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recombinant human integrin α v β 6 receptor  (R&D Systems)


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    Structured Review

    R&D Systems recombinant human integrin α v β 6 receptor
    Inhibition of biotinylated fibronectin binding to <t> α V β 6 integrin </t> compared with inhibition of biotinylated vitronectin binding to α V β 3 .
    Recombinant Human Integrin α V β 6 Receptor, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/recombinant+human+integrin+%CE%B1+v+%CE%B2+6+receptor/Recombinant+Human+Integrin+alpha+V+beta+6+Protein%2C+CF/pmc05664067-128-0-8
    Average 92 stars, based on 13 article reviews
    recombinant human integrin α v β 6 receptor - by Bioz Stars, 2026-10
    92/100 stars

    Images

    1) Product Images from "Investigating the Interaction of Cyclic RGD Peptidomimetics with α V β 6 Integrin by Biochemical and Molecular Docking Studies"

    Article Title: Investigating the Interaction of Cyclic RGD Peptidomimetics with α V β 6 Integrin by Biochemical and Molecular Docking Studies

    Journal: Cancers

    doi: 10.3390/cancers9100128

    Inhibition of biotinylated fibronectin binding to α V β 6 integrin compared with inhibition of biotinylated vitronectin binding to α V β 3 .
    Figure Legend Snippet: Inhibition of biotinylated fibronectin binding to α V β 6 integrin compared with inhibition of biotinylated vitronectin binding to α V β 3 .

    Techniques Used: Inhibition, Binding Assay

    Docking best poses of ( a ) ligand 1a (green) and ( b ) ligand 1c (green) overlaid to the X-ray structure of the TGF-β3 undecapeptide (grey, α-helix represented as a ribbon) into integrin α V β 6 (from 4UM9.pdb). Only selected integrin residues involved in interactions with the ligand are shown and labeled in blue for α V and red for β 6 . Non-polar hydrogens are hidden for clarity, while intermolecular hydrogen bonds are shown as black dashed lines.
    Figure Legend Snippet: Docking best poses of ( a ) ligand 1a (green) and ( b ) ligand 1c (green) overlaid to the X-ray structure of the TGF-β3 undecapeptide (grey, α-helix represented as a ribbon) into integrin α V β 6 (from 4UM9.pdb). Only selected integrin residues involved in interactions with the ligand are shown and labeled in blue for α V and red for β 6 . Non-polar hydrogens are hidden for clarity, while intermolecular hydrogen bonds are shown as black dashed lines.

    Techniques Used: Labeling

    Docking best poses of ( a ) ligands 2 (red), 4 (green) and 5 (blue) and ( b ) ligands 3 (red), 6 (green) and 7 (blue) into integrin α V β 6 (α V surface in grey, β 6 surface in yellow). The X-ray structure of the TGF-β3 α-helix portion is shown as a grey ribbon. Ligand aromatic rings are represented as space-filling spheres.
    Figure Legend Snippet: Docking best poses of ( a ) ligands 2 (red), 4 (green) and 5 (blue) and ( b ) ligands 3 (red), 6 (green) and 7 (blue) into integrin α V β 6 (α V surface in grey, β 6 surface in yellow). The X-ray structure of the TGF-β3 α-helix portion is shown as a grey ribbon. Ligand aromatic rings are represented as space-filling spheres.

    Techniques Used:

    Related Articles

    Recombinant:

    Article Title: Investigating the Interaction of Cyclic RGD Peptidomimetics with α V β 6 Integrin by Biochemical and Molecular Docking Studies
    Article Snippet: .. Recombinant human integrin α V β 6 receptor (R&D Systems, Minneapolis, MN, USA) was diluted to 1.0 μg/mL in coating buffer containing 20 mM Tris-HCl (pH 7.4), 150 mM NaCl, 1 mM MnCl 2 , 2 mM CaCl 2 , and 1 mM MgCl 2 . .. An aliquot of diluted receptor (100 μL/well) was added to 96-well microtiter plates (Nunc MaxiSorp, Thermo Fisher Scientific, Roskilde, Denmark) and incubated overnight at 4 °C.



