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    Name:
    Recombinant Murine VEGF
    Description:
    VEGF is a potent growth and angiogenic cytokine It stimulates proliferation and survival of endothelial cells and promotes angiogenesis and vascular permeability Expressed in vascularized tissues VEGF plays a prominent role in normal and pathological angiogenesis Substantial evidence implicates VEGF in the induction of tumor metastasis and intra ocular neovascular syndromes VEGF signals through the three receptors fms like tyrosine kinase flt 1 KDR gene product the murine homolog of KDR is the flk 1 gene product and the flt4 gene product Recombinant murine VEGF is a 39 0 kDa disulfide linked homodimeric protein consisting of two 165 amino acid polypeptide chains
    Catalog Number:
    450-32-100UG
    Price:
    780.00
    Category:
    Recombinant Proteins
    Source:
    E.coli
    Reactivity:
    Chicken Human Rabbit Rat
    Purity:
    98.0
    Quantity:
    100UG
    Buy from Supplier


    Structured Review

    PeproTech vegf a165
    Delivering GFs and laminin HBD peptide enhances skin wound healing. Full-thickness back-skin wounds in 10– 11-week-old C57BLKS/J-m/Lepr db (db/db) mice were treated with combined <t>VEGF-A165</t> (100 ng/wound) and PDGF-BB (50 ng/wound). Four groups were tested: fibrin only, fibrin functionalized with α 2 PI 1–8 -LAMA3 3043–3067 peptide, fibrin containing admixed GFs, and fibrin functionalized with α 2 PI 1–8 -LAMA3 3043–3067 peptide containing GFs. After 4, 7, and 10 days, a , b wound closure and c granulation tissue area were evaluated by histology (means ± SEM, day 4: n = 6, day 7: fibrin only, and α 2 PI 1–8 -LAMA3 3043–3067 peptide + GFs, n = 10; other treatment groups, n = 11, day 10: α 2 PI 1–8 -LAMA3 3043–3067 peptide, n = 8, α 2 PI 1–8 -LAMA3 3043–3067 peptide + GFs, n = 9, and other treatment groups, n = 7). b The proportions of the mice were categorized by the degree of healing after day 7 of wound treatment. d Wound histology (hematoxylin and eosin staining) at day 7. Red arrows indicate tips of the epithelium tongue. The granulation tissue (pink–violet) is characterized by a large number of granulocytes with nuclei that stain in dark-violet or black. Muscle under the wounds is stained in red. Fat tissue appears as transparent bubbles. Scale bar = 800 µm. e – g A total of 5 days after the wound treatment, e proliferation of CD31 + CD45 – endothelial cells is assessed by Ki67 + marker, and f the frequency of Ly6G + CD11b + neutrophils within CD45 + cells and g the frequency of Ly6C + CD11b + monocytes within CD45 + cells were determined using flow cytometry (means ± SEM). * P
    VEGF is a potent growth and angiogenic cytokine It stimulates proliferation and survival of endothelial cells and promotes angiogenesis and vascular permeability Expressed in vascularized tissues VEGF plays a prominent role in normal and pathological angiogenesis Substantial evidence implicates VEGF in the induction of tumor metastasis and intra ocular neovascular syndromes VEGF signals through the three receptors fms like tyrosine kinase flt 1 KDR gene product the murine homolog of KDR is the flk 1 gene product and the flt4 gene product Recombinant murine VEGF is a 39 0 kDa disulfide linked homodimeric protein consisting of two 165 amino acid polypeptide chains
    https://www.bioz.com/result/vegf a165/product/PeproTech
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    vegf a165 - by Bioz Stars, 2021-05
    99/100 stars

    Images

    1) Product Images from "Laminin heparin-binding peptides bind to several growth factors and enhance diabetic wound healing"

    Article Title: Laminin heparin-binding peptides bind to several growth factors and enhance diabetic wound healing

