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unbound human vegf  (R&D Systems)


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    R&D Systems unbound human vegf
    Schematic representation and biochemical characterization of traps. A Basic protein structure of traps. <t>VEGF-trap</t> is composed of the VEGF-binding region (domain 2 and 3 of VEGFR-1 and -2, respectively) and the Fc region of IgG1 (CH2 and CH3 domains). The Sticky-traps, Sticky-trap68, Sticky-trap78 and Sticky-trap678 contain the heparin-binding domains (HBDs) encoded by exons 6 and 8, 7 and 8, and 6, 7 and 8 of vascular endothelial growth factor, respectively. See Supplementary Fig S1A and methods for further details. <t>B–D</t> <t>Affinity</t> of traps to extracellular matrix (ECM). (B) Immunostaining (red signal) and Western blot analysis (on the right of the image) of traps in PC-3 cell monolayers and conditioned supernatant, respectively. Similar results are shown in Supplementary Fig S4A for the A-673 transgenic lines. Plus (+) dox samples were collected 48 h after addition of doxycycline-containing media. Scale bar, 100 μm. (C) Binding of recombinant traps to ECM. (D) Affinity of recombinant traps to heparin-Sepharose column. E, F Assessment of traps ability to bind human VEGF. (E) Free VEGF levels in the conditioned of PC-3 cancer transgenic cell lines, co-cultured of wild-type PC-3 cells. Media were collected after 48 h of culture with or without the addition of doxycycline. (F) Binding affinity (KD) of recombinant traps to human VEGF 165 (VEGF-trap; 9.0 pM, Short-trap; 12.2 pM, and Sticky-trap 13.9 pM). G Inhibition of VEGF-induced human umbilical vein endothelial cells proliferation by recombinant traps. Source data are available online for this figure.
    Unbound Human Vegf, supplied by R&D Systems, used in various techniques. Bioz Stars score: 97/100, based on 1226 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/unbound human vegf/product/R&D Systems
    Average 97 stars, based on 1226 article reviews
    unbound human vegf - by Bioz Stars, 2026-02
    97/100 stars

    Images

    1) Product Images from "Local acting Sticky-trap inhibits vascular endothelial growth factor dependent pathological angiogenesis in the eye"

    Article Title: Local acting Sticky-trap inhibits vascular endothelial growth factor dependent pathological angiogenesis in the eye