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    recombinant human integrin α v β 6 receptor  (R&D Systems)
    92
    R&D Systems recombinant human integrin α v β 6 receptor
    Inhibition of biotinylated fibronectin binding to <t> α V β 6 integrin </t> compared with inhibition of biotinylated vitronectin binding to α V β 3 .
    Recombinant Human Integrin α V β 6 Receptor, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/recombinant+human+integrin+%CE%B1+v+%CE%B2+6+receptor/Recombinant+Human+Integrin+alpha+V+beta+6+Protein%2C+CF/pmc05664067-128-0-8
    Average 92 stars, based on 1 article reviews
    recombinant human integrin α v β 6 receptor - by Bioz Stars, 2026-10
    92/100 stars
    		  Buy from Supplier

    Image Search Results


    Inhibition of biotinylated fibronectin binding to α V β 6 integrin compared with inhibition of biotinylated vitronectin binding to α V β 3 .

    Journal: Cancers

    Article Title: Investigating the Interaction of Cyclic RGD Peptidomimetics with α V β 6 Integrin by Biochemical and Molecular Docking Studies

    doi: 10.3390/cancers9100128

    Figure Lengend Snippet: Inhibition of biotinylated fibronectin binding to α V β 6 integrin compared with inhibition of biotinylated vitronectin binding to α V β 3 .

    Article Snippet: Recombinant human integrin α V β 6 receptor (R&D Systems, Minneapolis, MN, USA) was diluted to 1.0 μg/mL in coating buffer containing 20 mM Tris-HCl (pH 7.4), 150 mM NaCl, 1 mM MnCl 2 , 2 mM CaCl 2 , and 1 mM MgCl 2 .

    Techniques: Inhibition, Binding Assay

    Docking best poses of ( a ) ligand 1a (green) and ( b ) ligand 1c (green) overlaid to the X-ray structure of the TGF-β3 undecapeptide (grey, α-helix represented as a ribbon) into integrin α V β 6 (from 4UM9.pdb). Only selected integrin residues involved in interactions with the ligand are shown and labeled in blue for α V and red for β 6 . Non-polar hydrogens are hidden for clarity, while intermolecular hydrogen bonds are shown as black dashed lines.

    Journal: Cancers

    Article Title: Investigating the Interaction of Cyclic RGD Peptidomimetics with α V β 6 Integrin by Biochemical and Molecular Docking Studies

    doi: 10.3390/cancers9100128

    Figure Lengend Snippet: Docking best poses of ( a ) ligand 1a (green) and ( b ) ligand 1c (green) overlaid to the X-ray structure of the TGF-β3 undecapeptide (grey, α-helix represented as a ribbon) into integrin α V β 6 (from 4UM9.pdb). Only selected integrin residues involved in interactions with the ligand are shown and labeled in blue for α V and red for β 6 . Non-polar hydrogens are hidden for clarity, while intermolecular hydrogen bonds are shown as black dashed lines.

    Article Snippet: Recombinant human integrin α V β 6 receptor (R&D Systems, Minneapolis, MN, USA) was diluted to 1.0 μg/mL in coating buffer containing 20 mM Tris-HCl (pH 7.4), 150 mM NaCl, 1 mM MnCl 2 , 2 mM CaCl 2 , and 1 mM MgCl 2 .

    Techniques: Labeling

    Docking best poses of ( a ) ligands 2 (red), 4 (green) and 5 (blue) and ( b ) ligands 3 (red), 6 (green) and 7 (blue) into integrin α V β 6 (α V surface in grey, β 6 surface in yellow). The X-ray structure of the TGF-β3 α-helix portion is shown as a grey ribbon. Ligand aromatic rings are represented as space-filling spheres.

    Journal: Cancers

    Article Title: Investigating the Interaction of Cyclic RGD Peptidomimetics with α V β 6 Integrin by Biochemical and Molecular Docking Studies

    doi: 10.3390/cancers9100128

    Figure Lengend Snippet: Docking best poses of ( a ) ligands 2 (red), 4 (green) and 5 (blue) and ( b ) ligands 3 (red), 6 (green) and 7 (blue) into integrin α V β 6 (α V surface in grey, β 6 surface in yellow). The X-ray structure of the TGF-β3 α-helix portion is shown as a grey ribbon. Ligand aromatic rings are represented as space-filling spheres.

    Article Snippet: Recombinant human integrin α V β 6 receptor (R&D Systems, Minneapolis, MN, USA) was diluted to 1.0 μg/mL in coating buffer containing 20 mM Tris-HCl (pH 7.4), 150 mM NaCl, 1 mM MnCl 2 , 2 mM CaCl 2 , and 1 mM MgCl 2 .

    Techniques: