receptors in HEK293 cells transfected with individual members of a pooled duplex siRNA library targeting all conventional human RGS transcripts. Only knockdown of RGS11 increased both carbachol-mediated calcium mobilization and inositol phosphate accumulation. Surprisingly, we found that knockdown of RGS8 and RGS9,…
G protein signaling pathways in the retina are critically involved in reception and transduction of visual stimuli. The physiological operation of these pathway...
Approach and Results-We found a robust expression of RGS5 in native arteries of C57BL/6 mice and a highly significant downregulation within neointimal lesions 10 and 21 days after vascular injury as assessed by quantitative polymerase chain reaction, immunoblotting, and immunohistochemistry. In vitro, RGS5 was found significantly downregulated after mitogenic stimulation of human coronary artery SMCs. To restore RGS5 levels, SMCs were transduced with adenoviral vectors encoding wild-type RGS5 or a nondegradable mutant. RGS5-WT and, even more prominently, the C2A-RGS5 mutant prevented SMC proliferation and migration. In contrast, the siRNA-mediated knockdown of RGS5 significantly augmented SMC proliferation. Following overexpression of RGS5, FACS analysis of propidium iodide-stained cells indicated cell cycle arrest in G0/G1 phase. Mechanistically, inhibition of ERK1/2 phosphorylation and MAPK downstream signaling was shown to be responsible for the anti-proliferative effect of RGS5. Following ...
Complete information for RGS9 gene (Protein Coding), Regulator Of G Protein Signaling 9, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for RGS5 gene (Protein Coding), Regulator Of G Protein Signaling 5, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
RGS18 - RGS18 (untagged)-Human regulator of G-protein signaling 18 (RGS18) available for purchase from OriGene - Your Gene Company.
Rgs20 - mouse gene knockout kit via CRISPR, 1 kit. |dl||dt|Kit Component:|/dt||dd|- |strong|KN314737G1|/strong|, Rgs20 gRNA vector 1 in |a href=http://www.origene.com/CRISPR-CAS9/Detail.
Kit Component:- KN314739G1, Rgs3 gRNA vector 1 in pCas-Guide vector- KN314739G2, Rgs3 gRNA vector 2 in pCas-Guide vector- KN314739D, donor vector…
On the cover: Confocal microscopy of the thymus of wild-type mice reconstituted with G184S bone marrow previously immunostained for CD3 (blue), CD4 (green), CD8 (red), and UEA1 (white). The section shown is captured from the tiled entire thymus image. Hwang, I.-Y., C. Park, K. Harrison, and J. H. Kehrl. 2017. Normal thymocyte egress, T cell trafficking, and CD4+ T cell homeostasis require interactions between RGS proteins and Gαi2. J. Immunol. 198: 2721-2734. ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Plasmid pAG146 RGS7 3UTR from Dr. David Bartels lab contains the insert N11 3UTR and is published in Science. 2005 Dec 16. 310(5755):1817-21. This plasmid is available through Addgene.
This gene encodes a member of the sorting nexin family. Members of this family have a phox (PX) phosphoinositide binding domain and are involved in intracellular trafficking. The encoded protein also contains a regulator of G protein signaling (RGS) domain. Regulator of G protein signaling family members are regulatory molecules that act as GTPase activating proteins for G alpha subunits of heterotrimeric G proteins. Alternate splicing results in transcript variants encoding distinct isoforms. [provided by RefSeq, Jul 2014] ...
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As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
left rear iginitor continues to clik when knob is off pushing on the knob may cause the clicking to stop. When the - DCS RGS-486GD Gas Kitchen Range question
ウサギ・ポリクローナル抗体 ab36561 交差種: Dog,Hu 適用: WB,IHC-P,ICC/IF…RGS2抗体一覧…画像、プロトコール、文献などWeb上の情報が満載のアブカムの Antibody 製品。国内在庫と品質保証制度も充実。
RT @_BIST: The #BISTCommunity is meeting today to share what every working group has been up to in 2017. Very informative session! @CRGenom… - 7 hours 31 min ago ...
