u 73122 Search Results


plc inhibitor u 73122  (Tocris)
96
Tocris plc inhibitor u 73122
Plc Inhibitor U 73122, supplied by Tocris, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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u73122  (MedChemExpress)
95
MedChemExpress u73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
U73122, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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663684b u 73122 1 6 17b 3 methoxyestra 1 3 5 10 trien 17 yl amino hexyl 1h pyrrole 2 5 dione tocris  (Tocris)
95
Tocris 663684b u 73122 1 6 17b 3 methoxyestra 1 3 5 10 trien 17 yl amino hexyl 1h pyrrole 2 5 dione tocris
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
663684b U 73122 1 6 17b 3 Methoxyestra 1 3 5 10 Trien 17 Yl Amino Hexyl 1h Pyrrole 2 5 Dione Tocris, supplied by Tocris, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 95 stars, based on 1 article reviews
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u73122  (Santa Cruz Biotechnology)
93
Santa Cruz Biotechnology u73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
U73122, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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u73122  (TargetMol)
94
TargetMol u73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
U73122, supplied by TargetMol, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1-[6-[amino]hexyl]-1h-pyrrole-2,5-dione (u-73122)  (Funakoshi ltd)
90
Funakoshi ltd 1-[6-[amino]hexyl]-1h-pyrrole-2,5-dione (u-73122)
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
1 [6 [Amino]Hexyl] 1h Pyrrole 2,5 Dione (U 73122), supplied by Funakoshi ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1-[6-[amino]hexyl]-1h-pyrrole-2,5-dione (u-73122) - by Bioz Stars, 2026-04
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u-73122  (VASCO DRUG LABORATORIES)
90
VASCO DRUG LABORATORIES u-73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
U 73122, supplied by VASCO DRUG LABORATORIES, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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u73122  (FUJIFILM)
90
FUJIFILM u73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
U73122, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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u-73122  (Gartner Inc)
90
Gartner Inc u-73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
U 73122, supplied by Gartner Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1-6-17ß-3-methoxgestra-1,3,5 (10)-trien-17yl-aminohexyl-1-h-pirrole-2,5-dione (u-73122  (ICN Pharmaceuticals)
90
ICN Pharmaceuticals 1-6-17ß-3-methoxgestra-1,3,5 (10)-trien-17yl-aminohexyl-1-h-pirrole-2,5-dione (u-73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
1 6 17ß 3 Methoxgestra 1,3,5 (10) Trien 17yl Aminohexyl 1 H Pirrole 2,5 Dione (U 73122, supplied by ICN Pharmaceuticals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
1-6-17ß-3-methoxgestra-1,3,5 (10)-trien-17yl-aminohexyl-1-h-pirrole-2,5-dione (u-73122 - by Bioz Stars, 2026-04
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u-73122  (Chemie GmbH)
90
Chemie GmbH u-73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
U 73122, supplied by Chemie GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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u-73122  (Pfizer Inc)
90
Pfizer Inc u-73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
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( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor U73122 (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .

Journal: The EMBO Journal

Article Title: Dual interference with host neuropeptide signaling allows parasitoid wasp to hijack host sugar metabolism

doi: 10.1038/s44318-025-00636-5

Figure Lengend Snippet: ( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor U73122 (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .

Article Snippet: U73122 , MedChemExpress , HY-13419.

Techniques: Control, Inhibition, Expressing, Incubation, Binding Assay, Two Tailed Test, Comparison