vegfr2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc vegfr2
    Summary of network modules
    Vegfr2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "A genome-wide association study in autoimmune neurological syndromes with anti-GAD65 autoantibodies"

    Article Title: A genome-wide association study in autoimmune neurological syndromes with anti-GAD65 autoantibodies

    Journal: Brain

    doi: 10.1093/brain/awac119

    Summary of network modules
    Figure Legend Snippet: Summary of network modules

    Techniques Used: Transduction, Activity Assay

    vegfr2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc vegfr2
    Expression of integrin αvβ6, tissue factor, PARP-1, uPAR, VEGFR1, EpCAM, <t>VEGFR2,</t> Cathepsin E and integrin αvβ3 in primary tumor tissue of OSCC.
    Vegfr2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Potential of uPAR, αvβ6 Integrin, and Tissue Factor as Targets for Molecular Imaging of Oral Squamous Cell Carcinoma: Evaluation of Nine Targets in Primary Tumors and Metastases by Immunohistochemistry"

    Article Title: Potential of uPAR, αvβ6 Integrin, and Tissue Factor as Targets for Molecular Imaging of Oral Squamous Cell Carcinoma: Evaluation of Nine Targets in Primary Tumors and Metastases by Immunohistochemistry

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms24043853

    Expression of integrin αvβ6, tissue factor, PARP-1, uPAR, VEGFR1, EpCAM, VEGFR2, Cathepsin E and integrin αvβ3 in primary tumor tissue of OSCC.
    Figure Legend Snippet: Expression of integrin αvβ6, tissue factor, PARP-1, uPAR, VEGFR1, EpCAM, VEGFR2, Cathepsin E and integrin αvβ3 in primary tumor tissue of OSCC.

    Techniques Used: Expressing

    Median and interquartile ranges of intensity, proportion, and total immune staining scores for each target in primary tumor, lymph node metastases, and tissue from local recurrence.
    Figure Legend Snippet: Median and interquartile ranges of intensity, proportion, and total immune staining scores for each target in primary tumor, lymph node metastases, and tissue from local recurrence.

    Techniques Used: Staining

    Overview of the expression pattern for all nine included targets.
    Figure Legend Snippet: Overview of the expression pattern for all nine included targets.

    Techniques Used: Expressing

    Primary antibodies used for immunohistochemistry.
    Figure Legend Snippet: Primary antibodies used for immunohistochemistry.

    Techniques Used: Immunohistochemistry, Staining

    vegfr2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc vegfr2
    Andrographolide inhibits embryonic hyaloid vascular endothelial <t>VEGFR2</t> expression during murine hyaloid vasculature development. (A) Hypoxia conditions were induced in HUVEC-C by 200 μM CoCl 2 treatment following andrographolide treatment. Transcription levels of HIFs and VEGFR2 were evaluated by Real-time PCR ( n = 6). (B) Under hypoxia conditions, HUVEC-C was treated with different doses of andrographolide (1 μM, 5 μM and 10 μM); VEGFR2 protein levels were determined by western blotting. (C) The quantification of VEGFR2 protein levels in (B) ( n = 6). (D) Hypoxia conditions were induced in HUVEC-C by 200 μM CoCl 2 treatment, following 5 μM andrographolide treatment. Total protein harvested at 3, 6, 12, 24, and 36 h, and western blotting was performed to determine VEGFR2 expression. (E) The quantification of relative VEGFR2 protein levels in (D) ( n = 6). (F) Immunofluorescence staining against VEGFR2 and CD31 antibodies was performed to evaluate hyaloid vascular endothelial VEGFR2 expression at E18.5 after andrographolide treatment. (G) The quantification of hyaloid vascular endothelial VEGFR2 expression at E18.5 after andrographolide treatment ( n = 6). Quantitative data presented as mean ± SEM, * p < 0.05.
    Vegfr2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Andrographolide suppresses hypoxia-induced embryonic hyaloid vascular system development through HIF-1a/VEGFR2 signaling pathway"

    Article Title: Andrographolide suppresses hypoxia-induced embryonic hyaloid vascular system development through HIF-1a/VEGFR2 signaling pathway

    Journal: Frontiers in Cardiovascular Medicine

    doi: 10.3389/fcvm.2023.1090938

    Andrographolide inhibits embryonic hyaloid vascular endothelial VEGFR2 expression during murine hyaloid vasculature development. (A) Hypoxia conditions were induced in HUVEC-C by 200 μM CoCl 2 treatment following andrographolide treatment. Transcription levels of HIFs and VEGFR2 were evaluated by Real-time PCR ( n = 6). (B) Under hypoxia conditions, HUVEC-C was treated with different doses of andrographolide (1 μM, 5 μM and 10 μM); VEGFR2 protein levels were determined by western blotting. (C) The quantification of VEGFR2 protein levels in (B) ( n = 6). (D) Hypoxia conditions were induced in HUVEC-C by 200 μM CoCl 2 treatment, following 5 μM andrographolide treatment. Total protein harvested at 3, 6, 12, 24, and 36 h, and western blotting was performed to determine VEGFR2 expression. (E) The quantification of relative VEGFR2 protein levels in (D) ( n = 6). (F) Immunofluorescence staining against VEGFR2 and CD31 antibodies was performed to evaluate hyaloid vascular endothelial VEGFR2 expression at E18.5 after andrographolide treatment. (G) The quantification of hyaloid vascular endothelial VEGFR2 expression at E18.5 after andrographolide treatment ( n = 6). Quantitative data presented as mean ± SEM, * p < 0.05.
    Figure Legend Snippet: Andrographolide inhibits embryonic hyaloid vascular endothelial VEGFR2 expression during murine hyaloid vasculature development. (A) Hypoxia conditions were induced in HUVEC-C by 200 μM CoCl 2 treatment following andrographolide treatment. Transcription levels of HIFs and VEGFR2 were evaluated by Real-time PCR ( n = 6). (B) Under hypoxia conditions, HUVEC-C was treated with different doses of andrographolide (1 μM, 5 μM and 10 μM); VEGFR2 protein levels were determined by western blotting. (C) The quantification of VEGFR2 protein levels in (B) ( n = 6). (D) Hypoxia conditions were induced in HUVEC-C by 200 μM CoCl 2 treatment, following 5 μM andrographolide treatment. Total protein harvested at 3, 6, 12, 24, and 36 h, and western blotting was performed to determine VEGFR2 expression. (E) The quantification of relative VEGFR2 protein levels in (D) ( n = 6). (F) Immunofluorescence staining against VEGFR2 and CD31 antibodies was performed to evaluate hyaloid vascular endothelial VEGFR2 expression at E18.5 after andrographolide treatment. (G) The quantification of hyaloid vascular endothelial VEGFR2 expression at E18.5 after andrographolide treatment ( n = 6). Quantitative data presented as mean ± SEM, * p < 0.05.

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction, Western Blot, Immunofluorescence, Staining

    Andrographolide potentially interacts with HIF-1a and VEGFR2 in embryonic hyaloid vascular endothelial cells. (A) Hypoxia conditions were induced by 200 μM CoCl 2 treatment. Immunofluorescence staining against HIF-1a and VEGFR2 antibodies was used to validate co-localization expression of HIF-1a and VEGFR2 in HUVEC-C. (B) Immunofluorescence staining against HIF-1a and VEGFR2 antibodies was used to validate co-localization expression of HIF-1a and VEGFR2 in embryonic retinal endothelial at E18.5. (C) Molecular docking simulation was performed to evaluate the binding energy of andrographolide with HIF-1a and VEGFR2 using Autodock Vina 1.5.6 software developed by Olson’s research group. Andrographolide worked as receptor, HIF-1a and VEGFR2 were used as ligands to detect the docking sites between receptors and ligands. The three-dimensional structures of HIF-1a and VEGFR2 were obtained from the RCSBPDB database ( http://www.rcsb.org/ ). When a binding energy value was less than zero, those proteins were considered spontaneously binding and interacting with each other. (D) The binding energy of andrographolide with HIF-1a and VEGFR2 was based on Molecular docking simulation. (E) Hypoxia conditions were induced in HUVEC by 200 μM CoCl 2 treatment. The interaction between HIF-1a and VEGFR2 was validated by co-immunoprecipitation.
    Figure Legend Snippet: Andrographolide potentially interacts with HIF-1a and VEGFR2 in embryonic hyaloid vascular endothelial cells. (A) Hypoxia conditions were induced by 200 μM CoCl 2 treatment. Immunofluorescence staining against HIF-1a and VEGFR2 antibodies was used to validate co-localization expression of HIF-1a and VEGFR2 in HUVEC-C. (B) Immunofluorescence staining against HIF-1a and VEGFR2 antibodies was used to validate co-localization expression of HIF-1a and VEGFR2 in embryonic retinal endothelial at E18.5. (C) Molecular docking simulation was performed to evaluate the binding energy of andrographolide with HIF-1a and VEGFR2 using Autodock Vina 1.5.6 software developed by Olson’s research group. Andrographolide worked as receptor, HIF-1a and VEGFR2 were used as ligands to detect the docking sites between receptors and ligands. The three-dimensional structures of HIF-1a and VEGFR2 were obtained from the RCSBPDB database ( http://www.rcsb.org/ ). When a binding energy value was less than zero, those proteins were considered spontaneously binding and interacting with each other. (D) The binding energy of andrographolide with HIF-1a and VEGFR2 was based on Molecular docking simulation. (E) Hypoxia conditions were induced in HUVEC by 200 μM CoCl 2 treatment. The interaction between HIF-1a and VEGFR2 was validated by co-immunoprecipitation.

