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IL-2(E52K) does not support the assembly of the hCD25–CCR7 complex but supports canonical IL-2 signaling. A, 7G7B6 triggers IL-2-dependent hCD25–CCR7 complex. Anti-hCD25 antibodies (5 μg/ml), 7G7B6 or BC96, were incubated with HA-hCD25–expressing HEK293T cells in the presence or the absence of 1 μg/ml IL-2 and following lysis and immunoprecipitation with anti-HA were assayed for captured CCR7 or HA-hCD25 by immunoblotting. Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and HA-hCD25 from three independent experiments. B, IL-2(E52K) does not support the 7G7B6-induced the hCD25–CCR7 complex. IL-2(E52K) or wildtype IL-2 was assayed for capacity to support the 7G7B6-induced CD25–CCR7 complex as described in A . Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and CD25 from three independent experiments. C, IL2(E52K) mutation does not reduce binding of IL-2 to hCD25. <t>Microplates</t> coated with recombinant hCD25 extracellular domain or BSA were incubated with the indicated concentrations of IL-2 WT or IL-2(E52K), and bound IL-2 was quantified by ELISA. D, IL-2(E52K) triggers canonical IL-2 signaling. IL2Rα + YT-1 cells were stimulated with varying concentrations of IL-2 WT or IL-2(E52K) (for 30 min at 37 °C, followed by staining with APC-anti–phospho-STAT5 and analysis by flow cytometry (mean ± SEM; N = 3). ns, not significant, ∗∗∗ p < 0.0001, ∗∗∗∗ p < 0.0001 by one-way ANOVA. BSA, bovine serum albumin; HA, hemagglutinin; hCD25, human CD25; HEK293T, human embryonic kidney 293T cell line; IL, interleukin; STAT5, signal transducer and activator of transcription 5.
Microplates, supplied by Greiner Bio, 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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ex taq polymerase 1 25 u  (TaKaRa)
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IL-2(E52K) does not support the assembly of the hCD25–CCR7 complex but supports canonical IL-2 signaling. A, 7G7B6 triggers IL-2-dependent hCD25–CCR7 complex. Anti-hCD25 antibodies (5 μg/ml), 7G7B6 or BC96, were incubated with HA-hCD25–expressing HEK293T cells in the presence or the absence of 1 μg/ml IL-2 and following lysis and immunoprecipitation with anti-HA were assayed for captured CCR7 or HA-hCD25 by immunoblotting. Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and HA-hCD25 from three independent experiments. B, IL-2(E52K) does not support the 7G7B6-induced the hCD25–CCR7 complex. IL-2(E52K) or wildtype IL-2 was assayed for capacity to support the 7G7B6-induced CD25–CCR7 complex as described in A . Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and CD25 from three independent experiments. C, IL2(E52K) mutation does not reduce binding of IL-2 to hCD25. <t>Microplates</t> coated with recombinant hCD25 extracellular domain or BSA were incubated with the indicated concentrations of IL-2 WT or IL-2(E52K), and bound IL-2 was quantified by ELISA. D, IL-2(E52K) triggers canonical IL-2 signaling. IL2Rα + YT-1 cells were stimulated with varying concentrations of IL-2 WT or IL-2(E52K) (for 30 min at 37 °C, followed by staining with APC-anti–phospho-STAT5 and analysis by flow cytometry (mean ± SEM; N = 3). ns, not significant, ∗∗∗ p < 0.0001, ∗∗∗∗ p < 0.0001 by one-way ANOVA. BSA, bovine serum albumin; HA, hemagglutinin; hCD25, human CD25; HEK293T, human embryonic kidney 293T cell line; IL, interleukin; STAT5, signal transducer and activator of transcription 5.
