rabbit anti vegf  (Cell Signaling Technology Inc)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 86
    Name:
    Rabbit Anti Mouse IgG Light Chain Specific D3V2A mAb HRP Conjugate
    Description:
    This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase HRP via its amine groups
    Catalog Number:
    58802
    Price:
    None
    Category:
    Secondary Antibodies
    Source:
    Monoclonal antibody is produced by immunizing animals with native total mouse IgG.
    Applications:
    Western Blot
    		Buy from Supplier

    Structured Review

    Cell Signaling Technology Inc rabbit anti vegf
    The correlation analysis between the relative protein expression level of <t>Wnt1</t> and that of <t>VEGF</t> in the aorta of the rats. The protein expression level of Wnt1 in the aorta of the rats is positively correlated with that of VEGF (P
    This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase HRP via its amine groups
    https://www.bioz.com/result/rabbit anti vegf/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti vegf - by Bioz Stars, 2021-04
    86/100 stars

    Images

    1) Product Images from "The role of Wnt signaling pathway in atherosclerosis and its relationship with angiogenesis"

    Article Title: The role of Wnt signaling pathway in atherosclerosis and its relationship with angiogenesis

    Journal: Experimental and Therapeutic Medicine

    doi: 10.3892/etm.2018.6397

    The correlation analysis between the relative protein expression level of Wnt1 and that of VEGF in the aorta of the rats. The protein expression level of Wnt1 in the aorta of the rats is positively correlated with that of VEGF (P
    Figure Legend Snippet: The correlation analysis between the relative protein expression level of Wnt1 and that of VEGF in the aorta of the rats. The protein expression level of Wnt1 in the aorta of the rats is positively correlated with that of VEGF (P

    Techniques Used: Expressing

    Detection of relevant protein expression levels in the aorta of the rats in each group with western blot analysis. (A) Strip figure. (B) Relative protein expression level of Wnt1. (C) Relative protein expression level of β-catenin. (D) Relative protein expression level of DKK1. (E) Relative protein expression level of VEGF. The protein expression levels of Wnt1, β-catenin, DKK1 and VEGF in the aorta of the rats in the model group are significantly higher than those of the rats in the control group (**P
    Figure Legend Snippet: Detection of relevant protein expression levels in the aorta of the rats in each group with western blot analysis. (A) Strip figure. (B) Relative protein expression level of Wnt1. (C) Relative protein expression level of β-catenin. (D) Relative protein expression level of DKK1. (E) Relative protein expression level of VEGF. The protein expression levels of Wnt1, β-catenin, DKK1 and VEGF in the aorta of the rats in the model group are significantly higher than those of the rats in the control group (**P

    Techniques Used: Expressing, Western Blot, Stripping Membranes

    2) Product Images from "Hyperactivated FRS2α-mediated signaling in prostate cancer cells promotes tumor angiogenesis and predicts poor clinical outcome of patients"

    Article Title: Hyperactivated FRS2α-mediated signaling in prostate cancer cells promotes tumor angiogenesis and predicts poor clinical outcome of patients

    Journal: Oncogene

    doi: 10.1038/onc.2015.239

    Depletion of FRS2 α reduces expression of Vegf-a in mouse TRAMP tumors A. Real-time RT-PCR analyses of the indicated gene expression in TRAMP tumors with or without tissue-specific ablation of Frs2α in the epithelial cells. B C . Immunostaining (B) and Western blot (C) analyses of cJUN and HIF1α expression in the TRAMP tumors. F/F, Frs2α flox ; CN, Frs2α CN ; *, P
    Figure Legend Snippet: Depletion of FRS2 α reduces expression of Vegf-a in mouse TRAMP tumors A. Real-time RT-PCR analyses of the indicated gene expression in TRAMP tumors with or without tissue-specific ablation of Frs2α in the epithelial cells. B C . Immunostaining (B) and Western blot (C) analyses of cJUN and HIF1α expression in the TRAMP tumors. F/F, Frs2α flox ; CN, Frs2α CN ; *, P

    Techniques Used: Expressing, Quantitative RT-PCR, Immunostaining, Western Blot

    3) Product Images from "Effect of curcumin on vascular endothelial growth factor in hypoxic HepG2 cells via the insulin-like growth factor 1 receptor signaling pathway"

    Article Title: Effect of curcumin on vascular endothelial growth factor in hypoxic HepG2 cells via the insulin-like growth factor 1 receptor signaling pathway