    Techniques Used: Immunofluorescence, Staining, Expressing, Binding Assay, Software, Immunoprecipitation

    Interruption VEGF receptors further suppresses andrographolide mediated embryonic hyaloid vasculature development. (A) Hypoxia conditions were induced in HUVEC-C by 200 μM CoCl 2 treatment and VEGFR2 inhibition performed by Ki8751 treatment (Ki8751, a VEGFR2 inhibitor). Following BrdU labeling reagent labeled for 24 h after treatment of andrographolide. Immunofluorescence staining was performed to determine BrdU incorporation. (B) The quantification of BrdU positive cells from (A) ( n = 5). (C) Boyden chamber cell migration assay was performed to validate the role of VEGFR2 on cell migration after VEGFR2 inhibition following andrographolide under hypoxia conditions. (D) The quantification of migrated HUVEC-C from (C) ( n = 5). (E) Matrigel-based tube formation assay was performed to validate the role of VEGFR2 on tube formation after VEGFR2 inhibition with andrographolide treatment under hypoxia conditions. (F) Spheroid sprouting assay was performed to validate the role of VEGFR2 after VEGFR2 inhibition with andrographolide treatment under hypoxia conditions. (G) The schematic diagram indicates how andrographolide regulates embryonic hyaloid vascular development.
    Figure Legend Snippet: Interruption VEGF receptors further suppresses andrographolide mediated embryonic hyaloid vasculature development. (A) Hypoxia conditions were induced in HUVEC-C by 200 μM CoCl 2 treatment and VEGFR2 inhibition performed by Ki8751 treatment (Ki8751, a VEGFR2 inhibitor). Following BrdU labeling reagent labeled for 24 h after treatment of andrographolide. Immunofluorescence staining was performed to determine BrdU incorporation. (B) The quantification of BrdU positive cells from (A) ( n = 5). (C) Boyden chamber cell migration assay was performed to validate the role of VEGFR2 on cell migration after VEGFR2 inhibition following andrographolide under hypoxia conditions. (D) The quantification of migrated HUVEC-C from (C) ( n = 5). (E) Matrigel-based tube formation assay was performed to validate the role of VEGFR2 on tube formation after VEGFR2 inhibition with andrographolide treatment under hypoxia conditions. (F) Spheroid sprouting assay was performed to validate the role of VEGFR2 after VEGFR2 inhibition with andrographolide treatment under hypoxia conditions. (G) The schematic diagram indicates how andrographolide regulates embryonic hyaloid vascular development.

    Techniques Used: Inhibition, Labeling, Immunofluorescence, Staining, BrdU Incorporation Assay, Cell Migration Assay, Migration, Tube Formation Assay

    rabbit monoclonal phospho vegfr2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit monoclonal phospho vegfr2
    VEGF-A and VEGFRs protein content in whole mice ovaries. Representative western blot images of VEGF-A isoforms (VEGF 164 and VEGF 120), VEGFR1, and <t>VEGFR2</t> total and phosphorylated form <t>(p-VEGFR2,)</t> of late-reproductive multiparous (LM) and virgin (LV), and post-reproductive multiparous (PM) and virgin (PV) mice ( A ). VEGF-A isoforms ( B ), VEGFR1 ( C ), and VEGFR2 ( D ) values are expressed as arbitrary units (a.u.), considering LM values arbitrarily as 1. The p-VEGFR2/VEGFR2 ( E ) values are expressed as percentages (%) of the ratio of phosphorylated/total protein. Bar graph data represent the mean ± SEM ( B – D ) and the mean percentage ± relative error ( E ) after normalization of each protein with the respective actin used as loading control of at least four independent determinations. (†) indicates significant difference ( p < 0.05) related to age (LM vs. PM; LV vs. PV); (*) indicates significant difference ( p < 0.05) related to parity status (LM vs. LV; PM vs. PV).
    Rabbit Monoclonal Phospho Vegfr2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Do Aging and Parity Affect VEGF-A/VEGFR Content and Signaling in the Ovary?—A Mouse Model Study"

    Article Title: Do Aging and Parity Affect VEGF-A/VEGFR Content and Signaling in the Ovary?—A Mouse Model Study

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms24043318

    VEGF-A and VEGFRs protein content in whole mice ovaries. Representative western blot images of VEGF-A isoforms (VEGF 164 and VEGF 120), VEGFR1, and VEGFR2 total and phosphorylated form (p-VEGFR2,) of late-reproductive multiparous (LM) and virgin (LV), and post-reproductive multiparous (PM) and virgin (PV) mice ( A ). VEGF-A isoforms ( B ), VEGFR1 ( C ), and VEGFR2 ( D ) values are expressed as arbitrary units (a.u.), considering LM values arbitrarily as 1. The p-VEGFR2/VEGFR2 ( E ) values are expressed as percentages (%) of the ratio of phosphorylated/total protein. Bar graph data represent the mean ± SEM ( B – D ) and the mean percentage ± relative error ( E ) after normalization of each protein with the respective actin used as loading control of at least four independent determinations. (†) indicates significant difference ( p < 0.05) related to age (LM vs. PM; LV vs. PV); (*) indicates significant difference ( p < 0.05) related to parity status (LM vs. LV; PM vs. PV).
    Figure Legend Snippet: VEGF-A and VEGFRs protein content in whole mice ovaries. Representative western blot images of VEGF-A isoforms (VEGF 164 and VEGF 120), VEGFR1, and VEGFR2 total and phosphorylated form (p-VEGFR2,) of late-reproductive multiparous (LM) and virgin (LV), and post-reproductive multiparous (PM) and virgin (PV) mice ( A ). VEGF-A isoforms ( B ), VEGFR1 ( C ), and VEGFR2 ( D ) values are expressed as arbitrary units (a.u.), considering LM values arbitrarily as 1. The p-VEGFR2/VEGFR2 ( E ) values are expressed as percentages (%) of the ratio of phosphorylated/total protein. Bar graph data represent the mean ± SEM ( B – D ) and the mean percentage ± relative error ( E ) after normalization of each protein with the respective actin used as loading control of at least four independent determinations. (†) indicates significant difference ( p < 0.05) related to age (LM vs. PM; LV vs. PV); (*) indicates significant difference ( p < 0.05) related to parity status (LM vs. LV; PM vs. PV).

    Techniques Used: Western Blot

    Tissue localization of VEGF-A and p-VEGFR2 in mouse ovaries. Representative images of VEGF-A ( A , B ) and p-VEGFR2 ( C , D ) immunoreactivity in post-reproductive multiparous (PM) and virgin (PV) ovaries. Negative controls (NC; E , F ) and H&E staining ( G , H ) are presented. White circles indicate the presence of areas with small vessels; white arrowheads indicate the presence of ovarian surface epithelium, which appear to be multi-layered in PV ovaries ( B , D ). Magnification: ×100.
    Figure Legend Snippet: Tissue localization of VEGF-A and p-VEGFR2 in mouse ovaries. Representative images of VEGF-A ( A , B ) and p-VEGFR2 ( C , D ) immunoreactivity in post-reproductive multiparous (PM) and virgin (PV) ovaries. Negative controls (NC; E , F ) and H&E staining ( G , H ) are presented. White circles indicate the presence of areas with small vessels; white arrowheads indicate the presence of ovarian surface epithelium, which appear to be multi-layered in PV ovaries ( B , D ). Magnification: ×100.