Light stimulates rhodopsin in a retinal rod to activate the G protein transducin, which binds to phosphodiesterase (PDE), relieving PDE inhibition and decreasing guanosine 3′,5′-cyclic monophosphate (cGMP) concentration. The decrease in cGMP closes outer segment channels, producing the rod electrical response. Prolonged exposure to light decreases sensitivity and accelerates response kinetics in a process known as light adaptation, mediated at least in part by a decrease in outer segment Ca2+. Recent evidence indicates that one of the mechanisms of adaptation in mammalian rods is down-regulation of PDE. To investigate the effect of light and a possible role of rhodopsin kinase (G protein-coupled receptor kinase 1 [GRK1]) and the GRK1-regulating protein recoverin on PDE modulation, we used transgenic mice with decreased expression of GTPase-accelerating proteins (GAPs) and, consequently, a less rapid decay of the light response. This slowed decay made the effects of genetic manipulation of ...
For patients with bladder cancer, genetic variants in the regulator of G-protein signaling (RGS) pathway are associated with risk, recurrence, progression, and death.
Rgs3 - Lenti ORF clone of Rgs3 (Myc-DDK-tagged) - Mouse regulator of G-protein signaling 3 (Rgs3), transcript variant 3 available for purchase from OriGene - Your Gene Company.
Predicted to have G-protein alpha-subunit binding activity; G-protein beta-subunit binding activity; and GTPase activator activity. Involved in G protein-coupled receptor signaling pathway; regulation of G protein-coupled receptor signaling pathway; and regulation of postsynaptic membrane potential. Localizes to several cellular components, including the dendrite terminus; glutamatergic synapse; and postsynaptic membrane. Is expressed in bone; foot mesenchyme; nervous system; pelvic girdle skeleton; and sensory organ. Orthologous to human RGS7 (regulator of G protein signaling 7 ...
Enhances GTPase-activating protein (GAP) activity of regulator of G protein signaling (RGS) proteins, hence involved in the termination of the signaling initiated by the G protein coupled receptors (GPCRs) by accelerating the GTP hydrolysis on the G-alpha subunits, thereby promoting their inactivation (Probable). Increases RGS9 GTPase-activating protein (GAP) activity, hence contributes to the deactivation of G protein signaling initiated by D(2) dopamine receptors (By similarity). May play an important role in neuronal signaling, including in the parasympathetic, but not sympathetic, control of heart rate (By similarity).
Kao i kod drugih G protein-spregnutih receptora, signalizacija mi opioidnog receptora se prekida putem nekoliko različitih mehanizama. Oni su pojačani sa hroničnom upotrebom, što dovodi do rapidne tahifilaksije.[7] Najvažniji regulatorni proteini mi opioidnog receptora su β-arestini arestin beta 1 i arestin beta 2,[8][9][10] i RGS proteini RGS4, RGS9-2, RGS14 i RGSZ2.[11][12] Dugotrajna upotreba ili visoke doze opioida mogu takođe da dovedu do dodatnih mehanizama tolerancije. To obuhvata umanjenje izražavanja gena mi opioidnog receptora, tako da se broj receptora prisutnih na ćelijskoj površini smanjuje. Ovo se razlikuje od kratkotrajne desenziticije indukovane β-arestinima ili RGS proteinima.[13][14][15] Još jedna dugotrajna adaptacija na upotrebu opioida može da bude povišeno izražavanje glutamata i drugih puteva u mozgu koji mogu da imaju suprotno dejstvo opioidima, i da umanjuju efekte opioidnih lekova putem promena nizvodnih puteva, nezavisno od aktivacije mi opioidnog ...
Rabbit polyclonal antibody raised against synthetic peptide of GNAI1/GNAI2. A mixture of synthetic peptides corresponding to amino acids 345-354 of GNAI1 and 346-355 of GNAI2. (PAB9893) - Products - Abnova
RGS1 promotes leukocyte accumulation in the aortic wall during Ang II-induced vascular inflammation.Flow cytometric analysis of bead-labelled aortic leukocytes
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