    Journal: Experimental and Therapeutic Medicine

    doi: 10.3892/etm.2018.5783

    Effect of curcumin and hypoxia on IGF-1R, p-Akt, p-Erk1/2, HIF-1α, VEGF protein expression in IGF-1R knockout HepG2 cells. (A) IGF-1R, p-Akt, p-Erk1/2, HIF-1α, VEGF protein expression were detected by western blot analysis. Graphic representation of relative density of (B) IGF-1R, (C) p-Akt, (D) p-Erk1/2, (E) HIF-1α and (F) VEGF protein levels, which were normalized to those of β-actin, Akt or Erk1/2, respectively. *P
    Figure Legend Snippet: Effect of curcumin and hypoxia on IGF-1R, p-Akt, p-Erk1/2, HIF-1α, VEGF protein expression in IGF-1R knockout HepG2 cells. (A) IGF-1R, p-Akt, p-Erk1/2, HIF-1α, VEGF protein expression were detected by western blot analysis. Graphic representation of relative density of (B) IGF-1R, (C) p-Akt, (D) p-Erk1/2, (E) HIF-1α and (F) VEGF protein levels, which were normalized to those of β-actin, Akt or Erk1/2, respectively. *P

    Techniques Used: Expressing, Knock-Out, Western Blot

    Molecular mechanisms by which curcumin regulates the IGF-1R signaling pathway and the expression of VEGF in HepG2 cells under CoCl 2 -induced hypoxia. The arrow and blocked arrow (no arrowhead) indicate stimulation and inhibition, respectively. The dotted arrow indicates the translocation of HIF-1α and HIF-1β. The dotted blocked arrow indicates the potential effects of curcumin not directly examined in the present study. It was concluded that curcumin may suppress the expression of HIF-1 and VEGF by targeting IGF-1R or its downstream signaling pathways. VEGF, vascular endothelial growth factor; HIF-1α, hypoxia-inducible factor-1α; HIF-1β, hypoxia-inducible factor-1β; IGF-1, insulin-like growth factor-1; IGF-1R, insulin-like growth factor-1 receptor; PI3K, phosphoinositide-3-kinase; Akt, protein kinase B; MEK, mitogen-activated protein kinase-Erk kinase; Erk, extracellular signal-regulated kinase.
    Figure Legend Snippet: Molecular mechanisms by which curcumin regulates the IGF-1R signaling pathway and the expression of VEGF in HepG2 cells under CoCl 2 -induced hypoxia. The arrow and blocked arrow (no arrowhead) indicate stimulation and inhibition, respectively. The dotted arrow indicates the translocation of HIF-1α and HIF-1β. The dotted blocked arrow indicates the potential effects of curcumin not directly examined in the present study. It was concluded that curcumin may suppress the expression of HIF-1 and VEGF by targeting IGF-1R or its downstream signaling pathways. VEGF, vascular endothelial growth factor; HIF-1α, hypoxia-inducible factor-1α; HIF-1β, hypoxia-inducible factor-1β; IGF-1, insulin-like growth factor-1; IGF-1R, insulin-like growth factor-1 receptor; PI3K, phosphoinositide-3-kinase; Akt, protein kinase B; MEK, mitogen-activated protein kinase-Erk kinase; Erk, extracellular signal-regulated kinase.

    Techniques Used: Expressing, Inhibition, Translocation Assay

    Effect of CoCl 2 -induced hypoxia on IGF-1R, HIF-1α and VEGF protein expression in HepG2 cells. (A) Serum-starved IGF-1R knockout HepG2 cells were treated with different concentrations of CoCl 2 (0, 50, 100, 150, 200 and 400 µM) for 6 h. IGF-1R, HIF-1α and VEGF protein expression were detected by western blot analysis. (B) Western blot analysis data was quantified and the protein expression of IGF-1R, HIF-1α and VEGF are presented as a bar graph. *P
    Figure Legend Snippet: Effect of CoCl 2 -induced hypoxia on IGF-1R, HIF-1α and VEGF protein expression in HepG2 cells. (A) Serum-starved IGF-1R knockout HepG2 cells were treated with different concentrations of CoCl 2 (0, 50, 100, 150, 200 and 400 µM) for 6 h. IGF-1R, HIF-1α and VEGF protein expression were detected by western blot analysis. (B) Western blot analysis data was quantified and the protein expression of IGF-1R, HIF-1α and VEGF are presented as a bar graph. *P

    Techniques Used: Expressing, Knock-Out, Western Blot

    4) Product Images from "Effect of curcumin on vascular endothelial growth factor in hypoxic HepG2 cells via the insulin-like growth factor 1 receptor signaling pathway"

    Article Title: Effect of curcumin on vascular endothelial growth factor in hypoxic HepG2 cells via the insulin-like growth factor 1 receptor signaling pathway