    Techniques Used: Staining

    VEGFR2 signaling pathway activation: total and phosphorylated ERK1/2 and p38 in whole mice ovaries. Representative western blot images of ERK1/2 and p38 total and phosphorylated form (p-ERK1/2 and p-p38, respectively) of late-reproductive multiparous (LM) and virgin (LV), and post-reproductive multiparous (PM) and virgin (PV) mice ( A ). ERK1/2 ( B ) and p38 ( D ), values are expressed as arbitrary units (a.u.), considering LM values arbitrarily as 1. The p-ERK1/2/ERK1/2 ( C ), and p-p38/p38 ( E ) values are expressed as percentages (%) of the ratio of phosphorylated/total protein. Bar graph data represent the mean ± SEM ( B , D ) and the mean percentage ± relative error ( C , E ) after normalization of each protein with the respective actin used as loading control of at least four independent determinations. (†) indicates significant difference ( p < 0.05) related to age (LM vs. PM; LV vs. PV); (*) indicates significant difference ( p < 0.05) related to parity status (LM vs. LV; PM vs. PV).
    Figure Legend Snippet: VEGFR2 signaling pathway activation: total and phosphorylated ERK1/2 and p38 in whole mice ovaries. Representative western blot images of ERK1/2 and p38 total and phosphorylated form (p-ERK1/2 and p-p38, respectively) of late-reproductive multiparous (LM) and virgin (LV), and post-reproductive multiparous (PM) and virgin (PV) mice ( A ). ERK1/2 ( B ) and p38 ( D ), values are expressed as arbitrary units (a.u.), considering LM values arbitrarily as 1. The p-ERK1/2/ERK1/2 ( C ), and p-p38/p38 ( E ) values are expressed as percentages (%) of the ratio of phosphorylated/total protein. Bar graph data represent the mean ± SEM ( B , D ) and the mean percentage ± relative error ( C , E ) after normalization of each protein with the respective actin used as loading control of at least four independent determinations. (†) indicates significant difference ( p < 0.05) related to age (LM vs. PM; LV vs. PV); (*) indicates significant difference ( p < 0.05) related to parity status (LM vs. LV; PM vs. PV).

    Techniques Used: Activation Assay, Western Blot

    vegfr2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc vegfr2
    PDA activates the VEGF signaling pathway after vascular injury. ( A ) HUVEC-Cs were treated with PDA (10 μM) for 24 h. The transcription levels of the VEGF family were evaluated with real-time PCR ( n = 6). ( B ) Western blotting was performed to determine the expression of <t>VEGFR2</t> in HUVECs after PDA (10 μM, 24 h) treatment at different doses, and the quantification data are evaluated in ( C ) ( n = 8). ( D ) IF staining was performed to detect the expression of VEGFR2 in the HUVECs after PDA (10 μM) treatment for 24 h, and the quantification data are evaluated in ( E ) ( n = 8). ( F ) IHC staining was performed against CD31 and VEGFR2 antibodies to evaluate the expression of VEGFR2 in a left carotid artery partial ligation model following PDA treatment for 28 days. Yellow arrows indicate regions containing CD31–positive and VEGFR2-positive vascular endothelial cells. The quantification data are evaluated in ( G ) ( n = 8). ( H ) IF staining was used to evaluate the expression of VEGFR2 in blood vessels within the anterior tibial muscle of mice that were intramuscularly injected with cardiotoxin and treated with PDA (20 mg/kg) for 7 consecutive days, and the quantification data are evaluated in ( I ) ( n = 8). Analytical data are expressed as means ± SEM * p < 0.05.
    Vegfr2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Potassium Dehydroandrograpolide Succinate Targets NRP1 Mediated VEGFR2/VE-Cadherin Signaling Pathway to Promote Endothelial Barrier Repair"

    Article Title: Potassium Dehydroandrograpolide Succinate Targets NRP1 Mediated VEGFR2/VE-Cadherin Signaling Pathway to Promote Endothelial Barrier Repair

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms24043096

    PDA activates the VEGF signaling pathway after vascular injury. ( A ) HUVEC-Cs were treated with PDA (10 μM) for 24 h. The transcription levels of the VEGF family were evaluated with real-time PCR ( n = 6). ( B ) Western blotting was performed to determine the expression of VEGFR2 in HUVECs after PDA (10 μM, 24 h) treatment at different doses, and the quantification data are evaluated in ( C ) ( n = 8). ( D ) IF staining was performed to detect the expression of VEGFR2 in the HUVECs after PDA (10 μM) treatment for 24 h, and the quantification data are evaluated in ( E ) ( n = 8). ( F ) IHC staining was performed against CD31 and VEGFR2 antibodies to evaluate the expression of VEGFR2 in a left carotid artery partial ligation model following PDA treatment for 28 days. Yellow arrows indicate regions containing CD31–positive and VEGFR2-positive vascular endothelial cells. The quantification data are evaluated in ( G ) ( n = 8). ( H ) IF staining was used to evaluate the expression of VEGFR2 in blood vessels within the anterior tibial muscle of mice that were intramuscularly injected with cardiotoxin and treated with PDA (20 mg/kg) for 7 consecutive days, and the quantification data are evaluated in ( I ) ( n = 8). Analytical data are expressed as means ± SEM * p < 0.05.
    Figure Legend Snippet: PDA activates the VEGF signaling pathway after vascular injury. ( A ) HUVEC-Cs were treated with PDA (10 μM) for 24 h. The transcription levels of the VEGF family were evaluated with real-time PCR ( n = 6). ( B ) Western blotting was performed to determine the expression of VEGFR2 in HUVECs after PDA (10 μM, 24 h) treatment at different doses, and the quantification data are evaluated in ( C ) ( n = 8). ( D ) IF staining was performed to detect the expression of VEGFR2 in the HUVECs after PDA (10 μM) treatment for 24 h, and the quantification data are evaluated in ( E ) ( n = 8). ( F ) IHC staining was performed against CD31 and VEGFR2 antibodies to evaluate the expression of VEGFR2 in a left carotid artery partial ligation model following PDA treatment for 28 days. Yellow arrows indicate regions containing CD31–positive and VEGFR2-positive vascular endothelial cells. The quantification data are evaluated in ( G ) ( n = 8). ( H ) IF staining was used to evaluate the expression of VEGFR2 in blood vessels within the anterior tibial muscle of mice that were intramuscularly injected with cardiotoxin and treated with PDA (20 mg/kg) for 7 consecutive days, and the quantification data are evaluated in ( I ) ( n = 8). Analytical data are expressed as means ± SEM * p < 0.05.

    Techniques Used: Real-time Polymerase Chain Reaction, Western Blot, Expressing, Staining, Immunohistochemistry, Ligation, Injection

    PDA regulates interactions between NRP1, VEGFR and VE-Cad within vascular endothelial cells. ( A ) Molecular docking simulation performed to evaluate the binding energy of PDA with NRP1, VEGFR2 and VE-Cad using Autodock Vina 1.5.6 software, which was developed by Olson’s research group. PDA worked as a receptor, and NRP1, VEGFR2 and VE-Cad were used as ligands to detect the docking sites between receptors and ligands. The three-dimensional structures of VEGFR2 and NRP1 were obtained from the RCSBPDB database ( http://www.rcsb.org/ , accessed on 16 August 2022) and that of VE-Cad was obtained from the SWISS-Model database ( http://swissmodel.expasy.org/ , accessed on 20 August 2022). When values for the binding energy were less than zero, those proteins were considered to spontaneously bind and interact with each other. ( B ) The binding energies of PDA with NRP1, VEGFR2 and VE-Cad were determined based on a molecular docking simulation. ( C ) IF staining of NRP1 and VEGFR2 was performed in the skeletal muscle injury model to determine their co-localization expression in vascular endothelial cells. ( D ) Immunofluorescence staining of NRP1 and VE-Cad was performed in the skeletal muscle injury model to determine their co-localization expression in vascular endothelial cells. ( E ) The interaction between NRP1, VEGFR2 and VE-Cad was validated using the CO-immunoprecipitation assay in HUVECs.
    Figure Legend Snippet: PDA regulates interactions between NRP1, VEGFR and VE-Cad within vascular endothelial cells. ( A ) Molecular docking simulation performed to evaluate the binding energy of PDA with NRP1, VEGFR2 and VE-Cad using Autodock Vina 1.5.6 software, which was developed by Olson’s research group. PDA worked as a receptor, and NRP1, VEGFR2 and VE-Cad were used as ligands to detect the docking sites between receptors and ligands. The three-dimensional structures of VEGFR2 and NRP1 were obtained from the RCSBPDB database ( http://www.rcsb.org/ , accessed on 16 August 2022) and that of VE-Cad was obtained from the SWISS-Model database ( http://swissmodel.expasy.org/ , accessed on 20 August 2022). When values for the binding energy were less than zero, those proteins were considered to spontaneously bind and interact with each other. ( B ) The binding energies of PDA with NRP1, VEGFR2 and VE-Cad were determined based on a molecular docking simulation. ( C ) IF staining of NRP1 and VEGFR2 was performed in the skeletal muscle injury model to determine their co-localization expression in vascular endothelial cells. ( D ) Immunofluorescence staining of NRP1 and VE-Cad was performed in the skeletal muscle injury model to determine their co-localization expression in vascular endothelial cells. ( E ) The interaction between NRP1, VEGFR2 and VE-Cad was validated using the CO-immunoprecipitation assay in HUVECs.

    Techniques Used: Binding Assay, Software, Staining, Expressing, Immunofluorescence, Co-Immunoprecipitation Assay

    PDA regulates vascular endothelial barrier function through the NRP1/VEGFR2/VE-Cad signaling pathway. ( A ) After knockdown of NRP1 in HUVECs, real-time PCR was performed to evaluate transcription levels of NRP1-, VEGFR2- and VE-Cad-related genes ( n = 6). ( B ) After knockdown of NRP1, HUVECs were treated with PDA (10 μM) for 24 h and real-time PCR was performed to evaluate transcription levels of NRP1-, VEGFR2- and VE-Cad-related genes ( n = 6). ( C ) After knockdown of NRP1, IF staining was performed to detect the expression of VE-Cad in the HUVECs following PDA (10 μM) treatment for 24 h, and the quantification data are evaluated in ( D ) ( n = 8). ( E ) After knockdown of NRP1, HUVECs were treated with PDA (10 μM) for 24 h and real-time PCR was performed to evaluate transcription levels of inflammation-related genes ( n = 6). ( F ) After knockdown of NRP1, HUVEC-C and THP-1 were co-cultured and treated with PDA (10 μM) for 12 h, and the quantification data are evaluated in ( G ). ( H ) Schematic diagram indicating that PDA promoted endothelial barrier repair in pathological vascular remodeling. Analytical data are expressed as means ± SEM * p < 0.05.
    Figure Legend Snippet: PDA regulates vascular endothelial barrier function through the NRP1/VEGFR2/VE-Cad signaling pathway. ( A ) After knockdown of NRP1 in HUVECs, real-time PCR was performed to evaluate transcription levels of NRP1-, VEGFR2- and VE-Cad-related genes ( n = 6). ( B ) After knockdown of NRP1, HUVECs were treated with PDA (10 μM) for 24 h and real-time PCR was performed to evaluate transcription levels of NRP1-, VEGFR2- and VE-Cad-related genes ( n = 6). ( C ) After knockdown of NRP1, IF staining was performed to detect the expression of VE-Cad in the HUVECs following PDA (10 μM) treatment for 24 h, and the quantification data are evaluated in ( D ) ( n = 8). ( E ) After knockdown of NRP1, HUVECs were treated with PDA (10 μM) for 24 h and real-time PCR was performed to evaluate transcription levels of inflammation-related genes ( n = 6). ( F ) After knockdown of NRP1, HUVEC-C and THP-1 were co-cultured and treated with PDA (10 μM) for 12 h, and the quantification data are evaluated in ( G ). ( H ) Schematic diagram indicating that PDA promoted endothelial barrier repair in pathological vascular remodeling. Analytical data are expressed as means ± SEM * p < 0.05.

    Techniques Used: Real-time Polymerase Chain Reaction, Staining, Expressing, Cell Culture

    vegfr2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc vegfr2
    PDA activates the VEGF signaling pathway after vascular injury. ( A ) HUVEC-Cs were treated with PDA (10 μM) for 24 h. The transcription levels of the VEGF family were evaluated with real-time PCR ( n = 6). ( B ) Western blotting was performed to determine the expression of <t>VEGFR2</t> in HUVECs after PDA (10 μM, 24 h) treatment at different doses, and the quantification data are evaluated in ( C ) ( n = 8). ( D ) IF staining was performed to detect the expression of VEGFR2 in the HUVECs after PDA (10 μM) treatment for 24 h, and the quantification data are evaluated in ( E ) ( n = 8). ( F ) IHC staining was performed against CD31 and VEGFR2 antibodies to evaluate the expression of VEGFR2 in a left carotid artery partial ligation model following PDA treatment for 28 days. Yellow arrows indicate regions containing CD31–positive and VEGFR2-positive vascular endothelial cells. The quantification data are evaluated in ( G ) ( n = 8). ( H ) IF staining was used to evaluate the expression of VEGFR2 in blood vessels within the anterior tibial muscle of mice that were intramuscularly injected with cardiotoxin and treated with PDA (20 mg/kg) for 7 consecutive days, and the quantification data are evaluated in ( I ) ( n = 8). Analytical data are expressed as means ± SEM * p < 0.05.
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    1) Product Images from "Potassium Dehydroandrograpolide Succinate Targets NRP1 Mediated VEGFR2/VE-Cadherin Signaling Pathway to Promote Endothelial Barrier Repair"

    Article Title: Potassium Dehydroandrograpolide Succinate Targets NRP1 Mediated VEGFR2/VE-Cadherin Signaling Pathway to Promote Endothelial Barrier Repair

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms24043096

    PDA activates the VEGF signaling pathway after vascular injury. ( A ) HUVEC-Cs were treated with PDA (10 μM) for 24 h. The transcription levels of the VEGF family were evaluated with real-time PCR ( n = 6). ( B ) Western blotting was performed to determine the expression of VEGFR2 in HUVECs after PDA (10 μM, 24 h) treatment at different doses, and the quantification data are evaluated in ( C ) ( n = 8). ( D ) IF staining was performed to detect the expression of VEGFR2 in the HUVECs after PDA (10 μM) treatment for 24 h, and the quantification data are evaluated in ( E ) ( n = 8). ( F ) IHC staining was performed against CD31 and VEGFR2 antibodies to evaluate the expression of VEGFR2 in a left carotid artery partial ligation model following PDA treatment for 28 days. Yellow arrows indicate regions containing CD31–positive and VEGFR2-positive vascular endothelial cells. The quantification data are evaluated in ( G ) ( n = 8). ( H ) IF staining was used to evaluate the expression of VEGFR2 in blood vessels within the anterior tibial muscle of mice that were intramuscularly injected with cardiotoxin and treated with PDA (20 mg/kg) for 7 consecutive days, and the quantification data are evaluated in ( I ) ( n = 8). Analytical data are expressed as means ± SEM * p < 0.05.
    Figure Legend Snippet: PDA activates the VEGF signaling pathway after vascular injury. ( A ) HUVEC-Cs were treated with PDA (10 μM) for 24 h. The transcription levels of the VEGF family were evaluated with real-time PCR ( n = 6). ( B ) Western blotting was performed to determine the expression of VEGFR2 in HUVECs after PDA (10 μM, 24 h) treatment at different doses, and the quantification data are evaluated in ( C ) ( n = 8). ( D ) IF staining was performed to detect the expression of VEGFR2 in the HUVECs after PDA (10 μM) treatment for 24 h, and the quantification data are evaluated in ( E ) ( n = 8). ( F ) IHC staining was performed against CD31 and VEGFR2 antibodies to evaluate the expression of VEGFR2 in a left carotid artery partial ligation model following PDA treatment for 28 days. Yellow arrows indicate regions containing CD31–positive and VEGFR2-positive vascular endothelial cells. The quantification data are evaluated in ( G ) ( n = 8). ( H ) IF staining was used to evaluate the expression of VEGFR2 in blood vessels within the anterior tibial muscle of mice that were intramuscularly injected with cardiotoxin and treated with PDA (20 mg/kg) for 7 consecutive days, and the quantification data are evaluated in ( I ) ( n = 8). Analytical data are expressed as means ± SEM * p < 0.05.

