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vegfr2 antibody for staining af357  (R&D Systems)


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    R&D Systems vegfr2 antibody for staining af357
    Activin reduces expression of Rab11. A: Diagram of <t>VEGFR2</t> trafficking. Vascular endothelial growth factor (VEGF)–mediated activation of VEGFR2 triggers its internalization and trafficking. Rabs govern trafficking decisions that result in the degradation or recycling of VEGFR2. The destination of the activated VEGFR2, as well as its interaction with protein tyrosine phosphatase (PTP) 1b, influences VEGF-induced signaling. B: Confluent human retinal endothelial cells (HRECs) were treated for 24 hours with either vehicle [0.1% bovine serum albumin (BSA) in water; black bar] or activin (50 ng/mL; gray bar), harvested, and subjected to quantitative real-time PCR analysis. The resulting data were normalized to ACTB (β-actin) and expressed as relative expression. The data in the bar graph are the results of a single representative experiment. At least three independent experiments showed similar results. C: Same as B , except cells were harvested and subjected to Western blot analysis using the indicated antibodies. The images are representative Western blot analyses; the bar graphs show the mean expression in response to activin in three to five independent experiments. The molecular mass of Rab5 is 24 kDa; RABEP2, 64 kDa; Rab7, 2 kDa 2; Rab11, 25 kDa. RasGAP (124 kDa) was included as a loading control. D: Immunostaining for VEGFR2 (green) and Rab11 (red) in HRECs pretreated with activin (50 ng/mL) or vehicle for 24 hours before treatment with VEGF (100 ng/mL) or vehicle [phosphate-buffered saline (PBS)] for 30 minutes. The graph depicts the percentage of VEGFR2 that colocalized with Rab11. Activin reduced VEGFR2-Rab11 colocalization in VEGF-treated cells in two independent experiments; the same trend was observed in a third experiment, which did not reach statistical significance. The difference in means between two groups was analyzed using t -test. Data are given as means ± SEM ( B – D ). n = 4 to 6 fields of view per group. ∗ P < 0.05, ∗∗ P < 0.01, and ∗∗∗ P < 0.001. Scale bars = 10 μm ( D ). NS, not statistically significant.
    Vegfr2 Antibody For Staining Af357, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 105 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/vegfr2+antibody+for+staining+af357/Human+VEGFR2%2FKDR%2FFlk-1+Antibody/pmc12489374-31-7-15
    Average 93 stars, based on 105 article reviews
    vegfr2 antibody for staining af357 - by Bioz Stars, 2026-08
    93/100 stars

    Images

    1) Product Images from "Activin A Prevents Hyperresponsiveness to Vascular Endothelial Growth Factor in Pathologic Blood Vessels by Perturbing the Trafficking of Activated Vascular Endothelial Growth Factor Receptor 2"

    Article Title: Activin A Prevents Hyperresponsiveness to Vascular Endothelial Growth Factor in Pathologic Blood Vessels by Perturbing the Trafficking of Activated Vascular Endothelial Growth Factor Receptor 2