Ex Taq Polymerase 1 25 U, supplied by TaKaRa, 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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ex taq polymerase 1 25 u - by Bioz Stars, 2026-10
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u bottom 96 well plate  (Genesee Scientific)
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IL-2(E52K) does not support the assembly of the hCD25–CCR7 complex but supports canonical IL-2 signaling. A, 7G7B6 triggers IL-2-dependent hCD25–CCR7 complex. Anti-hCD25 antibodies (5 μg/ml), 7G7B6 or BC96, were incubated with HA-hCD25–expressing HEK293T cells in the presence or the absence of 1 μg/ml IL-2 and following lysis and immunoprecipitation with anti-HA were assayed for captured CCR7 or HA-hCD25 by immunoblotting. Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and HA-hCD25 from three independent experiments. B, IL-2(E52K) does not support the 7G7B6-induced the hCD25–CCR7 complex. IL-2(E52K) or wildtype IL-2 was assayed for capacity to support the 7G7B6-induced CD25–CCR7 complex as described in A . Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and CD25 from three independent experiments. C, IL2(E52K) mutation does not reduce binding of IL-2 to hCD25. <t>Microplates</t> coated with recombinant hCD25 extracellular domain or BSA were incubated with the indicated concentrations of IL-2 WT or IL-2(E52K), and bound IL-2 was quantified by ELISA. D, IL-2(E52K) triggers canonical IL-2 signaling. IL2Rα + YT-1 cells were stimulated with varying concentrations of IL-2 WT or IL-2(E52K) (for 30 min at 37 °C, followed by staining with APC-anti–phospho-STAT5 and analysis by flow cytometry (mean ± SEM; N = 3). ns, not significant, ∗∗∗ p < 0.0001, ∗∗∗∗ p < 0.0001 by one-way ANOVA. BSA, bovine serum albumin; HA, hemagglutinin; hCD25, human CD25; HEK293T, human embryonic kidney 293T cell line; IL, interleukin; STAT5, signal transducer and activator of transcription 5.
U Bottom 96 Well Plate, supplied by Genesee Scientific, 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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well tc  (Genesee Scientific)
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Genesee Scientific well tc
IL-2(E52K) does not support the assembly of the hCD25–CCR7 complex but supports canonical IL-2 signaling. A, 7G7B6 triggers IL-2-dependent hCD25–CCR7 complex. Anti-hCD25 antibodies (5 μg/ml), 7G7B6 or BC96, were incubated with HA-hCD25–expressing HEK293T cells in the presence or the absence of 1 μg/ml IL-2 and following lysis and immunoprecipitation with anti-HA were assayed for captured CCR7 or HA-hCD25 by immunoblotting. Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and HA-hCD25 from three independent experiments. B, IL-2(E52K) does not support the 7G7B6-induced the hCD25–CCR7 complex. IL-2(E52K) or wildtype IL-2 was assayed for capacity to support the 7G7B6-induced CD25–CCR7 complex as described in A . Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and CD25 from three independent experiments. C, IL2(E52K) mutation does not reduce binding of IL-2 to hCD25. <t>Microplates</t> coated with recombinant hCD25 extracellular domain or BSA were incubated with the indicated concentrations of IL-2 WT or IL-2(E52K), and bound IL-2 was quantified by ELISA. D, IL-2(E52K) triggers canonical IL-2 signaling. IL2Rα + YT-1 cells were stimulated with varying concentrations of IL-2 WT or IL-2(E52K) (for 30 min at 37 °C, followed by staining with APC-anti–phospho-STAT5 and analysis by flow cytometry (mean ± SEM; N = 3). ns, not significant, ∗∗∗ p < 0.0001, ∗∗∗∗ p < 0.0001 by one-way ANOVA. BSA, bovine serum albumin; HA, hemagglutinin; hCD25, human CD25; HEK293T, human embryonic kidney 293T cell line; IL, interleukin; STAT5, signal transducer and activator of transcription 5.
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u bottom suspension 96 well plates  (Genesee Scientific)
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IL-2(E52K) does not support the assembly of the hCD25–CCR7 complex but supports canonical IL-2 signaling. A, 7G7B6 triggers IL-2-dependent hCD25–CCR7 complex. Anti-hCD25 antibodies (5 μg/ml), 7G7B6 or BC96, were incubated with HA-hCD25–expressing HEK293T cells in the presence or the absence of 1 μg/ml IL-2 and following lysis and immunoprecipitation with anti-HA were assayed for captured CCR7 or HA-hCD25 by immunoblotting. Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and HA-hCD25 from three independent experiments. B, IL-2(E52K) does not support the 7G7B6-induced the hCD25–CCR7 complex. IL-2(E52K) or wildtype IL-2 was assayed for capacity to support the 7G7B6-induced CD25–CCR7 complex as described in A . Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and CD25 from three independent experiments. C, IL2(E52K) mutation does not reduce binding of IL-2 to hCD25. <t>Microplates</t> coated with recombinant hCD25 extracellular domain or BSA were incubated with the indicated concentrations of IL-2 WT or IL-2(E52K), and bound IL-2 was quantified by ELISA. D, IL-2(E52K) triggers canonical IL-2 signaling. IL2Rα + YT-1 cells were stimulated with varying concentrations of IL-2 WT or IL-2(E52K) (for 30 min at 37 °C, followed by staining with APC-anti–phospho-STAT5 and analysis by flow cytometry (mean ± SEM; N = 3). ns, not significant, ∗∗∗ p < 0.0001, ∗∗∗∗ p < 0.0001 by one-way ANOVA. BSA, bovine serum albumin; HA, hemagglutinin; hCD25, human CD25; HEK293T, human embryonic kidney 293T cell line; IL, interleukin; STAT5, signal transducer and activator of transcription 5.