    Journal: Nature Communications

    doi: 10.1038/s41467-018-04525-w

    Delivering GFs and laminin HBD peptide enhances skin wound healing. Full-thickness back-skin wounds in 10– 11-week-old C57BLKS/J-m/Lepr db (db/db) mice were treated with combined VEGF-A165 (100 ng/wound) and PDGF-BB (50 ng/wound). Four groups were tested: fibrin only, fibrin functionalized with α 2 PI 1–8 -LAMA3 3043–3067 peptide, fibrin containing admixed GFs, and fibrin functionalized with α 2 PI 1–8 -LAMA3 3043–3067 peptide containing GFs. After 4, 7, and 10 days, a , b wound closure and c granulation tissue area were evaluated by histology (means ± SEM, day 4: n = 6, day 7: fibrin only, and α 2 PI 1–8 -LAMA3 3043–3067 peptide + GFs, n = 10; other treatment groups, n = 11, day 10: α 2 PI 1–8 -LAMA3 3043–3067 peptide, n = 8, α 2 PI 1–8 -LAMA3 3043–3067 peptide + GFs, n = 9, and other treatment groups, n = 7). b The proportions of the mice were categorized by the degree of healing after day 7 of wound treatment. d Wound histology (hematoxylin and eosin staining) at day 7. Red arrows indicate tips of the epithelium tongue. The granulation tissue (pink–violet) is characterized by a large number of granulocytes with nuclei that stain in dark-violet or black. Muscle under the wounds is stained in red. Fat tissue appears as transparent bubbles. Scale bar = 800 µm. e – g A total of 5 days after the wound treatment, e proliferation of CD31 + CD45 – endothelial cells is assessed by Ki67 + marker, and f the frequency of Ly6G + CD11b + neutrophils within CD45 + cells and g the frequency of Ly6C + CD11b + monocytes within CD45 + cells were determined using flow cytometry (means ± SEM). * P
    Figure Legend Snippet: Delivering GFs and laminin HBD peptide enhances skin wound healing. Full-thickness back-skin wounds in 10– 11-week-old C57BLKS/J-m/Lepr db (db/db) mice were treated with combined VEGF-A165 (100 ng/wound) and PDGF-BB (50 ng/wound). Four groups were tested: fibrin only, fibrin functionalized with α 2 PI 1–8 -LAMA3 3043–3067 peptide, fibrin containing admixed GFs, and fibrin functionalized with α 2 PI 1–8 -LAMA3 3043–3067 peptide containing GFs. After 4, 7, and 10 days, a , b wound closure and c granulation tissue area were evaluated by histology (means ± SEM, day 4: n = 6, day 7: fibrin only, and α 2 PI 1–8 -LAMA3 3043–3067 peptide + GFs, n = 10; other treatment groups, n = 11, day 10: α 2 PI 1–8 -LAMA3 3043–3067 peptide, n = 8, α 2 PI 1–8 -LAMA3 3043–3067 peptide + GFs, n = 9, and other treatment groups, n = 7). b The proportions of the mice were categorized by the degree of healing after day 7 of wound treatment. d Wound histology (hematoxylin and eosin staining) at day 7. Red arrows indicate tips of the epithelium tongue. The granulation tissue (pink–violet) is characterized by a large number of granulocytes with nuclei that stain in dark-violet or black. Muscle under the wounds is stained in red. Fat tissue appears as transparent bubbles. Scale bar = 800 µm. e – g A total of 5 days after the wound treatment, e proliferation of CD31 + CD45 – endothelial cells is assessed by Ki67 + marker, and f the frequency of Ly6G + CD11b + neutrophils within CD45 + cells and g the frequency of Ly6C + CD11b + monocytes within CD45 + cells were determined using flow cytometry (means ± SEM). * P

    Techniques Used: Mouse Assay, Staining, Marker, Flow Cytometry, Cytometry

    Laminin HBD peptides promote cell adhesion in vitro. a , b A total of 3000 cells/well human lung fibroblasts were cultured a without or b with 5 mM EDTA in FGM-2 culture media containing 1% FBS. c , d A total of 3000 cells/well HUVEC were cultured c without or d with 5 mM EDTA in EBM-2 culture media containing 100 ng/mL VEGF-A165 and 1% FBS. Cells were plated on 1 μg/mL laminin peptide pre-coated non-tissue culture-treated plates and incubated for 30 min at 37 °C. After plate washes, cell numbers were quantified using a CyQUANT assay ( n = 10, mean ± SEM). The signals obtained from BSA-coated wells are normalized to 1, and relative fold increases of cell numbers were calculated. Statistical analyses were performed using ANOVA with Tukey’s test. Kruskal–Wallis test followed by Dunn’s multiple comparison was used in b , c . * p
    Figure Legend Snippet: Laminin HBD peptides promote cell adhesion in vitro. a , b A total of 3000 cells/well human lung fibroblasts were cultured a without or b with 5 mM EDTA in FGM-2 culture media containing 1% FBS. c , d A total of 3000 cells/well HUVEC were cultured c without or d with 5 mM EDTA in EBM-2 culture media containing 100 ng/mL VEGF-A165 and 1% FBS. Cells were plated on 1 μg/mL laminin peptide pre-coated non-tissue culture-treated plates and incubated for 30 min at 37 °C. After plate washes, cell numbers were quantified using a CyQUANT assay ( n = 10, mean ± SEM). The signals obtained from BSA-coated wells are normalized to 1, and relative fold increases of cell numbers were calculated. Statistical analyses were performed using ANOVA with Tukey’s test. Kruskal–Wallis test followed by Dunn’s multiple comparison was used in b , c . * p

