recombinant vegf  (R&D Systems)

 
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    Name:
    Recombinant Canine VEGF Protein
    Description:
    The Recombinant Canine VEGF Protein from R D Systems is derived from E coli The Recombinant Canine VEGF Protein has been validated for the following applications Bioactivity
    Catalog Number:
    1603-CV-010
    Price:
    329
    Category:
    Proteins and Enzymes
    Source:
    E. coli-derived Recombinant Canine VEGF Protein
    Applications:
    Bioactivity
    Purity:
    >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
    Conjugate:
    Unconjugated
    Size:
    10 ug
    Buy from Supplier


    Structured Review

    R&D Systems recombinant vegf
    <t>SLPI</t> promotes proliferation of adult neural stem cells and induces cyclin D1 . A: Proliferation of rat neural stem cells after treatment with SLPI or <t>VEGF,</t> respectively. Cells were treated with indicated amounts of SLPI or VEGF for three days. Afterwards, they were pulsed with 10 μM BrdU. Proportion of BrdU-positive cells (+ std dev) was determined with the FITC BrdU Flow Kit. Presentation of a representative result of three experiments. *:p
    The Recombinant Canine VEGF Protein from R D Systems is derived from E coli The Recombinant Canine VEGF Protein has been validated for the following applications Bioactivity
    https://www.bioz.com/result/recombinant vegf/product/R&D Systems
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    recombinant vegf - by Bioz Stars, 2021-09
    94/100 stars

    Images

    1) Product Images from "Novel role for SLPI in MOG-induced EAE revealed by spinal cord expression analysis"

    Article Title: Novel role for SLPI in MOG-induced EAE revealed by spinal cord expression analysis

    Journal: Journal of Neuroinflammation

    doi: 10.1186/1742-2094-5-20

    SLPI promotes proliferation of adult neural stem cells and induces cyclin D1 . A: Proliferation of rat neural stem cells after treatment with SLPI or VEGF, respectively. Cells were treated with indicated amounts of SLPI or VEGF for three days. Afterwards, they were pulsed with 10 μM BrdU. Proportion of BrdU-positive cells (+ std dev) was determined with the FITC BrdU Flow Kit. Presentation of a representative result of three experiments. *:p
    Figure Legend Snippet: SLPI promotes proliferation of adult neural stem cells and induces cyclin D1 . A: Proliferation of rat neural stem cells after treatment with SLPI or VEGF, respectively. Cells were treated with indicated amounts of SLPI or VEGF for three days. Afterwards, they were pulsed with 10 μM BrdU. Proportion of BrdU-positive cells (+ std dev) was determined with the FITC BrdU Flow Kit. Presentation of a representative result of three experiments. *:p

    Techniques Used: Flow Cytometry

    2) Product Images from "Differential effects of a soluble or immobilized VEGFR-binding peptide"

    Article Title: Differential effects of a soluble or immobilized VEGFR-binding peptide

    Journal: Integrative biology : quantitative biosciences from nano to macro

    doi: 10.1039/c2ib20055d

    HUVEC response to soluble morphogens. HUVECs starved overnight in 2% FBS were seeded on arrays presenting varied densities of GRGDSP in the presence of 2% FBS alone or with the addition of 10 ng/mL VR-BP (4.8 nM) or 10 ng/mL VEGF (0.26 nM). (Error bars indicate standard error of the mean and asterisk indicate significance compared to FBS alone, p
    Figure Legend Snippet: HUVEC response to soluble morphogens. HUVECs starved overnight in 2% FBS were seeded on arrays presenting varied densities of GRGDSP in the presence of 2% FBS alone or with the addition of 10 ng/mL VR-BP (4.8 nM) or 10 ng/mL VEGF (0.26 nM). (Error bars indicate standard error of the mean and asterisk indicate significance compared to FBS alone, p

    Techniques Used:

    3) Product Images from "Increased supply from blood vessels promotes the activation of dormant primordial follicles in mouse ovaries"

    Article Title: Increased supply from blood vessels promotes the activation of dormant primordial follicles in mouse ovaries

    Journal: The Journal of Reproduction and Development

    doi: 10.1262/jrd.2019-091

    Expression of KIT ligand (KITL) in 10-week-old ICR mouse ovaries in which a biodegradable gel containing vascular endothelial growth factor (VEGF) was transplanted and in cultured P0 mouse ovaries. (A) A primordial follicle that expressed KITL (KITL-positive primordial follicles) in a 10-week-old ICR mouse ovary. (B) Primordial follicles that did not express KITL in a 10-week-old ICR mouse ovary. (C) Ratio of KITL-positive primordial follicles in the ovaries in which a biodegradable gel containing 10 μg/ml recombinant VEGF was transplanted. (D) Ratio of KITL-positive primordial follicles in the cultured P0 mouse ovaries. Arrows indicate primordial follicles. Mean ± SD (n = 3 for 10 μg/ml recombinant VEGF, n = 5 for control; n = 3 for 10% fetal bovine serum (FBS), n = 4 for 5% FBS and n = 7 for 0% FBS). Scale bar: 50 μm. * P
    Figure Legend Snippet: Expression of KIT ligand (KITL) in 10-week-old ICR mouse ovaries in which a biodegradable gel containing vascular endothelial growth factor (VEGF) was transplanted and in cultured P0 mouse ovaries. (A) A primordial follicle that expressed KITL (KITL-positive primordial follicles) in a 10-week-old ICR mouse ovary. (B) Primordial follicles that did not express KITL in a 10-week-old ICR mouse ovary. (C) Ratio of KITL-positive primordial follicles in the ovaries in which a biodegradable gel containing 10 μg/ml recombinant VEGF was transplanted. (D) Ratio of KITL-positive primordial follicles in the cultured P0 mouse ovaries. Arrows indicate primordial follicles. Mean ± SD (n = 3 for 10 μg/ml recombinant VEGF, n = 5 for control; n = 3 for 10% fetal bovine serum (FBS), n = 4 for 5% FBS and n = 7 for 0% FBS). Scale bar: 50 μm. * P

    Techniques Used: Expressing, Cell Culture, Recombinant

    Effect of recombinant vascular endothelial growth factor (VEGF) on the activation of primordial follicles in cultured P0 Oog1pro3.9/R26-H2B-mCherry mouse ovaries. Mean ± SD (n = 3 for 200 ng/ml, n = 4 for 50 ng /ml, n = 5 for 100 ng /ml, and n = 12 for control.
    Figure Legend Snippet: Effect of recombinant vascular endothelial growth factor (VEGF) on the activation of primordial follicles in cultured P0 Oog1pro3.9/R26-H2B-mCherry mouse ovaries. Mean ± SD (n = 3 for 200 ng/ml, n = 4 for 50 ng /ml, n = 5 for 100 ng /ml, and n = 12 for control.

    Techniques Used: Recombinant, Activation Assay, Cell Culture

    4) Product Images from "Increased supply from blood vessels promotes the activation of dormant primordial follicles in mouse ovaries"

    Article Title: Increased supply from blood vessels promotes the activation of dormant primordial follicles in mouse ovaries

    Journal: The Journal of Reproduction and Development

    doi: 10.1262/jrd.2019-091

    Expression of KIT ligand (KITL) in 10-week-old ICR mouse ovaries in which a biodegradable gel containing vascular endothelial growth factor (VEGF) was transplanted and in cultured P0 mouse ovaries. (A) A primordial follicle that expressed KITL (KITL-positive primordial follicles) in a 10-week-old ICR mouse ovary. (B) Primordial follicles that did not express KITL in a 10-week-old ICR mouse ovary. (C) Ratio of KITL-positive primordial follicles in the ovaries in which a biodegradable gel containing 10 μg/ml recombinant VEGF was transplanted. (D) Ratio of KITL-positive primordial follicles in the cultured P0 mouse ovaries. Arrows indicate primordial follicles. Mean ± SD (n = 3 for 10 μg/ml recombinant VEGF, n = 5 for control; n = 3 for 10% fetal bovine serum (FBS), n = 4 for 5% FBS and n = 7 for 0% FBS). Scale bar: 50 μm. * P
    Figure Legend Snippet: Expression of KIT ligand (KITL) in 10-week-old ICR mouse ovaries in which a biodegradable gel containing vascular endothelial growth factor (VEGF) was transplanted and in cultured P0 mouse ovaries. (A) A primordial follicle that expressed KITL (KITL-positive primordial follicles) in a 10-week-old ICR mouse ovary. (B) Primordial follicles that did not express KITL in a 10-week-old ICR mouse ovary. (C) Ratio of KITL-positive primordial follicles in the ovaries in which a biodegradable gel containing 10 μg/ml recombinant VEGF was transplanted. (D) Ratio of KITL-positive primordial follicles in the cultured P0 mouse ovaries. Arrows indicate primordial follicles. Mean ± SD (n = 3 for 10 μg/ml recombinant VEGF, n = 5 for control; n = 3 for 10% fetal bovine serum (FBS), n = 4 for 5% FBS and n = 7 for 0% FBS). Scale bar: 50 μm. * P

    Techniques Used: Expressing, Cell Culture, Recombinant

    5) Product Images from "Heparanase-enhanced shedding of syndecan-1 by myeloma cells promotes endothelial invasion and angiogenesis"

    Article Title: Heparanase-enhanced shedding of syndecan-1 by myeloma cells promotes endothelial invasion and angiogenesis

    Journal: Blood

    doi: 10.1182/blood-2009-07-234757

    Shed syndecan-1 and VEGF act together to stimulate ERK activation and endothelial invasion . (A) Syndecan-1 enhances VEGF-mediated invasion of endothelial cells. An endothelial invasion assay was performed with conditioned medium from HPSE-high cells that
    Figure Legend Snippet: Shed syndecan-1 and VEGF act together to stimulate ERK activation and endothelial invasion . (A) Syndecan-1 enhances VEGF-mediated invasion of endothelial cells. An endothelial invasion assay was performed with conditioned medium from HPSE-high cells that

    Techniques Used: Activated Clotting Time Assay, Activation Assay, Invasion Assay

    Medium conditioned by heparanase high myeloma cells enhances endothelial invasion via activity of VEGF . (A) Endothelial cells were seeded on the top well of an invasion chamber coated with Matrigel and conditioned medium from either HPSE-low or HPSE-high
    Figure Legend Snippet: Medium conditioned by heparanase high myeloma cells enhances endothelial invasion via activity of VEGF . (A) Endothelial cells were seeded on the top well of an invasion chamber coated with Matrigel and conditioned medium from either HPSE-low or HPSE-high