U Bottom Suspension 96 Well Plates, supplied by Genesee Scientific, 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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25% dispase 5 u/ml  (STEMCELL Technologies Inc)
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STEMCELL Technologies Inc 25% dispase 5 u/ml
IL-2(E52K) does not support the assembly of the hCD25–CCR7 complex but supports canonical IL-2 signaling. A, 7G7B6 triggers IL-2-dependent hCD25–CCR7 complex. Anti-hCD25 antibodies (5 μg/ml), 7G7B6 or BC96, were incubated with HA-hCD25–expressing HEK293T cells in the presence or the absence of 1 μg/ml IL-2 and following lysis and immunoprecipitation with anti-HA were assayed for captured CCR7 or HA-hCD25 by immunoblotting. Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and HA-hCD25 from three independent experiments. B, IL-2(E52K) does not support the 7G7B6-induced the hCD25–CCR7 complex. IL-2(E52K) or wildtype IL-2 was assayed for capacity to support the 7G7B6-induced CD25–CCR7 complex as described in A . Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and CD25 from three independent experiments. C, IL2(E52K) mutation does not reduce binding of IL-2 to hCD25. <t>Microplates</t> coated with recombinant hCD25 extracellular domain or BSA were incubated with the indicated concentrations of IL-2 WT or IL-2(E52K), and bound IL-2 was quantified by ELISA. D, IL-2(E52K) triggers canonical IL-2 signaling. IL2Rα + YT-1 cells were stimulated with varying concentrations of IL-2 WT or IL-2(E52K) (for 30 min at 37 °C, followed by staining with APC-anti–phospho-STAT5 and analysis by flow cytometry (mean ± SEM; N = 3). ns, not significant, ∗∗∗ p < 0.0001, ∗∗∗∗ p < 0.0001 by one-way ANOVA. BSA, bovine serum albumin; HA, hemagglutinin; hCD25, human CD25; HEK293T, human embryonic kidney 293T cell line; IL, interleukin; STAT5, signal transducer and activator of transcription 5.
25% Dispase 5 U/Ml, supplied by STEMCELL Technologies 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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zetasizer nano zs u k at 25  (Malvern Panalytical)
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Malvern Panalytical zetasizer nano zs u k at 25
IL-2(E52K) does not support the assembly of the hCD25–CCR7 complex but supports canonical IL-2 signaling. A, 7G7B6 triggers IL-2-dependent hCD25–CCR7 complex. Anti-hCD25 antibodies (5 μg/ml), 7G7B6 or BC96, were incubated with HA-hCD25–expressing HEK293T cells in the presence or the absence of 1 μg/ml IL-2 and following lysis and immunoprecipitation with anti-HA were assayed for captured CCR7 or HA-hCD25 by immunoblotting. Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and HA-hCD25 from three independent experiments. B, IL-2(E52K) does not support the 7G7B6-induced the hCD25–CCR7 complex. IL-2(E52K) or wildtype IL-2 was assayed for capacity to support the 7G7B6-induced CD25–CCR7 complex as described in A . Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and CD25 from three independent experiments. C, IL2(E52K) mutation does not reduce binding of IL-2 to hCD25. <t>Microplates</t> coated with recombinant hCD25 extracellular domain or BSA were incubated with the indicated concentrations of IL-2 WT or IL-2(E52K), and bound IL-2 was quantified by ELISA. D, IL-2(E52K) triggers canonical IL-2 signaling. IL2Rα + YT-1 cells were stimulated with varying concentrations of IL-2 WT or IL-2(E52K) (for 30 min at 37 °C, followed by staining with APC-anti–phospho-STAT5 and analysis by flow cytometry (mean ± SEM; N = 3). ns, not significant, ∗∗∗ p < 0.0001, ∗∗∗∗ p < 0.0001 by one-way ANOVA. BSA, bovine serum albumin; HA, hemagglutinin; hCD25, human CD25; HEK293T, human embryonic kidney 293T cell line; IL, interleukin; STAT5, signal transducer and activator of transcription 5.