    Techniques Used: In Vitro, Cell Culture, Incubation, CyQUANT Assay

    GF retention in fibrin matrices is enhanced by incorporating laminin HBD peptide. a , b GF retention in the fibrin matrix. α 2 PI 1–8 -LAMA3 3043–3067 or α 2 PI 1–8 -LAMA5 3417–3436 peptide-functionalized fibrin matrices were made in the presence of VEGF-A165 or PDGF-BB, and incubated in eight volumes of physiological buffer for 5 days. The buffer was changed each day, and released GFs were quantified daily. The graphs show the cumulative release of a VEGF-A165 or b PDGF-BB over 5 days ( n = 4; mean ± SEM). All data points for laminin HBD peptides were statistically significant compared to controls without laminin HBD peptide ( p
    Figure Legend Snippet: GF retention in fibrin matrices is enhanced by incorporating laminin HBD peptide. a , b GF retention in the fibrin matrix. α 2 PI 1–8 -LAMA3 3043–3067 or α 2 PI 1–8 -LAMA5 3417–3436 peptide-functionalized fibrin matrices were made in the presence of VEGF-A165 or PDGF-BB, and incubated in eight volumes of physiological buffer for 5 days. The buffer was changed each day, and released GFs were quantified daily. The graphs show the cumulative release of a VEGF-A165 or b PDGF-BB over 5 days ( n = 4; mean ± SEM). All data points for laminin HBD peptides were statistically significant compared to controls without laminin HBD peptide ( p

    Techniques Used: Incubation

    Laminin binds promiscuously to GFs and chemokines. a Binding of multiple isoforms of full-length laminin (–111, –211, –332, –411, –421, –511, and –521) to GFs and CXCL chemokines were measured by ELISA. A450 nm represents absorbance at 450 nm. BSA-coated wells served as negative controls ( n = 4, mean ± SEM). Signals greater than 0.1 (gray box) are considered to be significant. b Affinities ( K D values are shown) of full-length laminin against VEGF-A165, PlGF-2, and PDGF-BB were measured by SPR. A SPR chip was functionalized with laminin-521 (~2000 resonance units (RU)), and each GF was flown over the chip at indicated concentrations. Curves represent the specific responses (in RU) to laminin obtained. Experimental curves were fitted with Langmuir binding kinetics. Binding kinetics values [dissociation constants ( K D ) and rate constants ( K on and K off )] determined from the fitted curves are shown. Two experimental replicates
    Figure Legend Snippet: Laminin binds promiscuously to GFs and chemokines. a Binding of multiple isoforms of full-length laminin (–111, –211, –332, –411, –421, –511, and –521) to GFs and CXCL chemokines were measured by ELISA. A450 nm represents absorbance at 450 nm. BSA-coated wells served as negative controls ( n = 4, mean ± SEM). Signals greater than 0.1 (gray box) are considered to be significant. b Affinities ( K D values are shown) of full-length laminin against VEGF-A165, PlGF-2, and PDGF-BB were measured by SPR. A SPR chip was functionalized with laminin-521 (~2000 resonance units (RU)), and each GF was flown over the chip at indicated concentrations. Curves represent the specific responses (in RU) to laminin obtained. Experimental curves were fitted with Langmuir binding kinetics. Binding kinetics values [dissociation constants ( K D ) and rate constants ( K on and K off )] determined from the fitted curves are shown. Two experimental replicates

    Techniques Used: Binding Assay, Enzyme-linked Immunosorbent Assay, SPR Assay, Chromatin Immunoprecipitation