    Journal: Experimental and Therapeutic Medicine

    doi: 10.3892/etm.2018.5783

    Effect of curcumin and hypoxia on IGF-1R, p-Akt, p-Erk1/2, HIF-1α, VEGF protein expression in IGF-1R knockout HepG2 cells. (A) IGF-1R, p-Akt, p-Erk1/2, HIF-1α, VEGF protein expression were detected by western blot analysis. Graphic representation of relative density of (B) IGF-1R, (C) p-Akt, (D) p-Erk1/2, (E) HIF-1α and (F) VEGF protein levels, which were normalized to those of β-actin, Akt or Erk1/2, respectively. *P
    Figure Legend Snippet: Effect of curcumin and hypoxia on IGF-1R, p-Akt, p-Erk1/2, HIF-1α, VEGF protein expression in IGF-1R knockout HepG2 cells. (A) IGF-1R, p-Akt, p-Erk1/2, HIF-1α, VEGF protein expression were detected by western blot analysis. Graphic representation of relative density of (B) IGF-1R, (C) p-Akt, (D) p-Erk1/2, (E) HIF-1α and (F) VEGF protein levels, which were normalized to those of β-actin, Akt or Erk1/2, respectively. *P

    Techniques Used: Expressing, Knock-Out, Western Blot

    Molecular mechanisms by which curcumin regulates the IGF-1R signaling pathway and the expression of VEGF in HepG2 cells under CoCl 2 -induced hypoxia. The arrow and blocked arrow (no arrowhead) indicate stimulation and inhibition, respectively. The dotted arrow indicates the translocation of HIF-1α and HIF-1β. The dotted blocked arrow indicates the potential effects of curcumin not directly examined in the present study. It was concluded that curcumin may suppress the expression of HIF-1 and VEGF by targeting IGF-1R or its downstream signaling pathways. VEGF, vascular endothelial growth factor; HIF-1α, hypoxia-inducible factor-1α; HIF-1β, hypoxia-inducible factor-1β; IGF-1, insulin-like growth factor-1; IGF-1R, insulin-like growth factor-1 receptor; PI3K, phosphoinositide-3-kinase; Akt, protein kinase B; MEK, mitogen-activated protein kinase-Erk kinase; Erk, extracellular signal-regulated kinase.
    Figure Legend Snippet: Molecular mechanisms by which curcumin regulates the IGF-1R signaling pathway and the expression of VEGF in HepG2 cells under CoCl 2 -induced hypoxia. The arrow and blocked arrow (no arrowhead) indicate stimulation and inhibition, respectively. The dotted arrow indicates the translocation of HIF-1α and HIF-1β. The dotted blocked arrow indicates the potential effects of curcumin not directly examined in the present study. It was concluded that curcumin may suppress the expression of HIF-1 and VEGF by targeting IGF-1R or its downstream signaling pathways. VEGF, vascular endothelial growth factor; HIF-1α, hypoxia-inducible factor-1α; HIF-1β, hypoxia-inducible factor-1β; IGF-1, insulin-like growth factor-1; IGF-1R, insulin-like growth factor-1 receptor; PI3K, phosphoinositide-3-kinase; Akt, protein kinase B; MEK, mitogen-activated protein kinase-Erk kinase; Erk, extracellular signal-regulated kinase.

    Techniques Used: Expressing, Inhibition, Translocation Assay

    Effect of CoCl 2 -induced hypoxia on IGF-1R, HIF-1α and VEGF protein expression in HepG2 cells. (A) Serum-starved IGF-1R knockout HepG2 cells were treated with different concentrations of CoCl 2 (0, 50, 100, 150, 200 and 400 µM) for 6 h. IGF-1R, HIF-1α and VEGF protein expression were detected by western blot analysis. (B) Western blot analysis data was quantified and the protein expression of IGF-1R, HIF-1α and VEGF are presented as a bar graph. *P
    Figure Legend Snippet: Effect of CoCl 2 -induced hypoxia on IGF-1R, HIF-1α and VEGF protein expression in HepG2 cells. (A) Serum-starved IGF-1R knockout HepG2 cells were treated with different concentrations of CoCl 2 (0, 50, 100, 150, 200 and 400 µM) for 6 h. IGF-1R, HIF-1α and VEGF protein expression were detected by western blot analysis. (B) Western blot analysis data was quantified and the protein expression of IGF-1R, HIF-1α and VEGF are presented as a bar graph. *P

    Techniques Used: Expressing, Knock-Out, Western Blot

    5) Product Images from "The role of Wnt signaling pathway in atherosclerosis and its relationship with angiogenesis"

    Article Title: The role of Wnt signaling pathway in atherosclerosis and its relationship with angiogenesis

    Journal: Experimental and Therapeutic Medicine

    doi: 10.3892/etm.2018.6397

    The correlation analysis between the relative protein expression level of Wnt1 and that of VEGF in the aorta of the rats. The protein expression level of Wnt1 in the aorta of the rats is positively correlated with that of VEGF (P
    Figure Legend Snippet: The correlation analysis between the relative protein expression level of Wnt1 and that of VEGF in the aorta of the rats. The protein expression level of Wnt1 in the aorta of the rats is positively correlated with that of VEGF (P

