recombinant human vegf a165  (R&D Systems)

 
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    Name:
    Recombinant Human VEGF 165 Protein
    Description:
    The Recombinant Human VEGF 165 Protein from R D Systems is derived from Sf 21 baculovirus The Recombinant Human VEGF 165 Protein has been validated for the following applications Bioactivity
    Catalog Number:
    293-VE-010
    Price:
    289
    Category:
    Proteins and Enzymes
    Source:
    Sf 21 (baculovirus)-derived Recombinant Human VEGF 165 Protein
    Applications:
    Bioactivity
    Purity:
    >97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie« Blue Staining.
    Conjugate:
    Unconjugated
    Size:
    10 ug
    Buy from Supplier


    Structured Review

    R&D Systems recombinant human vegf a165
    Recombinant Human VEGF 165 Protein
    The Recombinant Human VEGF 165 Protein from R D Systems is derived from Sf 21 baculovirus The Recombinant Human VEGF 165 Protein has been validated for the following applications Bioactivity
    https://www.bioz.com/result/recombinant human vegf a165/product/R&D Systems
    Average 98 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    recombinant human vegf a165 - by Bioz Stars, 2021-07
    98/100 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 "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

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    Article Snippet: SKLB1002, GF109293X and cycloheximide were from EMD Millipore (Billerica, MA). .. Recombinant human VEGF 165, ELISA Kits for human PlGF, VEGF and human sVEGF R1 and anti-sFlt1 antibody (AF321) were obtained from R & D Systems (Minneapolis, MN). .. Other antibodies, anti-HA antibody (Y-11), anti-Flt1 antibody (sc-316), HRP-conjugated goat anti-mouse IgG and HRP-conjugated donkey anti-goat IgG were from Santa Cruz Biotechnology (Santa Cruz, CA).

    Positive Control:

    Article Title: Anti-PD1 ‘SHR-1210ʹ aberrantly targets pro-angiogenic receptors and this polyspecificity can be ablated by paratope refinement
    Article Snippet: IgGs were diluted in assay buffer (99% RPMI 1640/1% FBS) and added to the assay plates containing the VEGFR2/NFAT luciferase/HEK-293 cells. .. Positive control protein was human VEGF-165 (R & D systems). .. Mab005, SHR-1210, MAB04, MAB08, 06D02 and 12H04 in IgG1null form were also tested across a broad concentration range.

    other:

    Article Title: MicroRNA 139-5p coordinates APLNR-CXCR4 crosstalk during vascular maturation
    Article Snippet: The medium was changed every other day, and SDF-1α and VEGF 165 were added daily.

    Incubation:

    Article Title: Binding and Structural Properties of DNA Aptamers with VEGF-A-Mimic Activity
    Article Snippet: HUVECs were trypsinized, pelleted by low-speed centrifugation, and suspended in Medium 200PRF supplemented with LSGS. .. HUVECs (1.1 × 105 cells/well) were placed into 24-well flat-bottomed plates pre-coated with Matrigel and then incubated with aptamers (10 μM) or VEGF165 (Recombinant Human VEGF 165 Protein, Cat. No. 293-VE [R & D Systems, USA]; 10 ng/mL, 0.26 nM) for 24 h. In the experiment of dose dependency, the Apt02 concentration of more than 10 μM showed the significant difference from control group (data not shown). .. After incubation, cell tube or network formation was observed using a phase-contrast microscope (IX51S8F-3; Olympus, Japan).

    Article Title: Regulation of Caveolin-1 Expression and Phosphorylation by VEGF in Ovine Amnion Cells
    Article Snippet: To determine the effects of VEGF treatment, the culture medium was replaced with serum-free DMEM/F12 supplemented with antibiotics, glutamine, and albumin (Cellgro, Mediatech, Voigt Global Distribution, Inc, Lawrence, Kansas). .. Recombinant human VEGF165 (VEGF, R & D Systems, Minneapolis, Minnesota) at 0, 1, 5, 10, or 25 ng/mL were added to the culture medium and the cells were incubated in the presence of VEGF for 6, 12, or 24 hours. .. At the end of each time period, cells were collected for RNA extraction to analyze caveolin-1 messenger RNA (mRNA) expression, or lysed with a protein lysis buffer to determine caveolin-1 protein levels.

    Concentration Assay:

    Article Title: Binding and Structural Properties of DNA Aptamers with VEGF-A-Mimic Activity
    Article Snippet: HUVECs were trypsinized, pelleted by low-speed centrifugation, and suspended in Medium 200PRF supplemented with LSGS. .. HUVECs (1.1 × 105 cells/well) were placed into 24-well flat-bottomed plates pre-coated with Matrigel and then incubated with aptamers (10 μM) or VEGF165 (Recombinant Human VEGF 165 Protein, Cat. No. 293-VE [R & D Systems, USA]; 10 ng/mL, 0.26 nM) for 24 h. In the experiment of dose dependency, the Apt02 concentration of more than 10 μM showed the significant difference from control group (data not shown). .. After incubation, cell tube or network formation was observed using a phase-contrast microscope (IX51S8F-3; Olympus, Japan).