    Excess heparin inhibits GF–laminin binding. Inhibition of GF-binding to laminin (–111, –211, –221, –411, –421, –511, and –521) by excess heparin. ELISA plates were coated with 10 µg/mL laminin and further incubated with 1 μg/mL a VEGF-A165, b PlGF-2, or c FGF-2 solution in the absence or presence of excess (10 μM) heparin. Bound GFs were detected using a specific antibody for each GF ( n = 4, mean ± SEM). Statistical analyses were performed using the Mann–Whitney U test by comparing the signals with and without heparin. * p
    Figure Legend Snippet: Excess heparin inhibits GF–laminin binding. Inhibition of GF-binding to laminin (–111, –211, –221, –411, –421, –511, and –521) by excess heparin. ELISA plates were coated with 10 µg/mL laminin and further incubated with 1 μg/mL a VEGF-A165, b PlGF-2, or c FGF-2 solution in the absence or presence of excess (10 μM) heparin. Bound GFs were detected using a specific antibody for each GF ( n = 4, mean ± SEM). Statistical analyses were performed using the Mann–Whitney U test by comparing the signals with and without heparin. * p

    Techniques Used: Binding Assay, Inhibition, Enzyme-linked Immunosorbent Assay, Incubation, MANN-WHITNEY

    GFs bind to laminin HBD derived from LAMA3, LAMA4, and LAMA5. a The location of laminin-derived peptides in the LG domain of LAMA3, LAMA4, and LAMA5 chains. b–f Affinity of heparin and GFs against chemically synthesized peptides derived from the LG domain of LAMA3, LAMA4, and LAMA5 chains. ELISA plates were coated with 10 µg/mL laminin peptide and further incubated with b biotinylated heparin, c VEGF-A165 and VEGF-A121, d PlGF-2 and PlGF-1, e PDGF-BB, or f FGF-2. Concentrations were 1 μg/mL for GFs and 10 µg/mL for heparin. Bound heparin was detected with streptavidin, and bound GFs with a specific antibody for each GF ( n = 4, mean ± SEM). Statistical analyses were performed using the Mann–Whitney U test by comparing the signals obtained from the laminin peptide- and the BSA-coated wells. * p
    Figure Legend Snippet: GFs bind to laminin HBD derived from LAMA3, LAMA4, and LAMA5. a The location of laminin-derived peptides in the LG domain of LAMA3, LAMA4, and LAMA5 chains. b–f Affinity of heparin and GFs against chemically synthesized peptides derived from the LG domain of LAMA3, LAMA4, and LAMA5 chains. ELISA plates were coated with 10 µg/mL laminin peptide and further incubated with b biotinylated heparin, c VEGF-A165 and VEGF-A121, d PlGF-2 and PlGF-1, e PDGF-BB, or f FGF-2. Concentrations were 1 μg/mL for GFs and 10 µg/mL for heparin. Bound heparin was detected with streptavidin, and bound GFs with a specific antibody for each GF ( n = 4, mean ± SEM). Statistical analyses were performed using the Mann–Whitney U test by comparing the signals obtained from the laminin peptide- and the BSA-coated wells. * p

    Techniques Used: Derivative Assay, Synthesized, Enzyme-linked Immunosorbent Assay, Incubation, MANN-WHITNEY

    GFs bind to LG domain derived from LAMA3, LAMA4, and LAMA5. Affinity of GFs against recombinant laminin LG domains. ELISA plates were coated with 1 µg/mL a LAMA3 2928–3150 , b LAMA4 826–1816 , or c LAMA5 3026–3482 and further incubated with 1 μg/mL of VEGF-A165, VEGF-A121, PlGF-2, PlGF-1, PDGF-BB, or FGF-2 solution. Bound GFs were detected using a specific antibody for each GF ( n = 4, mean ± SEM). Statistical analyses were performed using the Mann–Whitney U test by comparing the signals obtained from the laminin domain- and the BSA-coated wells. * p
    Figure Legend Snippet: GFs bind to LG domain derived from LAMA3, LAMA4, and LAMA5. Affinity of GFs against recombinant laminin LG domains. ELISA plates were coated with 1 µg/mL a LAMA3 2928–3150 , b LAMA4 826–1816 , or c LAMA5 3026–3482 and further incubated with 1 μg/mL of VEGF-A165, VEGF-A121, PlGF-2, PlGF-1, PDGF-BB, or FGF-2 solution. Bound GFs were detected using a specific antibody for each GF ( n = 4, mean ± SEM). Statistical analyses were performed using the Mann–Whitney U test by comparing the signals obtained from the laminin domain- and the BSA-coated wells. * p

    Techniques Used: Derivative Assay, Recombinant, Enzyme-linked Immunosorbent Assay, Incubation, MANN-WHITNEY

    2) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    3) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    4) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    5) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    6) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    7) Product Images from "Laminin heparin-binding peptides bind to several growth factors and enhance diabetic wound healing"

    Article Title: Laminin heparin-binding peptides bind to several growth factors and enhance diabetic wound healing