    Techniques Used: Real-time Polymerase Chain Reaction, Western Blot, Expressing, Staining, Immunohistochemistry, Ligation, Injection

    PDA regulates interactions between NRP1, VEGFR and VE-Cad within vascular endothelial cells. ( A ) Molecular docking simulation performed to evaluate the binding energy of PDA with NRP1, VEGFR2 and VE-Cad using Autodock Vina 1.5.6 software, which was developed by Olson’s research group. PDA worked as a receptor, and NRP1, VEGFR2 and VE-Cad were used as ligands to detect the docking sites between receptors and ligands. The three-dimensional structures of VEGFR2 and NRP1 were obtained from the RCSBPDB database ( http://www.rcsb.org/ , accessed on 16 August 2022) and that of VE-Cad was obtained from the SWISS-Model database ( http://swissmodel.expasy.org/ , accessed on 20 August 2022). When values for the binding energy were less than zero, those proteins were considered to spontaneously bind and interact with each other. ( B ) The binding energies of PDA with NRP1, VEGFR2 and VE-Cad were determined based on a molecular docking simulation. ( C ) IF staining of NRP1 and VEGFR2 was performed in the skeletal muscle injury model to determine their co-localization expression in vascular endothelial cells. ( D ) Immunofluorescence staining of NRP1 and VE-Cad was performed in the skeletal muscle injury model to determine their co-localization expression in vascular endothelial cells. ( E ) The interaction between NRP1, VEGFR2 and VE-Cad was validated using the CO-immunoprecipitation assay in HUVECs.
    Figure Legend Snippet: PDA regulates interactions between NRP1, VEGFR and VE-Cad within vascular endothelial cells. ( A ) Molecular docking simulation performed to evaluate the binding energy of PDA with NRP1, VEGFR2 and VE-Cad using Autodock Vina 1.5.6 software, which was developed by Olson’s research group. PDA worked as a receptor, and NRP1, VEGFR2 and VE-Cad were used as ligands to detect the docking sites between receptors and ligands. The three-dimensional structures of VEGFR2 and NRP1 were obtained from the RCSBPDB database ( http://www.rcsb.org/ , accessed on 16 August 2022) and that of VE-Cad was obtained from the SWISS-Model database ( http://swissmodel.expasy.org/ , accessed on 20 August 2022). When values for the binding energy were less than zero, those proteins were considered to spontaneously bind and interact with each other. ( B ) The binding energies of PDA with NRP1, VEGFR2 and VE-Cad were determined based on a molecular docking simulation. ( C ) IF staining of NRP1 and VEGFR2 was performed in the skeletal muscle injury model to determine their co-localization expression in vascular endothelial cells. ( D ) Immunofluorescence staining of NRP1 and VE-Cad was performed in the skeletal muscle injury model to determine their co-localization expression in vascular endothelial cells. ( E ) The interaction between NRP1, VEGFR2 and VE-Cad was validated using the CO-immunoprecipitation assay in HUVECs.

    Techniques Used: Binding Assay, Software, Staining, Expressing, Immunofluorescence, Co-Immunoprecipitation Assay

    PDA regulates vascular endothelial barrier function through the NRP1/VEGFR2/VE-Cad signaling pathway. ( A ) After knockdown of NRP1 in HUVECs, real-time PCR was performed to evaluate transcription levels of NRP1-, VEGFR2- and VE-Cad-related genes ( n = 6). ( B ) After knockdown of NRP1, HUVECs were treated with PDA (10 μM) for 24 h and real-time PCR was performed to evaluate transcription levels of NRP1-, VEGFR2- and VE-Cad-related genes ( n = 6). ( C ) After knockdown of NRP1, IF staining was performed to detect the expression of VE-Cad in the HUVECs following PDA (10 μM) treatment for 24 h, and the quantification data are evaluated in ( D ) ( n = 8). ( E ) After knockdown of NRP1, HUVECs were treated with PDA (10 μM) for 24 h and real-time PCR was performed to evaluate transcription levels of inflammation-related genes ( n = 6). ( F ) After knockdown of NRP1, HUVEC-C and THP-1 were co-cultured and treated with PDA (10 μM) for 12 h, and the quantification data are evaluated in ( G ). ( H ) Schematic diagram indicating that PDA promoted endothelial barrier repair in pathological vascular remodeling. Analytical data are expressed as means ± SEM * p < 0.05.
    Figure Legend Snippet: PDA regulates vascular endothelial barrier function through the NRP1/VEGFR2/VE-Cad signaling pathway. ( A ) After knockdown of NRP1 in HUVECs, real-time PCR was performed to evaluate transcription levels of NRP1-, VEGFR2- and VE-Cad-related genes ( n = 6). ( B ) After knockdown of NRP1, HUVECs were treated with PDA (10 μM) for 24 h and real-time PCR was performed to evaluate transcription levels of NRP1-, VEGFR2- and VE-Cad-related genes ( n = 6). ( C ) After knockdown of NRP1, IF staining was performed to detect the expression of VE-Cad in the HUVECs following PDA (10 μM) treatment for 24 h, and the quantification data are evaluated in ( D ) ( n = 8). ( E ) After knockdown of NRP1, HUVECs were treated with PDA (10 μM) for 24 h and real-time PCR was performed to evaluate transcription levels of inflammation-related genes ( n = 6). ( F ) After knockdown of NRP1, HUVEC-C and THP-1 were co-cultured and treated with PDA (10 μM) for 12 h, and the quantification data are evaluated in ( G ). ( H ) Schematic diagram indicating that PDA promoted endothelial barrier repair in pathological vascular remodeling. Analytical data are expressed as means ± SEM * p < 0.05.

    Techniques Used: Real-time Polymerase Chain Reaction, Staining, Expressing, Cell Culture

    vegfr2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc vegfr2
    CCL2 promotes proliferation, migration and angiogenesis via the PI3K/AKT, MAPK/ERK1/2 and Wnt/β-catenin signaling pathways in HUVECs. (A) Western blot analysis of Rock1, Rock2, N-cadherin, c-Myc, <t>VEGFR2</t> and α-tubulin in HUVECs treated with CCL2 at the indicated doses for 48 h. (B) Western blot analysis of p-PI3K,PI3K, p-AKT, AKT and α-tubulin in HUVECs treated with CCL2 at the indicated doses for 48 h. (C) Western blot analysis of p-ERK1/2, ERK1/2, MMP9 and α-tubulin in HUVECs treated with CCL2 at the indicated doses for 48 h. (D) Western blot analysis of LRP-6, Wnt5a/b, β-catenin and GAPDH in HUVECs treated with CCL2 at the indicated doses for 48 h. Gray analysis of protein bands was performed using ImageJ. * P<0.05, ** P<0.01, *** P<0.001 vs. control group. CCL2, CC motif ligand 2; HUVECs, human umbilical vein endothelial cells; Rock, rho-associated coiled-coil-containing protein kinase; p-, phosphorylated; LRP-6, low-density lipoprotein receptor related protein 6.
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    1) Product Images from "CCL2 promotes proliferation, migration and angiogenesis through the MAPK/ERK1/2/MMP9, PI3K/AKT, Wnt/β‑catenin signaling pathways in HUVECs"

    Article Title: CCL2 promotes proliferation, migration and angiogenesis through the MAPK/ERK1/2/MMP9, PI3K/AKT, Wnt/β‑catenin signaling pathways in HUVECs

    Journal: Experimental and Therapeutic Medicine

    doi: 10.3892/etm.2022.11776

    CCL2 promotes proliferation, migration and angiogenesis via the PI3K/AKT, MAPK/ERK1/2 and Wnt/β-catenin signaling pathways in HUVECs. (A) Western blot analysis of Rock1, Rock2, N-cadherin, c-Myc, VEGFR2 and α-tubulin in HUVECs treated with CCL2 at the indicated doses for 48 h. (B) Western blot analysis of p-PI3K,PI3K, p-AKT, AKT and α-tubulin in HUVECs treated with CCL2 at the indicated doses for 48 h. (C) Western blot analysis of p-ERK1/2, ERK1/2, MMP9 and α-tubulin in HUVECs treated with CCL2 at the indicated doses for 48 h. (D) Western blot analysis of LRP-6, Wnt5a/b, β-catenin and GAPDH in HUVECs treated with CCL2 at the indicated doses for 48 h. Gray analysis of protein bands was performed using ImageJ. * P<0.05, ** P<0.01, *** P<0.001 vs. control group. CCL2, CC motif ligand 2; HUVECs, human umbilical vein endothelial cells; Rock, rho-associated coiled-coil-containing protein kinase; p-, phosphorylated; LRP-6, low-density lipoprotein receptor related protein 6.
    Figure Legend Snippet: CCL2 promotes proliferation, migration and angiogenesis via the PI3K/AKT, MAPK/ERK1/2 and Wnt/β-catenin signaling pathways in HUVECs. (A) Western blot analysis of Rock1, Rock2, N-cadherin, c-Myc, VEGFR2 and α-tubulin in HUVECs treated with CCL2 at the indicated doses for 48 h. (B) Western blot analysis of p-PI3K,PI3K, p-AKT, AKT and α-tubulin in HUVECs treated with CCL2 at the indicated doses for 48 h. (C) Western blot analysis of p-ERK1/2, ERK1/2, MMP9 and α-tubulin in HUVECs treated with CCL2 at the indicated doses for 48 h. (D) Western blot analysis of LRP-6, Wnt5a/b, β-catenin and GAPDH in HUVECs treated with CCL2 at the indicated doses for 48 h. Gray analysis of protein bands was performed using ImageJ. * P<0.05, ** P<0.01, *** P<0.001 vs. control group. CCL2, CC motif ligand 2; HUVECs, human umbilical vein endothelial cells; Rock, rho-associated coiled-coil-containing protein kinase; p-, phosphorylated; LRP-6, low-density lipoprotein receptor related protein 6.