    Journal: EMBO Molecular Medicine

    doi: 10.1002/emmm.201303708

    Schematic representation and biochemical characterization of traps. A Basic protein structure of traps. VEGF-trap is composed of the VEGF-binding region (domain 2 and 3 of VEGFR-1 and -2, respectively) and the Fc region of IgG1 (CH2 and CH3 domains). The Sticky-traps, Sticky-trap68, Sticky-trap78 and Sticky-trap678 contain the heparin-binding domains (HBDs) encoded by exons 6 and 8, 7 and 8, and 6, 7 and 8 of vascular endothelial growth factor, respectively. See Supplementary Fig S1A and methods for further details. B–D Affinity of traps to extracellular matrix (ECM). (B) Immunostaining (red signal) and Western blot analysis (on the right of the image) of traps in PC-3 cell monolayers and conditioned supernatant, respectively. Similar results are shown in Supplementary Fig S4A for the A-673 transgenic lines. Plus (+) dox samples were collected 48 h after addition of doxycycline-containing media. Scale bar, 100 μm. (C) Binding of recombinant traps to ECM. (D) Affinity of recombinant traps to heparin-Sepharose column. E, F Assessment of traps ability to bind human VEGF. (E) Free VEGF levels in the conditioned of PC-3 cancer transgenic cell lines, co-cultured of wild-type PC-3 cells. Media were collected after 48 h of culture with or without the addition of doxycycline. (F) Binding affinity (KD) of recombinant traps to human VEGF 165 (VEGF-trap; 9.0 pM, Short-trap; 12.2 pM, and Sticky-trap 13.9 pM). G Inhibition of VEGF-induced human umbilical vein endothelial cells proliferation by recombinant traps. Source data are available online for this figure.
    Figure Legend Snippet: Schematic representation and biochemical characterization of traps. A Basic protein structure of traps. VEGF-trap is composed of the VEGF-binding region (domain 2 and 3 of VEGFR-1 and -2, respectively) and the Fc region of IgG1 (CH2 and CH3 domains). The Sticky-traps, Sticky-trap68, Sticky-trap78 and Sticky-trap678 contain the heparin-binding domains (HBDs) encoded by exons 6 and 8, 7 and 8, and 6, 7 and 8 of vascular endothelial growth factor, respectively. See Supplementary Fig S1A and methods for further details. B–D Affinity of traps to extracellular matrix (ECM). (B) Immunostaining (red signal) and Western blot analysis (on the right of the image) of traps in PC-3 cell monolayers and conditioned supernatant, respectively. Similar results are shown in Supplementary Fig S4A for the A-673 transgenic lines. Plus (+) dox samples were collected 48 h after addition of doxycycline-containing media. Scale bar, 100 μm. (C) Binding of recombinant traps to ECM. (D) Affinity of recombinant traps to heparin-Sepharose column. E, F Assessment of traps ability to bind human VEGF. (E) Free VEGF levels in the conditioned of PC-3 cancer transgenic cell lines, co-cultured of wild-type PC-3 cells. Media were collected after 48 h of culture with or without the addition of doxycycline. (F) Binding affinity (KD) of recombinant traps to human VEGF 165 (VEGF-trap; 9.0 pM, Short-trap; 12.2 pM, and Sticky-trap 13.9 pM). G Inhibition of VEGF-induced human umbilical vein endothelial cells proliferation by recombinant traps. Source data are available online for this figure.

    Techniques Used: Binding Assay, Immunostaining, Western Blot, Transgenic Assay, Recombinant, Cell Culture, Inhibition

    Pharmacokinetic profile and tissue distribution of traps. A Traps (100 μg) were injected subcutaneously into C57BL/6J mice, and serum levels were estimated using an ELISA assay. Error bars represent s.e.m. ( n = 5). B Serum levels of VEGF at various time points after subcutaneous injection of traps (100 μg) into C57BL/6J mice. Error bars represent s.e.m. ( n = 5; *** P < 0.001, one-way ANOVA). C–F Trap levels in various tissues 48 h post-subcutaneous injection of traps (100 μg) into C57BL/6J mice. Error bars represent s.e.m. ( n = 5; *** P < 0.001, one-way ANOVA).
    Figure Legend Snippet: Pharmacokinetic profile and tissue distribution of traps. A Traps (100 μg) were injected subcutaneously into C57BL/6J mice, and serum levels were estimated using an ELISA assay. Error bars represent s.e.m. ( n = 5). B Serum levels of VEGF at various time points after subcutaneous injection of traps (100 μg) into C57BL/6J mice. Error bars represent s.e.m. ( n = 5; *** P < 0.001, one-way ANOVA). C–F Trap levels in various tissues 48 h post-subcutaneous injection of traps (100 μg) into C57BL/6J mice. Error bars represent s.e.m. ( n = 5; *** P < 0.001, one-way ANOVA).