    Techniques Used: Expressing

    Detection of relevant protein expression levels in the aorta of the rats in each group with western blot analysis. (A) Strip figure. (B) Relative protein expression level of Wnt1. (C) Relative protein expression level of β-catenin. (D) Relative protein expression level of DKK1. (E) Relative protein expression level of VEGF. The protein expression levels of Wnt1, β-catenin, DKK1 and VEGF in the aorta of the rats in the model group are significantly higher than those of the rats in the control group (**P
    Figure Legend Snippet: Detection of relevant protein expression levels in the aorta of the rats in each group with western blot analysis. (A) Strip figure. (B) Relative protein expression level of Wnt1. (C) Relative protein expression level of β-catenin. (D) Relative protein expression level of DKK1. (E) Relative protein expression level of VEGF. The protein expression levels of Wnt1, β-catenin, DKK1 and VEGF in the aorta of the rats in the model group are significantly higher than those of the rats in the control group (**P

    Techniques Used: Expressing, Western Blot, Stripping Membranes

    6) Product Images from "VEGF silencing inhibits human osteosarcoma angiogenesis and promotes cell apoptosis via PI3K/AKT signaling pathway"

    Article Title: VEGF silencing inhibits human osteosarcoma angiogenesis and promotes cell apoptosis via PI3K/AKT signaling pathway

    Journal: International Journal of Clinical and Experimental Medicine

    doi:

    VEGF silencing inhibits the activation of PI3K and AKT in U2OS cells. The levels of p-PI3K, total PI3K, p-AKT and total AKT were detected with western blotting GAPDH was used as a control for normalization of the total protein loading.
    Figure Legend Snippet: VEGF silencing inhibits the activation of PI3K and AKT in U2OS cells. The levels of p-PI3K, total PI3K, p-AKT and total AKT were detected with western blotting GAPDH was used as a control for normalization of the total protein loading.

    Techniques Used: Activation Assay, Western Blot

    Related Articles

    Immunofluorescence:

    Article Title: Mitochondrial inner membrane permeabilisation enables mt DNA release during apoptosis
    Article Snippet: Primary antibodies for Western blotting were as follows: rabbit anti‐BAX, rabbit anti‐BAK, rabbit anti‐DRP1, rabbit anti‐STING (Cell Signaling), mouse MitoProfile Membrane Integrity Cocktail (for cyclophilin D; Abcam) and β‐actin (Sigma). .. Primary antibodies for immunofluorescence were as follows: rabbit anti‐TOM20 (Santa Cruz), mouse anti‐DNA (Progen), rabbit anti‐AIF, rabbit anti‐TFAM (Cell Signaling), mouse anti‐cytochrome c (BD Transduction Laboratories), mouse anti‐active BAX (6A7, Santa Cruz). .. Stable cell line generation For retroviral transduction, 293FT cells were transfected with 5 μg of selected plasmid in combination with 1.2 μg gag/pol (Addgene #14887) and 2.4 μg UVSVG (Addgene #12260) using Lipofectamine 2000 (Life Technologies).

    Western Blot:

    Article Title: Pten loss promotes MAPK pathway dependency in HER2/neu breast carcinomas
    Article Snippet: Blots were incubated with HRP-linked secondary antibodies and developed with chemiluminescence. .. Western blots were probed with antibodies against the following: rabbit anti-PTEN (1:1,000, Cell Signaling 9559), rabbit anti-phospho-AKT Ser473 (1:1,000, Cell Signaling 4060), rabbit anti-phospho-AKT Thr308 (1:1,000, Cell Signaling 2965), rabbit anti-AKT (1:1,000, Cell Signaling 9272), rabbit anti-phospho-p44/42 MAPK (for p-Erk; 1:400, Cell Signaling 4376), mouse anti-p44/42 MAPK (for Erk1/2; 1:2,000, Cell Signaling 9107), rabbit anti-GFP (1:1,000, Cell Signaling 2956), rabbit anti-phospho-S6 ribosomal protein S235/236 (1:2,000, Cell Signaling 4858), mouse anti-S6 ribosomal protein (1:500, Cell Signaling 2317), mouse anti-β-Actin-HRP (1:5,000, monoclonal AC15 clone, Sigma #A3854), and rabbit anti-phospho-MEK1/2 S217/221 (1:1,000, Cell Signaling 9154). ..

