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fty720 (s)-phosphate  (Cayman Chemical)


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    Cayman Chemical fty720 (s)-phosphate
    Fty720 (S) Phosphate, supplied by Cayman Chemical, 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/fty720 (s)-phosphate/product/Cayman Chemical
    Average 90 stars, based on 1 article reviews
    fty720 (s)-phosphate - by Bioz Stars, 2026-05
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    ( A ) Dose-response curves of S1PR2 and S1PR3 for the TGFα shedding assay using <t>FTY720-P.</t> The chemical structure of FTY720-P is shown. Data are means ± SD ( n = 3). The membrane expression of S1PRs is shown in figs. S4A and S6C. EV, empty vector. ( B ) JTE-013 reduces the FTY720-P–induced activation of S1PR2 but not S1PR3. The chemical structure of JTE-013 is shown. Data are means ± SD ( n = 3). ( C ) Structural comparisons among S1PRs imply the unique roles of residue F274 of S1PR2. The residues are shown in sticks. ( D ) The sequence alignment of S1PR2-TM7 from different species. The conserved residues are highlighted. The residue F274 is indicated by a star. ( E and G ) Mutagenesis analysis of S1PR2 F274I for S1P (E) and FTY720-P (G). The representative dose-response curves from same-day experiment are shown. Data are means ± SD ( n = 3). ( F and H ) RAi of each varient for S1P (F) and FTY720-P (H). Each LogRAi plot denotes a single measurement from a dose-response experiment. Data are means ± SD ( n = 3 to 5 independent experiments). * P < 0.05, *** P < 0.001, and **** P < 0.0001; mutant versus wild-type values according to one-way ANOVA with Dunnett’s multiple comparison test.
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    ( A ) Dose-response curves of S1PR2 and S1PR3 for the TGFα shedding assay using <t>FTY720-P.</t> The chemical structure of FTY720-P is shown. Data are means ± SD ( n = 3). The membrane expression of S1PRs is shown in figs. S4A and S6C. EV, empty vector. ( B ) JTE-013 reduces the FTY720-P–induced activation of S1PR2 but not S1PR3. The chemical structure of JTE-013 is shown. Data are means ± SD ( n = 3). ( C ) Structural comparisons among S1PRs imply the unique roles of residue F274 of S1PR2. The residues are shown in sticks. ( D ) The sequence alignment of S1PR2-TM7 from different species. The conserved residues are highlighted. The residue F274 is indicated by a star. ( E and G ) Mutagenesis analysis of S1PR2 F274I for S1P (E) and FTY720-P (G). The representative dose-response curves from same-day experiment are shown. Data are means ± SD ( n = 3). ( F and H ) RAi of each varient for S1P (F) and FTY720-P (H). Each LogRAi plot denotes a single measurement from a dose-response experiment. Data are means ± SD ( n = 3 to 5 independent experiments). * P < 0.05, *** P < 0.001, and **** P < 0.0001; mutant versus wild-type values according to one-way ANOVA with Dunnett’s multiple comparison test.
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    ( A ) Dose-response curves of S1PR2 and S1PR3 for the TGFα shedding assay using <t>FTY720-P.</t> The chemical structure of FTY720-P is shown. Data are means ± SD ( n = 3). The membrane expression of S1PRs is shown in figs. S4A and S6C. EV, empty vector. ( B ) JTE-013 reduces the FTY720-P–induced activation of S1PR2 but not S1PR3. The chemical structure of JTE-013 is shown. Data are means ± SD ( n = 3). ( C ) Structural comparisons among S1PRs imply the unique roles of residue F274 of S1PR2. The residues are shown in sticks. ( D ) The sequence alignment of S1PR2-TM7 from different species. The conserved residues are highlighted. The residue F274 is indicated by a star. ( E and G ) Mutagenesis analysis of S1PR2 F274I for S1P (E) and FTY720-P (G). The representative dose-response curves from same-day experiment are shown. Data are means ± SD ( n = 3). ( F and H ) RAi of each varient for S1P (F) and FTY720-P (H). Each LogRAi plot denotes a single measurement from a dose-response experiment. Data are means ± SD ( n = 3 to 5 independent experiments). * P < 0.05, *** P < 0.001, and **** P < 0.0001; mutant versus wild-type values according to one-way ANOVA with Dunnett’s multiple comparison test.
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    ( A ) Dose-response curves of S1PR2 and S1PR3 for the TGFα shedding assay using <t>FTY720-P.</t> The chemical structure of FTY720-P is shown. Data are means ± SD ( n = 3). The membrane expression of S1PRs is shown in figs. S4A and S6C. EV, empty vector. ( B ) JTE-013 reduces the FTY720-P–induced activation of S1PR2 but not S1PR3. The chemical structure of JTE-013 is shown. Data are means ± SD ( n = 3). ( C ) Structural comparisons among S1PRs imply the unique roles of residue F274 of S1PR2. The residues are shown in sticks. ( D ) The sequence alignment of S1PR2-TM7 from different species. The conserved residues are highlighted. The residue F274 is indicated by a star. ( E and G ) Mutagenesis analysis of S1PR2 F274I for S1P (E) and FTY720-P (G). The representative dose-response curves from same-day experiment are shown. Data are means ± SD ( n = 3). ( F and H ) RAi of each varient for S1P (F) and FTY720-P (H). Each LogRAi plot denotes a single measurement from a dose-response experiment. Data are means ± SD ( n = 3 to 5 independent experiments). * P < 0.05, *** P < 0.001, and **** P < 0.0001; mutant versus wild-type values according to one-way ANOVA with Dunnett’s multiple comparison test.
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    ( A ) Dose-response curves of S1PR2 and S1PR3 for the TGFα shedding assay using FTY720-P. The chemical structure of FTY720-P is shown. Data are means ± SD ( n = 3). The membrane expression of S1PRs is shown in figs. S4A and S6C. EV, empty vector. ( B ) JTE-013 reduces the FTY720-P–induced activation of S1PR2 but not S1PR3. The chemical structure of JTE-013 is shown. Data are means ± SD ( n = 3). ( C ) Structural comparisons among S1PRs imply the unique roles of residue F274 of S1PR2. The residues are shown in sticks. ( D ) The sequence alignment of S1PR2-TM7 from different species. The conserved residues are highlighted. The residue F274 is indicated by a star. ( E and G ) Mutagenesis analysis of S1PR2 F274I for S1P (E) and FTY720-P (G). The representative dose-response curves from same-day experiment are shown. Data are means ± SD ( n = 3). ( F and H ) RAi of each varient for S1P (F) and FTY720-P (H). Each LogRAi plot denotes a single measurement from a dose-response experiment. Data are means ± SD ( n = 3 to 5 independent experiments). * P < 0.05, *** P < 0.001, and **** P < 0.0001; mutant versus wild-type values according to one-way ANOVA with Dunnett’s multiple comparison test.