    Techniques Used: Migration, Western Blot

    p vegfr2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p vegfr2
    Breast CAF-derived CCL2 and CCL5 activate P38 MAPK signaling in endothelial cells. (A-B) Western blotting was used to analyze p-P38, P38, <t>p-VEGFR2,</t> VEGFR2, ZO-1, and Occludin levels in HUVECs incubated with CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5. The pixel intensity of p-P38 was normalized to that of β-Actin for the quantification of p-P38 levels (B). (C-D) Western blotting was used to analyze the levels of p-P38, P38, p-VEGFR2, VEGFR2, ZO-1 and Occludin in HUVECs incubated with FBS-free medium with DMSO, rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc. Levels of p-P38 (D) were quantified by normalizing its relative pixel intensity to β-Actin. (E-F) Effects of CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5 on tube formation (E) and permeability (F) of HUVECs. (G-H) Effects of rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc on tube formation (G) and permeability (H) of HUVECs. Data are presented as the mean ± SD (* P < 0.05, ** P < 0.01, *** P < 0.001).
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    1) Product Images from "Cancer-associated fibroblasts facilitate premetastatic niche formation through lncRNA SNHG5-mediated angiogenesis and vascular permeability in breast cancer"

    Article Title: Cancer-associated fibroblasts facilitate premetastatic niche formation through lncRNA SNHG5-mediated angiogenesis and vascular permeability in breast cancer

    Journal: Theranostics

    doi: 10.7150/thno.74753

    Breast CAF-derived CCL2 and CCL5 activate P38 MAPK signaling in endothelial cells. (A-B) Western blotting was used to analyze p-P38, P38, p-VEGFR2, VEGFR2, ZO-1, and Occludin levels in HUVECs incubated with CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5. The pixel intensity of p-P38 was normalized to that of β-Actin for the quantification of p-P38 levels (B). (C-D) Western blotting was used to analyze the levels of p-P38, P38, p-VEGFR2, VEGFR2, ZO-1 and Occludin in HUVECs incubated with FBS-free medium with DMSO, rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc. Levels of p-P38 (D) were quantified by normalizing its relative pixel intensity to β-Actin. (E-F) Effects of CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5 on tube formation (E) and permeability (F) of HUVECs. (G-H) Effects of rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc on tube formation (G) and permeability (H) of HUVECs. Data are presented as the mean ± SD (* P < 0.05, ** P < 0.01, *** P < 0.001).
    Figure Legend Snippet: Breast CAF-derived CCL2 and CCL5 activate P38 MAPK signaling in endothelial cells. (A-B) Western blotting was used to analyze p-P38, P38, p-VEGFR2, VEGFR2, ZO-1, and Occludin levels in HUVECs incubated with CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5. The pixel intensity of p-P38 was normalized to that of β-Actin for the quantification of p-P38 levels (B). (C-D) Western blotting was used to analyze the levels of p-P38, P38, p-VEGFR2, VEGFR2, ZO-1 and Occludin in HUVECs incubated with FBS-free medium with DMSO, rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc. Levels of p-P38 (D) were quantified by normalizing its relative pixel intensity to β-Actin. (E-F) Effects of CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5 on tube formation (E) and permeability (F) of HUVECs. (G-H) Effects of rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc on tube formation (G) and permeability (H) of HUVECs. Data are presented as the mean ± SD (* P < 0.05, ** P < 0.01, *** P < 0.001).

    Techniques Used: Derivative Assay, Western Blot, Incubation, Permeability

    vegfr2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc vegfr2
    Breast CAF-derived CCL2 and CCL5 activate P38 MAPK signaling in endothelial cells. (A-B) Western blotting was used to analyze p-P38, P38, <t>p-VEGFR2,</t> VEGFR2, ZO-1, and Occludin levels in HUVECs incubated with CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5. The pixel intensity of p-P38 was normalized to that of β-Actin for the quantification of p-P38 levels (B). (C-D) Western blotting was used to analyze the levels of p-P38, P38, p-VEGFR2, VEGFR2, ZO-1 and Occludin in HUVECs incubated with FBS-free medium with DMSO, rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc. Levels of p-P38 (D) were quantified by normalizing its relative pixel intensity to β-Actin. (E-F) Effects of CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5 on tube formation (E) and permeability (F) of HUVECs. (G-H) Effects of rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc on tube formation (G) and permeability (H) of HUVECs. Data are presented as the mean ± SD (* P < 0.05, ** P < 0.01, *** P < 0.001).
    Vegfr2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Cancer-associated fibroblasts facilitate premetastatic niche formation through lncRNA SNHG5-mediated angiogenesis and vascular permeability in breast cancer"

    Article Title: Cancer-associated fibroblasts facilitate premetastatic niche formation through lncRNA SNHG5-mediated angiogenesis and vascular permeability in breast cancer

    Journal: Theranostics

    doi: 10.7150/thno.74753

    Breast CAF-derived CCL2 and CCL5 activate P38 MAPK signaling in endothelial cells. (A-B) Western blotting was used to analyze p-P38, P38, p-VEGFR2, VEGFR2, ZO-1, and Occludin levels in HUVECs incubated with CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5. The pixel intensity of p-P38 was normalized to that of β-Actin for the quantification of p-P38 levels (B). (C-D) Western blotting was used to analyze the levels of p-P38, P38, p-VEGFR2, VEGFR2, ZO-1 and Occludin in HUVECs incubated with FBS-free medium with DMSO, rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc. Levels of p-P38 (D) were quantified by normalizing its relative pixel intensity to β-Actin. (E-F) Effects of CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5 on tube formation (E) and permeability (F) of HUVECs. (G-H) Effects of rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc on tube formation (G) and permeability (H) of HUVECs. Data are presented as the mean ± SD (* P < 0.05, ** P < 0.01, *** P < 0.001).
    Figure Legend Snippet: Breast CAF-derived CCL2 and CCL5 activate P38 MAPK signaling in endothelial cells. (A-B) Western blotting was used to analyze p-P38, P38, p-VEGFR2, VEGFR2, ZO-1, and Occludin levels in HUVECs incubated with CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5. The pixel intensity of p-P38 was normalized to that of β-Actin for the quantification of p-P38 levels (B). (C-D) Western blotting was used to analyze the levels of p-P38, P38, p-VEGFR2, VEGFR2, ZO-1 and Occludin in HUVECs incubated with FBS-free medium with DMSO, rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc. Levels of p-P38 (D) were quantified by normalizing its relative pixel intensity to β-Actin. (E-F) Effects of CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5 on tube formation (E) and permeability (F) of HUVECs. (G-H) Effects of rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc on tube formation (G) and permeability (H) of HUVECs. Data are presented as the mean ± SD (* P < 0.05, ** P < 0.01, *** P < 0.001).