    Journal: The American Journal of Pathology

    doi: 10.1016/j.ajpath.2025.05.022

    Activin reduces expression of Rab11. A: Diagram of VEGFR2 trafficking. Vascular endothelial growth factor (VEGF)–mediated activation of VEGFR2 triggers its internalization and trafficking. Rabs govern trafficking decisions that result in the degradation or recycling of VEGFR2. The destination of the activated VEGFR2, as well as its interaction with protein tyrosine phosphatase (PTP) 1b, influences VEGF-induced signaling. B: Confluent human retinal endothelial cells (HRECs) were treated for 24 hours with either vehicle [0.1% bovine serum albumin (BSA) in water; black bar] or activin (50 ng/mL; gray bar), harvested, and subjected to quantitative real-time PCR analysis. The resulting data were normalized to ACTB (β-actin) and expressed as relative expression. The data in the bar graph are the results of a single representative experiment. At least three independent experiments showed similar results. C: Same as B , except cells were harvested and subjected to Western blot analysis using the indicated antibodies. The images are representative Western blot analyses; the bar graphs show the mean expression in response to activin in three to five independent experiments. The molecular mass of Rab5 is 24 kDa; RABEP2, 64 kDa; Rab7, 2 kDa 2; Rab11, 25 kDa. RasGAP (124 kDa) was included as a loading control. D: Immunostaining for VEGFR2 (green) and Rab11 (red) in HRECs pretreated with activin (50 ng/mL) or vehicle for 24 hours before treatment with VEGF (100 ng/mL) or vehicle [phosphate-buffered saline (PBS)] for 30 minutes. The graph depicts the percentage of VEGFR2 that colocalized with Rab11. Activin reduced VEGFR2-Rab11 colocalization in VEGF-treated cells in two independent experiments; the same trend was observed in a third experiment, which did not reach statistical significance. The difference in means between two groups was analyzed using t -test. Data are given as means ± SEM ( B – D ). n = 4 to 6 fields of view per group. ∗ P < 0.05, ∗∗ P < 0.01, and ∗∗∗ P < 0.001. Scale bars = 10 μm ( D ). NS, not statistically significant.
    Figure Legend Snippet: Activin reduces expression of Rab11. A: Diagram of VEGFR2 trafficking. Vascular endothelial growth factor (VEGF)–mediated activation of VEGFR2 triggers its internalization and trafficking. Rabs govern trafficking decisions that result in the degradation or recycling of VEGFR2. The destination of the activated VEGFR2, as well as its interaction with protein tyrosine phosphatase (PTP) 1b, influences VEGF-induced signaling. B: Confluent human retinal endothelial cells (HRECs) were treated for 24 hours with either vehicle [0.1% bovine serum albumin (BSA) in water; black bar] or activin (50 ng/mL; gray bar), harvested, and subjected to quantitative real-time PCR analysis. The resulting data were normalized to ACTB (β-actin) and expressed as relative expression. The data in the bar graph are the results of a single representative experiment. At least three independent experiments showed similar results. C: Same as B , except cells were harvested and subjected to Western blot analysis using the indicated antibodies. The images are representative Western blot analyses; the bar graphs show the mean expression in response to activin in three to five independent experiments. The molecular mass of Rab5 is 24 kDa; RABEP2, 64 kDa; Rab7, 2 kDa 2; Rab11, 25 kDa. RasGAP (124 kDa) was included as a loading control. D: Immunostaining for VEGFR2 (green) and Rab11 (red) in HRECs pretreated with activin (50 ng/mL) or vehicle for 24 hours before treatment with VEGF (100 ng/mL) or vehicle [phosphate-buffered saline (PBS)] for 30 minutes. The graph depicts the percentage of VEGFR2 that colocalized with Rab11. Activin reduced VEGFR2-Rab11 colocalization in VEGF-treated cells in two independent experiments; the same trend was observed in a third experiment, which did not reach statistical significance. The difference in means between two groups was analyzed using t -test. Data are given as means ± SEM ( B – D ). n = 4 to 6 fields of view per group. ∗ P < 0.05, ∗∗ P < 0.01, and ∗∗∗ P < 0.001. Scale bars = 10 μm ( D ). NS, not statistically significant.

    Techniques Used: Expressing, Activation Assay, Real-time Polymerase Chain Reaction, Western Blot, Control, Immunostaining, Saline