    Journal: Nature Communications

    doi: 10.1038/s41467-018-04525-w

    Delivering GFs and laminin HBD peptide enhances skin wound healing. Full-thickness back-skin wounds in 10– 11-week-old C57BLKS/J-m/Lepr db (db/db) mice were treated with combined VEGF-A165 (100 ng/wound) and PDGF-BB (50 ng/wound). Four groups were tested: fibrin only, fibrin functionalized with α 2 PI 1–8 -LAMA3 3043–3067 peptide, fibrin containing admixed GFs, and fibrin functionalized with α 2 PI 1–8 -LAMA3 3043–3067 peptide containing GFs. After 4, 7, and 10 days, a , b wound closure and c granulation tissue area were evaluated by histology (means ± SEM, day 4: n = 6, day 7: fibrin only, and α 2 PI 1–8 -LAMA3 3043–3067 peptide + GFs, n = 10; other treatment groups, n = 11, day 10: α 2 PI 1–8 -LAMA3 3043–3067 peptide, n = 8, α 2 PI 1–8 -LAMA3 3043–3067 peptide + GFs, n = 9, and other treatment groups, n = 7). b The proportions of the mice were categorized by the degree of healing after day 7 of wound treatment. d Wound histology (hematoxylin and eosin staining) at day 7. Red arrows indicate tips of the epithelium tongue. The granulation tissue (pink–violet) is characterized by a large number of granulocytes with nuclei that stain in dark-violet or black. Muscle under the wounds is stained in red. Fat tissue appears as transparent bubbles. Scale bar = 800 µm. e – g A total of 5 days after the wound treatment, e proliferation of CD31 + CD45 – endothelial cells is assessed by Ki67 + marker, and f the frequency of Ly6G + CD11b + neutrophils within CD45 + cells and g the frequency of Ly6C + CD11b + monocytes within CD45 + cells were determined using flow cytometry (means ± SEM). * P
    Figure Legend Snippet: Delivering GFs and laminin HBD peptide enhances skin wound healing. Full-thickness back-skin wounds in 10– 11-week-old C57BLKS/J-m/Lepr db (db/db) mice were treated with combined VEGF-A165 (100 ng/wound) and PDGF-BB (50 ng/wound). Four groups were tested: fibrin only, fibrin functionalized with α 2 PI 1–8 -LAMA3 3043–3067 peptide, fibrin containing admixed GFs, and fibrin functionalized with α 2 PI 1–8 -LAMA3 3043–3067 peptide containing GFs. After 4, 7, and 10 days, a , b wound closure and c granulation tissue area were evaluated by histology (means ± SEM, day 4: n = 6, day 7: fibrin only, and α 2 PI 1–8 -LAMA3 3043–3067 peptide + GFs, n = 10; other treatment groups, n = 11, day 10: α 2 PI 1–8 -LAMA3 3043–3067 peptide, n = 8, α 2 PI 1–8 -LAMA3 3043–3067 peptide + GFs, n = 9, and other treatment groups, n = 7). b The proportions of the mice were categorized by the degree of healing after day 7 of wound treatment. d Wound histology (hematoxylin and eosin staining) at day 7. Red arrows indicate tips of the epithelium tongue. The granulation tissue (pink–violet) is characterized by a large number of granulocytes with nuclei that stain in dark-violet or black. Muscle under the wounds is stained in red. Fat tissue appears as transparent bubbles. Scale bar = 800 µm. e – g A total of 5 days after the wound treatment, e proliferation of CD31 + CD45 – endothelial cells is assessed by Ki67 + marker, and f the frequency of Ly6G + CD11b + neutrophils within CD45 + cells and g the frequency of Ly6C + CD11b + monocytes within CD45 + cells were determined using flow cytometry (means ± SEM). * P