    Techniques Used: Derivative Assay, Western Blot, Incubation, Permeability

    vegfr2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc vegfr2
    Differential spinal cord VEGFA pathway expression in each group as determined by Western blot. (a–d) Molecular expression and quantification in each group. The expression of VEGFR1 (a, b) and AKT (c, d) were not different in each group, while that of p-p38 was increased after SNI surgery compared with the SHAM group, but did not different from that in the sFlt1+SNI and in rpVEGFA+sFlt1+ SNI group (c, d). The increased expression of VEGFA, <t>VEGFR2,</t> p-AKT, and TRPV1 was ameliorated by sFIt1 treatment (green bar, B and D), and rpVEGFA inhibited the sFIt1-induced downregulation (blue bar, B and D). The data are shown as the mean ± SEM ( n = 3). The results were analyzed by One-way analysis of variance ANOVA and by multiple comparisons. ⁎ p < 0.05, ⁎⁎ p < .01, and ⁎⁎⁎ p < .001. SNI: spare nerve injury.
    Vegfr2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/vegfr2/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    vegfr2 - by Bioz Stars, 2023-03
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    Images

    1) Product Images from "Targeting Vascular endothelial growth factor A with soluble vascular endothelial growth factor receptor 1 ameliorates nerve injury-induced neuropathic pain"

    Article Title: Targeting Vascular endothelial growth factor A with soluble vascular endothelial growth factor receptor 1 ameliorates nerve injury-induced neuropathic pain

    Journal: Molecular Pain

    doi: 10.1177/17448069221094528

    Differential spinal cord VEGFA pathway expression in each group as determined by Western blot. (a–d) Molecular expression and quantification in each group. The expression of VEGFR1 (a, b) and AKT (c, d) were not different in each group, while that of p-p38 was increased after SNI surgery compared with the SHAM group, but did not different from that in the sFlt1+SNI and in rpVEGFA+sFlt1+ SNI group (c, d). The increased expression of VEGFA, VEGFR2, p-AKT, and TRPV1 was ameliorated by sFIt1 treatment (green bar, B and D), and rpVEGFA inhibited the sFIt1-induced downregulation (blue bar, B and D). The data are shown as the mean ± SEM ( n = 3). The results were analyzed by One-way analysis of variance ANOVA and by multiple comparisons. ⁎ p < 0.05, ⁎⁎ p < .01, and ⁎⁎⁎ p < .001. SNI: spare nerve injury.
    Figure Legend Snippet: Differential spinal cord VEGFA pathway expression in each group as determined by Western blot. (a–d) Molecular expression and quantification in each group. The expression of VEGFR1 (a, b) and AKT (c, d) were not different in each group, while that of p-p38 was increased after SNI surgery compared with the SHAM group, but did not different from that in the sFlt1+SNI and in rpVEGFA+sFlt1+ SNI group (c, d). The increased expression of VEGFA, VEGFR2, p-AKT, and TRPV1 was ameliorated by sFIt1 treatment (green bar, B and D), and rpVEGFA inhibited the sFIt1-induced downregulation (blue bar, B and D). The data are shown as the mean ± SEM ( n = 3). The results were analyzed by One-way analysis of variance ANOVA and by multiple comparisons. ⁎ p < 0.05, ⁎⁎ p < .01, and ⁎⁎⁎ p < .001. SNI: spare nerve injury.

    Techniques Used: Expressing, Western Blot

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    • vegfr2  (Cell Signaling Technology Inc)
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    Cell Signaling Technology Inc vegfr2
    Summary of network modules
    Vegfr2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/vegfr2/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    vegfr2 - by Bioz Stars, 2023-03
    86/100 stars
    		  Buy from Supplier
    rabbit monoclonal phospho vegfr2  (Cell Signaling Technology Inc)
    86
    Cell Signaling Technology Inc rabbit monoclonal phospho vegfr2
    VEGF-A and VEGFRs protein content in whole mice ovaries. Representative western blot images of VEGF-A isoforms (VEGF 164 and VEGF 120), VEGFR1, and <t>VEGFR2</t> total and phosphorylated form <t>(p-VEGFR2,)</t> of late-reproductive multiparous (LM) and virgin (LV), and post-reproductive multiparous (PM) and virgin (PV) mice ( A ). VEGF-A isoforms ( B ), VEGFR1 ( C ), and VEGFR2 ( D ) values are expressed as arbitrary units (a.u.), considering LM values arbitrarily as 1. The p-VEGFR2/VEGFR2 ( E ) values are expressed as percentages (%) of the ratio of phosphorylated/total protein. Bar graph data represent the mean ± SEM ( B – D ) and the mean percentage ± relative error ( E ) after normalization of each protein with the respective actin used as loading control of at least four independent determinations. (†) indicates significant difference ( p < 0.05) related to age (LM vs. PM; LV vs. PV); (*) indicates significant difference ( p < 0.05) related to parity status (LM vs. LV; PM vs. PV).
    Rabbit Monoclonal Phospho Vegfr2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit monoclonal phospho vegfr2/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit monoclonal phospho vegfr2 - by Bioz Stars, 2023-03
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    p vegfr2  (Cell Signaling Technology Inc)
    86
    Cell Signaling Technology Inc p vegfr2
    Breast CAF-derived CCL2 and CCL5 activate P38 MAPK signaling in endothelial cells. (A-B) Western blotting was used to analyze p-P38, P38, <t>p-VEGFR2,</t> VEGFR2, ZO-1, and Occludin levels in HUVECs incubated with CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5. The pixel intensity of p-P38 was normalized to that of β-Actin for the quantification of p-P38 levels (B). (C-D) Western blotting was used to analyze the levels of p-P38, P38, p-VEGFR2, VEGFR2, ZO-1 and Occludin in HUVECs incubated with FBS-free medium with DMSO, rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc. Levels of p-P38 (D) were quantified by normalizing its relative pixel intensity to β-Actin. (E-F) Effects of CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5 on tube formation (E) and permeability (F) of HUVECs. (G-H) Effects of rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc on tube formation (G) and permeability (H) of HUVECs. Data are presented as the mean ± SD (* P < 0.05, ** P < 0.01, *** P < 0.001).
    P Vegfr2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p vegfr2/product/Cell Signaling Technology Inc
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    Image Search Results


    Summary of network modules

    Journal: Brain

    Article Title: A genome-wide association study in autoimmune neurological syndromes with anti-GAD65 autoantibodies

    doi: 10.1093/brain/awac119

    Figure Lengend Snippet: Summary of network modules

    Article Snippet: 0 , Lilac , 17 , ATG4D , ATP6V1G2 , CAV1 , DNM2 , EGFR , GABBR1 , GJB6 , GJC3 , GNAI2 , HCN4 , NEO1 , PPP2CA , PRKCB , PTK2 , S1PR5 , SRC , TRIP6 , 49 , Signalling events mediated by VEGFR1 and VEGFR2, LPA receptor mediated events, Thromboxane A2 receptor signalling , Cell signalling mediating immune and neuronal processes.

    Techniques: Transduction, Activity Assay

    VEGF-A and VEGFRs protein content in whole mice ovaries. Representative western blot images of VEGF-A isoforms (VEGF 164 and VEGF 120), VEGFR1, and VEGFR2 total and phosphorylated form (p-VEGFR2,) of late-reproductive multiparous (LM) and virgin (LV), and post-reproductive multiparous (PM) and virgin (PV) mice ( A ). VEGF-A isoforms ( B ), VEGFR1 ( C ), and VEGFR2 ( D ) values are expressed as arbitrary units (a.u.), considering LM values arbitrarily as 1. The p-VEGFR2/VEGFR2 ( E ) values are expressed as percentages (%) of the ratio of phosphorylated/total protein. Bar graph data represent the mean ± SEM ( B – D ) and the mean percentage ± relative error ( E ) after normalization of each protein with the respective actin used as loading control of at least four independent determinations. (†) indicates significant difference ( p < 0.05) related to age (LM vs. PM; LV vs. PV); (*) indicates significant difference ( p < 0.05) related to parity status (LM vs. LV; PM vs. PV).

    Journal: International Journal of Molecular Sciences

    Article Title: Do Aging and Parity Affect VEGF-A/VEGFR Content and Signaling in the Ovary?—A Mouse Model Study

    doi: 10.3390/ijms24043318

    Figure Lengend Snippet: VEGF-A and VEGFRs protein content in whole mice ovaries. Representative western blot images of VEGF-A isoforms (VEGF 164 and VEGF 120), VEGFR1, and VEGFR2 total and phosphorylated form (p-VEGFR2,) of late-reproductive multiparous (LM) and virgin (LV), and post-reproductive multiparous (PM) and virgin (PV) mice ( A ). VEGF-A isoforms ( B ), VEGFR1 ( C ), and VEGFR2 ( D ) values are expressed as arbitrary units (a.u.), considering LM values arbitrarily as 1. The p-VEGFR2/VEGFR2 ( E ) values are expressed as percentages (%) of the ratio of phosphorylated/total protein. Bar graph data represent the mean ± SEM ( B – D ) and the mean percentage ± relative error ( E ) after normalization of each protein with the respective actin used as loading control of at least four independent determinations. (†) indicates significant difference ( p < 0.05) related to age (LM vs. PM; LV vs. PV); (*) indicates significant difference ( p < 0.05) related to parity status (LM vs. LV; PM vs. PV).