    Techniques Used: Activity Assay

    6) Product Images from "Experimental orthotopic transplantation of a tissue-engineered oesophagus in rats"

    Article Title: Experimental orthotopic transplantation of a tissue-engineered oesophagus in rats

    Journal: Nature Communications

    doi: 10.1038/ncomms4562

    Protein content and functional assays. ( a – d ) Expression of collagen I and IV in native ( a , c ) and decellularized ( b , d ) oesophagus (scale bar—Col I—50 μm, Col IV—20 μm, mu indicating muscular layer, l—lumen). An intact basement membrane is indicated by collagen IV expression ( c , d , red arrows). ( e – j ) Expression of elastin, fibronectin and laminin in native ( e , g , i , mu indicating muscular layer, sm submucosa) and decellularized ( f , h , j ) oesophagus (scale bar—25 μm). ( k , l ) Expression of VEGF factor in native ( k ) and decellularized ( l ) oesophagus (l—lumen, sm—submucosa, mu—muscular layer). VEGF and laminin-stained tubular structures, suggesting intact vasculature, are found in native and decellularized tissue ( i – l , inserts, scale bar—10 μm). ( m ) Protein quantification of extracellular matrix proteins ( n =3 biological replicates). ( n – q ) Angiogenesis assay implanted with gelfoam (control, asterisk in n ) and with fragments of decellularized oesophagus (asterisk in o ). The oesophagus induced new vessels, proving the scaffolds’ positive influence of vessel organization. SEM micrographs of vessel and the scaffold sample ( p , * ) and newly built vessel ( p , ↓) (scale bar—100 μm), higher magnification on one of the vessels( q ; scale bar—25 μm). ( r ) Quantification of blood vessels converging to the samples, indicating the strong angiogenic induction by the scaffold, at the levels of the positive control ( n =3). ( s ) The scaffold was inflated and deflated over 10,000 times, a stable plateau phase ( s ) proves the scaffold’s integrity in the last cycle, as there is no leakage from the scaffold ( n =3, one representative graph shown). ( t ) Axial strength was evaluated using burst pressure measurements, without any difference between native, decellularized or reseeded groups ( n =5). ( u , v ) Tensile test showed that strength lost during decellularization was regained after reseeding: force at break ( u ) and strain at break ( v ) ( n =5). ( w ) Distensibility assay showed that the lost distensibility after decellularization (black series) was regained after reseeding (green series) ( n =5), highly resembling the native organ (red series). * P
    Figure Legend Snippet: Protein content and functional assays. ( a – d ) Expression of collagen I and IV in native ( a , c ) and decellularized ( b , d ) oesophagus (scale bar—Col I—50 μm, Col IV—20 μm, mu indicating muscular layer, l—lumen). An intact basement membrane is indicated by collagen IV expression ( c , d , red arrows). ( e – j ) Expression of elastin, fibronectin and laminin in native ( e , g , i , mu indicating muscular layer, sm submucosa) and decellularized ( f , h , j ) oesophagus (scale bar—25 μm). ( k , l ) Expression of VEGF factor in native ( k ) and decellularized ( l ) oesophagus (l—lumen, sm—submucosa, mu—muscular layer). VEGF and laminin-stained tubular structures, suggesting intact vasculature, are found in native and decellularized tissue ( i – l , inserts, scale bar—10 μm). ( m ) Protein quantification of extracellular matrix proteins ( n =3 biological replicates). ( n – q ) Angiogenesis assay implanted with gelfoam (control, asterisk in n ) and with fragments of decellularized oesophagus (asterisk in o ). The oesophagus induced new vessels, proving the scaffolds’ positive influence of vessel organization. SEM micrographs of vessel and the scaffold sample ( p , * ) and newly built vessel ( p , ↓) (scale bar—100 μm), higher magnification on one of the vessels( q ; scale bar—25 μm). ( r ) Quantification of blood vessels converging to the samples, indicating the strong angiogenic induction by the scaffold, at the levels of the positive control ( n =3). ( s ) The scaffold was inflated and deflated over 10,000 times, a stable plateau phase ( s ) proves the scaffold’s integrity in the last cycle, as there is no leakage from the scaffold ( n =3, one representative graph shown). ( t ) Axial strength was evaluated using burst pressure measurements, without any difference between native, decellularized or reseeded groups ( n =5). ( u , v ) Tensile test showed that strength lost during decellularization was regained after reseeding: force at break ( u ) and strain at break ( v ) ( n =5). ( w ) Distensibility assay showed that the lost distensibility after decellularization (black series) was regained after reseeding (green series) ( n =5), highly resembling the native organ (red series). * P

    Techniques Used: Functional Assay, Expressing, Staining, Angiogenesis Assay, Positive Control

    7) Product Images from "Heparanase-enhanced shedding of syndecan-1 by myeloma cells promotes endothelial invasion and angiogenesis"

    Article Title: Heparanase-enhanced shedding of syndecan-1 by myeloma cells promotes endothelial invasion and angiogenesis

    Journal: Blood

    doi: 10.1182/blood-2009-07-234757

    Shed syndecan-1 and VEGF act together to stimulate ERK activation and endothelial invasion . (A) Syndecan-1 enhances VEGF-mediated invasion of endothelial cells. An endothelial invasion assay was performed with conditioned medium from HPSE-high cells that
    Figure Legend Snippet: Shed syndecan-1 and VEGF act together to stimulate ERK activation and endothelial invasion . (A) Syndecan-1 enhances VEGF-mediated invasion of endothelial cells. An endothelial invasion assay was performed with conditioned medium from HPSE-high cells that

    Techniques Used: Activated Clotting Time Assay, Activation Assay, Invasion Assay

    Medium conditioned by heparanase high myeloma cells enhances endothelial invasion via activity of VEGF . (A) Endothelial cells were seeded on the top well of an invasion chamber coated with Matrigel and conditioned medium from either HPSE-low or HPSE-high
    Figure Legend Snippet: Medium conditioned by heparanase high myeloma cells enhances endothelial invasion via activity of VEGF . (A) Endothelial cells were seeded on the top well of an invasion chamber coated with Matrigel and conditioned medium from either HPSE-low or HPSE-high

    Techniques Used: Activity Assay

    8) Product Images from "Key endothelial cell angiogenic mechanisms are stimulated by the circulating milieu in sickle cell disease and attenuated by hydroxyurea"

    Article Title: Key endothelial cell angiogenic mechanisms are stimulated by the circulating milieu in sickle cell disease and attenuated by hydroxyurea

    Journal: Haematologica

    doi: 10.3324/haematol.2014.119727

    In vivo angiogenesis is augmented in SCD chimeric mice and inhibited by hydroxyurea. A Matrigel plug neovascularization assay was employed to compare neovascularization in SCD chimeric (SS) and C57BL/6 mice and observe the effects of hydroxyurea on in vivo vessel formation. The following were injected subcutaneously into C57BL/6 and SS mice; a mixture of Matrigel and heparin without vascular endothelial growth factor (VEGF−, negative control); Matrigel, heparin and VEGF (VEGF +, positive control) or Matrigel, heparin, VEGF and 100 μM hydroxy -urea (VEGF+HU). Matrigel plugs were left in place for 7 days. (A) Quantification of hemoglobin (Hb) in the homogenized Matrigel plugs using Drabkin solution, results are expressed as Hb content in the Matrigel plug (mg/g) (mean±SEM; C57BL/6, n=5; SS, n=4–6). (B) Representative photomicrographs of Matrigel plugs. Scale bars, 1 cm.* P
    Figure Legend Snippet: In vivo angiogenesis is augmented in SCD chimeric mice and inhibited by hydroxyurea. A Matrigel plug neovascularization assay was employed to compare neovascularization in SCD chimeric (SS) and C57BL/6 mice and observe the effects of hydroxyurea on in vivo vessel formation. The following were injected subcutaneously into C57BL/6 and SS mice; a mixture of Matrigel and heparin without vascular endothelial growth factor (VEGF−, negative control); Matrigel, heparin and VEGF (VEGF +, positive control) or Matrigel, heparin, VEGF and 100 μM hydroxy -urea (VEGF+HU). Matrigel plugs were left in place for 7 days. (A) Quantification of hemoglobin (Hb) in the homogenized Matrigel plugs using Drabkin solution, results are expressed as Hb content in the Matrigel plug (mg/g) (mean±SEM; C57BL/6, n=5; SS, n=4–6). (B) Representative photomicrographs of Matrigel plugs. Scale bars, 1 cm.* P

    Techniques Used: In Vivo, Mouse Assay, Injection, Negative Control, Positive Control

    9) Product Images from "Biliary Infection May Exacerbate Biliary Cystogenesis Through the Induction of VEGF in Cholangiocytes of the Polycystic Kidney (PCK) Rat"

    Article Title: Biliary Infection May Exacerbate Biliary Cystogenesis Through the Induction of VEGF in Cholangiocytes of the Polycystic Kidney (PCK) Rat

    Journal: The American Journal of Pathology

    doi: 10.1016/j.ajpath.2011.08.028

    VEGF expression and effects of LPS on its expression of PCK cholangiocytes. A: Cholangiocytes were treated with LPS (10 μg/mL), and expression of VEGF was examined. RT-PCR analysis confirmed that cholangiocytes expressed TLR4 as well as Flk-1
    Figure Legend Snippet: VEGF expression and effects of LPS on its expression of PCK cholangiocytes. A: Cholangiocytes were treated with LPS (10 μg/mL), and expression of VEGF was examined. RT-PCR analysis confirmed that cholangiocytes expressed TLR4 as well as Flk-1

    Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction

    Cell signaling pathways involved in the VEGF expression of PCK cholangiocytes. A: After stimulation with LPS (10 μg/mL), activation of NF-κB was examined as described under Materials and Methods . LPS induced NF-κB activation in
    Figure Legend Snippet: Cell signaling pathways involved in the VEGF expression of PCK cholangiocytes. A: After stimulation with LPS (10 μg/mL), activation of NF-κB was examined as described under Materials and Methods . LPS induced NF-κB activation in

    Techniques Used: Expressing, Activation Assay

    Effect of LPS and VEGF on cell proliferation of PCK cholangiocytes. A: Normal and PCK cholangiocytes were treated with LPS and VEGF at the concentrations indicated, and cell proliferative activity was determined using the WST-1 assay. In both normal and
    Figure Legend Snippet: Effect of LPS and VEGF on cell proliferation of PCK cholangiocytes. A: Normal and PCK cholangiocytes were treated with LPS and VEGF at the concentrations indicated, and cell proliferative activity was determined using the WST-1 assay. In both normal and

    Techniques Used: Activity Assay, WST-1 Assay

    10) Product Images from "Key endothelial cell angiogenic mechanisms are stimulated by the circulating milieu in sickle cell disease and attenuated by hydroxyurea"

    Article Title: Key endothelial cell angiogenic mechanisms are stimulated by the circulating milieu in sickle cell disease and attenuated by hydroxyurea

    Journal: Haematologica

    doi: 10.3324/haematol.2014.119727

    In vivo angiogenesis is augmented in SCD chimeric mice and inhibited by hydroxyurea. A Matrigel plug neovascularization assay was employed to compare neovascularization in SCD chimeric (SS) and C57BL/6 mice and observe the effects of hydroxyurea on in vivo vessel formation. The following were injected subcutaneously into C57BL/6 and SS mice; a mixture of Matrigel and heparin without vascular endothelial growth factor (VEGF−, negative control); Matrigel, heparin and VEGF (VEGF +, positive control) or Matrigel, heparin, VEGF and 100 μM hydroxy -urea (VEGF+HU). Matrigel plugs were left in place for 7 days. (A) Quantification of hemoglobin (Hb) in the homogenized Matrigel plugs using Drabkin solution, results are expressed as Hb content in the Matrigel plug (mg/g) (mean±SEM; C57BL/6, n=5; SS, n=4–6). (B) Representative photomicrographs of Matrigel plugs. Scale bars, 1 cm.* P
    Figure Legend Snippet: In vivo angiogenesis is augmented in SCD chimeric mice and inhibited by hydroxyurea. A Matrigel plug neovascularization assay was employed to compare neovascularization in SCD chimeric (SS) and C57BL/6 mice and observe the effects of hydroxyurea on in vivo vessel formation. The following were injected subcutaneously into C57BL/6 and SS mice; a mixture of Matrigel and heparin without vascular endothelial growth factor (VEGF−, negative control); Matrigel, heparin and VEGF (VEGF +, positive control) or Matrigel, heparin, VEGF and 100 μM hydroxy -urea (VEGF+HU). Matrigel plugs were left in place for 7 days. (A) Quantification of hemoglobin (Hb) in the homogenized Matrigel plugs using Drabkin solution, results are expressed as Hb content in the Matrigel plug (mg/g) (mean±SEM; C57BL/6, n=5; SS, n=4–6). (B) Representative photomicrographs of Matrigel plugs. Scale bars, 1 cm.* P

    Techniques Used: In Vivo, Mouse Assay, Injection, Negative Control, Positive Control

    11) Product Images from "Novel role for SLPI in MOG-induced EAE revealed by spinal cord expression analysis"

    Article Title: Novel role for SLPI in MOG-induced EAE revealed by spinal cord expression analysis

    Journal: Journal of Neuroinflammation

    doi: 10.1186/1742-2094-5-20

    SLPI promotes proliferation of adult neural stem cells and induces cyclin D1 . A: Proliferation of rat neural stem cells after treatment with SLPI or VEGF, respectively. Cells were treated with indicated amounts of SLPI or VEGF for three days. Afterwards, they were pulsed with 10 μM BrdU. Proportion of BrdU-positive cells (+ std dev) was determined with the FITC BrdU Flow Kit. Presentation of a representative result of three experiments. *:p
    Figure Legend Snippet: SLPI promotes proliferation of adult neural stem cells and induces cyclin D1 . A: Proliferation of rat neural stem cells after treatment with SLPI or VEGF, respectively. Cells were treated with indicated amounts of SLPI or VEGF for three days. Afterwards, they were pulsed with 10 μM BrdU. Proportion of BrdU-positive cells (+ std dev) was determined with the FITC BrdU Flow Kit. Presentation of a representative result of three experiments. *:p

    Techniques Used: Flow Cytometry

    12) Product Images from "Lipoprotein-associated phospholipase A2 (Lp-PLA2) as a therapeutic target to prevent retinal vasopermeability during diabetes"

    Article Title: Lipoprotein-associated phospholipase A2 (Lp-PLA2) as a therapeutic target to prevent retinal vasopermeability during diabetes

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi: 10.1073/pnas.1514213113

    Inhibition of retinal vasopermeability by Lp-PLA 2 . Effect of combined SB435495 and intravitreal DMS1529 (anti-VEGF domain antibody) on retinal vasopermeability in diabetic (DB) rats. SB435495 was given i.p. daily at the indicated doses. VEGF antibody
    Figure Legend Snippet: Inhibition of retinal vasopermeability by Lp-PLA 2 . Effect of combined SB435495 and intravitreal DMS1529 (anti-VEGF domain antibody) on retinal vasopermeability in diabetic (DB) rats. SB435495 was given i.p. daily at the indicated doses. VEGF antibody

    Techniques Used: Inhibition, Proximity Ligation Assay

    13) Product Images from "Virus-Induced Decline in Soluble Vascular Endothelial Growth Receptor 2 Is Associated with Plasma Leakage in Dengue Hemorrhagic Fever ▿"

    Article Title: Virus-Induced Decline in Soluble Vascular Endothelial Growth Receptor 2 Is Associated with Plasma Leakage in Dengue Hemorrhagic Fever ▿

    Journal: Journal of Virology

    doi: 10.1128/JVI.01642-06

    Effects of dengue virus immune plasma on viral replication, sVEGFR2 production, and VEGF signaling in HUVEC. HUVEC were exposed to live dengue 2 virus with or without diluted immune plasma or to inactivated virus in the presence of immune plasma. Viral
    Figure Legend Snippet: Effects of dengue virus immune plasma on viral replication, sVEGFR2 production, and VEGF signaling in HUVEC. HUVEC were exposed to live dengue 2 virus with or without diluted immune plasma or to inactivated virus in the presence of immune plasma. Viral

    Techniques Used:

    14) Product Images from "Netrin-4 inhibits angiogenesis via binding to neogenin and recruitment of Unc5B"

    Article Title: Netrin-4 inhibits angiogenesis via binding to neogenin and recruitment of Unc5B

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi: 10.1073/pnas.0804008105

    N4 inhibits EC tube formation and migration induced by VEGF. ( A ) HUAEC were transfected with control siRNA or N4 siRNA before being incubated on top of Matrigel. Silencing the N4 gene in HUAEC increased both the branching and their ability to form tubular structures on Matrigel compared with nontransfected cells (NT) or with cells transfected with the control siRNA. RT-PCR analysis indicates that the N4 gene has been selectively silenced in N4 siRNA-treated HUAEC. ( B ) N4 does not affect the basal migration of growth-arrested HUAEC (C) but inhibits the migration induced by VEGF (V) as well as N1 (N1). ( C ) N1 and N4 inhibit the VEGF-induced FAK phosphorylation in HUAEC ( Upper ). ( Lower ) The total FAK immunoprecipitated. The ratio of phosphorylated FAK to total FAK is normalized to unstimulated HUAEC. **, P
    Figure Legend Snippet: N4 inhibits EC tube formation and migration induced by VEGF. ( A ) HUAEC were transfected with control siRNA or N4 siRNA before being incubated on top of Matrigel. Silencing the N4 gene in HUAEC increased both the branching and their ability to form tubular structures on Matrigel compared with nontransfected cells (NT) or with cells transfected with the control siRNA. RT-PCR analysis indicates that the N4 gene has been selectively silenced in N4 siRNA-treated HUAEC. ( B ) N4 does not affect the basal migration of growth-arrested HUAEC (C) but inhibits the migration induced by VEGF (V) as well as N1 (N1). ( C ) N1 and N4 inhibit the VEGF-induced FAK phosphorylation in HUAEC ( Upper ). ( Lower ) The total FAK immunoprecipitated. The ratio of phosphorylated FAK to total FAK is normalized to unstimulated HUAEC. **, P

    Techniques Used: Migration, Transfection, Incubation, Reverse Transcription Polymerase Chain Reaction, Immunoprecipitation

    ) or from retinal pigment epithelium (RPE) that have been exposed to VEGF (V) or not (0). Blots were probed for thrombospondin-1 (TSP-1), NPC-2, and N4. Band intensity ratios were normalized to 1 for non-VEGF-exposed cells.
    Figure Legend Snippet: ) or from retinal pigment epithelium (RPE) that have been exposed to VEGF (V) or not (0). Blots were probed for thrombospondin-1 (TSP-1), NPC-2, and N4. Band intensity ratios were normalized to 1 for non-VEGF-exposed cells.

    Techniques Used:

    Neogenin and Unc5B are required for N1- and N4-induced inhibition of HUAEC migration. ( A ) Anti-neogenin (red) antibody staining shows that NE is localized in filipodia of HUAEC. Upon incubation with N4, NE staining is relocalized in the perinuclear area. Nuclei are labeled in blue with DAPI. (Scale bars: 10 μm.) ( B ) Silencing either Unc5B or NE is sufficient to abrogate the chemotactic effect of N1 or N4. ( C ) The inhibition of N4 binding to NE abolishes its function whereas the inhibition of its binding to Unc5B or Unc5C has no effect. ( D ) Neogenin is equally detected in N4-unstimulated (0) and Netrin-4-stimulated HUAEC (0N4) or in VEGF-stimulated (V) or FGF-2-stimulated (F) HUAEC, whereas N4 increases the interaction between UNC5B and neogenin in VEGF-stimulated (VN4) or FGF-2-stimulated (FN4) HUAEC. Detection of neogenin in CHO-transfected cells served as a control (far right lane, NEO).
    Figure Legend Snippet: Neogenin and Unc5B are required for N1- and N4-induced inhibition of HUAEC migration. ( A ) Anti-neogenin (red) antibody staining shows that NE is localized in filipodia of HUAEC. Upon incubation with N4, NE staining is relocalized in the perinuclear area. Nuclei are labeled in blue with DAPI. (Scale bars: 10 μm.) ( B ) Silencing either Unc5B or NE is sufficient to abrogate the chemotactic effect of N1 or N4. ( C ) The inhibition of N4 binding to NE abolishes its function whereas the inhibition of its binding to Unc5B or Unc5C has no effect. ( D ) Neogenin is equally detected in N4-unstimulated (0) and Netrin-4-stimulated HUAEC (0N4) or in VEGF-stimulated (V) or FGF-2-stimulated (F) HUAEC, whereas N4 increases the interaction between UNC5B and neogenin in VEGF-stimulated (VN4) or FGF-2-stimulated (FN4) HUAEC. Detection of neogenin in CHO-transfected cells served as a control (far right lane, NEO).