    Activin suppresses VEGFR2 phosphorylation after ≥30 minutes of stimulation with vascular endothelial growth factor (VEGF). A: Cells were pretreated for 24 hours with either activin (50 ng/mL; +) or vehicle [0.1% bovine serum albumin (BSA) in water; −] and were then stimulated with phosphate-buffered saline (PBS; −) or VEGF (100 ng/mL; +) for the indicated durations. Cells were then harvested, and clarified lysates were subjected to Western blot analysis using the indicated antibodies. The phosphorylated VEGFR2 (pVEGFR2) band signal was quantified and normalized to the indicated loading control. The bar graph represents the mean ratio of normalized VEGFR2 signal in resting and VEGF-stimulated cells from at least five independent experiments. B and C: Confluent human retinal endothelial cells (HRECs) were pretreated with activin vehicle (0.1% BSA in water; −) or activin (50 ng/mL; +) for 24 hours and then stimulated with PBS (−) or VEGF (100 ng/mL; +) for the indicated duration. Because the duration of stimulation with VEGF was so long in C (6 hours), the cells were pretreated with activin for only 18 hours so that the total duration of treatment with activin at the time of harvest would match the other panels in this series of experiments. Cells were harvested, and clarified lysates were subjected to Western blot analysis using the indicated antibodies. The signal intensity of the phosphorylated Y1175 (p-Y1175) band was quantified and normalized to the loading control (β-actin or RasGAP). The bar graph shows the mean ratio of the normalized p-Y1175 signal in resting and VEGF-stimulated cells from at least three independent experiments. Data are given as means ± SEM ( A – C ). ∗ P < 0.05. NS, not statistically significant.
    Figure Legend Snippet: Activin suppresses VEGFR2 phosphorylation after ≥30 minutes of stimulation with vascular endothelial growth factor (VEGF). A: Cells were pretreated for 24 hours with either activin (50 ng/mL; +) or vehicle [0.1% bovine serum albumin (BSA) in water; −] and were then stimulated with phosphate-buffered saline (PBS; −) or VEGF (100 ng/mL; +) for the indicated durations. Cells were then harvested, and clarified lysates were subjected to Western blot analysis using the indicated antibodies. The phosphorylated VEGFR2 (pVEGFR2) band signal was quantified and normalized to the indicated loading control. The bar graph represents the mean ratio of normalized VEGFR2 signal in resting and VEGF-stimulated cells from at least five independent experiments. B and C: Confluent human retinal endothelial cells (HRECs) were pretreated with activin vehicle (0.1% BSA in water; −) or activin (50 ng/mL; +) for 24 hours and then stimulated with PBS (−) or VEGF (100 ng/mL; +) for the indicated duration. Because the duration of stimulation with VEGF was so long in C (6 hours), the cells were pretreated with activin for only 18 hours so that the total duration of treatment with activin at the time of harvest would match the other panels in this series of experiments. Cells were harvested, and clarified lysates were subjected to Western blot analysis using the indicated antibodies. The signal intensity of the phosphorylated Y1175 (p-Y1175) band was quantified and normalized to the loading control (β-actin or RasGAP). The bar graph shows the mean ratio of the normalized p-Y1175 signal in resting and VEGF-stimulated cells from at least three independent experiments. Data are given as means ± SEM ( A – C ). ∗ P < 0.05. NS, not statistically significant.

    Techniques Used: Phospho-proteomics, Saline, Western Blot, Control



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    vegfr2 antibody for staining af357  (R&D Systems)
    93
    R&D Systems vegfr2 antibody for staining af357
    Activin reduces expression of Rab11. A: Diagram of <t>VEGFR2</t> trafficking. Vascular endothelial growth factor (VEGF)–mediated activation of VEGFR2 triggers its internalization and trafficking. Rabs govern trafficking decisions that result in the degradation or recycling of VEGFR2. The destination of the activated VEGFR2, as well as its interaction with protein tyrosine phosphatase (PTP) 1b, influences VEGF-induced signaling. B: Confluent human retinal endothelial cells (HRECs) were treated for 24 hours with either vehicle [0.1% bovine serum albumin (BSA) in water; black bar] or activin (50 ng/mL; gray bar), harvested, and subjected to quantitative real-time PCR analysis. The resulting data were normalized to ACTB (β-actin) and expressed as relative expression. The data in the bar graph are the results of a single representative experiment. At least three independent experiments showed similar results. C: Same as B , except cells were harvested and subjected to Western blot analysis using the indicated antibodies. The images are representative Western blot analyses; the bar graphs show the mean expression in response to activin in three to five independent experiments. The molecular mass of Rab5 is 24 kDa; RABEP2, 64 kDa; Rab7, 2 kDa 2; Rab11, 25 kDa. RasGAP (124 kDa) was included as a loading control. D: Immunostaining for VEGFR2 (green) and Rab11 (red) in HRECs pretreated with activin (50 ng/mL) or vehicle for 24 hours before treatment with VEGF (100 ng/mL) or vehicle [phosphate-buffered saline (PBS)] for 30 minutes. The graph depicts the percentage of VEGFR2 that colocalized with Rab11. Activin reduced VEGFR2-Rab11 colocalization in VEGF-treated cells in two independent experiments; the same trend was observed in a third experiment, which did not reach statistical significance. The difference in means between two groups was analyzed using t -test. Data are given as means ± SEM ( B – D ). n = 4 to 6 fields of view per group. ∗ P < 0.05, ∗∗ P < 0.01, and ∗∗∗ P < 0.001. Scale bars = 10 μm ( D ). NS, not statistically significant.
    Vegfr2 Antibody For Staining Af357, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/vegfr2+antibody+for+staining+af357/Human+VEGFR2%2FKDR%2FFlk-1+Antibody/pmc12489374-31-7-15
    Average 93 stars, based on 1 article reviews
    vegfr2 antibody for staining af357 - by Bioz Stars, 2026-08
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    Activin reduces expression of Rab11. A: Diagram of VEGFR2 trafficking. Vascular endothelial growth factor (VEGF)–mediated activation of VEGFR2 triggers its internalization and trafficking. Rabs govern trafficking decisions that result in the degradation or recycling of VEGFR2. The destination of the activated VEGFR2, as well as its interaction with protein tyrosine phosphatase (PTP) 1b, influences VEGF-induced signaling. B: Confluent human retinal endothelial cells (HRECs) were treated for 24 hours with either vehicle [0.1% bovine serum albumin (BSA) in water; black bar] or activin (50 ng/mL; gray bar), harvested, and subjected to quantitative real-time PCR analysis. The resulting data were normalized to ACTB (β-actin) and expressed as relative expression. The data in the bar graph are the results of a single representative experiment. At least three independent experiments showed similar results. C: Same as B , except cells were harvested and subjected to Western blot analysis using the indicated antibodies. The images are representative Western blot analyses; the bar graphs show the mean expression in response to activin in three to five independent experiments. The molecular mass of Rab5 is 24 kDa; RABEP2, 64 kDa; Rab7, 2 kDa 2; Rab11, 25 kDa. RasGAP (124 kDa) was included as a loading control. D: Immunostaining for VEGFR2 (green) and Rab11 (red) in HRECs pretreated with activin (50 ng/mL) or vehicle for 24 hours before treatment with VEGF (100 ng/mL) or vehicle [phosphate-buffered saline (PBS)] for 30 minutes. The graph depicts the percentage of VEGFR2 that colocalized with Rab11. Activin reduced VEGFR2-Rab11 colocalization in VEGF-treated cells in two independent experiments; the same trend was observed in a third experiment, which did not reach statistical significance. The difference in means between two groups was analyzed using t -test. Data are given as means ± SEM ( B – D ). n = 4 to 6 fields of view per group. ∗ P < 0.05, ∗∗ P < 0.01, and ∗∗∗ P < 0.001. Scale bars = 10 μm ( D ). NS, not statistically significant.

    Journal: The American Journal of Pathology

    Article Title: Activin A Prevents Hyperresponsiveness to Vascular Endothelial Growth Factor in Pathologic Blood Vessels by Perturbing the Trafficking of Activated Vascular Endothelial Growth Factor Receptor 2

    doi: 10.1016/j.ajpath.2025.05.022

    Figure Lengend Snippet: Activin reduces expression of Rab11. A: Diagram of VEGFR2 trafficking. Vascular endothelial growth factor (VEGF)–mediated activation of VEGFR2 triggers its internalization and trafficking. Rabs govern trafficking decisions that result in the degradation or recycling of VEGFR2. The destination of the activated VEGFR2, as well as its interaction with protein tyrosine phosphatase (PTP) 1b, influences VEGF-induced signaling. B: Confluent human retinal endothelial cells (HRECs) were treated for 24 hours with either vehicle [0.1% bovine serum albumin (BSA) in water; black bar] or activin (50 ng/mL; gray bar), harvested, and subjected to quantitative real-time PCR analysis. The resulting data were normalized to ACTB (β-actin) and expressed as relative expression. The data in the bar graph are the results of a single representative experiment. At least three independent experiments showed similar results. C: Same as B , except cells were harvested and subjected to Western blot analysis using the indicated antibodies. The images are representative Western blot analyses; the bar graphs show the mean expression in response to activin in three to five independent experiments. The molecular mass of Rab5 is 24 kDa; RABEP2, 64 kDa; Rab7, 2 kDa 2; Rab11, 25 kDa. RasGAP (124 kDa) was included as a loading control. D: Immunostaining for VEGFR2 (green) and Rab11 (red) in HRECs pretreated with activin (50 ng/mL) or vehicle for 24 hours before treatment with VEGF (100 ng/mL) or vehicle [phosphate-buffered saline (PBS)] for 30 minutes. The graph depicts the percentage of VEGFR2 that colocalized with Rab11. Activin reduced VEGFR2-Rab11 colocalization in VEGF-treated cells in two independent experiments; the same trend was observed in a third experiment, which did not reach statistical significance. The difference in means between two groups was analyzed using t -test. Data are given as means ± SEM ( B – D ). n = 4 to 6 fields of view per group. ∗ P < 0.05, ∗∗ P < 0.01, and ∗∗∗ P < 0.001. Scale bars = 10 μm ( D ). NS, not statistically significant.

    Article Snippet: Human vascular endothelial (VE)–cadherin antibody (MAB9381-SP) and VEGFR2 antibody for staining (AF357) were purchased from R&D Systems (Minneapolis, MN).

    Techniques: Expressing, Activation Assay, Real-time Polymerase Chain Reaction, Western Blot, Control, Immunostaining, Saline

    Activin suppresses VEGFR2 phosphorylation after ≥30 minutes of stimulation with vascular endothelial growth factor (VEGF). A: Cells were pretreated for 24 hours with either activin (50 ng/mL; +) or vehicle [0.1% bovine serum albumin (BSA) in water; −] and were then stimulated with phosphate-buffered saline (PBS; −) or VEGF (100 ng/mL; +) for the indicated durations. Cells were then harvested, and clarified lysates were subjected to Western blot analysis using the indicated antibodies. The phosphorylated VEGFR2 (pVEGFR2) band signal was quantified and normalized to the indicated loading control. The bar graph represents the mean ratio of normalized VEGFR2 signal in resting and VEGF-stimulated cells from at least five independent experiments. B and C: Confluent human retinal endothelial cells (HRECs) were pretreated with activin vehicle (0.1% BSA in water; −) or activin (50 ng/mL; +) for 24 hours and then stimulated with PBS (−) or VEGF (100 ng/mL; +) for the indicated duration. Because the duration of stimulation with VEGF was so long in C (6 hours), the cells were pretreated with activin for only 18 hours so that the total duration of treatment with activin at the time of harvest would match the other panels in this series of experiments. Cells were harvested, and clarified lysates were subjected to Western blot analysis using the indicated antibodies. The signal intensity of the phosphorylated Y1175 (p-Y1175) band was quantified and normalized to the loading control (β-actin or RasGAP). The bar graph shows the mean ratio of the normalized p-Y1175 signal in resting and VEGF-stimulated cells from at least three independent experiments. Data are given as means ± SEM ( A – C ). ∗ P < 0.05. NS, not statistically significant.

    Journal: The American Journal of Pathology

    Article Title: Activin A Prevents Hyperresponsiveness to Vascular Endothelial Growth Factor in Pathologic Blood Vessels by Perturbing the Trafficking of Activated Vascular Endothelial Growth Factor Receptor 2

    doi: 10.1016/j.ajpath.2025.05.022

    Figure Lengend Snippet: Activin suppresses VEGFR2 phosphorylation after ≥30 minutes of stimulation with vascular endothelial growth factor (VEGF). A: Cells were pretreated for 24 hours with either activin (50 ng/mL; +) or vehicle [0.1% bovine serum albumin (BSA) in water; −] and were then stimulated with phosphate-buffered saline (PBS; −) or VEGF (100 ng/mL; +) for the indicated durations. Cells were then harvested, and clarified lysates were subjected to Western blot analysis using the indicated antibodies. The phosphorylated VEGFR2 (pVEGFR2) band signal was quantified and normalized to the indicated loading control. The bar graph represents the mean ratio of normalized VEGFR2 signal in resting and VEGF-stimulated cells from at least five independent experiments. B and C: Confluent human retinal endothelial cells (HRECs) were pretreated with activin vehicle (0.1% BSA in water; −) or activin (50 ng/mL; +) for 24 hours and then stimulated with PBS (−) or VEGF (100 ng/mL; +) for the indicated duration. Because the duration of stimulation with VEGF was so long in C (6 hours), the cells were pretreated with activin for only 18 hours so that the total duration of treatment with activin at the time of harvest would match the other panels in this series of experiments. Cells were harvested, and clarified lysates were subjected to Western blot analysis using the indicated antibodies. The signal intensity of the phosphorylated Y1175 (p-Y1175) band was quantified and normalized to the loading control (β-actin or RasGAP). The bar graph shows the mean ratio of the normalized p-Y1175 signal in resting and VEGF-stimulated cells from at least three independent experiments. Data are given as means ± SEM ( A – C ). ∗ P < 0.05. NS, not statistically significant.

    Article Snippet: Human vascular endothelial (VE)–cadherin antibody (MAB9381-SP) and VEGFR2 antibody for staining (AF357) were purchased from R&D Systems (Minneapolis, MN).

    Techniques: Phospho-proteomics, Saline, Western Blot, Control