glosensor tm reagent Search Results


90
Promega glosensor tm camp reagent
a , b The receptor–α5 interface in zGPR4 6.5 . Interacting residues are shown as sticks and are labeled. c , d Mutagenesis analysis of residues in zGPR4 ( c ) and hGPR4 ( d ) on the potency of G protein-coupling by the <t>GloSensor</t> cAMP assay. The maximum and minimum activation levels of WT GPR4 were set to 100 and 0%, respectively. The ΔpH 50 was calculated by dividing the potency (pH 50 ) of the mutant by the pH 50 of WT. Data are shown as means ± SEM from at least three independent experiments performed in triplicate. Source data are provided as a Source Data file.
Glosensor Tm Camp Reagent, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/glosensor tm camp reagent/product/Promega
Average 90 stars, based on 1 article reviews
glosensor tm camp reagent - by Bioz Stars, 2026-04
90/100 stars
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90
Promega glosensor tm reagent
Effects of OT on inhibition of intracellular cAMP production induced by each KOR agonist in HEK293 cells stably coexpressing human KOR and <t>Glosensor</t> 22F protein. The cells were pretreated with 10 −6 M U50488 ( A ), 10 −6 dynorphin A ( B ), or 10 −5 M of morphine ( C ) in the absence and presence of 10 −6 M OT for 10 min and treated with forskolin (3 µM). The data are presented in terms of mean ± SEM values (( A ); n = 3, ( B ); n = 3, ( C ); n = 3). Two-way ANOVA was performed, followed by Bonferroni’s test, *** p < 0.001 compared to vehicle. # p < 0.05 and ## p < 0.01 compared to each agonist alone.
Glosensor Tm Reagent, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/glosensor tm reagent/product/Promega
Average 90 stars, based on 1 article reviews
glosensor tm reagent - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier

Image Search Results


a , b The receptor–α5 interface in zGPR4 6.5 . Interacting residues are shown as sticks and are labeled. c , d Mutagenesis analysis of residues in zGPR4 ( c ) and hGPR4 ( d ) on the potency of G protein-coupling by the GloSensor cAMP assay. The maximum and minimum activation levels of WT GPR4 were set to 100 and 0%, respectively. The ΔpH 50 was calculated by dividing the potency (pH 50 ) of the mutant by the pH 50 of WT. Data are shown as means ± SEM from at least three independent experiments performed in triplicate. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Cryo-EM structure of an activated GPR4–Gs signaling complex

doi: 10.1038/s41467-025-55901-2

Figure Lengend Snippet: a , b The receptor–α5 interface in zGPR4 6.5 . Interacting residues are shown as sticks and are labeled. c , d Mutagenesis analysis of residues in zGPR4 ( c ) and hGPR4 ( d ) on the potency of G protein-coupling by the GloSensor cAMP assay. The maximum and minimum activation levels of WT GPR4 were set to 100 and 0%, respectively. The ΔpH 50 was calculated by dividing the potency (pH 50 ) of the mutant by the pH 50 of WT. Data are shown as means ± SEM from at least three independent experiments performed in triplicate. Source data are provided as a Source Data file.

Article Snippet: After incubating overnight, transfected cells were resuspended in DMEM added with 1% dialyzed FBS and then seeded into poly-l-lysine-coated 384-well plates (2 × 10 4 cells/well) (Costar, USA) for 9–24 h. After removing the culture medium, the cells were incubated with GloSensor TM cAMP reagent (Promega, USA) made in assay buffer (pH 8.4) for 1.5 h at 37 °C.

Techniques: Labeling, Mutagenesis, cAMP Assay, Activation Assay

a – e Mutagenesis analysis of residues in zGPR4 on the proton potency by the GloSensor cAMP assay. Mutagenesis analysis of histidine residues in ECLs ( a ), highly conserved acidic residues in ECLs ( b ), partially conserved acidic residues ( c ), the Na coordinating residues ( d ), and the aromatic residues within the orthosteric pocket ( e ). The maximum and minimum activation levels of WT GPR4 were set to 100 and 0%, respectively. The ΔpH 50 was calculated by dividing the pH 50 of the mutant by the pH 50 of WT. Data are shown as means ± SEM from at least three independent experiments performed in triplicate. f Mapping the tested mutations on the zGPR4 structure. Mutations with positive effect (ΔpH 50 > 0.2 unit) are colored blue; mutations with negative effect (ΔpH 50 < −0.2 unit) are colored red; mutations with negligible effect (0.2 > ΔpH 50 > −0.2) are colored gray. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Cryo-EM structure of an activated GPR4–Gs signaling complex

doi: 10.1038/s41467-025-55901-2

Figure Lengend Snippet: a – e Mutagenesis analysis of residues in zGPR4 on the proton potency by the GloSensor cAMP assay. Mutagenesis analysis of histidine residues in ECLs ( a ), highly conserved acidic residues in ECLs ( b ), partially conserved acidic residues ( c ), the Na coordinating residues ( d ), and the aromatic residues within the orthosteric pocket ( e ). The maximum and minimum activation levels of WT GPR4 were set to 100 and 0%, respectively. The ΔpH 50 was calculated by dividing the pH 50 of the mutant by the pH 50 of WT. Data are shown as means ± SEM from at least three independent experiments performed in triplicate. f Mapping the tested mutations on the zGPR4 structure. Mutations with positive effect (ΔpH 50 > 0.2 unit) are colored blue; mutations with negative effect (ΔpH 50 < −0.2 unit) are colored red; mutations with negligible effect (0.2 > ΔpH 50 > −0.2) are colored gray. Source data are provided as a Source Data file.

Article Snippet: After incubating overnight, transfected cells were resuspended in DMEM added with 1% dialyzed FBS and then seeded into poly-l-lysine-coated 384-well plates (2 × 10 4 cells/well) (Costar, USA) for 9–24 h. After removing the culture medium, the cells were incubated with GloSensor TM cAMP reagent (Promega, USA) made in assay buffer (pH 8.4) for 1.5 h at 37 °C.

Techniques: Mutagenesis, cAMP Assay, Activation Assay

Effects of OT on inhibition of intracellular cAMP production induced by each KOR agonist in HEK293 cells stably coexpressing human KOR and Glosensor 22F protein. The cells were pretreated with 10 −6 M U50488 ( A ), 10 −6 dynorphin A ( B ), or 10 −5 M of morphine ( C ) in the absence and presence of 10 −6 M OT for 10 min and treated with forskolin (3 µM). The data are presented in terms of mean ± SEM values (( A ); n = 3, ( B ); n = 3, ( C ); n = 3). Two-way ANOVA was performed, followed by Bonferroni’s test, *** p < 0.001 compared to vehicle. # p < 0.05 and ## p < 0.01 compared to each agonist alone.

Journal: Cells

Article Title: Oxytocin Is a Positive Allosteric Modulator of κ-Opioid Receptors but Not δ-Opioid Receptors in the G Protein Signaling Pathway

doi: 10.3390/cells10102651

Figure Lengend Snippet: Effects of OT on inhibition of intracellular cAMP production induced by each KOR agonist in HEK293 cells stably coexpressing human KOR and Glosensor 22F protein. The cells were pretreated with 10 −6 M U50488 ( A ), 10 −6 dynorphin A ( B ), or 10 −5 M of morphine ( C ) in the absence and presence of 10 −6 M OT for 10 min and treated with forskolin (3 µM). The data are presented in terms of mean ± SEM values (( A ); n = 3, ( B ); n = 3, ( C ); n = 3). Two-way ANOVA was performed, followed by Bonferroni’s test, *** p < 0.001 compared to vehicle. # p < 0.05 and ## p < 0.01 compared to each agonist alone.

Article Snippet: Briefly, HEK293 cells stably coexpressing human KOR and Glosensor TM 22F protein were seeded at 4.0 × 10 4 cells/well in a BioCoat TM poly- d -Lysine 96-well plate (Corning; Corning, NY, USA) and incubated in 5% CO 2 at 37 °C for 24 h. The cells were washed with Hanks’ balanced salt solution and incubated with GloSensor TM reagent (Promega) at 25 ± 3 °C for 2 h. The cells were treated with test compounds (vehicle, U50488, dynorphin A and morphine) diluted with Hanks’ balanced salt solution containing 50 μM IBMX and Ro 20-1724 for 10 min.

Techniques: Inhibition, Stable Transfection