    Techniques Used: Injection, Enzyme-linked Immunosorbent Assay



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    unbound human vegf  (R&D Systems)
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    R&D Systems unbound human vegf
    Schematic representation and biochemical characterization of traps. A Basic protein structure of traps. <t>VEGF-trap</t> is composed of the VEGF-binding region (domain 2 and 3 of VEGFR-1 and -2, respectively) and the Fc region of IgG1 (CH2 and CH3 domains). The Sticky-traps, Sticky-trap68, Sticky-trap78 and Sticky-trap678 contain the heparin-binding domains (HBDs) encoded by exons 6 and 8, 7 and 8, and 6, 7 and 8 of vascular endothelial growth factor, respectively. See Supplementary Fig S1A and methods for further details. <t>B–D</t> <t>Affinity</t> of traps to extracellular matrix (ECM). (B) Immunostaining (red signal) and Western blot analysis (on the right of the image) of traps in PC-3 cell monolayers and conditioned supernatant, respectively. Similar results are shown in Supplementary Fig S4A for the A-673 transgenic lines. Plus (+) dox samples were collected 48 h after addition of doxycycline-containing media. Scale bar, 100 μm. (C) Binding of recombinant traps to ECM. (D) Affinity of recombinant traps to heparin-Sepharose column. E, F Assessment of traps ability to bind human VEGF. (E) Free VEGF levels in the conditioned of PC-3 cancer transgenic cell lines, co-cultured of wild-type PC-3 cells. Media were collected after 48 h of culture with or without the addition of doxycycline. (F) Binding affinity (KD) of recombinant traps to human VEGF 165 (VEGF-trap; 9.0 pM, Short-trap; 12.2 pM, and Sticky-trap 13.9 pM). G Inhibition of VEGF-induced human umbilical vein endothelial cells proliferation by recombinant traps. Source data are available online for this figure.
    Unbound Human Vegf, supplied by R&D Systems, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/unbound human vegf/product/R&D Systems
    Average 97 stars, based on 1 article reviews
    unbound human vegf - by Bioz Stars, 2026-02
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    R&D Systems vegf 165 (unbound to bevacizumab)
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    Vegf 165 (Unbound To Bevacizumab), supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Schematic representation and biochemical characterization of traps. A Basic protein structure of traps. VEGF-trap is composed of the VEGF-binding region (domain 2 and 3 of VEGFR-1 and -2, respectively) and the Fc region of IgG1 (CH2 and CH3 domains). The Sticky-traps, Sticky-trap68, Sticky-trap78 and Sticky-trap678 contain the heparin-binding domains (HBDs) encoded by exons 6 and 8, 7 and 8, and 6, 7 and 8 of vascular endothelial growth factor, respectively. See Supplementary Fig S1A and methods for further details. B–D Affinity of traps to extracellular matrix (ECM). (B) Immunostaining (red signal) and Western blot analysis (on the right of the image) of traps in PC-3 cell monolayers and conditioned supernatant, respectively. Similar results are shown in Supplementary Fig S4A for the A-673 transgenic lines. Plus (+) dox samples were collected 48 h after addition of doxycycline-containing media. Scale bar, 100 μm. (C) Binding of recombinant traps to ECM. (D) Affinity of recombinant traps to heparin-Sepharose column. E, F Assessment of traps ability to bind human VEGF. (E) Free VEGF levels in the conditioned of PC-3 cancer transgenic cell lines, co-cultured of wild-type PC-3 cells. Media were collected after 48 h of culture with or without the addition of doxycycline. (F) Binding affinity (KD) of recombinant traps to human VEGF 165 (VEGF-trap; 9.0 pM, Short-trap; 12.2 pM, and Sticky-trap 13.9 pM). G Inhibition of VEGF-induced human umbilical vein endothelial cells proliferation by recombinant traps. Source data are available online for this figure.

    Journal: EMBO Molecular Medicine

    Article Title: Local acting Sticky-trap inhibits vascular endothelial growth factor dependent pathological angiogenesis in the eye

    doi: 10.1002/emmm.201303708

    Figure Lengend Snippet: Schematic representation and biochemical characterization of traps. A Basic protein structure of traps. VEGF-trap is composed of the VEGF-binding region (domain 2 and 3 of VEGFR-1 and -2, respectively) and the Fc region of IgG1 (CH2 and CH3 domains). The Sticky-traps, Sticky-trap68, Sticky-trap78 and Sticky-trap678 contain the heparin-binding domains (HBDs) encoded by exons 6 and 8, 7 and 8, and 6, 7 and 8 of vascular endothelial growth factor, respectively. See Supplementary Fig S1A and methods for further details. B–D Affinity of traps to extracellular matrix (ECM). (B) Immunostaining (red signal) and Western blot analysis (on the right of the image) of traps in PC-3 cell monolayers and conditioned supernatant, respectively. Similar results are shown in Supplementary Fig S4A for the A-673 transgenic lines. Plus (+) dox samples were collected 48 h after addition of doxycycline-containing media. Scale bar, 100 μm. (C) Binding of recombinant traps to ECM. (D) Affinity of recombinant traps to heparin-Sepharose column. E, F Assessment of traps ability to bind human VEGF. (E) Free VEGF levels in the conditioned of PC-3 cancer transgenic cell lines, co-cultured of wild-type PC-3 cells. Media were collected after 48 h of culture with or without the addition of doxycycline. (F) Binding affinity (KD) of recombinant traps to human VEGF 165 (VEGF-trap; 9.0 pM, Short-trap; 12.2 pM, and Sticky-trap 13.9 pM). G Inhibition of VEGF-induced human umbilical vein endothelial cells proliferation by recombinant traps. Source data are available online for this figure.

    Article Snippet: Binding affinity of traps was determined using an ELISA able to detect unbound human VEGF (R&D Systems, cat. # DVE00).

    Techniques: Binding Assay, Immunostaining, Western Blot, Transgenic Assay, Recombinant, Cell Culture, Inhibition

    Pharmacokinetic profile and tissue distribution of traps. A Traps (100 μg) were injected subcutaneously into C57BL/6J mice, and serum levels were estimated using an ELISA assay. Error bars represent s.e.m. ( n = 5). B Serum levels of VEGF at various time points after subcutaneous injection of traps (100 μg) into C57BL/6J mice. Error bars represent s.e.m. ( n = 5; *** P < 0.001, one-way ANOVA). C–F Trap levels in various tissues 48 h post-subcutaneous injection of traps (100 μg) into C57BL/6J mice. Error bars represent s.e.m. ( n = 5; *** P < 0.001, one-way ANOVA).

    Journal: EMBO Molecular Medicine

    Article Title: Local acting Sticky-trap inhibits vascular endothelial growth factor dependent pathological angiogenesis in the eye

    doi: 10.1002/emmm.201303708

    Figure Lengend Snippet: Pharmacokinetic profile and tissue distribution of traps. A Traps (100 μg) were injected subcutaneously into C57BL/6J mice, and serum levels were estimated using an ELISA assay. Error bars represent s.e.m. ( n = 5). B Serum levels of VEGF at various time points after subcutaneous injection of traps (100 μg) into C57BL/6J mice. Error bars represent s.e.m. ( n = 5; *** P < 0.001, one-way ANOVA). C–F Trap levels in various tissues 48 h post-subcutaneous injection of traps (100 μg) into C57BL/6J mice. Error bars represent s.e.m. ( n = 5; *** P < 0.001, one-way ANOVA).

    Article Snippet: Binding affinity of traps was determined using an ELISA able to detect unbound human VEGF (R&D Systems, cat. # DVE00).

    Techniques: Injection, Enzyme-linked Immunosorbent Assay

    Patient and study characteristics

    Journal: Cancer Chemotherapy and Pharmacology

    Article Title: A pharmacokinetic binding model for bevacizumab and VEGF 165 in colorectal cancer patients

    doi: 10.1007/s00280-015-2701-3

    Figure Lengend Snippet: Patient and study characteristics

    Article Snippet: The concentration of free VEGF 165 (unbound to bevacizumab) in serum was measured by a commercially available ELISA kit for VEGF 165 (Quantikine ® human VEGF, R&D Systems ® Europe).

    Techniques:

    In vitro VEGF 165 concentrations after addition of bevacizumab

    Journal: Cancer Chemotherapy and Pharmacology

    Article Title: A pharmacokinetic binding model for bevacizumab and VEGF 165 in colorectal cancer patients

    doi: 10.1007/s00280-015-2701-3

    Figure Lengend Snippet: In vitro VEGF 165 concentrations after addition of bevacizumab

    Article Snippet: The concentration of free VEGF 165 (unbound to bevacizumab) in serum was measured by a commercially available ELISA kit for VEGF 165 (Quantikine ® human VEGF, R&D Systems ® Europe).

    Techniques: In Vitro

    Population parameter estimates from the PK model (bevacizumab analyzed alone) and TMDD model (bevacizumab and VEGF 165 analyzed simultaneously)

    Journal: Cancer Chemotherapy and Pharmacology

    Article Title: A pharmacokinetic binding model for bevacizumab and VEGF 165 in colorectal cancer patients

    doi: 10.1007/s00280-015-2701-3

    Figure Lengend Snippet: Population parameter estimates from the PK model (bevacizumab analyzed alone) and TMDD model (bevacizumab and VEGF 165 analyzed simultaneously)

    Article Snippet: The concentration of free VEGF 165 (unbound to bevacizumab) in serum was measured by a commercially available ELISA kit for VEGF 165 (Quantikine ® human VEGF, R&D Systems ® Europe).

    Techniques:

    Structure of the binding model for bevacizumab–VEGF 165 interaction. The approximation CL RC = CL was used for purposes of model fitting

    Journal: Cancer Chemotherapy and Pharmacology

    Article Title: A pharmacokinetic binding model for bevacizumab and VEGF 165 in colorectal cancer patients

    doi: 10.1007/s00280-015-2701-3

    Figure Lengend Snippet: Structure of the binding model for bevacizumab–VEGF 165 interaction. The approximation CL RC = CL was used for purposes of model fitting

    Article Snippet: The concentration of free VEGF 165 (unbound to bevacizumab) in serum was measured by a commercially available ELISA kit for VEGF 165 (Quantikine ® human VEGF, R&D Systems ® Europe).

    Techniques: Binding Assay

    Prediction-corrected visual predictive checks of the binding model based on 1000 simulations (panel a total bevacizumab, panel b free VEGF 165 ). Median ( solid line ), 10th and 90th percentiles ( dashed lines ) of the observed data ( circles ) are compared to the 95 % confidence intervals ( shaded areas ) for the median, 10th and 90th percentiles of the simulated data

    Journal: Cancer Chemotherapy and Pharmacology

    Article Title: A pharmacokinetic binding model for bevacizumab and VEGF 165 in colorectal cancer patients

    doi: 10.1007/s00280-015-2701-3

    Figure Lengend Snippet: Prediction-corrected visual predictive checks of the binding model based on 1000 simulations (panel a total bevacizumab, panel b free VEGF 165 ). Median ( solid line ), 10th and 90th percentiles ( dashed lines ) of the observed data ( circles ) are compared to the 95 % confidence intervals ( shaded areas ) for the median, 10th and 90th percentiles of the simulated data

    Article Snippet: The concentration of free VEGF 165 (unbound to bevacizumab) in serum was measured by a commercially available ELISA kit for VEGF 165 (Quantikine ® human VEGF, R&D Systems ® Europe).

    Techniques: Binding Assay

    Model-predicted concentrations of total bevacizumab, total and free VEGF 165 for a typical patient of 70 kg. Panels a , b show the total bevacizumab and free VEGF 165 concentration profiles at doses of 5 and 7.5 mg/kg, respectively. Panel c depicts the total VEGF 165 profiles over time for the two dosing regimens

    Journal: Cancer Chemotherapy and Pharmacology

    Article Title: A pharmacokinetic binding model for bevacizumab and VEGF 165 in colorectal cancer patients

    doi: 10.1007/s00280-015-2701-3

    Figure Lengend Snippet: Model-predicted concentrations of total bevacizumab, total and free VEGF 165 for a typical patient of 70 kg. Panels a , b show the total bevacizumab and free VEGF 165 concentration profiles at doses of 5 and 7.5 mg/kg, respectively. Panel c depicts the total VEGF 165 profiles over time for the two dosing regimens

    Article Snippet: The concentration of free VEGF 165 (unbound to bevacizumab) in serum was measured by a commercially available ELISA kit for VEGF 165 (Quantikine ® human VEGF, R&D Systems ® Europe).

    Techniques: Concentration Assay