    Techniques Used: Inhibition, Migration, Staining, Incubation, Labeling, Binding Assay, Transfection

    N4 is a neogenin ligand. ( A ) HUAEC and HUVEC express Unc5B (UB), Unc5C (UC), and neogenin (NE). The results are expressed relative to their abundance in human fetal brain and normalized to the β-actin mRNA content. ( B ) Immunoprecipitation of N1 and N4 by chimera of human Fc IgG fused to neogenin (NE), Unc5B (UB), or Unc5C (UC). VEGFR2 (VR2) is used as a negative control. ( C ) VEGF-driven HUAEC migration is inhibited by N4 and N1. The activity of N4 is almost totally abolished by addition of the chimera NE but not by chimera UB or UC. In contrast, N1 activity is inhibited by the three chimeras.
    Figure Legend Snippet: N4 is a neogenin ligand. ( A ) HUAEC and HUVEC express Unc5B (UB), Unc5C (UC), and neogenin (NE). The results are expressed relative to their abundance in human fetal brain and normalized to the β-actin mRNA content. ( B ) Immunoprecipitation of N1 and N4 by chimera of human Fc IgG fused to neogenin (NE), Unc5B (UB), or Unc5C (UC). VEGFR2 (VR2) is used as a negative control. ( C ) VEGF-driven HUAEC migration is inhibited by N4 and N1. The activity of N4 is almost totally abolished by addition of the chimera NE but not by chimera UB or UC. In contrast, N1 activity is inhibited by the three chimeras.

    Techniques Used: Immunoprecipitation, Negative Control, Migration, Activity Assay

    15) Product Images from "Heparanase-enhanced shedding of syndecan-1 by myeloma cells promotes endothelial invasion and angiogenesis"

    Article Title: Heparanase-enhanced shedding of syndecan-1 by myeloma cells promotes endothelial invasion and angiogenesis

    Journal: Blood

    doi: 10.1182/blood-2009-07-234757

    Shed syndecan-1 and VEGF act together to stimulate ERK activation and endothelial invasion . (A) Syndecan-1 enhances VEGF-mediated invasion of endothelial cells. An endothelial invasion assay was performed with conditioned medium from HPSE-high cells that
    Figure Legend Snippet: Shed syndecan-1 and VEGF act together to stimulate ERK activation and endothelial invasion . (A) Syndecan-1 enhances VEGF-mediated invasion of endothelial cells. An endothelial invasion assay was performed with conditioned medium from HPSE-high cells that

    Techniques Used: Activated Clotting Time Assay, Activation Assay, Invasion Assay

    Medium conditioned by heparanase high myeloma cells enhances endothelial invasion via activity of VEGF . (A) Endothelial cells were seeded on the top well of an invasion chamber coated with Matrigel and conditioned medium from either HPSE-low or HPSE-high
    Figure Legend Snippet: Medium conditioned by heparanase high myeloma cells enhances endothelial invasion via activity of VEGF . (A) Endothelial cells were seeded on the top well of an invasion chamber coated with Matrigel and conditioned medium from either HPSE-low or HPSE-high

    Techniques Used: Activity Assay

    16) Product Images from "Soluble VEGF receptor 1 (sFLT1) induces non-apoptotic death in ovarian and colorectal cancer cells"

    Article Title: Soluble VEGF receptor 1 (sFLT1) induces non-apoptotic death in ovarian and colorectal cancer cells

    Journal: Scientific Reports

    doi: 10.1038/srep24853

    Both transfected and exogenously applied sFLT1 has cytotoxic activity. ( a ) Comparison of the LDH leakage assays after transfection with pLV- EGFP or pLV- sFLT1 . In the 3 pLV- sFLT1 -expressing tumour derived cell lines, the level of LDH release was significantly higher than for the pLV- EGFP -transfected group. With the addition of recombinant VEGF to the pLV- sFLT1 groups, the levels of LDH release were restored to near those of the pLV- EGFP groups. Data are presented as a percentage of the control. *P
    Figure Legend Snippet: Both transfected and exogenously applied sFLT1 has cytotoxic activity. ( a ) Comparison of the LDH leakage assays after transfection with pLV- EGFP or pLV- sFLT1 . In the 3 pLV- sFLT1 -expressing tumour derived cell lines, the level of LDH release was significantly higher than for the pLV- EGFP -transfected group. With the addition of recombinant VEGF to the pLV- sFLT1 groups, the levels of LDH release were restored to near those of the pLV- EGFP groups. Data are presented as a percentage of the control. *P

    Techniques Used: Transfection, Activity Assay, Expressing, Derivative Assay, Recombinant

    17) Product Images from "Experimental and theoretical investigation of the precise transduction mechanism in giant magnetoresistive biosensors"

    Article Title: Experimental and theoretical investigation of the precise transduction mechanism in giant magnetoresistive biosensors

    Journal: Scientific Reports

    doi: 10.1038/srep18692

    VEGF and GCSF duplex assay. Anti-VEGF and anti-GCSF antibodies were immobilized on different sensors with quadruplicates. The sample containing VEGF at 500 pg/ml and GCSF at 500 pg/ml was measured. The nanoparticles were added to the chip at 2 min. The extra distance between the nanoparticles and the surface still produced the same positive signals with respect to the baseline signal (before adding the nanoparticles). BSA signals were the same as the baseline after adding the nanoparticles. The error bars are the standard deviations of 4 identical sensor signals.
    Figure Legend Snippet: VEGF and GCSF duplex assay. Anti-VEGF and anti-GCSF antibodies were immobilized on different sensors with quadruplicates. The sample containing VEGF at 500 pg/ml and GCSF at 500 pg/ml was measured. The nanoparticles were added to the chip at 2 min. The extra distance between the nanoparticles and the surface still produced the same positive signals with respect to the baseline signal (before adding the nanoparticles). BSA signals were the same as the baseline after adding the nanoparticles. The error bars are the standard deviations of 4 identical sensor signals.

    Techniques Used: Chromatin Immunoprecipitation, Produced

    18) Product Images from "Heparanase-enhanced shedding of syndecan-1 by myeloma cells promotes endothelial invasion and angiogenesis"

    Article Title: Heparanase-enhanced shedding of syndecan-1 by myeloma cells promotes endothelial invasion and angiogenesis

    Journal: Blood

    doi: 10.1182/blood-2009-07-234757

    Shed syndecan-1 and VEGF act together to stimulate ERK activation and endothelial invasion . (A) Syndecan-1 enhances VEGF-mediated invasion of endothelial cells. An endothelial invasion assay was performed with conditioned medium from HPSE-high cells that
    Figure Legend Snippet: Shed syndecan-1 and VEGF act together to stimulate ERK activation and endothelial invasion . (A) Syndecan-1 enhances VEGF-mediated invasion of endothelial cells. An endothelial invasion assay was performed with conditioned medium from HPSE-high cells that

    Techniques Used: Activated Clotting Time Assay, Activation Assay, Invasion Assay

    19) Product Images from "Retinal Inhibition of CCR3 Induces Retinal Cell Death in a Murine Model of Choroidal Neovascularization"

    Article Title: Retinal Inhibition of CCR3 Induces Retinal Cell Death in a Murine Model of Choroidal Neovascularization

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0157748

    Inhibition of CCR3 promotes cell death events in cultured human Műller cells. In cultured human MIO-M1 cells treated with PBS, CCL11, VEGF, or CCL11 and VEGF with pretreatment with CCR3i or control (DMSO), (A) western blots of CCR3 and VEGFR2. (B) TUNEL staining. (C) Quantification of TUNEL+ cells. (D) Western blots of cleaved caspase-3 and total caspase-3. (E) Western blots and quanfication of (F) BCL2 and (G) of AIF. (H) Western blots and (I) quanfication of BDNF (*p
    Figure Legend Snippet: Inhibition of CCR3 promotes cell death events in cultured human Műller cells. In cultured human MIO-M1 cells treated with PBS, CCL11, VEGF, or CCL11 and VEGF with pretreatment with CCR3i or control (DMSO), (A) western blots of CCR3 and VEGFR2. (B) TUNEL staining. (C) Quantification of TUNEL+ cells. (D) Western blots of cleaved caspase-3 and total caspase-3. (E) Western blots and quanfication of (F) BCL2 and (G) of AIF. (H) Western blots and (I) quanfication of BDNF (*p

    Techniques Used: Inhibition, Cell Culture, Western Blot, TUNEL Assay, Staining

    Inhibition of CCR3 in cultured human CECS reduces VEGF signaling without inducing cell death. In cultured human CECs treated with PBS or CCL11, VEGF or CCL11 and VEGF with or without pretreatment with CCR3i or control, (A) western blots of phosphorylated VEGFR2 (p-VEGFR2) and CCR3 and (B) quanfication of p-VEGFR2 (pretreatment with SU5416 was used as a control for inhibition of VEGFR2 activation) (**p
    Figure Legend Snippet: Inhibition of CCR3 in cultured human CECS reduces VEGF signaling without inducing cell death. In cultured human CECs treated with PBS or CCL11, VEGF or CCL11 and VEGF with or without pretreatment with CCR3i or control, (A) western blots of phosphorylated VEGFR2 (p-VEGFR2) and CCR3 and (B) quanfication of p-VEGFR2 (pretreatment with SU5416 was used as a control for inhibition of VEGFR2 activation) (**p

    Techniques Used: Inhibition, Cell Culture, Western Blot, Activation Assay

    Related Articles

    Enzyme-linked Immunosorbent Assay:

    Article Title: Biologization of Pcl-Mesh Using Platelet Rich Fibrin (Prf) Enhances Its Regenerative Potential In Vitro
    Article Snippet: .. Enzyme-Linked Immunosorbent Assay (ELISA) After 3 and 7 days of cultivation, cell culture supernatants of the pOBs cultivated on the PRF-coated scaffolds as well as control supernatants were collected and analyzed for amount of Vascular endothelial growth factor (VEGF), Transforming growth factor β1 (TGF β1), Platelet-derived growth factor (PDGF), Osteoprotegerin (OPG), and Interleukin 8 (IL-8). ..

    Article Title: Exosomes Secreted from Hypoxia-Preconditioned Mesenchymal Stem Cells Prevent Steroid-Induced Osteonecrosis of the Femoral Head by Promoting Angiogenesis in Rats
    Article Snippet: .. Enzyme-Linked Immunosorbent Assay (ELISA) Concentrations of vascular endothelial growth factor (VEGF) in the cellular supernatant of HUVECs were tested by ELISA. ..