    Enzyme-linked Immunosorbent Assay:

    Article Title: Protein kinase C regulates FLT1 abundance and stimulates its cleavage in vascular endothelial cells with the release of a soluble PlGF/VEGF antagonist
    Article Snippet: SKLB1002, GF109293X and cycloheximide were from EMD Millipore (Billerica, MA). .. Recombinant human VEGF 165, ELISA Kits for human PlGF, VEGF and human sVEGF R1 and anti-sFlt1 antibody (AF321) were obtained from R & D Systems (Minneapolis, MN). .. Other antibodies, anti-HA antibody (Y-11), anti-Flt1 antibody (sc-316), HRP-conjugated goat anti-mouse IgG and HRP-conjugated donkey anti-goat IgG were from Santa Cruz Biotechnology (Santa Cruz, CA).

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  • 94
    R&D Systems recombinant vegf
    HUVEC response to soluble morphogens. HUVECs starved overnight in 2% <t>FBS</t> were seeded on arrays presenting varied densities of GRGDSP in the presence of 2% FBS alone or with the addition of 10 ng/mL VR-BP (4.8 nM) or 10 ng/mL <t>VEGF</t> (0.26 nM). (Error bars indicate standard error of the mean and asterisk indicate significance compared to FBS alone, p
    Recombinant Vegf, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant vegf/product/R&D Systems
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    recombinant vegf - by Bioz Stars, 2021-07
    94/100 stars
      Buy from Supplier

    98
    R&D Systems recombinant human 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
    Recombinant Human Vegf A165, supplied by R&D Systems, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant human vegf a165/product/R&D Systems
    Average 98 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    recombinant human vegf a165 - by Bioz Stars, 2021-07
    98/100 stars
      Buy from Supplier

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

    Journal: Integrative biology : quantitative biosciences from nano to macro

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

    doi: 10.1039/c2ib20055d

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

    Article Snippet: After imaging, media was replaced with m199 with 2% FBS containing varied concentrations soluble factors such as recombinant VEGF (VEGF-A165 , R & D systems, Minneapolis, MN) or VR-BP.

    Techniques:

    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

    Journal: Nature Communications

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

    doi: 10.1038/s41467-018-04525-w

    Figure Lengend 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

    Article Snippet: Recombinant human VEGF-A165 remaining in the fibrinous matrix and in the tissue surrounding the wound was quantified by ELISA (DuoSet, R & D Systems), using 200 ng of recombinant human VEGF-A165 as 100%.

    Techniques: 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

    Journal: Nature Communications

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

    doi: 10.1038/s41467-018-04525-w

    Figure Lengend 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

    Article Snippet: Recombinant human VEGF-A165 remaining in the fibrinous matrix and in the tissue surrounding the wound was quantified by ELISA (DuoSet, R & D Systems), using 200 ng of recombinant human VEGF-A165 as 100%.

    Techniques: 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

    Journal: Nature Communications

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

    doi: 10.1038/s41467-018-04525-w

    Figure Lengend 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

    Article Snippet: Recombinant human VEGF-A165 remaining in the fibrinous matrix and in the tissue surrounding the wound was quantified by ELISA (DuoSet, R & D Systems), using 200 ng of recombinant human VEGF-A165 as 100%.

    Techniques: 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

    Journal: Nature Communications

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

    doi: 10.1038/s41467-018-04525-w

    Figure Lengend 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

    Article Snippet: Recombinant human VEGF-A165 remaining in the fibrinous matrix and in the tissue surrounding the wound was quantified by ELISA (DuoSet, R & D Systems), using 200 ng of recombinant human VEGF-A165 as 100%.

    Techniques: 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

    Journal: Nature Communications

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

    doi: 10.1038/s41467-018-04525-w

    Figure Lengend 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

    Article Snippet: Recombinant human VEGF-A165 remaining in the fibrinous matrix and in the tissue surrounding the wound was quantified by ELISA (DuoSet, R & D Systems), using 200 ng of recombinant human VEGF-A165 as 100%.

    Techniques: 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

    Journal: Nature Communications

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

    doi: 10.1038/s41467-018-04525-w

    Figure Lengend 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

    Article Snippet: Recombinant human VEGF-A165 remaining in the fibrinous matrix and in the tissue surrounding the wound was quantified by ELISA (DuoSet, R & D Systems), using 200 ng of recombinant human VEGF-A165 as 100%.

    Techniques: 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

    Journal: Nature Communications

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

    doi: 10.1038/s41467-018-04525-w

    Figure Lengend 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

    Article Snippet: Recombinant human VEGF-A165 remaining in the fibrinous matrix and in the tissue surrounding the wound was quantified by ELISA (DuoSet, R & D Systems), using 200 ng of recombinant human VEGF-A165 as 100%.

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