    Article Snippet: Rabbit monoclonal phospho-VEGFR2 (Tyr1175; #2478) and rabbit polyclonal phospho-p38 (Thr180/Tyr182; #9211) were purchased from Cell Signaling Technology (Beverly, MA, USA).

    Techniques: Western Blot

    Tissue localization of VEGF-A and p-VEGFR2 in mouse ovaries. Representative images of VEGF-A ( A , B ) and p-VEGFR2 ( C , D ) immunoreactivity in post-reproductive multiparous (PM) and virgin (PV) ovaries. Negative controls (NC; E , F ) and H&E staining ( G , H ) are presented. White circles indicate the presence of areas with small vessels; white arrowheads indicate the presence of ovarian surface epithelium, which appear to be multi-layered in PV ovaries ( B , D ). Magnification: ×100.

    Journal: International Journal of Molecular Sciences

    Article Title: Do Aging and Parity Affect VEGF-A/VEGFR Content and Signaling in the Ovary?—A Mouse Model Study

    doi: 10.3390/ijms24043318

    Figure Lengend Snippet: Tissue localization of VEGF-A and p-VEGFR2 in mouse ovaries. Representative images of VEGF-A ( A , B ) and p-VEGFR2 ( C , D ) immunoreactivity in post-reproductive multiparous (PM) and virgin (PV) ovaries. Negative controls (NC; E , F ) and H&E staining ( G , H ) are presented. White circles indicate the presence of areas with small vessels; white arrowheads indicate the presence of ovarian surface epithelium, which appear to be multi-layered in PV ovaries ( B , D ). Magnification: ×100.

    Article Snippet: Rabbit monoclonal phospho-VEGFR2 (Tyr1175; #2478) and rabbit polyclonal phospho-p38 (Thr180/Tyr182; #9211) were purchased from Cell Signaling Technology (Beverly, MA, USA).

    Techniques: Staining

    VEGFR2 signaling pathway activation: total and phosphorylated ERK1/2 and p38 in whole mice ovaries. Representative western blot images of ERK1/2 and p38 total and phosphorylated form (p-ERK1/2 and p-p38, respectively) of late-reproductive multiparous (LM) and virgin (LV), and post-reproductive multiparous (PM) and virgin (PV) mice ( A ). ERK1/2 ( B ) and p38 ( D ), values are expressed as arbitrary units (a.u.), considering LM values arbitrarily as 1. The p-ERK1/2/ERK1/2 ( C ), and p-p38/p38 ( E ) values are expressed as percentages (%) of the ratio of phosphorylated/total protein. Bar graph data represent the mean ± SEM ( B , D ) and the mean percentage ± relative error ( C , E ) after normalization of each protein with the respective actin used as loading control of at least four independent determinations. (†) indicates significant difference ( p < 0.05) related to age (LM vs. PM; LV vs. PV); (*) indicates significant difference ( p < 0.05) related to parity status (LM vs. LV; PM vs. PV).

    Journal: International Journal of Molecular Sciences

    Article Title: Do Aging and Parity Affect VEGF-A/VEGFR Content and Signaling in the Ovary?—A Mouse Model Study

    doi: 10.3390/ijms24043318

    Figure Lengend Snippet: VEGFR2 signaling pathway activation: total and phosphorylated ERK1/2 and p38 in whole mice ovaries. Representative western blot images of ERK1/2 and p38 total and phosphorylated form (p-ERK1/2 and p-p38, respectively) of late-reproductive multiparous (LM) and virgin (LV), and post-reproductive multiparous (PM) and virgin (PV) mice ( A ). ERK1/2 ( B ) and p38 ( D ), values are expressed as arbitrary units (a.u.), considering LM values arbitrarily as 1. The p-ERK1/2/ERK1/2 ( C ), and p-p38/p38 ( E ) values are expressed as percentages (%) of the ratio of phosphorylated/total protein. Bar graph data represent the mean ± SEM ( B , D ) and the mean percentage ± relative error ( C , E ) after normalization of each protein with the respective actin used as loading control of at least four independent determinations. (†) indicates significant difference ( p < 0.05) related to age (LM vs. PM; LV vs. PV); (*) indicates significant difference ( p < 0.05) related to parity status (LM vs. LV; PM vs. PV).

    Article Snippet: Rabbit monoclonal phospho-VEGFR2 (Tyr1175; #2478) and rabbit polyclonal phospho-p38 (Thr180/Tyr182; #9211) were purchased from Cell Signaling Technology (Beverly, MA, USA).

    Techniques: Activation Assay, Western Blot

    Breast CAF-derived CCL2 and CCL5 activate P38 MAPK signaling in endothelial cells. (A-B) Western blotting was used to analyze p-P38, P38, p-VEGFR2, VEGFR2, ZO-1, and Occludin levels in HUVECs incubated with CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5. The pixel intensity of p-P38 was normalized to that of β-Actin for the quantification of p-P38 levels (B). (C-D) Western blotting was used to analyze the levels of p-P38, P38, p-VEGFR2, VEGFR2, ZO-1 and Occludin in HUVECs incubated with FBS-free medium with DMSO, rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc. Levels of p-P38 (D) were quantified by normalizing its relative pixel intensity to β-Actin. (E-F) Effects of CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5 on tube formation (E) and permeability (F) of HUVECs. (G-H) Effects of rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc on tube formation (G) and permeability (H) of HUVECs. Data are presented as the mean ± SD (* P < 0.05, ** P < 0.01, *** P < 0.001).

    Journal: Theranostics

    Article Title: Cancer-associated fibroblasts facilitate premetastatic niche formation through lncRNA SNHG5-mediated angiogenesis and vascular permeability in breast cancer

    doi: 10.7150/thno.74753

    Figure Lengend Snippet: Breast CAF-derived CCL2 and CCL5 activate P38 MAPK signaling in endothelial cells. (A-B) Western blotting was used to analyze p-P38, P38, p-VEGFR2, VEGFR2, ZO-1, and Occludin levels in HUVECs incubated with CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5. The pixel intensity of p-P38 was normalized to that of β-Actin for the quantification of p-P38 levels (B). (C-D) Western blotting was used to analyze the levels of p-P38, P38, p-VEGFR2, VEGFR2, ZO-1 and Occludin in HUVECs incubated with FBS-free medium with DMSO, rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc. Levels of p-P38 (D) were quantified by normalizing its relative pixel intensity to β-Actin. (E-F) Effects of CM from NF/Ctrl, CCL2, CCL5, CCL2/CCL5 or CAF/shNC, shCCL2, shCCL5, shCCL2/shCCL5 on tube formation (E) and permeability (F) of HUVECs. (G-H) Effects of rCCL2, rCCL5, rCCL2 and rCCL5 or rCCL2 and rCCL5 combined with axitinib, RS102895, maraviroc, or cenicriviroc on tube formation (G) and permeability (H) of HUVECs. Data are presented as the mean ± SD (* P < 0.05, ** P < 0.01, *** P < 0.001).

    Article Snippet: A total of 50-80 μg protein was separated using 8-12% SDS-PAGE gel and electrically transferred to 0.22 μM PVDF membrane (Bio-Rad, USA), which was blocked with 5% nonfat milk at room temperature for 3 h and then incubated at 4 °C overnight with the special primary antibodies: Occludin (Abcam, ab216327, 1:1000), ZO-1 (Cell Signaling, #8193, 1:1000), ZNF281 (SAB, #43566, 1:1000), IGF2BP2 (Proteintech, 11601-1-AP, 1:2000), VEGFA (Abcam, ab1316, 1:1000), CCL2 (SAB, #45065, 1:500), CCL5 (SAB, #32935, 1:500), p-AKT (CST, #12694, 1:1000), AKT (CST, #9272, 1:1000), p-STAT3 (CST, #9131, 1:500), STAT3 (CST, #4904, 1:500), p-P38 (CST, #4631, 1:500), P38 (CST, #9212, 1:1000), p-VEGFR2 (Sangon, D155165, 1:800), VEGFR2 (Sangon, D151118, 1:800), and β-Actin (Biosharp, 1:1000).

    Techniques: Derivative Assay, Western Blot, Incubation, Permeability