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • vegfr2  (Cell Signaling Technology Inc)
    93
    Cell Signaling Technology Inc vegfr2
    Fbln7-C inhibits <t>VEGFR2</t> phosphorylation and ERK phosphorylation in the VEGF-VEGFRs signaling pathway. ( A , B ) VEGFR2 Tyr1175, and ( C , D ) ERK phosphorylation levels with Fbln7-C (100 µg/ml) pretreatment and after VEGF (5 ng/ml) stimulation were confirmed by western blotting. C: control, F7C: Fbln7-C *P
    Vegfr2, supplied by Cell Signaling Technology Inc, 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/result/vegfr2/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    vegfr2 - by Bioz Stars, 2021-04
    93/100 stars
    		  Buy from Supplier
    rabbit anti kdr vegfr 2 mab  (Cell Signaling Technology Inc)
    93
    Cell Signaling Technology Inc rabbit anti kdr vegfr 2 mab
    A model for the role of autophagy in promoting the formation of VM and BEV resistance by GSCs. ROS mediates autophagy-induced phosphorylation of <t>KDR/VEGFR-2</t> by VEGF-independent manner in GSCs through the PI3K-AKT pathway.
    Rabbit Anti Kdr Vegfr 2 Mab, supplied by Cell Signaling Technology Inc, 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/result/rabbit anti kdr vegfr 2 mab/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti kdr vegfr 2 mab - by Bioz Stars, 2021-04
    93/100 stars
    		  Buy from Supplier
    vegfr 2  (Cell Signaling Technology Inc)
    99
    Cell Signaling Technology Inc vegfr 2
    BVD demonstrated by positive <t>VEGFR-2</t> staining showed decreased vascularity in ST-CH (B) compared with SC (A) and LT-CH (C) animals.
    Vegfr 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/vegfr 2/product/Cell Signaling Technology Inc
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    vegfr 2 - by Bioz Stars, 2021-04
    99/100 stars
    		  Buy from Supplier

    Image Search Results


    Fbln7-C inhibits VEGFR2 phosphorylation and ERK phosphorylation in the VEGF-VEGFRs signaling pathway. ( A , B ) VEGFR2 Tyr1175, and ( C , D ) ERK phosphorylation levels with Fbln7-C (100 µg/ml) pretreatment and after VEGF (5 ng/ml) stimulation were confirmed by western blotting. C: control, F7C: Fbln7-C *P

    Journal: Scientific Reports

    Article Title: Extracellular Protein Fibulin-7 and Its C-Terminal Fragment Have In Vivo Antiangiogenic Activity

    doi: 10.1038/s41598-018-36182-w

    Figure Lengend Snippet: Fbln7-C inhibits VEGFR2 phosphorylation and ERK phosphorylation in the VEGF-VEGFRs signaling pathway. ( A , B ) VEGFR2 Tyr1175, and ( C , D ) ERK phosphorylation levels with Fbln7-C (100 µg/ml) pretreatment and after VEGF (5 ng/ml) stimulation were confirmed by western blotting. C: control, F7C: Fbln7-C *P

    Article Snippet: VEGFR2 (VEGF Receptor 2 (55B11) Rabbit mAb, #2479), phopho-VEGFR2 (Phospho-VEGF Receptor 2 (Tyr1175) (19A10) Rabbit mAb, #2478), ERK (p44/42 MAPK (Erk1/2) (137F5) Rabbit mAb, #4695), phospho-ERK (Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E) XP Rabbit mAb, #4370) were purchased from Cell Signaling Technology Inc. (Beverly, MA).

    Techniques: Western Blot

    Fbln7 and Fbln7-C bind to VEGFR2, but not to VEGFR1 or VEGF. Binding between Fbln7-FL/Fbln7-C and ( A ) VEGF, ( B ) VEGFR1, or ( C ) VEGFR2 by ELISA. FN: Fibronectin, FL: Fbln7-FL, C: Fbln7-C, V: VEGF. **P

    Journal: Scientific Reports

    Article Title: Extracellular Protein Fibulin-7 and Its C-Terminal Fragment Have In Vivo Antiangiogenic Activity

    doi: 10.1038/s41598-018-36182-w

    Figure Lengend Snippet: Fbln7 and Fbln7-C bind to VEGFR2, but not to VEGFR1 or VEGF. Binding between Fbln7-FL/Fbln7-C and ( A ) VEGF, ( B ) VEGFR1, or ( C ) VEGFR2 by ELISA. FN: Fibronectin, FL: Fbln7-FL, C: Fbln7-C, V: VEGF. **P

    Article Snippet: VEGFR2 (VEGF Receptor 2 (55B11) Rabbit mAb, #2479), phopho-VEGFR2 (Phospho-VEGF Receptor 2 (Tyr1175) (19A10) Rabbit mAb, #2478), ERK (p44/42 MAPK (Erk1/2) (137F5) Rabbit mAb, #4695), phospho-ERK (Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E) XP Rabbit mAb, #4370) were purchased from Cell Signaling Technology Inc. (Beverly, MA).

    Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay

    A model for the role of autophagy in promoting the formation of VM and BEV resistance by GSCs. ROS mediates autophagy-induced phosphorylation of KDR/VEGFR-2 by VEGF-independent manner in GSCs through the PI3K-AKT pathway.

    Journal: Autophagy

    Article Title: Autophagy-induced KDR/VEGFR-2 activation promotes the formation of vasculogenic mimicry by glioma stem cells

    doi: 10.1080/15548627.2017.1336277

    Figure Lengend Snippet: A model for the role of autophagy in promoting the formation of VM and BEV resistance by GSCs. ROS mediates autophagy-induced phosphorylation of KDR/VEGFR-2 by VEGF-independent manner in GSCs through the PI3K-AKT pathway.

    Article Snippet: Antibodies used include mouse anti-LAMB2/laminin B2 monoclonal antibody (mAb; BD Biosciences, 610722), rabbit anti-CDH5/cadherin 5 mAb (Cell Signaling Technology, 2158), rabbit anti-PROM1/CD133 polyclonal antibody (pAb; Santa Cruz Biotechnology, sc-30220), rabbit anti-GFAP pAb (Abcam, ab7260), mouse anti-CD34 mAb (Abcam, ab187282), rabbit anti-VEGF pAb (Proteintech, 19003–1-AP), rabbit anti-phospho- KDR/VEGFR-2 mAb (Cell Signaling Technology, 2478), rabbit anti-KDR/VEGFR-2 mAb (Cell Signaling Technology, 2479), mouse anti-LC3B mAb (Santa Cruz Biotechnology, sc-376404), rabbit anti-ATG5 mAb (Cell Signaling Technology, 8540), rabbit anti-ATG7 mAb (Cell Signaling Technology, 8558), rabbit anti-SQSTM1/p62 pAb (Sigma-Aldrich, P0067), rabbit anti-BECN1 mAb (Abcam, ab51031), mouse anti-PI3K p85 mAb (Abcam, ab86714), rabbit anti-pan-AKT pAb (Abcam, ab8805), rabbit anti-phospho-PI3K p85 (Y607) pAb (Abcam, ab182651), rabbit anti-phospho-pan-AKT pAb (Abcam, ab38449).

    Techniques:

    Endorepellin evokes a concurrent internalization and down-regulation of α2β1 integrin and VEGFR2. A–C , representative confocal images of human endothelial cells before or after endorepellin treatment for 10 and 20 min as indicated. The cells were permeabilized with 0.1% Triton X-100 for 10 s and immunostained with an antibody against the α2 integrin subunit ( green ), VEGFR2 ( red ), or DAPI ( blue ). Note the progressive co-localization of α2β1 integrin and VEGFR2 within subplasmalemmal ( B , yellow arrows ) and perinuclear ( B and C , white arrows ) vesicles. All images were captured with the same exposure and gain. Bar ∼ 5 μm. D and E , immunoblotting with anti-VEGFR2 of total HUVEC lysates following endorepellin treatment in the absence ( D ) or presence ( E ) of Na 3 VO 4 . T he bottom parts of the gels were stained with Coomassie Blue and serve as loading control. F , quantification of VEGFR2 levels following endorepellin treatment for the indicated time intervals in the absence ( black circles ) or presence ( red circles ) of Na 3 VO 4 . Data represent the mean ± S.E. from three experiments. G , immunoblotting with an antibody against the α2 integrin subunit or against GAPDH as indicated following treatment with endorepellin for various time intervals. H , quantification of α2β1 integrin levels following endorepellin treatment for the indicated time intervals in the absence ( black triangles ) or presence ( red triangles ) of Na 3 VO 4 . Data represent the mean ± S.E. from three experiments.

    Journal: The Journal of Biological Chemistry

    Article Title: Endorepellin, the Angiostatic Module of Perlecan, Interacts with Both the ?2?1 Integrin and Vascular Endothelial Growth Factor Receptor 2 (VEGFR2)

    doi: 10.1074/jbc.M111.243626

    Figure Lengend Snippet: Endorepellin evokes a concurrent internalization and down-regulation of α2β1 integrin and VEGFR2. A–C , representative confocal images of human endothelial cells before or after endorepellin treatment for 10 and 20 min as indicated. The cells were permeabilized with 0.1% Triton X-100 for 10 s and immunostained with an antibody against the α2 integrin subunit ( green ), VEGFR2 ( red ), or DAPI ( blue ). Note the progressive co-localization of α2β1 integrin and VEGFR2 within subplasmalemmal ( B , yellow arrows ) and perinuclear ( B and C , white arrows ) vesicles. All images were captured with the same exposure and gain. Bar ∼ 5 μm. D and E , immunoblotting with anti-VEGFR2 of total HUVEC lysates following endorepellin treatment in the absence ( D ) or presence ( E ) of Na 3 VO 4 . T he bottom parts of the gels were stained with Coomassie Blue and serve as loading control. F , quantification of VEGFR2 levels following endorepellin treatment for the indicated time intervals in the absence ( black circles ) or presence ( red circles ) of Na 3 VO 4 . Data represent the mean ± S.E. from three experiments. G , immunoblotting with an antibody against the α2 integrin subunit or against GAPDH as indicated following treatment with endorepellin for various time intervals. H , quantification of α2β1 integrin levels following endorepellin treatment for the indicated time intervals in the absence ( black triangles ) or presence ( red triangles ) of Na 3 VO 4 . Data represent the mean ± S.E. from three experiments.

    Article Snippet: The following antibodies were used in this study: anti-GAPDH from Advanced Immunochemical (Long Beach, CA), anti-integrin α2 I-domain blocking monoclonal antibody (1998Z) from Millipore (Billerica, MA), monoclonal rabbit anti-human VEGFR2 and anti-phospho-VEGFR2 at Tyr-1175 from Cell Signaling Technology (Beverly, MA), polyclonal rabbit antibodies against VEGFR2, SHP-1, and α2 integrin from Santa Cruz Biotechnology (Santa Cruz, CA), monoclonal mouse HRP-anti-phosphotyrosine (pTyr-20) from BD Biosciences (Franklin Lakes, NJ), and mouse anti-β-actin from Sigma-Aldrich.

    Techniques: Staining

    Dual receptor antagonism for endorepellin. The schematic depicts our current working model. Endorepellin might act as an allosteric inhibitor of VEGFR2 by binding to a region different than VEGFA, which is known to bind Ig 2–3 . This binding likely occurs via the two proximal LG1 and LG2 domains, whereas LG3 wound bind to the α2β1 integrin. This dual receptor binding leads to rapid internalization of both receptors and degradation. On the other hand, endorepellin activates the phosphatase SHP-1, which in turn would dephosphorylate key tyrosine residues in the VEGFR2, thereby blocking prosurvival and proangiogenic downstream signaling pathways. Attenuation of VEGFR2 signaling also leads to a repression of VEGF gene transcription, which causes reduced VEGFA protein production and secretion by endothelial cells.

    Journal: The Journal of Biological Chemistry

    Article Title: Endorepellin, the Angiostatic Module of Perlecan, Interacts with Both the ?2?1 Integrin and Vascular Endothelial Growth Factor Receptor 2 (VEGFR2)

    doi: 10.1074/jbc.M111.243626

    Figure Lengend Snippet: Dual receptor antagonism for endorepellin. The schematic depicts our current working model. Endorepellin might act as an allosteric inhibitor of VEGFR2 by binding to a region different than VEGFA, which is known to bind Ig 2–3 . This binding likely occurs via the two proximal LG1 and LG2 domains, whereas LG3 wound bind to the α2β1 integrin. This dual receptor binding leads to rapid internalization of both receptors and degradation. On the other hand, endorepellin activates the phosphatase SHP-1, which in turn would dephosphorylate key tyrosine residues in the VEGFR2, thereby blocking prosurvival and proangiogenic downstream signaling pathways. Attenuation of VEGFR2 signaling also leads to a repression of VEGF gene transcription, which causes reduced VEGFA protein production and secretion by endothelial cells.

    Article Snippet: The following antibodies were used in this study: anti-GAPDH from Advanced Immunochemical (Long Beach, CA), anti-integrin α2 I-domain blocking monoclonal antibody (1998Z) from Millipore (Billerica, MA), monoclonal rabbit anti-human VEGFR2 and anti-phospho-VEGFR2 at Tyr-1175 from Cell Signaling Technology (Beverly, MA), polyclonal rabbit antibodies against VEGFR2, SHP-1, and α2 integrin from Santa Cruz Biotechnology (Santa Cruz, CA), monoclonal mouse HRP-anti-phosphotyrosine (pTyr-20) from BD Biosciences (Franklin Lakes, NJ), and mouse anti-β-actin from Sigma-Aldrich.

    Techniques: Activated Clotting Time Assay, Binding Assay, Blocking Assay

    BVD demonstrated by positive VEGFR-2 staining showed decreased vascularity in ST-CH (B) compared with SC (A) and LT-CH (C) animals.

    Journal: Journal of the neurological sciences

    Article Title: VEGF/VEGFR-2 changes in frontal cortex, choroid plexus, and CSF after chronic obstructive hydrocephalus

    doi: 10.1016/j.jns.2010.06.012

    Figure Lengend Snippet: BVD demonstrated by positive VEGFR-2 staining showed decreased vascularity in ST-CH (B) compared with SC (A) and LT-CH (C) animals.

    Article Snippet: Proteins were transferred onto a polyvinylidene fluoride (PVDF) microporous membrane (LC2005, Invitrogen Corporation, Carlsbad, CA) and probed with antibodies against VEGF (goat antibody, 1:1000 dilution, AF1603, R & D Systems, Inc., Minneapolis, MN) or VEGFR-2 (rabbit antibody, 1:1000 dilution, #2479, Cell Signaling Technology, Inc., Danvers, MA) and with second antibodies of mouse anti-goat IgG –HRP (for VEGF, 1:2000 dilution) or goat anti-rabbit IgG –HRP (for VEGFR-2, 1:5000 dilution, Santa Cruz Biotechnology, CA).

    Techniques: Staining

    IHC photomicrographs of VEGF (A, B) and VEGFR-2 (C, D) expression in choroid plexus. Cobblestone-shaped epithelial cells (arrowheads) showed similar expression of VEGF in both control (A) and hydrocephalic (B) animals. VEGFR-2 showed robust expression

    Journal: Journal of the neurological sciences

    Article Title: VEGF/VEGFR-2 changes in frontal cortex, choroid plexus, and CSF after chronic obstructive hydrocephalus

    doi: 10.1016/j.jns.2010.06.012

    Figure Lengend Snippet: IHC photomicrographs of VEGF (A, B) and VEGFR-2 (C, D) expression in choroid plexus. Cobblestone-shaped epithelial cells (arrowheads) showed similar expression of VEGF in both control (A) and hydrocephalic (B) animals. VEGFR-2 showed robust expression

    Article Snippet: Proteins were transferred onto a polyvinylidene fluoride (PVDF) microporous membrane (LC2005, Invitrogen Corporation, Carlsbad, CA) and probed with antibodies against VEGF (goat antibody, 1:1000 dilution, AF1603, R & D Systems, Inc., Minneapolis, MN) or VEGFR-2 (rabbit antibody, 1:1000 dilution, #2479, Cell Signaling Technology, Inc., Danvers, MA) and with second antibodies of mouse anti-goat IgG –HRP (for VEGF, 1:2000 dilution) or goat anti-rabbit IgG –HRP (for VEGFR-2, 1:5000 dilution, Santa Cruz Biotechnology, CA).

    Techniques: Immunohistochemistry, Expressing

    Scatterplots showing significant correlation between cerebral blood flow and VEGFR-2 expression levels (P=0.024) ( A ), but no correlation with VEGF expression levels ( B ) in frontal cortex.

    Journal: Journal of the neurological sciences

    Article Title: VEGF/VEGFR-2 changes in frontal cortex, choroid plexus, and CSF after chronic obstructive hydrocephalus

    doi: 10.1016/j.jns.2010.06.012

    Figure Lengend Snippet: Scatterplots showing significant correlation between cerebral blood flow and VEGFR-2 expression levels (P=0.024) ( A ), but no correlation with VEGF expression levels ( B ) in frontal cortex.

    Article Snippet: Proteins were transferred onto a polyvinylidene fluoride (PVDF) microporous membrane (LC2005, Invitrogen Corporation, Carlsbad, CA) and probed with antibodies against VEGF (goat antibody, 1:1000 dilution, AF1603, R & D Systems, Inc., Minneapolis, MN) or VEGFR-2 (rabbit antibody, 1:1000 dilution, #2479, Cell Signaling Technology, Inc., Danvers, MA) and with second antibodies of mouse anti-goat IgG –HRP (for VEGF, 1:2000 dilution) or goat anti-rabbit IgG –HRP (for VEGFR-2, 1:5000 dilution, Santa Cruz Biotechnology, CA).

    Techniques: Flow Cytometry, Expressing

    VEGFR-2 expression levels in frontal cortex shown by immunohistochemistry (A–C) and Western blot (D). (E) Quantitative analysis of band intensity in Western blot. Overall, IHC staining with anti-VEGFR-2 antibody showed decreased staining in ST-CH

    Journal: Journal of the neurological sciences

    Article Title: VEGF/VEGFR-2 changes in frontal cortex, choroid plexus, and CSF after chronic obstructive hydrocephalus

    doi: 10.1016/j.jns.2010.06.012

    Figure Lengend Snippet: VEGFR-2 expression levels in frontal cortex shown by immunohistochemistry (A–C) and Western blot (D). (E) Quantitative analysis of band intensity in Western blot. Overall, IHC staining with anti-VEGFR-2 antibody showed decreased staining in ST-CH

    Article Snippet: Proteins were transferred onto a polyvinylidene fluoride (PVDF) microporous membrane (LC2005, Invitrogen Corporation, Carlsbad, CA) and probed with antibodies against VEGF (goat antibody, 1:1000 dilution, AF1603, R & D Systems, Inc., Minneapolis, MN) or VEGFR-2 (rabbit antibody, 1:1000 dilution, #2479, Cell Signaling Technology, Inc., Danvers, MA) and with second antibodies of mouse anti-goat IgG –HRP (for VEGF, 1:2000 dilution) or goat anti-rabbit IgG –HRP (for VEGFR-2, 1:5000 dilution, Santa Cruz Biotechnology, CA).

    Techniques: Expressing, Immunohistochemistry, Western Blot, Staining