Zetasizer Nano Zs U K At 25, supplied by Malvern Panalytical, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/25+u/Zetasizer+Advance/pm40410655-62-55-54
Average 99 stars, based on 1 article reviews
zetasizer nano zs u k at 25 - by Bioz Stars, 2026-10
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IL-2(E52K) does not support the assembly of the hCD25–CCR7 complex but supports canonical IL-2 signaling. A, 7G7B6 triggers IL-2-dependent hCD25–CCR7 complex. Anti-hCD25 antibodies (5 μg/ml), 7G7B6 or BC96, were incubated with HA-hCD25–expressing HEK293T cells in the presence or the absence of 1 μg/ml IL-2 and following lysis and immunoprecipitation with anti-HA were assayed for captured CCR7 or HA-hCD25 by immunoblotting. Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and HA-hCD25 from three independent experiments. B, IL-2(E52K) does not support the 7G7B6-induced the hCD25–CCR7 complex. IL-2(E52K) or wildtype IL-2 was assayed for capacity to support the 7G7B6-induced CD25–CCR7 complex as described in A . Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and CD25 from three independent experiments. C, IL2(E52K) mutation does not reduce binding of IL-2 to hCD25. Microplates coated with recombinant hCD25 extracellular domain or BSA were incubated with the indicated concentrations of IL-2 WT or IL-2(E52K), and bound IL-2 was quantified by ELISA. D, IL-2(E52K) triggers canonical IL-2 signaling. IL2Rα + YT-1 cells were stimulated with varying concentrations of IL-2 WT or IL-2(E52K) (for 30 min at 37 °C, followed by staining with APC-anti–phospho-STAT5 and analysis by flow cytometry (mean ± SEM; N = 3). ns, not significant, ∗∗∗ p < 0.0001, ∗∗∗∗ p < 0.0001 by one-way ANOVA. BSA, bovine serum albumin; HA, hemagglutinin; hCD25, human CD25; HEK293T, human embryonic kidney 293T cell line; IL, interleukin; STAT5, signal transducer and activator of transcription 5.

Journal: The Journal of Biological Chemistry

Article Title: A CD25–chemokine receptor complex initiates noncanonical IL-2 signaling

doi: 10.1016/j.jbc.2025.110981

Figure Lengend Snippet: IL-2(E52K) does not support the assembly of the hCD25–CCR7 complex but supports canonical IL-2 signaling. A, 7G7B6 triggers IL-2-dependent hCD25–CCR7 complex. Anti-hCD25 antibodies (5 μg/ml), 7G7B6 or BC96, were incubated with HA-hCD25–expressing HEK293T cells in the presence or the absence of 1 μg/ml IL-2 and following lysis and immunoprecipitation with anti-HA were assayed for captured CCR7 or HA-hCD25 by immunoblotting. Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and HA-hCD25 from three independent experiments. B, IL-2(E52K) does not support the 7G7B6-induced the hCD25–CCR7 complex. IL-2(E52K) or wildtype IL-2 was assayed for capacity to support the 7G7B6-induced CD25–CCR7 complex as described in A . Scatter plots on the right show the mean (horizontal line) quantified intensities of CCR7 and CD25 from three independent experiments. C, IL2(E52K) mutation does not reduce binding of IL-2 to hCD25. Microplates coated with recombinant hCD25 extracellular domain or BSA were incubated with the indicated concentrations of IL-2 WT or IL-2(E52K), and bound IL-2 was quantified by ELISA. D, IL-2(E52K) triggers canonical IL-2 signaling. IL2Rα + YT-1 cells were stimulated with varying concentrations of IL-2 WT or IL-2(E52K) (for 30 min at 37 °C, followed by staining with APC-anti–phospho-STAT5 and analysis by flow cytometry (mean ± SEM; N = 3). ns, not significant, ∗∗∗ p < 0.0001, ∗∗∗∗ p < 0.0001 by one-way ANOVA. BSA, bovine serum albumin; HA, hemagglutinin; hCD25, human CD25; HEK293T, human embryonic kidney 293T cell line; IL, interleukin; STAT5, signal transducer and activator of transcription 5.

Article Snippet: Microplates (Greiner Bio-One) were coated with hCD25 (2 μg/ml) in carbonate/bicarbonate coating buffer (pH 9.2) and blocked with 2% bovine serum albumin.

Techniques: Incubation, Expressing, Lysis, Immunoprecipitation, Western Blot, Mutagenesis, Binding Assay, Recombinant, Enzyme-linked Immunosorbent Assay, Staining, Flow Cytometry