biotinylated bt vegf a165  (R&D Systems)

 
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    Name:
    Recombinant Human VEGF 165 Biotinylated Protein CF
    Description:
    The Recombinant Human VEGF 165 Biotinylated Protein from R D Systems is derived from Sf 21 baculovirus The Recombinant Human VEGF 165 Biotinylated Protein has been validated for the following applications Bioactivity
    Catalog Number:
    BT293-010/CF
    Price:
    369
    Category:
    Proteins and Enzymes
    Source:
    Sf 21 (baculovirus)-derived Recombinant Human VEGF 165 Biotinylated Protein
    Applications:
    Bioactivity
    Purity:
    >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie« Blue Staining.
    Conjugate:
    Biotin
    Size:
    10 ug
    Buy from Supplier


    Structured Review

    R&D Systems biotinylated bt vegf a165
    Recombinant Human VEGF 165 Biotinylated Protein CF
    The Recombinant Human VEGF 165 Biotinylated Protein from R D Systems is derived from Sf 21 baculovirus The Recombinant Human VEGF 165 Biotinylated Protein has been validated for the following applications Bioactivity
    https://www.bioz.com/result/biotinylated bt vegf a165/product/R&D Systems
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    biotinylated bt vegf a165 - by Bioz Stars, 2021-09
    93/100 stars

    Images

    1) Product Images from "Production of Soluble Human Vascular Endothelial Growth Factor VEGF-A165-Heparin Binding Domain in Escherichia coli"

    Article Title: Production of Soluble Human Vascular Endothelial Growth Factor VEGF-A165-Heparin Binding Domain in Escherichia coli

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0055690

    Binding of VEGF-A 165 -HBD to NRP as detected by a cell based assay and size exclusion chromatography. (a) Binding of VEGF-A 165 -HBD to NRP1 was determined in DU145 cells expressing an adenoviral construct encoding NRP1 [17] . These cells do not express other VEGF receptors [21] . Cells were incubated with biotinylated VEGF-A 165 in the presence of the indicated concentrations of either unlabelled VEGF-A 165 (positive control), or VEGF-A 165 -HBD containing a His 6 tag or VEGF-A 165 -HBD without the tag. Values presented are the means (±SEM) obtained from two independent experiments. Other experimental details are described in Materials and Methods. (b) Binding of VEGF-A 165 -HBD to b1 domains of NRP1 and NRP2 was assessed by size exclusion chromatography. The protein mixtures of a tenfold molar excess of VEGF-A 165 -HBD with the purified b1 domain from either NRP1 or NRP2 were incubated at room temperature for 30 minutes. The FPLC profile for VEGF-A 165 -HBD and NRP1 b1 mixture is shown. SDS-PAGE analysis was used to evaluate samples of NRP1 b1, VEGF-A 165 -HBD, and the protein mixture before being loaded onto the size exclusion column (lanes 1–3, respectively) as well as samples of fractions which eluted from the single peak (lanes 4–6), showing that VEGF-A 165 -HBD and NRP1 b1 co-eluted from the preparative Superdex 75 column. A similar result was seen for VEGF-A 165 -HBD and NRP2 b1. (c) Formation of the molecular complexes was also investigated by analytical size exclusion chromatography. NRP1 b1 and b1b2 domains as well VEGF-A 165 -HBD were initially loaded separately onto the analytical Superdex 75 column and their corresponding FPLC traces are shown in solid and dashed lines, respectively. To detect binding, NRP1 b1 or b1b2 domains were mixed with VEGF-A 165 -HBD in solution at a molar ratio of 1∶10 and 1∶28, respectively and incubated for an hour at room temperature. The mixtures were then applied to the column. The main peaks in the elution profiles revealed a shift to the left of the peak positions corresponding to the unbound NRP1 b1 or b1b2 domains (indicated by vertical black lines), suggesting complex formation.
    Figure Legend Snippet: Binding of VEGF-A 165 -HBD to NRP as detected by a cell based assay and size exclusion chromatography. (a) Binding of VEGF-A 165 -HBD to NRP1 was determined in DU145 cells expressing an adenoviral construct encoding NRP1 [17] . These cells do not express other VEGF receptors [21] . Cells were incubated with biotinylated VEGF-A 165 in the presence of the indicated concentrations of either unlabelled VEGF-A 165 (positive control), or VEGF-A 165 -HBD containing a His 6 tag or VEGF-A 165 -HBD without the tag. Values presented are the means (±SEM) obtained from two independent experiments. Other experimental details are described in Materials and Methods. (b) Binding of VEGF-A 165 -HBD to b1 domains of NRP1 and NRP2 was assessed by size exclusion chromatography. The protein mixtures of a tenfold molar excess of VEGF-A 165 -HBD with the purified b1 domain from either NRP1 or NRP2 were incubated at room temperature for 30 minutes. The FPLC profile for VEGF-A 165 -HBD and NRP1 b1 mixture is shown. SDS-PAGE analysis was used to evaluate samples of NRP1 b1, VEGF-A 165 -HBD, and the protein mixture before being loaded onto the size exclusion column (lanes 1–3, respectively) as well as samples of fractions which eluted from the single peak (lanes 4–6), showing that VEGF-A 165 -HBD and NRP1 b1 co-eluted from the preparative Superdex 75 column. A similar result was seen for VEGF-A 165 -HBD and NRP2 b1. (c) Formation of the molecular complexes was also investigated by analytical size exclusion chromatography. NRP1 b1 and b1b2 domains as well VEGF-A 165 -HBD were initially loaded separately onto the analytical Superdex 75 column and their corresponding FPLC traces are shown in solid and dashed lines, respectively. To detect binding, NRP1 b1 or b1b2 domains were mixed with VEGF-A 165 -HBD in solution at a molar ratio of 1∶10 and 1∶28, respectively and incubated for an hour at room temperature. The mixtures were then applied to the column. The main peaks in the elution profiles revealed a shift to the left of the peak positions corresponding to the unbound NRP1 b1 or b1b2 domains (indicated by vertical black lines), suggesting complex formation.

    Techniques Used: Binding Assay, Cell Based Assay, Size-exclusion Chromatography, Expressing, Construct, Incubation, Positive Control, Purification, Fast Protein Liquid Chromatography, SDS Page

    Related Articles

    other:

    Article Title: Characterization of Human Sclera Barrier Properties for Transscleral Delivery of Bevacizumab and Ranibizumab
    Article Snippet: Subsequently, 100 µL biotinylated rhVEGF (R & D System, Minneapolis, Minnesota) diluted with 0.05% (w/v) BSA in PBS was added to each well and allowed to incubate for 1 h, followed by three washings with 0.05% Tween-20 (Sigma–Aldrich) in PBS.

    Negative Control:

    Article Title: Direct binding of hepatocyte growth factor and vascular endothelial growth factor to CD44v6
    Article Snippet: .. Where indicated, cells were treated with 100 ng/ml rat v6 peptide or 100 ng/ml control peptide for 1 h at 4°C prior to the induction with 20 ng/ml biotinylated human HGF, 20 ng/ml biotinylated human VEGF165 (as performed for HGF) or 20 ng/ml biotinylated soybean trypsin inhibitor (used as negative control) (R & D Systems) for 1 h on ice. ..

    Recombinant:

    Article Title: Multifunctional Peptide-Conjugated Hybrid Silica Nanoparticles for Photodynamic Therapy and MRI
    Article Snippet: .. Biotinylated VEGF165 bound to NRP-1 was greatly displaced by the peptide-conjugated nanoparticles NP-TPC-ATWLPPR, indicating that the conjugated nanoparticles bound to recombinant NRP-1 chimeric protein. ..

    Article Title: High-Throughput Screening Assay for Embryoid Body Differentiation of Human Embryonic Stem Cells
    Article Snippet: .. Recombinant human vascular endothelial growth factor 165 (VEGF; R & D Systems cat. no. 293-VE) Reconstitute at 10 to 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. ..

    Article Title: Calcium dobesilate reduces VEGF signaling by interfering with heparan sulfate binding site and protects from vascular complications in diabetic mice
    Article Snippet: .. The recombinant VEGF165 , VEGF121 and biotinylated-VEGF165 (bt-VEGF165 ), VEGFR-1, VEGFR-2 and recombinant Human Active Heparanase (HPSE; 7570-GH) were from R & D Systems Inc. (Wiesbaden-Nordenstadt, Germany). ..

    Article Title: Development and Comparison of Two Immuno-disaggregation Based Bioassays for Cell Secretome Analysis
    Article Snippet: .. Recombinant human VEGF-165 protein and biotinylated recombinant human VEGF protein were purchased from R & D Systems (Minneapolis, MN, USA). ..

    Injection:

    Article Title: Plasma Kallikrein-Kinin System as a VEGF-Independent Mediator of Diabetic Macular Edema
    Article Snippet: .. Briefly, the eyes were dilated and received intravitreal injection of BK (2 μmol/L; Sigma-Aldrich), DABK (2 μmol/L; Sigma-Aldrich), VEGF (0.02 ng/mL in vitreous) (rhVEGF 165; R & D Systems), or PBS. ..

    Staining:

    Article Title: Multifunctional Peptide-Conjugated Hybrid Silica Nanoparticles for Photodynamic Therapy and MRI
    Article Snippet: .. After a 2 h-incubation at room temperature, the wells were washed and the amount of bound biotinylated VEGF165 was stained with streptavidin horseradish peroxidase conjugate (R & D Systems) for 20 min at room temperature. ..

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    R&D Systems biotinylated bt vegf a165
    Binding of <t>VEGF-A</t> 165 -HBD to NRP as detected by a cell based assay and size exclusion chromatography. (a) Binding of VEGF-A 165 -HBD to NRP1 was determined in DU145 cells expressing an adenoviral construct encoding NRP1 [17] . These cells do not express other VEGF receptors [21] . Cells were incubated with <t>biotinylated</t> VEGF-A 165 in the presence of the indicated concentrations of either unlabelled VEGF-A 165 (positive control), or VEGF-A 165 -HBD containing a His 6 tag or VEGF-A 165 -HBD without the tag. Values presented are the means (±SEM) obtained from two independent experiments. Other experimental details are described in Materials and Methods. (b) Binding of VEGF-A 165 -HBD to b1 domains of NRP1 and NRP2 was assessed by size exclusion chromatography. The protein mixtures of a tenfold molar excess of VEGF-A 165 -HBD with the purified b1 domain from either NRP1 or NRP2 were incubated at room temperature for 30 minutes. The FPLC profile for VEGF-A 165 -HBD and NRP1 b1 mixture is shown. SDS-PAGE analysis was used to evaluate samples of NRP1 b1, VEGF-A 165 -HBD, and the protein mixture before being loaded onto the size exclusion column (lanes 1–3, respectively) as well as samples of fractions which eluted from the single peak (lanes 4–6), showing that VEGF-A 165 -HBD and NRP1 b1 co-eluted from the preparative Superdex 75 column. A similar result was seen for VEGF-A 165 -HBD and NRP2 b1. (c) Formation of the molecular complexes was also investigated by analytical size exclusion chromatography. NRP1 b1 and b1b2 domains as well VEGF-A 165 -HBD were initially loaded separately onto the analytical Superdex 75 column and their corresponding FPLC traces are shown in solid and dashed lines, respectively. To detect binding, NRP1 b1 or b1b2 domains were mixed with VEGF-A 165 -HBD in solution at a molar ratio of 1∶10 and 1∶28, respectively and incubated for an hour at room temperature. The mixtures were then applied to the column. The main peaks in the elution profiles revealed a shift to the left of the peak positions corresponding to the unbound NRP1 b1 or b1b2 domains (indicated by vertical black lines), suggesting complex formation.
    Biotinylated Bt Vegf A165, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated bt vegf a165/product/R&D Systems
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    biotinylated bt vegf a165 - by Bioz Stars, 2021-09
    93/100 stars
      Buy from Supplier

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    Binding of VEGF-A 165 -HBD to NRP as detected by a cell based assay and size exclusion chromatography. (a) Binding of VEGF-A 165 -HBD to NRP1 was determined in DU145 cells expressing an adenoviral construct encoding NRP1 [17] . These cells do not express other VEGF receptors [21] . Cells were incubated with biotinylated VEGF-A 165 in the presence of the indicated concentrations of either unlabelled VEGF-A 165 (positive control), or VEGF-A 165 -HBD containing a His 6 tag or VEGF-A 165 -HBD without the tag. Values presented are the means (±SEM) obtained from two independent experiments. Other experimental details are described in Materials and Methods. (b) Binding of VEGF-A 165 -HBD to b1 domains of NRP1 and NRP2 was assessed by size exclusion chromatography. The protein mixtures of a tenfold molar excess of VEGF-A 165 -HBD with the purified b1 domain from either NRP1 or NRP2 were incubated at room temperature for 30 minutes. The FPLC profile for VEGF-A 165 -HBD and NRP1 b1 mixture is shown. SDS-PAGE analysis was used to evaluate samples of NRP1 b1, VEGF-A 165 -HBD, and the protein mixture before being loaded onto the size exclusion column (lanes 1–3, respectively) as well as samples of fractions which eluted from the single peak (lanes 4–6), showing that VEGF-A 165 -HBD and NRP1 b1 co-eluted from the preparative Superdex 75 column. A similar result was seen for VEGF-A 165 -HBD and NRP2 b1. (c) Formation of the molecular complexes was also investigated by analytical size exclusion chromatography. NRP1 b1 and b1b2 domains as well VEGF-A 165 -HBD were initially loaded separately onto the analytical Superdex 75 column and their corresponding FPLC traces are shown in solid and dashed lines, respectively. To detect binding, NRP1 b1 or b1b2 domains were mixed with VEGF-A 165 -HBD in solution at a molar ratio of 1∶10 and 1∶28, respectively and incubated for an hour at room temperature. The mixtures were then applied to the column. The main peaks in the elution profiles revealed a shift to the left of the peak positions corresponding to the unbound NRP1 b1 or b1b2 domains (indicated by vertical black lines), suggesting complex formation.

    Journal: PLoS ONE

    Article Title: Production of Soluble Human Vascular Endothelial Growth Factor VEGF-A165-Heparin Binding Domain in Escherichia coli

    doi: 10.1371/journal.pone.0055690

    Figure Lengend Snippet: Binding of VEGF-A 165 -HBD to NRP as detected by a cell based assay and size exclusion chromatography. (a) Binding of VEGF-A 165 -HBD to NRP1 was determined in DU145 cells expressing an adenoviral construct encoding NRP1 [17] . These cells do not express other VEGF receptors [21] . Cells were incubated with biotinylated VEGF-A 165 in the presence of the indicated concentrations of either unlabelled VEGF-A 165 (positive control), or VEGF-A 165 -HBD containing a His 6 tag or VEGF-A 165 -HBD without the tag. Values presented are the means (±SEM) obtained from two independent experiments. Other experimental details are described in Materials and Methods. (b) Binding of VEGF-A 165 -HBD to b1 domains of NRP1 and NRP2 was assessed by size exclusion chromatography. The protein mixtures of a tenfold molar excess of VEGF-A 165 -HBD with the purified b1 domain from either NRP1 or NRP2 were incubated at room temperature for 30 minutes. The FPLC profile for VEGF-A 165 -HBD and NRP1 b1 mixture is shown. SDS-PAGE analysis was used to evaluate samples of NRP1 b1, VEGF-A 165 -HBD, and the protein mixture before being loaded onto the size exclusion column (lanes 1–3, respectively) as well as samples of fractions which eluted from the single peak (lanes 4–6), showing that VEGF-A 165 -HBD and NRP1 b1 co-eluted from the preparative Superdex 75 column. A similar result was seen for VEGF-A 165 -HBD and NRP2 b1. (c) Formation of the molecular complexes was also investigated by analytical size exclusion chromatography. NRP1 b1 and b1b2 domains as well VEGF-A 165 -HBD were initially loaded separately onto the analytical Superdex 75 column and their corresponding FPLC traces are shown in solid and dashed lines, respectively. To detect binding, NRP1 b1 or b1b2 domains were mixed with VEGF-A 165 -HBD in solution at a molar ratio of 1∶10 and 1∶28, respectively and incubated for an hour at room temperature. The mixtures were then applied to the column. The main peaks in the elution profiles revealed a shift to the left of the peak positions corresponding to the unbound NRP1 b1 or b1b2 domains (indicated by vertical black lines), suggesting complex formation.

    Article Snippet: The binding assay was performed 48 hours after adenoviral infection by the addition of various concentrations of either VEGF-A165 (R & D Systems) (positive control) or VEGF-A165 -HBD diluted in binding medium with or without 0.1% bovine serum albumin (BSA), followed by addition of 1 nM biotinylated (bt) VEGF-A165 (R & D Systems).

    Techniques: Binding Assay, Cell Based Assay, Size-exclusion Chromatography, Expressing, Construct, Incubation, Positive Control, Purification, Fast Protein Liquid Chromatography, SDS Page

    Screening of NRP-1/VEGF-A165 inhibitors by in cell western. (A) schematic of VEGF-A triggered phosphorylation of VEGF-R2. Screening of NRP-1/VEGF-A165 inhibitors by in-cell Western. Cathecholamine A differentiated (CAD) cells were grown in 96 well plates. Cells were treated with the NRP-1/VEGF-A165 inhibitors at 12.5 µM or SARS-CoV-2 Spike (100 nM) in combination with 1nM VEGF-A165 as indicated. Cells were stained for pY1175 VEGFR2 as a marker of the activation of the pathway by VEGF-A165. (B) representative micrographs showing the lack of signal in controls with omission of the secondary antibody. Phosphorylated VEGFR2 was increased by the addition of 1 nM VEGF-A165 on the cells. (C) Bar graph showing the levels of pY1175 VEGFR2 normalized to the quantity of cells in each well. # p

    Journal: bioRxiv

    Article Title: In silico identification and validation of inhibitors of the interaction between neuropilin receptor 1 and SARS-CoV-2 Spike protein

    doi: 10.1101/2020.09.22.308783

    Figure Lengend Snippet: Screening of NRP-1/VEGF-A165 inhibitors by in cell western. (A) schematic of VEGF-A triggered phosphorylation of VEGF-R2. Screening of NRP-1/VEGF-A165 inhibitors by in-cell Western. Cathecholamine A differentiated (CAD) cells were grown in 96 well plates. Cells were treated with the NRP-1/VEGF-A165 inhibitors at 12.5 µM or SARS-CoV-2 Spike (100 nM) in combination with 1nM VEGF-A165 as indicated. Cells were stained for pY1175 VEGFR2 as a marker of the activation of the pathway by VEGF-A165. (B) representative micrographs showing the lack of signal in controls with omission of the secondary antibody. Phosphorylated VEGFR2 was increased by the addition of 1 nM VEGF-A165 on the cells. (C) Bar graph showing the levels of pY1175 VEGFR2 normalized to the quantity of cells in each well. # p

    Article Snippet: SARS-CoV2 Spike protein (100 nM, S1 domain aa16-685, Cat# Z03485, Genscript, Piscataway, NJ), EG00229 (Cat#6986, Tocris) or the indicated compounds were added at 12.5µM and incubated for 30 min at room temperature prior to adding biotinylated human VEGF-A165 (Cat#BT293, R & D systems) at 10 nM.

    Techniques: In-Cell ELISA, Staining, Marker, Activation Assay