    Cell Culture:

    Article Title: Biologization of Pcl-Mesh Using Platelet Rich Fibrin (Prf) Enhances Its Regenerative Potential In Vitro
    Article Snippet: .. Enzyme-Linked Immunosorbent Assay (ELISA) After 3 and 7 days of cultivation, cell culture supernatants of the pOBs cultivated on the PRF-coated scaffolds as well as control supernatants were collected and analyzed for amount of Vascular endothelial growth factor (VEGF), Transforming growth factor β1 (TGF β1), Platelet-derived growth factor (PDGF), Osteoprotegerin (OPG), and Interleukin 8 (IL-8). ..

    Concentration Assay:

    Article Title: Grape Seed Extract Positively Modulates Blood Pressure and Perceived Stress: A Randomized, Double-Blind, Placebo-Controlled Study in Healthy Volunteers
    Article Snippet: .. Vascular endothelial growth factor (VEGF) was tested at 10 ng/mL concentration as a positive control, and medium as a negative control. ..

    Positive Control:

    Article Title: Grape Seed Extract Positively Modulates Blood Pressure and Perceived Stress: A Randomized, Double-Blind, Placebo-Controlled Study in Healthy Volunteers
    Article Snippet: .. Vascular endothelial growth factor (VEGF) was tested at 10 ng/mL concentration as a positive control, and medium as a negative control. ..

    Negative Control:

    Article Title: Grape Seed Extract Positively Modulates Blood Pressure and Perceived Stress: A Randomized, Double-Blind, Placebo-Controlled Study in Healthy Volunteers
    Article Snippet: .. Vascular endothelial growth factor (VEGF) was tested at 10 ng/mL concentration as a positive control, and medium as a negative control. ..

    Activation Assay:

    Article Title: Melatonin improves brain function in a model of chronic Gulf War Illness with modulation of oxidative stress, NLRP3 inflammasomes, and BDNF-ERK-CREB pathway in the hippocampus
    Article Snippet: .. These comprised tumor necrosis factor-alpha (TNF-α), vascular endothelial growth factor (VEGF), fibroblast growth factor-beta (FGF-β), interferon-gamma (IFN-γ), leptin, monocyte chemoattractant protein-1 (MCP-1), stem cell factor (SCF), macrophage inflammatory protein-1 alpha (MIP-1α), interleukin-1 alpha (IL-1α), IL-1β, IL-5, IL-6, IL-15, IFN-γ inducible protein-10 (IP-10), regulated upon activation, normal T cell expressed and presumably secreted (rantes) and transforming growth factor- β (TGF-β). ..

    other:

    Article Title: Clinical and immunologic impact of short-course enzalutamide alone and with immunotherapy in non-metastatic castration sensitive prostate cancer
    Article Snippet: Impact of enzalutamide on vascular endothelial growth factorPreliminary data have suggested that enzalutamide could potentially impact vascular endothelial growth factor (VEGF) and this study involving enzalutamide without ADT provided an opportunity to evaluate that, independent of the immune analysis.

    Article Title: Low-dose decitabine for refractory prolonged isolated thrombocytopenia after HCT: a randomized multicenter trial
    Article Snippet: These included vascular endothelial growth factor (VEGF), endothelia-1, C-X-C chemokine receptor type 4 (CXCR4), stromal cell–derived factor-1 (SDF-1), and fibroblast growth factor-4 (FGF-4).

    Article Title: Bone Marrow Soluble Mediator Signatures of Patients With Philadelphia Chromosome-Negative Myeloproliferative Neoplasms
    Article Snippet: The growth factors granulocyte-macrophage colony stimulating factor (GM-CSF), macrophage colony stimulating factor (M-CSF), granulocyte colony stimulating factor (G-CSF), hepatocyte growth factor (HGF), vascular endothelial growth factor (VEGF), and VEGF receptor 2 (VEGF-R2) were also quantified.

    Crocin Bleaching Assay:

    Article Title: Vitreous expression of cytokines and growth factors in patients with diabetic retinopathy—An investigation of their expression based on clinical diabetic retinopathy grade
    Article Snippet: .. Interleukin-6 (IL-6), interleukin-8 (IL-8), interferon gamma-inducible protein-10 (IP-10), monocyte chemoattractant protein-1 (MCP-1), vascular endothelial growth factor (VEGF) and intercellular adhesion molecule-1 (CD54) were measured and quantified using Cytometric Bead Array (CBA) and Flex sets [ – ]. ..

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  • 93
    R&D Systems vegf d
    Measurement of the specificity of TTAC-0001. ( a ) Binding of TTAC-0001 to VEGF isoforms. Black bar represents VEGF-165. Gray bar represents VEGF-C and blank bar represents <t>VEGF-D.</t> hIgG and bevacizumab were used as controls. ( b ) Specificity measurement of TTAC-0001 on VEGFRs by Biacore. Line, hVEGFR1-Fc coated chip; dashed line (–), hVEGFR2-Fc coated chip; dashed line (—), hVEGFR-3-Fc coated chip. 50 nM of TTAC-0001 was injected at a flow rate of 30 μl/min. ( c ) Inhibition of TTAC-0001 in binding VEGF isoforms to VEGFR-2. Closed rectangular represents <t>VEGF165.</t> Closed circle represents VEGF-C and Open circle represents VEGF-D. ( d ) Immunohistochemistry showed positive staining of TTAC-0001 in endothelial cells of mouse aorta and mouse brain bEND.3 cells from Balb/c mice. HUVECs and human GBM tumor tissues were used as controls. Triangle represents stained regions of each cell.
    Vegf D, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/vegf d/product/R&D Systems
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    92
    R&D Systems recombinant mouse vegf rmvegf
    <t>VEGF</t> promotes increased MMP-2 expression in retinal NV in vivo and in human PDR tissue. A , top : Schematic demonstrating intravitreal injections of <t>rmVEGF</t> or PBS control. A , bottom : Mmp-2 mRNA from the neurosensory retina of animals injected with rmVEGF over time normalized to cyclophilin B mRNA and reported as fold induction compared with control (PBS-injected) eyes. Representative immunofluorescence analysis of MMP-2 (green arrows) in cross-section ( B ) and flat mount ( C ) from eyes injected with rmVEGF or PBS (control). The EC marker CD31 highlights tip cells of retinal microvasculature (arrowheads). All experiments were performed in duplicate and are representative of at least three independent experiments. n = 3 animals in each group. Student t test: * P
    Recombinant Mouse Vegf Rmvegf, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    R&D Systems recombinant vegf a
    Mechanism of action of anti-VEGFR-1 D16F7 mAb ( A ) D16F7 binding to VEGFR-1 does not affect VEGFR-1 interaction with PlGF or <t>VEGF-A.</t> The influence of D16F7 mAb on PlGF and VEGF-A binding to VEGFR-1 was analyzed using 96-well plates precoated with VEGFR-1/Fc chimera. Selected wells were pre-incubated with 5 μg/ml D16F7 mAb or control mouse IgG mAb (CTR mAb). VEGF-A or PlGF were allowed to bind the receptor, alone (No Ab) or in combination with neutralizing antibodies (NTR Ab). VEGF-A or PlGF bound to VEGFR-1/Fc chimera were detected using biotinylated anti-VEGF-A or anti-PlGF mAbs and streptavidin-alkaline phosphatase-conjugated. ( B ) D16F7 binding to VEGFR-1. The mAb binding to VEGFR-1 was assessed by incubating selected VEGFR-1/Fc chimera or BSA precoated wells with the mAb and using an alkaline phosphatase-conjugated anti-mouse antibody. The results (A, B) are expressed as absorbance at 405 nm, and represent the arithmetic mean values ± SD of three independent determinations. ( C ) D16F7 mAb inhibits endothelial cell migration in response to sVEGFR-1. Migration of HUV-ST cells (1.5 × 10 5 cells/chamber, 18 h incubation) induced by 5 μg/ml recombinant sVEGFR-1 or by 100 ng/ml FGF-2 was tested in Boyden chambers containing gelatin coated filters. Assays were performed by including 5 μg/ml D16F7 mAb or control mouse IgG mAb (CTR mAb) together with sVEGFR-1 or FGF-2 in the lower compartment of the chamber. Photographs from a representative experiment out of three are shown (×200 magnification) (left panel). Histograms represent the arithmetic mean values of migrated cells/microscopic field ± SD of three independent determinations. NS, non-stimulated cells (right panel). ( D ) D16F7 mAb hampers VEGFR-1 homodimerization. The influence of D16F7 mAb on VEGFR-1 homodimerization or heterodimerization with other VEGF-A receptors was evaluated in plates coated with sVEGFR-1. Chimeras containing the extracellular region of the different VEGFRs (i.e., VEGFR-1, VEGFR-2 and NRP-1) and the Fc region of human immunoglobulins were allowed to bind to the sVEGFR-1 on the wells previously treated or not with 5 μg/ml of D16F7 mAb. Results are expressed as percentage of binding inhibition and represent the mean values ± SD of six independent determinations. ( E ) D16F7 mAb inhibits VEGFR-1 auto-phosphorylation in response to VEGF-A and PlGF. VEGFR-1 auto-phosphorylation was analyzed by ELISA using extracts of CR-Mel cells stimulated at 37°C with VEGF-A or PlGF (200 ng/ml) for 10 min, after incubation of the cells with 5 μg/ml of D16F7 mAb or control mouse IgG mAb (CTR mAb) for 30 min. Results are expressed as percentage of binding inhibition and represent the mean values ± SD of three independent determinations.
    Recombinant Vegf A, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    R&D Systems recombinant human fc vegfr2 chimera
    Impact of VEGFf on VEGF-Receptor binding differs when VEGFf interacts with VEGFR1 and NP-1 . Simulation results for (A) Model 1 (VEGFf can bind to VEGFR1 and NP-1) and (B) Model 2 (VEGFf cannot bind to VEGFR1 and NP-1) 3 h after introduction of VEGF(1 ng/ml or 0.023 nM) and VEGFf to the cell system. VEGF bound to VEGFR1 (open), <t>VEGFR2</t> (filled), and sum of VEGF bound to VEGFR1, VEGFR2, NRP, and ECM (solid line)
    Recombinant Human Fc Vegfr2 Chimera, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Measurement of the specificity of TTAC-0001. ( a ) Binding of TTAC-0001 to VEGF isoforms. Black bar represents VEGF-165. Gray bar represents VEGF-C and blank bar represents VEGF-D. hIgG and bevacizumab were used as controls. ( b ) Specificity measurement of TTAC-0001 on VEGFRs by Biacore. Line, hVEGFR1-Fc coated chip; dashed line (–), hVEGFR2-Fc coated chip; dashed line (—), hVEGFR-3-Fc coated chip. 50 nM of TTAC-0001 was injected at a flow rate of 30 μl/min. ( c ) Inhibition of TTAC-0001 in binding VEGF isoforms to VEGFR-2. Closed rectangular represents VEGF165. Closed circle represents VEGF-C and Open circle represents VEGF-D. ( d ) Immunohistochemistry showed positive staining of TTAC-0001 in endothelial cells of mouse aorta and mouse brain bEND.3 cells from Balb/c mice. HUVECs and human GBM tumor tissues were used as controls. Triangle represents stained regions of each cell.