    Techniques Used: Mouse Assay, Staining, Marker, Flow Cytometry, Cytometry

    Laminin HBD peptides promote cell adhesion in vitro. a , b A total of 3000 cells/well human lung fibroblasts were cultured a without or b with 5 mM EDTA in FGM-2 culture media containing 1% FBS. c , d A total of 3000 cells/well HUVEC were cultured c without or d with 5 mM EDTA in EBM-2 culture media containing 100 ng/mL VEGF-A165 and 1% FBS. Cells were plated on 1 μg/mL laminin peptide pre-coated non-tissue culture-treated plates and incubated for 30 min at 37 °C. After plate washes, cell numbers were quantified using a CyQUANT assay ( n = 10, mean ± SEM). The signals obtained from BSA-coated wells are normalized to 1, and relative fold increases of cell numbers were calculated. Statistical analyses were performed using ANOVA with Tukey’s test. Kruskal–Wallis test followed by Dunn’s multiple comparison was used in b , c . * p
    Figure Legend Snippet: Laminin HBD peptides promote cell adhesion in vitro. a , b A total of 3000 cells/well human lung fibroblasts were cultured a without or b with 5 mM EDTA in FGM-2 culture media containing 1% FBS. c , d A total of 3000 cells/well HUVEC were cultured c without or d with 5 mM EDTA in EBM-2 culture media containing 100 ng/mL VEGF-A165 and 1% FBS. Cells were plated on 1 μg/mL laminin peptide pre-coated non-tissue culture-treated plates and incubated for 30 min at 37 °C. After plate washes, cell numbers were quantified using a CyQUANT assay ( n = 10, mean ± SEM). The signals obtained from BSA-coated wells are normalized to 1, and relative fold increases of cell numbers were calculated. Statistical analyses were performed using ANOVA with Tukey’s test. Kruskal–Wallis test followed by Dunn’s multiple comparison was used in b , c . * p

    Techniques Used: In Vitro, Cell Culture, Incubation, CyQUANT Assay

    GF retention in fibrin matrices is enhanced by incorporating laminin HBD peptide. a , b GF retention in the fibrin matrix. α 2 PI 1–8 -LAMA3 3043–3067 or α 2 PI 1–8 -LAMA5 3417–3436 peptide-functionalized fibrin matrices were made in the presence of VEGF-A165 or PDGF-BB, and incubated in eight volumes of physiological buffer for 5 days. The buffer was changed each day, and released GFs were quantified daily. The graphs show the cumulative release of a VEGF-A165 or b PDGF-BB over 5 days ( n = 4; mean ± SEM). All data points for laminin HBD peptides were statistically significant compared to controls without laminin HBD peptide ( p
    Figure Legend Snippet: GF retention in fibrin matrices is enhanced by incorporating laminin HBD peptide. a , b GF retention in the fibrin matrix. α 2 PI 1–8 -LAMA3 3043–3067 or α 2 PI 1–8 -LAMA5 3417–3436 peptide-functionalized fibrin matrices were made in the presence of VEGF-A165 or PDGF-BB, and incubated in eight volumes of physiological buffer for 5 days. The buffer was changed each day, and released GFs were quantified daily. The graphs show the cumulative release of a VEGF-A165 or b PDGF-BB over 5 days ( n = 4; mean ± SEM). All data points for laminin HBD peptides were statistically significant compared to controls without laminin HBD peptide ( p

    Techniques Used: Incubation

    Laminin binds promiscuously to GFs and chemokines. a Binding of multiple isoforms of full-length laminin (–111, –211, –332, –411, –421, –511, and –521) to GFs and CXCL chemokines were measured by ELISA. A450 nm represents absorbance at 450 nm. BSA-coated wells served as negative controls ( n = 4, mean ± SEM). Signals greater than 0.1 (gray box) are considered to be significant. b Affinities ( K D values are shown) of full-length laminin against VEGF-A165, PlGF-2, and PDGF-BB were measured by SPR. A SPR chip was functionalized with laminin-521 (~2000 resonance units (RU)), and each GF was flown over the chip at indicated concentrations. Curves represent the specific responses (in RU) to laminin obtained. Experimental curves were fitted with Langmuir binding kinetics. Binding kinetics values [dissociation constants ( K D ) and rate constants ( K on and K off )] determined from the fitted curves are shown. Two experimental replicates
    Figure Legend Snippet: Laminin binds promiscuously to GFs and chemokines. a Binding of multiple isoforms of full-length laminin (–111, –211, –332, –411, –421, –511, and –521) to GFs and CXCL chemokines were measured by ELISA. A450 nm represents absorbance at 450 nm. BSA-coated wells served as negative controls ( n = 4, mean ± SEM). Signals greater than 0.1 (gray box) are considered to be significant. b Affinities ( K D values are shown) of full-length laminin against VEGF-A165, PlGF-2, and PDGF-BB were measured by SPR. A SPR chip was functionalized with laminin-521 (~2000 resonance units (RU)), and each GF was flown over the chip at indicated concentrations. Curves represent the specific responses (in RU) to laminin obtained. Experimental curves were fitted with Langmuir binding kinetics. Binding kinetics values [dissociation constants ( K D ) and rate constants ( K on and K off )] determined from the fitted curves are shown. Two experimental replicates

    Techniques Used: Binding Assay, Enzyme-linked Immunosorbent Assay, SPR Assay, Chromatin Immunoprecipitation

    Excess heparin inhibits GF–laminin binding. Inhibition of GF-binding to laminin (–111, –211, –221, –411, –421, –511, and –521) by excess heparin. ELISA plates were coated with 10 µg/mL laminin and further incubated with 1 μg/mL a VEGF-A165, b PlGF-2, or c FGF-2 solution in the absence or presence of excess (10 μM) heparin. Bound GFs were detected using a specific antibody for each GF ( n = 4, mean ± SEM). Statistical analyses were performed using the Mann–Whitney U test by comparing the signals with and without heparin. * p
    Figure Legend Snippet: Excess heparin inhibits GF–laminin binding. Inhibition of GF-binding to laminin (–111, –211, –221, –411, –421, –511, and –521) by excess heparin. ELISA plates were coated with 10 µg/mL laminin and further incubated with 1 μg/mL a VEGF-A165, b PlGF-2, or c FGF-2 solution in the absence or presence of excess (10 μM) heparin. Bound GFs were detected using a specific antibody for each GF ( n = 4, mean ± SEM). Statistical analyses were performed using the Mann–Whitney U test by comparing the signals with and without heparin. * p

    Techniques Used: Binding Assay, Inhibition, Enzyme-linked Immunosorbent Assay, Incubation, MANN-WHITNEY

    GFs bind to laminin HBD derived from LAMA3, LAMA4, and LAMA5. a The location of laminin-derived peptides in the LG domain of LAMA3, LAMA4, and LAMA5 chains. b–f Affinity of heparin and GFs against chemically synthesized peptides derived from the LG domain of LAMA3, LAMA4, and LAMA5 chains. ELISA plates were coated with 10 µg/mL laminin peptide and further incubated with b biotinylated heparin, c VEGF-A165 and VEGF-A121, d PlGF-2 and PlGF-1, e PDGF-BB, or f FGF-2. Concentrations were 1 μg/mL for GFs and 10 µg/mL for heparin. Bound heparin was detected with streptavidin, and bound GFs with a specific antibody for each GF ( n = 4, mean ± SEM). Statistical analyses were performed using the Mann–Whitney U test by comparing the signals obtained from the laminin peptide- and the BSA-coated wells. * p
    Figure Legend Snippet: GFs bind to laminin HBD derived from LAMA3, LAMA4, and LAMA5. a The location of laminin-derived peptides in the LG domain of LAMA3, LAMA4, and LAMA5 chains. b–f Affinity of heparin and GFs against chemically synthesized peptides derived from the LG domain of LAMA3, LAMA4, and LAMA5 chains. ELISA plates were coated with 10 µg/mL laminin peptide and further incubated with b biotinylated heparin, c VEGF-A165 and VEGF-A121, d PlGF-2 and PlGF-1, e PDGF-BB, or f FGF-2. Concentrations were 1 μg/mL for GFs and 10 µg/mL for heparin. Bound heparin was detected with streptavidin, and bound GFs with a specific antibody for each GF ( n = 4, mean ± SEM). Statistical analyses were performed using the Mann–Whitney U test by comparing the signals obtained from the laminin peptide- and the BSA-coated wells. * p

    Techniques Used: Derivative Assay, Synthesized, Enzyme-linked Immunosorbent Assay, Incubation, MANN-WHITNEY

    GFs bind to LG domain derived from LAMA3, LAMA4, and LAMA5. Affinity of GFs against recombinant laminin LG domains. ELISA plates were coated with 1 µg/mL a LAMA3 2928–3150 , b LAMA4 826–1816 , or c LAMA5 3026–3482 and further incubated with 1 μg/mL of VEGF-A165, VEGF-A121, PlGF-2, PlGF-1, PDGF-BB, or FGF-2 solution. Bound GFs were detected using a specific antibody for each GF ( n = 4, mean ± SEM). Statistical analyses were performed using the Mann–Whitney U test by comparing the signals obtained from the laminin domain- and the BSA-coated wells. * p
    Figure Legend Snippet: GFs bind to LG domain derived from LAMA3, LAMA4, and LAMA5. Affinity of GFs against recombinant laminin LG domains. ELISA plates were coated with 1 µg/mL a LAMA3 2928–3150 , b LAMA4 826–1816 , or c LAMA5 3026–3482 and further incubated with 1 μg/mL of VEGF-A165, VEGF-A121, PlGF-2, PlGF-1, PDGF-BB, or FGF-2 solution. Bound GFs were detected using a specific antibody for each GF ( n = 4, mean ± SEM). Statistical analyses were performed using the Mann–Whitney U test by comparing the signals obtained from the laminin domain- and the BSA-coated wells. * p

    Techniques Used: Derivative Assay, Recombinant, Enzyme-linked Immunosorbent Assay, Incubation, MANN-WHITNEY

    8) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    9) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    10) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    11) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    12) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    13) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    14) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    15) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    16) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    17) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    18) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    19) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    20) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    21) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    22) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    23) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    24) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    25) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

    26) Product Images from "Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization"

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    Journal: Blood

    doi: 10.1182/blood-2007-12-125856

    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do
    Figure Legend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Techniques Used: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31
    Figure Legend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Techniques Used:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200
    Figure Legend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Techniques Used:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,
    Figure Legend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Techniques Used: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased
    Figure Legend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Techniques Used:

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    Article Snippet: Adult male mice ( n = 6–8/genotype, 8–12 weeks) under normal diet and environmental conditions were injected intravenously with Evans blue dye (100 μl of a 1% solution in 0.9% NaCl). .. After 20 min, 400 ng of recombinant murine VEGF (Peprotech) dissolved in 20 μl of PBS and 0.1% BSA or 20 μl of vehicle alone was injected intradermally into the shaved right or left flank of the mouse, respectively. .. The area of skin containing the injection site was removed using a 5-mm biopsy punch (Miltex).

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    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of <t>VEGF/VEGF</t> receptor complexes induced by <t>VEGF-A165,</t> VEGF-A121, and VEGF-E-NZ2. Note that we do
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    Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Journal: Blood

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    doi: 10.1182/blood-2007-12-125856

    Figure Lengend Snippet: Schematic outline of the contribution of ligand binding to HS and NRP1 in endothelial cell responses. (A) Outline of symbols used in panel B. (B) Depiction of VEGF/VEGF receptor complexes induced by VEGF-A165, VEGF-A121, and VEGF-E-NZ2. Note that we do

    Article Snippet: VEGF-A165 was from PeproTech (Rocky Hill, NJ) and VEGF-A121 from R & D Systems.

    Techniques: Ligand Binding Assay

    Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Journal: Blood

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    doi: 10.1182/blood-2007-12-125856

    Figure Lengend Snippet: Sprouting angiogenesis and vessel formation in response to the different VEGF ligands. (A) Sprouting of EBs in 3D collagen cultures was induced in response to VEGF-A165 and VEGF-E-NZ2 (arrows) but not to VEGF-A121 or vehicle, as visualized by anti-CD31

    Article Snippet: VEGF-A165 was from PeproTech (Rocky Hill, NJ) and VEGF-A121 from R & D Systems.

    Techniques:

    VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Journal: Blood

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    doi: 10.1182/blood-2007-12-125856

    Figure Lengend Snippet: VEGF-A121 fails to rescue ISV sprouting and caudal plexus remodeling defect in vegfa knockdown zebrafish. (A) Vegfa MO (9 ng) alone alternatively vegfa MO (9 ng) combined with vegfa mRNA encoding VEGF-A165, VEGF-A121 (100 pg each), or VEGF-E-NZ2 (200

    Article Snippet: VEGF-A165 was from PeproTech (Rocky Hill, NJ) and VEGF-A121 from R & D Systems.

    Techniques:

    p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Journal: Blood

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    doi: 10.1182/blood-2007-12-125856

    Figure Lengend Snippet: p38MAPK induction by VEGF-A165 and VEGF-E-NZ2, but not by VEGF-A121. (A) PAE/VEGFR-2, NRP1 cells were incubated for different time periods with 2 nM of VEGF-A165, VEGF-A121, or VEGF-E-NZ2, followed by analyses, as indicated, for induction of p38MAPK,

    Article Snippet: VEGF-A165 was from PeproTech (Rocky Hill, NJ) and VEGF-A121 from R & D Systems.

    Techniques: Incubation

    VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Journal: Blood

    Article Title: Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization

    doi: 10.1182/blood-2007-12-125856

    Figure Lengend Snippet: VEGF-A165, VEGF-A121, and VEGF-E-NZ2 interaction with VEGFR-2, HS, and NRP1. (A) Schematic outline of VEGF ligands used in this study with VEGF-A exon structure and bindings sites for VEGFR-2, HS, and NRP1 indicated. VEGF-A165 and VEGF-A121 were purchased

    Article Snippet: VEGF-A165 was from PeproTech (Rocky Hill, NJ) and VEGF-A121 from R & D Systems.

    Techniques: