pglosensor-22f (glosensor Search Results


luciferase-based pglosensor-22f camp reporter plasmid glosensor  (Promega)
90
Promega luciferase-based pglosensor-22f camp reporter plasmid glosensor
Luciferase Based Pglosensor 22f Camp Reporter Plasmid Glosensor, 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/luciferase-based pglosensor-22f camp reporter plasmid glosensor/product/Promega
Average 90 stars, based on 1 article reviews
luciferase-based pglosensor-22f camp reporter plasmid glosensor - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier
glosensor pglosensor-22f  (Promega)
90
Promega glosensor pglosensor-22f
COMMD8 promotes β-arrestin–mediated signaling of CXCR4. (A) IB analysis for Gα i activation induced by CXCL12 in control and Commd8 Δ B cells. (B) CXCR4-mediated inhibition of <t>cAMP</t> production was assessed by the GloSensor reporter in vector-transfected control and COMMD8-deficient (sg COMMD8 <t>)</t> <t>HEK293</t> cells expressing Flag-tagged CXCR4. The amounts of cAMP are plotted as fold increases of luminescence over the levels in unstimulated cells. Data are shown as the mean ± SD of triplicates and representative of three independent experiments. (C) Intracellular calcium responses to CXCL12 in control and Commd8 Δ B cells. Responses are plotted as the ratio of Cal-520 to Fura Red fluorescence. Data are representative of two independent experiments. (D) IP assay for the recruitment of endogenous β-arrestin-2 to Flag-tagged CXCR4 in vector-transfected control and COMMD8-deficient (sg Commd8 ) 2PK-3 cells after stimulation with CXCL12. (E–H) IB analysis for the phosphorylation of ERK (E and G) and p38 (F and H) in Commd8 Δ (E and F) and Arrb2 −/− (G and H) B cells after stimulation with CXCL12. B cells from littermate Commd8 f/+ Mb1 Cre/+ and Commd8 f/f Mb1 +/+ (E and F) or Arrb2 +/+ (G and H) mice served as the control. Error bars represent the mean ± SD of three (A and E–H) or four (D) independent experiments, and representative blots are shown. *, P < 0.05; **, P < 0.01; ns, not significant. The P values were obtained by two-tailed unpaired (A and D–H) or paired (B) t test. Asterisk indicates nonspecific bands (A, D, and H). coIP, coimmunoprecipitation.
Glosensor Pglosensor 22f, 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 pglosensor-22f/product/Promega
Average 90 stars, based on 1 article reviews
glosensor pglosensor-22f - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier

Image Search Results


COMMD8 promotes β-arrestin–mediated signaling of CXCR4. (A) IB analysis for Gα i activation induced by CXCL12 in control and Commd8 Δ B cells. (B) CXCR4-mediated inhibition of cAMP production was assessed by the GloSensor reporter in vector-transfected control and COMMD8-deficient (sg COMMD8 ) HEK293 cells expressing Flag-tagged CXCR4. The amounts of cAMP are plotted as fold increases of luminescence over the levels in unstimulated cells. Data are shown as the mean ± SD of triplicates and representative of three independent experiments. (C) Intracellular calcium responses to CXCL12 in control and Commd8 Δ B cells. Responses are plotted as the ratio of Cal-520 to Fura Red fluorescence. Data are representative of two independent experiments. (D) IP assay for the recruitment of endogenous β-arrestin-2 to Flag-tagged CXCR4 in vector-transfected control and COMMD8-deficient (sg Commd8 ) 2PK-3 cells after stimulation with CXCL12. (E–H) IB analysis for the phosphorylation of ERK (E and G) and p38 (F and H) in Commd8 Δ (E and F) and Arrb2 −/− (G and H) B cells after stimulation with CXCL12. B cells from littermate Commd8 f/+ Mb1 Cre/+ and Commd8 f/f Mb1 +/+ (E and F) or Arrb2 +/+ (G and H) mice served as the control. Error bars represent the mean ± SD of three (A and E–H) or four (D) independent experiments, and representative blots are shown. *, P < 0.05; **, P < 0.01; ns, not significant. The P values were obtained by two-tailed unpaired (A and D–H) or paired (B) t test. Asterisk indicates nonspecific bands (A, D, and H). coIP, coimmunoprecipitation.

Journal: The Journal of Experimental Medicine

Article Title: The COMMD3/8 complex determines GRK6 specificity for chemoattractant receptors

doi: 10.1084/jem.20181494

Figure Lengend Snippet: COMMD8 promotes β-arrestin–mediated signaling of CXCR4. (A) IB analysis for Gα i activation induced by CXCL12 in control and Commd8 Δ B cells. (B) CXCR4-mediated inhibition of cAMP production was assessed by the GloSensor reporter in vector-transfected control and COMMD8-deficient (sg COMMD8 ) HEK293 cells expressing Flag-tagged CXCR4. The amounts of cAMP are plotted as fold increases of luminescence over the levels in unstimulated cells. Data are shown as the mean ± SD of triplicates and representative of three independent experiments. (C) Intracellular calcium responses to CXCL12 in control and Commd8 Δ B cells. Responses are plotted as the ratio of Cal-520 to Fura Red fluorescence. Data are representative of two independent experiments. (D) IP assay for the recruitment of endogenous β-arrestin-2 to Flag-tagged CXCR4 in vector-transfected control and COMMD8-deficient (sg Commd8 ) 2PK-3 cells after stimulation with CXCL12. (E–H) IB analysis for the phosphorylation of ERK (E and G) and p38 (F and H) in Commd8 Δ (E and F) and Arrb2 −/− (G and H) B cells after stimulation with CXCL12. B cells from littermate Commd8 f/+ Mb1 Cre/+ and Commd8 f/f Mb1 +/+ (E and F) or Arrb2 +/+ (G and H) mice served as the control. Error bars represent the mean ± SD of three (A and E–H) or four (D) independent experiments, and representative blots are shown. *, P < 0.05; **, P < 0.01; ns, not significant. The P values were obtained by two-tailed unpaired (A and D–H) or paired (B) t test. Asterisk indicates nonspecific bands (A, D, and H). coIP, coimmunoprecipitation.

Article Snippet: To assess CXCR4-mediated inhibition of cAMP production, control and COMMD8- or COMMD3-deficient HEK293 cells were transfected with plasmids encoding Flag-tagged CXCR4 and a luciferase-based cAMP biosensor, GloSensor (pGloSensor-22F; Promega) at a 1:1 ratio.

Techniques: Activation Assay, Inhibition, Plasmid Preparation, Transfection, Expressing, Fluorescence, Two Tailed Test

COMMD8 is involved in β-arrestin-mediated signaling of β 2 AR. (A) Confocal microscopy for the subcellular localization and colocalization of Flagg-tagged β 2 AR (red) and Myc-tagged COMMD8 (green) in HEK293 cells before and at 1 min after treatment with pan-βAR agonist isoproterenol. Colocalization of the signals (arrowheads) was quantified as in . Each symbol represents an individual cell, and bars indicate means (0 min, n = 20; 1 min, n = 20). Representative images are shown. Bar, 10 µm. (B) IP assay for the interaction of Myc-tagged COMMD8 with Flag-tagged β 2 AR in 2PK-3 cells after stimulation with selective β 2 AR agonist clenbuterol. (C) cAMP production assessed by GloSensor in vector-transfected control and COMMD8-deficient (sg COMMD8 ) HEK293 cells after stimulation with isoproterenol. The amounts of cAMP are plotted as fold increases of luminescence over the levels in unstimulated cells. Data are shown as the mean ± SD of triplicates and representative of three experiments. (D) IP assay for the recruitment of endogenous β-arrestin-2 to Flag-tagged β 2 AR in vector-transfected control and COMMD8-deficient (sg Commd8 ) 2PK-3 cells after stimulation with isoproterenol. Asterisks indicate nonspecific bands. (E) IB analysis for the phosphorylation of ERK in vector-transfected control and sg Commd8 2PK-3 cells after stimulation with isoproterenol. (F) IB analysis for GRK6-mediated phosphorylation (p) at S355/356 of Flag-tagged β 2 AR in vector-transfected control and sg Commd8 2PK-3 cells after stimulation with isoproterenol. Error bars represent the mean ± SD of three (B), four (E and F), or five (D) independent experiments, and representative blots are shown. (G) Tango assay for the association of COMMD8 with β 2 AR in the presence of paroxetine. (H) Tango assay for the association of COMMD8 with a C terminus–truncated β 2 AR mutant lacking GRK2 phosphorylation sites. The luminescence from the tTA-dependent firefly luciferase reporter was normalized to that from the cotransfected Renilla luciferase and plotted as fold increases over the levels in unstimulated cells (G and H). *, P < 0.05; **, P < 0.01; ns, not significant. The P values were obtained by two-tailed unpaired (A and D–H) or paired (B and C) t test. coIP, coimmunoprecipitation; DIC, differential interference contrast.

Journal: The Journal of Experimental Medicine

Article Title: The COMMD3/8 complex determines GRK6 specificity for chemoattractant receptors

doi: 10.1084/jem.20181494

Figure Lengend Snippet: COMMD8 is involved in β-arrestin-mediated signaling of β 2 AR. (A) Confocal microscopy for the subcellular localization and colocalization of Flagg-tagged β 2 AR (red) and Myc-tagged COMMD8 (green) in HEK293 cells before and at 1 min after treatment with pan-βAR agonist isoproterenol. Colocalization of the signals (arrowheads) was quantified as in . Each symbol represents an individual cell, and bars indicate means (0 min, n = 20; 1 min, n = 20). Representative images are shown. Bar, 10 µm. (B) IP assay for the interaction of Myc-tagged COMMD8 with Flag-tagged β 2 AR in 2PK-3 cells after stimulation with selective β 2 AR agonist clenbuterol. (C) cAMP production assessed by GloSensor in vector-transfected control and COMMD8-deficient (sg COMMD8 ) HEK293 cells after stimulation with isoproterenol. The amounts of cAMP are plotted as fold increases of luminescence over the levels in unstimulated cells. Data are shown as the mean ± SD of triplicates and representative of three experiments. (D) IP assay for the recruitment of endogenous β-arrestin-2 to Flag-tagged β 2 AR in vector-transfected control and COMMD8-deficient (sg Commd8 ) 2PK-3 cells after stimulation with isoproterenol. Asterisks indicate nonspecific bands. (E) IB analysis for the phosphorylation of ERK in vector-transfected control and sg Commd8 2PK-3 cells after stimulation with isoproterenol. (F) IB analysis for GRK6-mediated phosphorylation (p) at S355/356 of Flag-tagged β 2 AR in vector-transfected control and sg Commd8 2PK-3 cells after stimulation with isoproterenol. Error bars represent the mean ± SD of three (B), four (E and F), or five (D) independent experiments, and representative blots are shown. (G) Tango assay for the association of COMMD8 with β 2 AR in the presence of paroxetine. (H) Tango assay for the association of COMMD8 with a C terminus–truncated β 2 AR mutant lacking GRK2 phosphorylation sites. The luminescence from the tTA-dependent firefly luciferase reporter was normalized to that from the cotransfected Renilla luciferase and plotted as fold increases over the levels in unstimulated cells (G and H). *, P < 0.05; **, P < 0.01; ns, not significant. The P values were obtained by two-tailed unpaired (A and D–H) or paired (B and C) t test. coIP, coimmunoprecipitation; DIC, differential interference contrast.

Article Snippet: To assess CXCR4-mediated inhibition of cAMP production, control and COMMD8- or COMMD3-deficient HEK293 cells were transfected with plasmids encoding Flag-tagged CXCR4 and a luciferase-based cAMP biosensor, GloSensor (pGloSensor-22F; Promega) at a 1:1 ratio.

Techniques: Confocal Microscopy, Plasmid Preparation, Transfection, Mutagenesis, Luciferase, Two Tailed Test