    Journal: mAbs

    Article Title: TTAC-0001, a human monoclonal antibody targeting VEGFR-2/KDR, blocks tumor angiogenesis

    doi: 10.1080/19420862.2015.1045168

    Figure Lengend Snippet: Measurement of the specificity of TTAC-0001. ( a ) Binding of TTAC-0001 to VEGF isoforms. Black bar represents VEGF-165. Gray bar represents VEGF-C and blank bar represents VEGF-D. hIgG and bevacizumab were used as controls. ( b ) Specificity measurement of TTAC-0001 on VEGFRs by Biacore. Line, hVEGFR1-Fc coated chip; dashed line (–), hVEGFR2-Fc coated chip; dashed line (—), hVEGFR-3-Fc coated chip. 50 nM of TTAC-0001 was injected at a flow rate of 30 μl/min. ( c ) Inhibition of TTAC-0001 in binding VEGF isoforms to VEGFR-2. Closed rectangular represents VEGF165. Closed circle represents VEGF-C and Open circle represents VEGF-D. ( d ) Immunohistochemistry showed positive staining of TTAC-0001 in endothelial cells of mouse aorta and mouse brain bEND.3 cells from Balb/c mice. HUVECs and human GBM tumor tissues were used as controls. Triangle represents stained regions of each cell.

    Article Snippet: Recombinant human VEGF121, VEGF165, VEGF-C, VEGF-D and KDR (ECD1–7)-Fc were also purchased from R & D systems.

    Techniques: Binding Assay, Chromatin Immunoprecipitation, Injection, Flow Cytometry, Inhibition, Immunohistochemistry, Staining, Mouse Assay

    VEGF promotes increased MMP-2 expression in retinal NV in vivo and in human PDR tissue. A , top : Schematic demonstrating intravitreal injections of rmVEGF or PBS control. A , bottom : Mmp-2 mRNA from the neurosensory retina of animals injected with rmVEGF over time normalized to cyclophilin B mRNA and reported as fold induction compared with control (PBS-injected) eyes. Representative immunofluorescence analysis of MMP-2 (green arrows) in cross-section ( B ) and flat mount ( C ) from eyes injected with rmVEGF or PBS (control). The EC marker CD31 highlights tip cells of retinal microvasculature (arrowheads). All experiments were performed in duplicate and are representative of at least three independent experiments. n = 3 animals in each group. Student t test: * P

    Journal: Diabetes

    Article Title: VEGF Secreted by Hypoxic Müller Cells Induces MMP-2 Expression and Activity in Endothelial Cells to Promote Retinal Neovascularization in Proliferative Diabetic Retinopathy

    doi: 10.2337/db13-0014

    Figure Lengend Snippet: VEGF promotes increased MMP-2 expression in retinal NV in vivo and in human PDR tissue. A , top : Schematic demonstrating intravitreal injections of rmVEGF or PBS control. A , bottom : Mmp-2 mRNA from the neurosensory retina of animals injected with rmVEGF over time normalized to cyclophilin B mRNA and reported as fold induction compared with control (PBS-injected) eyes. Representative immunofluorescence analysis of MMP-2 (green arrows) in cross-section ( B ) and flat mount ( C ) from eyes injected with rmVEGF or PBS (control). The EC marker CD31 highlights tip cells of retinal microvasculature (arrowheads). All experiments were performed in duplicate and are representative of at least three independent experiments. n = 3 animals in each group. Student t test: * P

    Article Snippet: Recombinant mouse VEGF (rmVEGF), recombinant human VEGF (rhVEGF), MMP-2, and VEGF ELISA kits were obtained from R & D Systems.

    Techniques: Expressing, In Vivo, Injection, Immunofluorescence, Marker

    Mechanism of action of anti-VEGFR-1 D16F7 mAb ( A ) D16F7 binding to VEGFR-1 does not affect VEGFR-1 interaction with PlGF or VEGF-A. The influence of D16F7 mAb on PlGF and VEGF-A binding to VEGFR-1 was analyzed using 96-well plates precoated with VEGFR-1/Fc chimera. Selected wells were pre-incubated with 5 μg/ml D16F7 mAb or control mouse IgG mAb (CTR mAb). VEGF-A or PlGF were allowed to bind the receptor, alone (No Ab) or in combination with neutralizing antibodies (NTR Ab). VEGF-A or PlGF bound to VEGFR-1/Fc chimera were detected using biotinylated anti-VEGF-A or anti-PlGF mAbs and streptavidin-alkaline phosphatase-conjugated. ( B ) D16F7 binding to VEGFR-1. The mAb binding to VEGFR-1 was assessed by incubating selected VEGFR-1/Fc chimera or BSA precoated wells with the mAb and using an alkaline phosphatase-conjugated anti-mouse antibody. The results (A, B) are expressed as absorbance at 405 nm, and represent the arithmetic mean values ± SD of three independent determinations. ( C ) D16F7 mAb inhibits endothelial cell migration in response to sVEGFR-1. Migration of HUV-ST cells (1.5 × 10 5 cells/chamber, 18 h incubation) induced by 5 μg/ml recombinant sVEGFR-1 or by 100 ng/ml FGF-2 was tested in Boyden chambers containing gelatin coated filters. Assays were performed by including 5 μg/ml D16F7 mAb or control mouse IgG mAb (CTR mAb) together with sVEGFR-1 or FGF-2 in the lower compartment of the chamber. Photographs from a representative experiment out of three are shown (×200 magnification) (left panel). Histograms represent the arithmetic mean values of migrated cells/microscopic field ± SD of three independent determinations. NS, non-stimulated cells (right panel). ( D ) D16F7 mAb hampers VEGFR-1 homodimerization. The influence of D16F7 mAb on VEGFR-1 homodimerization or heterodimerization with other VEGF-A receptors was evaluated in plates coated with sVEGFR-1. Chimeras containing the extracellular region of the different VEGFRs (i.e., VEGFR-1, VEGFR-2 and NRP-1) and the Fc region of human immunoglobulins were allowed to bind to the sVEGFR-1 on the wells previously treated or not with 5 μg/ml of D16F7 mAb. Results are expressed as percentage of binding inhibition and represent the mean values ± SD of six independent determinations. ( E ) D16F7 mAb inhibits VEGFR-1 auto-phosphorylation in response to VEGF-A and PlGF. VEGFR-1 auto-phosphorylation was analyzed by ELISA using extracts of CR-Mel cells stimulated at 37°C with VEGF-A or PlGF (200 ng/ml) for 10 min, after incubation of the cells with 5 μg/ml of D16F7 mAb or control mouse IgG mAb (CTR mAb) for 30 min. Results are expressed as percentage of binding inhibition and represent the mean values ± SD of three independent determinations.

    Journal: Oncotarget

    Article Title: Antitumor activity of a novel anti-vascular endothelial growth factor receptor-1 monoclonal antibody that does not interfere with ligand binding

    doi: 10.18632/oncotarget.12108

    Figure Lengend Snippet: Mechanism of action of anti-VEGFR-1 D16F7 mAb ( A ) D16F7 binding to VEGFR-1 does not affect VEGFR-1 interaction with PlGF or VEGF-A. The influence of D16F7 mAb on PlGF and VEGF-A binding to VEGFR-1 was analyzed using 96-well plates precoated with VEGFR-1/Fc chimera. Selected wells were pre-incubated with 5 μg/ml D16F7 mAb or control mouse IgG mAb (CTR mAb). VEGF-A or PlGF were allowed to bind the receptor, alone (No Ab) or in combination with neutralizing antibodies (NTR Ab). VEGF-A or PlGF bound to VEGFR-1/Fc chimera were detected using biotinylated anti-VEGF-A or anti-PlGF mAbs and streptavidin-alkaline phosphatase-conjugated. ( B ) D16F7 binding to VEGFR-1. The mAb binding to VEGFR-1 was assessed by incubating selected VEGFR-1/Fc chimera or BSA precoated wells with the mAb and using an alkaline phosphatase-conjugated anti-mouse antibody. The results (A, B) are expressed as absorbance at 405 nm, and represent the arithmetic mean values ± SD of three independent determinations. ( C ) D16F7 mAb inhibits endothelial cell migration in response to sVEGFR-1. Migration of HUV-ST cells (1.5 × 10 5 cells/chamber, 18 h incubation) induced by 5 μg/ml recombinant sVEGFR-1 or by 100 ng/ml FGF-2 was tested in Boyden chambers containing gelatin coated filters. Assays were performed by including 5 μg/ml D16F7 mAb or control mouse IgG mAb (CTR mAb) together with sVEGFR-1 or FGF-2 in the lower compartment of the chamber. Photographs from a representative experiment out of three are shown (×200 magnification) (left panel). Histograms represent the arithmetic mean values of migrated cells/microscopic field ± SD of three independent determinations. NS, non-stimulated cells (right panel). ( D ) D16F7 mAb hampers VEGFR-1 homodimerization. The influence of D16F7 mAb on VEGFR-1 homodimerization or heterodimerization with other VEGF-A receptors was evaluated in plates coated with sVEGFR-1. Chimeras containing the extracellular region of the different VEGFRs (i.e., VEGFR-1, VEGFR-2 and NRP-1) and the Fc region of human immunoglobulins were allowed to bind to the sVEGFR-1 on the wells previously treated or not with 5 μg/ml of D16F7 mAb. Results are expressed as percentage of binding inhibition and represent the mean values ± SD of six independent determinations. ( E ) D16F7 mAb inhibits VEGFR-1 auto-phosphorylation in response to VEGF-A and PlGF. VEGFR-1 auto-phosphorylation was analyzed by ELISA using extracts of CR-Mel cells stimulated at 37°C with VEGF-A or PlGF (200 ng/ml) for 10 min, after incubation of the cells with 5 μg/ml of D16F7 mAb or control mouse IgG mAb (CTR mAb) for 30 min. Results are expressed as percentage of binding inhibition and represent the mean values ± SD of three independent determinations.

    Article Snippet: Recombinant VEGF-A and PlGF homodimers, polyclonal antibodies against VEGF-A or PlGF, and recombinant VEGFR-1/Fc, VEGFR-2/Fc, neuropilin-1/Fc (NRP-1/Fc) and platelet derived growth factor receptor β/Fc (PDGFR/Fc) chimeras were from R & D Systems (Abingdon, UK).

    Techniques: Binding Assay, Incubation, Migration, Recombinant, Inhibition, Enzyme-linked Immunosorbent Assay

    D16F7 inhibits migration and vasculogenic mimicry of murine melanoma cells ( A ) B16F10 cells but not B16F0 cells express VEGFR-1. PlGF and VEGFR-1 expression in B16F0 and B16F10 cells was evaluated by RT-PCR analysis. ( B ) B16F10 cells are characterized by a highly invasive phenotype. The ability of B16F0 and B16F10 cells to invade the extracellular matrix was analyzed in Boyden chambers equipped with matrigel coated filters (2 × 10 5 cells/chamber, 4 h incubation). Histogram represents the arithmetic mean values of the number of invading cells/field ± SD of three independent determinations. ( C ) D16F7 mAb inhibits D16F10 cell migration in response to PlGF. Migration of B16F10 cells (1.5 × 10 5 cells/chamber) induced by PlGF (50 ng/ml, 18 h incubation) was evaluated in Boyden chambers equipped with gelatin coated filters, in the absence (No Ab) or presence of 2.5 μg/ml D16F7 mAb or control mouse IgG mAb (CTR mAb). Histogram represents the mean values of the number of migrated cells/field ± SD of three independent determinations. NS, non-stimulated. ( D ) Effect of D16F7 mAb on B16F10 cell ability to form tube-like structures. Cells (4 × 10 4 /well), untreated or pre-incubated with 5 μg/ml D16F7 mAb or control mouse IgG mAb at room temperature for 30 min, were seeded in the absence or presence of 50 ng/ml VEGF-A on 24-wells plates coated with matrigel. Tube-like structures formation was analyzed after 48 h. Photographs from a representative experiment out of three are shown (×50 magnification). Histogram represents the arithmetic mean values of the number of tube-like structures ± SD, counted in ten different microscopic fields for each experimental group, for a representative experiment out of three.

    Journal: Oncotarget

    Article Title: Antitumor activity of a novel anti-vascular endothelial growth factor receptor-1 monoclonal antibody that does not interfere with ligand binding

    doi: 10.18632/oncotarget.12108

    Figure Lengend Snippet: D16F7 inhibits migration and vasculogenic mimicry of murine melanoma cells ( A ) B16F10 cells but not B16F0 cells express VEGFR-1. PlGF and VEGFR-1 expression in B16F0 and B16F10 cells was evaluated by RT-PCR analysis. ( B ) B16F10 cells are characterized by a highly invasive phenotype. The ability of B16F0 and B16F10 cells to invade the extracellular matrix was analyzed in Boyden chambers equipped with matrigel coated filters (2 × 10 5 cells/chamber, 4 h incubation). Histogram represents the arithmetic mean values of the number of invading cells/field ± SD of three independent determinations. ( C ) D16F7 mAb inhibits D16F10 cell migration in response to PlGF. Migration of B16F10 cells (1.5 × 10 5 cells/chamber) induced by PlGF (50 ng/ml, 18 h incubation) was evaluated in Boyden chambers equipped with gelatin coated filters, in the absence (No Ab) or presence of 2.5 μg/ml D16F7 mAb or control mouse IgG mAb (CTR mAb). Histogram represents the mean values of the number of migrated cells/field ± SD of three independent determinations. NS, non-stimulated. ( D ) Effect of D16F7 mAb on B16F10 cell ability to form tube-like structures. Cells (4 × 10 4 /well), untreated or pre-incubated with 5 μg/ml D16F7 mAb or control mouse IgG mAb at room temperature for 30 min, were seeded in the absence or presence of 50 ng/ml VEGF-A on 24-wells plates coated with matrigel. Tube-like structures formation was analyzed after 48 h. Photographs from a representative experiment out of three are shown (×50 magnification). Histogram represents the arithmetic mean values of the number of tube-like structures ± SD, counted in ten different microscopic fields for each experimental group, for a representative experiment out of three.

    Article Snippet: Recombinant VEGF-A and PlGF homodimers, polyclonal antibodies against VEGF-A or PlGF, and recombinant VEGFR-1/Fc, VEGFR-2/Fc, neuropilin-1/Fc (NRP-1/Fc) and platelet derived growth factor receptor β/Fc (PDGFR/Fc) chimeras were from R & D Systems (Abingdon, UK).

    Techniques: Migration, Expressing, Reverse Transcription Polymerase Chain Reaction, Incubation

    Effects of D16F7 mAb on endothelial cells ( A, B ) D16F7 mAb inhibits endothelial cells migration in response to PlGF and VEGF-A in vitro . Migration of HUV-ST cells (1.5 × 10 5 cells/chamber, 18 h incubation), non stimulated (NS) or exposed to VEGFR-1 activating stimuli (50 ng/ml PlGF; 20 ng/ml VEGF-A) or to an unrelated stimulus (5 μg/ml fibronectin, FN), was tested in Boyden chambers containing gelatin coated filters in the presence or absence of 2.5 μg/ml of D16F7 mAb or control mouse IgG mAb (CTR mAb). Photographs from a representative experiment with PlGF out of three are shown (x200 magnification) (A). Histograms represent the arithmetic mean values of migrated cells/microscopic field ± SD of three independent determinations (B). ( C ) D16F7 mAb inhibits angiogenesis in vivo . Matrigel, containing (VEGF-A) or not (no VEGF-A) 100 ng/ml VEGF-A, was injected s.c. in the flank of C57BL/6 mice. In selected samples containing the angiogenic stimulus, 10 μg/ml D16F7 mAb or control mouse IgG mAb (CTR mAb) were included. The presence of newly formed blood vessels in matrigel plugs was observed macroscopically and the hemoglobin (Hb) content was quantified by the Drabkin's method. Histogram represents the mean values of the hemoglobin content, evaluated as A 540 /100 mg of matrigel in quadruplicate samples, ± SD.

    Journal: Oncotarget

    Article Title: Antitumor activity of a novel anti-vascular endothelial growth factor receptor-1 monoclonal antibody that does not interfere with ligand binding

    doi: 10.18632/oncotarget.12108

    Figure Lengend Snippet: Effects of D16F7 mAb on endothelial cells ( A, B ) D16F7 mAb inhibits endothelial cells migration in response to PlGF and VEGF-A in vitro . Migration of HUV-ST cells (1.5 × 10 5 cells/chamber, 18 h incubation), non stimulated (NS) or exposed to VEGFR-1 activating stimuli (50 ng/ml PlGF; 20 ng/ml VEGF-A) or to an unrelated stimulus (5 μg/ml fibronectin, FN), was tested in Boyden chambers containing gelatin coated filters in the presence or absence of 2.5 μg/ml of D16F7 mAb or control mouse IgG mAb (CTR mAb). Photographs from a representative experiment with PlGF out of three are shown (x200 magnification) (A). Histograms represent the arithmetic mean values of migrated cells/microscopic field ± SD of three independent determinations (B). ( C ) D16F7 mAb inhibits angiogenesis in vivo . Matrigel, containing (VEGF-A) or not (no VEGF-A) 100 ng/ml VEGF-A, was injected s.c. in the flank of C57BL/6 mice. In selected samples containing the angiogenic stimulus, 10 μg/ml D16F7 mAb or control mouse IgG mAb (CTR mAb) were included. The presence of newly formed blood vessels in matrigel plugs was observed macroscopically and the hemoglobin (Hb) content was quantified by the Drabkin's method. Histogram represents the mean values of the hemoglobin content, evaluated as A 540 /100 mg of matrigel in quadruplicate samples, ± SD.

    Article Snippet: Recombinant VEGF-A and PlGF homodimers, polyclonal antibodies against VEGF-A or PlGF, and recombinant VEGFR-1/Fc, VEGFR-2/Fc, neuropilin-1/Fc (NRP-1/Fc) and platelet derived growth factor receptor β/Fc (PDGFR/Fc) chimeras were from R & D Systems (Abingdon, UK).

    Techniques: Migration, In Vitro, Incubation, In Vivo, Injection, Mouse Assay

    Impact of VEGFf on VEGF-Receptor binding differs when VEGFf interacts with VEGFR1 and NP-1 . Simulation results for (A) Model 1 (VEGFf can bind to VEGFR1 and NP-1) and (B) Model 2 (VEGFf cannot bind to VEGFR1 and NP-1) 3 h after introduction of VEGF(1 ng/ml or 0.023 nM) and VEGFf to the cell system. VEGF bound to VEGFR1 (open), VEGFR2 (filled), and sum of VEGF bound to VEGFR1, VEGFR2, NRP, and ECM (solid line)

    Journal: BMC Systems Biology

    Article Title: Complex receptor-ligand dynamics control the response of the VEGF system to protease injury

    doi: 10.1186/1752-0509-5-170

    Figure Lengend Snippet: Impact of VEGFf on VEGF-Receptor binding differs when VEGFf interacts with VEGFR1 and NP-1 . Simulation results for (A) Model 1 (VEGFf can bind to VEGFR1 and NP-1) and (B) Model 2 (VEGFf cannot bind to VEGFR1 and NP-1) 3 h after introduction of VEGF(1 ng/ml or 0.023 nM) and VEGFf to the cell system. VEGF bound to VEGFR1 (open), VEGFR2 (filled), and sum of VEGF bound to VEGFR1, VEGFR2, NRP, and ECM (solid line)

    Article Snippet: Materials Human recombinant VEGF165 , recombinant human Fc-VEGFR2 chimera, Fc-VEGFR1 chimera and Fc-Neuropilin 1 chimera were purchased from R & D systems (Minneapolis, MN).

    Techniques: Binding Assay

    VEGF-mediated endocytosis and relative receptor levels impacts VEGF binding to VEGFR2 . A. Simulations were performed for Model 1 (VEGFf can bind to VEGFR1 and NP-1) and Model 2 (VEGFf cannot bind to VEGFR1 and NP-1) with VEGF (0.023 nM) and variable VEGFf for 3 h using base parameter values except for the internalization rate for VEGF-bound receptors. Total VEGFR2 bound to VEGF (surface and internal) is shown. B. Similar simulations were performed using all base parameter values but the initial conditions were altered to have 12,000 VEGFR1, VEGFR2, and NP-1 (VEGFR1 = VEGFR2 = NP-1), or 12,000 VEGFR1 and NP-1 but 120,000 VEGFR2 (10*VEGFR2), or 12,000 VEGFR2 and NP-1 but 120,000 VEGFR1 (10*VEGFR1), or 12,000 VEGFR1 and VEGFR2 but 120,000 NP-1 (10*NP-1). Model 1 is open circles and Model 2 is the filled circles in both A and B.

    Journal: BMC Systems Biology

    Article Title: Complex receptor-ligand dynamics control the response of the VEGF system to protease injury

    doi: 10.1186/1752-0509-5-170

    Figure Lengend Snippet: VEGF-mediated endocytosis and relative receptor levels impacts VEGF binding to VEGFR2 . A. Simulations were performed for Model 1 (VEGFf can bind to VEGFR1 and NP-1) and Model 2 (VEGFf cannot bind to VEGFR1 and NP-1) with VEGF (0.023 nM) and variable VEGFf for 3 h using base parameter values except for the internalization rate for VEGF-bound receptors. Total VEGFR2 bound to VEGF (surface and internal) is shown. B. Similar simulations were performed using all base parameter values but the initial conditions were altered to have 12,000 VEGFR1, VEGFR2, and NP-1 (VEGFR1 = VEGFR2 = NP-1), or 12,000 VEGFR1 and NP-1 but 120,000 VEGFR2 (10*VEGFR2), or 12,000 VEGFR2 and NP-1 but 120,000 VEGFR1 (10*VEGFR1), or 12,000 VEGFR1 and VEGFR2 but 120,000 NP-1 (10*NP-1). Model 1 is open circles and Model 2 is the filled circles in both A and B.

    Article Snippet: Materials Human recombinant VEGF165 , recombinant human Fc-VEGFR2 chimera, Fc-VEGFR1 chimera and Fc-Neuropilin 1 chimera were purchased from R & D systems (Minneapolis, MN).

    Techniques: Binding Assay

    Coupling rate constant between VEGFR1 and NP-1 impacts VEGF binding to VEGFR2 . Simulations were performed with Model 1 (VEGFf can bind to VEGFR1 and NP-1 - dashed line) and Model 2 (VEGFf cannot bind to VEGFR1 and NP-1 - filled circles) with VEGF (0.023 nM) and variable VEGFf for 3 h using base parameter values except for the coupling rate between VEGFR1 and NP-1. Total VEGFR2 bound to VEGF (surface and internal) is shown. kc0 is the base value shown in Table 2. kc = 0 is equivalent for both models and is shown in the solid line.

    Journal: BMC Systems Biology

    Article Title: Complex receptor-ligand dynamics control the response of the VEGF system to protease injury

    doi: 10.1186/1752-0509-5-170

    Figure Lengend Snippet: Coupling rate constant between VEGFR1 and NP-1 impacts VEGF binding to VEGFR2 . Simulations were performed with Model 1 (VEGFf can bind to VEGFR1 and NP-1 - dashed line) and Model 2 (VEGFf cannot bind to VEGFR1 and NP-1 - filled circles) with VEGF (0.023 nM) and variable VEGFf for 3 h using base parameter values except for the coupling rate between VEGFR1 and NP-1. Total VEGFR2 bound to VEGF (surface and internal) is shown. kc0 is the base value shown in Table 2. kc = 0 is equivalent for both models and is shown in the solid line.

    Article Snippet: Materials Human recombinant VEGF165 , recombinant human Fc-VEGFR2 chimera, Fc-VEGFR1 chimera and Fc-Neuropilin 1 chimera were purchased from R & D systems (Minneapolis, MN).

    Techniques: Binding Assay

    ECM Density Impacts Receptor Binding of VEGF at High Densities . Simulation results following introduction of VEGF (0.023 nM or 1 ng/ml) at time zero. VEGF retained by VEGFR1 (open) or VEGFR2 (filled) after 3 h of VEGF exposure is shown. All other parameter values were at base values (Table 2) except for ECM site density.

    Journal: BMC Systems Biology

    Article Title: Complex receptor-ligand dynamics control the response of the VEGF system to protease injury

    doi: 10.1186/1752-0509-5-170

    Figure Lengend Snippet: ECM Density Impacts Receptor Binding of VEGF at High Densities . Simulation results following introduction of VEGF (0.023 nM or 1 ng/ml) at time zero. VEGF retained by VEGFR1 (open) or VEGFR2 (filled) after 3 h of VEGF exposure is shown. All other parameter values were at base values (Table 2) except for ECM site density.

    Article Snippet: Materials Human recombinant VEGF165 , recombinant human Fc-VEGFR2 chimera, Fc-VEGFR1 chimera and Fc-Neuropilin 1 chimera were purchased from R & D systems (Minneapolis, MN).

    Techniques: Binding Assay

    NP-1 sequestering by VEGFR1 is key to difference in VEGF binding to VEGFR2 . (A) Simulations were run with VEGF (0.023 nM) and variable VEGFf for 3 h using standard parameter values (Table 2). VEGFR1 bound to NP-1 or unbound VEGFR1 are shown for Model 1 (VEGFf can bind to VEGFR1 and NP-1 - open) and Model 2 (VEGFf cannot bind to VEGFR1 and NP-1 -filled). Note the direct overlap of the unbound VEGFR1 for the two models. (B) Similar simulations were run but with 0 (solid line) or 1 nM VEGFf for Model 1 (open) and Model 2 (filled) with variable levels of NP-1. VEGF bound to VEGFR2 is shown.

    Journal: BMC Systems Biology

    Article Title: Complex receptor-ligand dynamics control the response of the VEGF system to protease injury

    doi: 10.1186/1752-0509-5-170

    Figure Lengend Snippet: NP-1 sequestering by VEGFR1 is key to difference in VEGF binding to VEGFR2 . (A) Simulations were run with VEGF (0.023 nM) and variable VEGFf for 3 h using standard parameter values (Table 2). VEGFR1 bound to NP-1 or unbound VEGFR1 are shown for Model 1 (VEGFf can bind to VEGFR1 and NP-1 - open) and Model 2 (VEGFf cannot bind to VEGFR1 and NP-1 -filled). Note the direct overlap of the unbound VEGFR1 for the two models. (B) Similar simulations were run but with 0 (solid line) or 1 nM VEGFf for Model 1 (open) and Model 2 (filled) with variable levels of NP-1. VEGF bound to VEGFR2 is shown.

    Article Snippet: Materials Human recombinant VEGF165 , recombinant human Fc-VEGFR2 chimera, Fc-VEGFR1 chimera and Fc-Neuropilin 1 chimera were purchased from R & D systems (Minneapolis, MN).

    Techniques: Binding Assay

    Model illustrating VEGF and VEGFf binding interactions . The following abbreviations are used: R1 for VEGFR1, R2 for VEGFR2, NP-1 for neuropilin-1. Question mark indicates that it is unknown if the binding reaction occurs.

    Journal: BMC Systems Biology

    Article Title: Complex receptor-ligand dynamics control the response of the VEGF system to protease injury

    doi: 10.1186/1752-0509-5-170

    Figure Lengend Snippet: Model illustrating VEGF and VEGFf binding interactions . The following abbreviations are used: R1 for VEGFR1, R2 for VEGFR2, NP-1 for neuropilin-1. Question mark indicates that it is unknown if the binding reaction occurs.

    Article Snippet: Materials Human recombinant VEGF165 , recombinant human Fc-VEGFR2 chimera, Fc-VEGFR1 chimera and Fc-Neuropilin 1 chimera were purchased from R & D systems (Minneapolis, MN).

    Techniques: Binding Assay

    VEGF Conversion to VEGFf Impacts Binding to VEGFR1 and VEGFR2 . Simulations were run for 2 h using baseline parameter values. The total concentration of VEGF and VEGFf was kept constant at 0.45 nM and VEGFR1, VEGFR2, and NP-1 equal at 12,000 #/cell. (A) VEGF bound to VEGFR2 or VEGFR1 for Model 1 (VEGFf can bind to VEGFR1 alone or when VEGFR1 is bound to NP-1 -open) and Model 2 (VEGFf cannot bind to VEGFR1 bound to NP-1 - filled) are shown. (B) VEGFR1 binding by VEGFf (Model 1- open circle, Model 2 -filled circle), or the sum of both VEGF and VEGFf bound to VEGFR1 (Model 1 - open square, Model 2 -filled triangle) is plotted. (C). NP-1 complexes increase for Model 1. VEGF-VEGFR2-NP-1 complexes (Model 1-open square), VEGF-VEGFR1-NP-1 (Model 1 - open triangle), and the sum of VEGF-VEGFR1-NP-1 and VEGF-VEGFR2-NP-1 complexes (Model 1 -open circle, Model 2 - filled circle). Note that there are no VEGF-VEGFR1-NP-1 complexes with Model 2.

    Journal: BMC Systems Biology

    Article Title: Complex receptor-ligand dynamics control the response of the VEGF system to protease injury

    doi: 10.1186/1752-0509-5-170

    Figure Lengend Snippet: VEGF Conversion to VEGFf Impacts Binding to VEGFR1 and VEGFR2 . Simulations were run for 2 h using baseline parameter values. The total concentration of VEGF and VEGFf was kept constant at 0.45 nM and VEGFR1, VEGFR2, and NP-1 equal at 12,000 #/cell. (A) VEGF bound to VEGFR2 or VEGFR1 for Model 1 (VEGFf can bind to VEGFR1 alone or when VEGFR1 is bound to NP-1 -open) and Model 2 (VEGFf cannot bind to VEGFR1 bound to NP-1 - filled) are shown. (B) VEGFR1 binding by VEGFf (Model 1- open circle, Model 2 -filled circle), or the sum of both VEGF and VEGFf bound to VEGFR1 (Model 1 - open square, Model 2 -filled triangle) is plotted. (C). NP-1 complexes increase for Model 1. VEGF-VEGFR2-NP-1 complexes (Model 1-open square), VEGF-VEGFR1-NP-1 (Model 1 - open triangle), and the sum of VEGF-VEGFR1-NP-1 and VEGF-VEGFR2-NP-1 complexes (Model 1 -open circle, Model 2 - filled circle). Note that there are no VEGF-VEGFR1-NP-1 complexes with Model 2.

    Article Snippet: Materials Human recombinant VEGF165 , recombinant human Fc-VEGFR2 chimera, Fc-VEGFR1 chimera and Fc-Neuropilin 1 chimera were purchased from R & D systems (Minneapolis, MN).

    Techniques: Binding Assay, Concentration Assay