    Journal: Science Advances

    Article Title: Structure of S1PR2–heterotrimeric G 13 signaling complex

    doi: 10.1126/sciadv.abn0067

    Figure Lengend Snippet: ( A ) Dose-response curves of S1PR2 and S1PR3 for the TGFα shedding assay using FTY720-P. The chemical structure of FTY720-P is shown. Data are means ± SD ( n = 3). The membrane expression of S1PRs is shown in figs. S4A and S6C. EV, empty vector. ( B ) JTE-013 reduces the FTY720-P–induced activation of S1PR2 but not S1PR3. The chemical structure of JTE-013 is shown. Data are means ± SD ( n = 3). ( C ) Structural comparisons among S1PRs imply the unique roles of residue F274 of S1PR2. The residues are shown in sticks. ( D ) The sequence alignment of S1PR2-TM7 from different species. The conserved residues are highlighted. The residue F274 is indicated by a star. ( E and G ) Mutagenesis analysis of S1PR2 F274I for S1P (E) and FTY720-P (G). The representative dose-response curves from same-day experiment are shown. Data are means ± SD ( n = 3). ( F and H ) RAi of each varient for S1P (F) and FTY720-P (H). Each LogRAi plot denotes a single measurement from a dose-response experiment. Data are means ± SD ( n = 3 to 5 independent experiments). * P < 0.05, *** P < 0.001, and **** P < 0.0001; mutant versus wild-type values according to one-way ANOVA with Dunnett’s multiple comparison test.

    Article Snippet: The ligand S1P (Tocris) or FTY720 (S)-phosphate (FTY720-P, Echelon) was serially diluted in HBSS supplemented with 5 mM Hepes (pH 7.4) and 0.01% fatty acid–free bovine serum albumin (BSA; GoldBio) to prepare 10× stock solutions.

    Techniques: Expressing, Plasmid Preparation, Activation Assay, Sequencing, Mutagenesis

    ( A ) The immunofluorescence staining of HEK293 cells that express S1PR2 or its variants after vehicle or 1 μM ligand treatment. Scale bar, 10 μm. DAPI, 4′,6-diamidino-2-phenylindole. ( B ) Internalization of S1PR2 WT or S1PR2 R108A in WEHI-231 cells in response to the indicated amounts of S1P or FTY720-P treatment. Graphs show percent cells with detectable S1PR2 surface staining determined using flow cytometry. ( C ) Cell migration inhibition assay with S1PR2 WT WEHI-231 cells in response to S1P or FTY720-P at the indicated concentrations. Data are means ± SD (pooled from three independent experiments).

    Journal: Science Advances

    Article Title: Structure of S1PR2–heterotrimeric G 13 signaling complex

    doi: 10.1126/sciadv.abn0067

    Figure Lengend Snippet: ( A ) The immunofluorescence staining of HEK293 cells that express S1PR2 or its variants after vehicle or 1 μM ligand treatment. Scale bar, 10 μm. DAPI, 4′,6-diamidino-2-phenylindole. ( B ) Internalization of S1PR2 WT or S1PR2 R108A in WEHI-231 cells in response to the indicated amounts of S1P or FTY720-P treatment. Graphs show percent cells with detectable S1PR2 surface staining determined using flow cytometry. ( C ) Cell migration inhibition assay with S1PR2 WT WEHI-231 cells in response to S1P or FTY720-P at the indicated concentrations. Data are means ± SD (pooled from three independent experiments).

    Article Snippet: The ligand S1P (Tocris) or FTY720 (S)-phosphate (FTY720-P, Echelon) was serially diluted in HBSS supplemented with 5 mM Hepes (pH 7.4) and 0.01% fatty acid–free bovine serum albumin (BSA; GoldBio) to prepare 10× stock solutions.

    Techniques: Immunofluorescence, Staining, Flow Cytometry, Migration, Inhibition