Review



recombinant human integrin α5β1  (MedChemExpress)


Bioz Verified Symbol MedChemExpress is a verified supplier
Bioz Manufacturer Symbol MedChemExpress manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    MedChemExpress recombinant human integrin α5β1
    (A) Strategies for modification of GS, including amino acid mutation, covalent modification, cyclization, and multivalency. (B) SPR sensorgrams demonstrating the binding affinity of GS and GR for human integrin <t>α5β1</t> in a concentration-dependent manner. The equilibrium dissociation constant (K D ) of each peptide was calculated based on SPR measurements. The K D values of each precursor are shown. (C) Molecular docking of GR and GS binding integrin a5b1 protein (grey; PDB: 7NWL) showing the selected possible ligation residues. (D-F) Analysis of integrin α5β1 expression in U87MG cells and tumor tissues by western blot ( D ), and immunohistochemistry ( E-F ) analysis. The band for integrin α5 was approximately 150 kDa. M, marker. C, cell. T, tumor. For immunofluorescence images, green is for integrin α5, red for integrin β1, and blue for nucleus. Scale bar, 50□μm ( E-F ). (G) In vitro cellular uptake of [ 68 Ga]GS and [ 68 Ga]GR in U87MG cell lines. All results are expressed as means ± SEM, as indicated in at least three independent experiments. “*” represents differences compared with the [ 68 Ga]GS. * p < 0.05.
    Recombinant Human Integrin α5β1, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant human integrin α5β1/product/MedChemExpress
    Average 94 stars, based on 3 article reviews
    recombinant human integrin α5β1 - by Bioz Stars, 2026-03
    94/100 stars

    Images

    1) Product Images from "Development of Integrin α5β1-targeted PET/NIR imaging probes for glioblastoma intraoperative navigation and intracavity targeted radionuclide therapy"

    Article Title: Development of Integrin α5β1-targeted PET/NIR imaging probes for glioblastoma intraoperative navigation and intracavity targeted radionuclide therapy

    Journal: bioRxiv

    doi: 10.64898/2026.01.09.698741

    (A) Strategies for modification of GS, including amino acid mutation, covalent modification, cyclization, and multivalency. (B) SPR sensorgrams demonstrating the binding affinity of GS and GR for human integrin α5β1 in a concentration-dependent manner. The equilibrium dissociation constant (K D ) of each peptide was calculated based on SPR measurements. The K D values of each precursor are shown. (C) Molecular docking of GR and GS binding integrin a5b1 protein (grey; PDB: 7NWL) showing the selected possible ligation residues. (D-F) Analysis of integrin α5β1 expression in U87MG cells and tumor tissues by western blot ( D ), and immunohistochemistry ( E-F ) analysis. The band for integrin α5 was approximately 150 kDa. M, marker. C, cell. T, tumor. For immunofluorescence images, green is for integrin α5, red for integrin β1, and blue for nucleus. Scale bar, 50□μm ( E-F ). (G) In vitro cellular uptake of [ 68 Ga]GS and [ 68 Ga]GR in U87MG cell lines. All results are expressed as means ± SEM, as indicated in at least three independent experiments. “*” represents differences compared with the [ 68 Ga]GS. * p < 0.05.
    Figure Legend Snippet: (A) Strategies for modification of GS, including amino acid mutation, covalent modification, cyclization, and multivalency. (B) SPR sensorgrams demonstrating the binding affinity of GS and GR for human integrin α5β1 in a concentration-dependent manner. The equilibrium dissociation constant (K D ) of each peptide was calculated based on SPR measurements. The K D values of each precursor are shown. (C) Molecular docking of GR and GS binding integrin a5b1 protein (grey; PDB: 7NWL) showing the selected possible ligation residues. (D-F) Analysis of integrin α5β1 expression in U87MG cells and tumor tissues by western blot ( D ), and immunohistochemistry ( E-F ) analysis. The band for integrin α5 was approximately 150 kDa. M, marker. C, cell. T, tumor. For immunofluorescence images, green is for integrin α5, red for integrin β1, and blue for nucleus. Scale bar, 50□μm ( E-F ). (G) In vitro cellular uptake of [ 68 Ga]GS and [ 68 Ga]GR in U87MG cell lines. All results are expressed as means ± SEM, as indicated in at least three independent experiments. “*” represents differences compared with the [ 68 Ga]GS. * p < 0.05.

    Techniques Used: Modification, Mutagenesis, Binding Assay, Concentration Assay, Ligation, Expressing, Western Blot, Immunohistochemistry, Marker, Immunofluorescence, In Vitro

    (A) Immunofluorescence images show the expression of integrin α5β1, GFAP, and NEUN of U87MG tumors in orthotopic glioblastoma tumor-bearing mice. Green indicates integrin α5, Red for NEUN, yellow for GFAP, and blue for nucleus. Scale bar, 1 mm. (B-C) Representative fluorescence imaging of mice bearing in orthotopic U87MG tumors ( B ) and ex vivo brains ( C ). Cy5-GS and Cy5-GR were intravenously injected with a dose of 5 mg/kg. (D) Quantification of fluorescence intensity in tumors corresponding to ( C ). (E) Immunohistochemical analysis of integrin α5β1 expression in brain tissue sections from orthotopic glioblastoma tumor-bearing mice. Scale bar, 1 mm. (F-G) Immunofluorescence images of brain tissue sections from orthotopic glioblastoma tumor-bearing mice treated with Cy5-GS ( F ) and Cy5-GR ( G ). Green indicates integrin α5, Red for GS or GR, and blue for nucleus. Scale bar, 1 mm. (H-I) Magnific imaging of brain tissue sections from orthotopic glioblastoma tumor-bearing mice treated with GS-Cy5. Scale bar, 50 μm. All results are expressed as means ± SEM, as indicated in at least three independent experiments. A multiple t-test was used when two groups were compared. The symbol “*” represents differences compared with the Cy5-GS. *** p < 0.001.
    Figure Legend Snippet: (A) Immunofluorescence images show the expression of integrin α5β1, GFAP, and NEUN of U87MG tumors in orthotopic glioblastoma tumor-bearing mice. Green indicates integrin α5, Red for NEUN, yellow for GFAP, and blue for nucleus. Scale bar, 1 mm. (B-C) Representative fluorescence imaging of mice bearing in orthotopic U87MG tumors ( B ) and ex vivo brains ( C ). Cy5-GS and Cy5-GR were intravenously injected with a dose of 5 mg/kg. (D) Quantification of fluorescence intensity in tumors corresponding to ( C ). (E) Immunohistochemical analysis of integrin α5β1 expression in brain tissue sections from orthotopic glioblastoma tumor-bearing mice. Scale bar, 1 mm. (F-G) Immunofluorescence images of brain tissue sections from orthotopic glioblastoma tumor-bearing mice treated with Cy5-GS ( F ) and Cy5-GR ( G ). Green indicates integrin α5, Red for GS or GR, and blue for nucleus. Scale bar, 1 mm. (H-I) Magnific imaging of brain tissue sections from orthotopic glioblastoma tumor-bearing mice treated with GS-Cy5. Scale bar, 50 μm. All results are expressed as means ± SEM, as indicated in at least three independent experiments. A multiple t-test was used when two groups were compared. The symbol “*” represents differences compared with the Cy5-GS. *** p < 0.001.

    Techniques Used: Immunofluorescence, Expressing, Fluorescence, Imaging, Ex Vivo, Injection, Immunohistochemical staining



    Similar Products

    94
    MedChemExpress recombinant human integrin α5β1
    (A) Strategies for modification of GS, including amino acid mutation, covalent modification, cyclization, and multivalency. (B) SPR sensorgrams demonstrating the binding affinity of GS and GR for human integrin <t>α5β1</t> in a concentration-dependent manner. The equilibrium dissociation constant (K D ) of each peptide was calculated based on SPR measurements. The K D values of each precursor are shown. (C) Molecular docking of GR and GS binding integrin a5b1 protein (grey; PDB: 7NWL) showing the selected possible ligation residues. (D-F) Analysis of integrin α5β1 expression in U87MG cells and tumor tissues by western blot ( D ), and immunohistochemistry ( E-F ) analysis. The band for integrin α5 was approximately 150 kDa. M, marker. C, cell. T, tumor. For immunofluorescence images, green is for integrin α5, red for integrin β1, and blue for nucleus. Scale bar, 50□μm ( E-F ). (G) In vitro cellular uptake of [ 68 Ga]GS and [ 68 Ga]GR in U87MG cell lines. All results are expressed as means ± SEM, as indicated in at least three independent experiments. “*” represents differences compared with the [ 68 Ga]GS. * p < 0.05.
    Recombinant Human Integrin α5β1, supplied by MedChemExpress, 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 human integrin α5β1/product/MedChemExpress
    Average 94 stars, based on 1 article reviews
    recombinant human integrin α5β1 - by Bioz Stars, 2026-03
    94/100 stars
      Buy from Supplier

    93
    R&D Systems human integrins α5β1
    (A) Strategies for modification of GS, including amino acid mutation, covalent modification, cyclization, and multivalency. (B) SPR sensorgrams demonstrating the binding affinity of GS and GR for human integrin <t>α5β1</t> in a concentration-dependent manner. The equilibrium dissociation constant (K D ) of each peptide was calculated based on SPR measurements. The K D values of each precursor are shown. (C) Molecular docking of GR and GS binding integrin a5b1 protein (grey; PDB: 7NWL) showing the selected possible ligation residues. (D-F) Analysis of integrin α5β1 expression in U87MG cells and tumor tissues by western blot ( D ), and immunohistochemistry ( E-F ) analysis. The band for integrin α5 was approximately 150 kDa. M, marker. C, cell. T, tumor. For immunofluorescence images, green is for integrin α5, red for integrin β1, and blue for nucleus. Scale bar, 50□μm ( E-F ). (G) In vitro cellular uptake of [ 68 Ga]GS and [ 68 Ga]GR in U87MG cell lines. All results are expressed as means ± SEM, as indicated in at least three independent experiments. “*” represents differences compared with the [ 68 Ga]GS. * p < 0.05.
    Human Integrins α5β1, 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/human integrins α5β1/product/R&D Systems
    Average 93 stars, based on 1 article reviews
    human integrins α5β1 - by Bioz Stars, 2026-03
    93/100 stars
      Buy from Supplier

    95
    R&D Systems recombinant human integrin α5β1
    (A) Strategies for modification of GS, including amino acid mutation, covalent modification, cyclization, and multivalency. (B) SPR sensorgrams demonstrating the binding affinity of GS and GR for human integrin <t>α5β1</t> in a concentration-dependent manner. The equilibrium dissociation constant (K D ) of each peptide was calculated based on SPR measurements. The K D values of each precursor are shown. (C) Molecular docking of GR and GS binding integrin a5b1 protein (grey; PDB: 7NWL) showing the selected possible ligation residues. (D-F) Analysis of integrin α5β1 expression in U87MG cells and tumor tissues by western blot ( D ), and immunohistochemistry ( E-F ) analysis. The band for integrin α5 was approximately 150 kDa. M, marker. C, cell. T, tumor. For immunofluorescence images, green is for integrin α5, red for integrin β1, and blue for nucleus. Scale bar, 50□μm ( E-F ). (G) In vitro cellular uptake of [ 68 Ga]GS and [ 68 Ga]GR in U87MG cell lines. All results are expressed as means ± SEM, as indicated in at least three independent experiments. “*” represents differences compared with the [ 68 Ga]GS. * p < 0.05.
    Recombinant Human Integrin α5β1, supplied by R&D Systems, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant human integrin α5β1/product/R&D Systems
    Average 95 stars, based on 1 article reviews
    recombinant human integrin α5β1 - by Bioz Stars, 2026-03
    95/100 stars
      Buy from Supplier

    93
    R&D Systems α5β1 integrins
    F4 binds to αvβ3 and <t>α5β1</t> <t>integrins</t> on HUVEC . (a) HUVECs were analyzed by flow cytometry for the expression of αvβ3 and α5β1 integrins. (b) HUVEC extracts were submitted to F4 affinity chromatography. Bound proteins were eluted with increasing concentrations of NaCl (0.15, 0.6 and 1 M) and the elution profile was checked by recording the absorbance at 280 nm. (c) Eluted samples were then analyzed by SDS-PAGE and western blot HUVEC total extracts and recombinant αvβ3 and α5β1 integrins were used as positive controls. The 0.6 M eluted sample revealed bands which matched the molecular weight of the α5, β1, αv and β3 recombinant integrin subunits. The experiment was repeated twice (N = 2)
    α5β1 Integrins, 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/α5β1 integrins/product/R&D Systems
    Average 93 stars, based on 1 article reviews
    α5β1 integrins - by Bioz Stars, 2026-03
    93/100 stars
      Buy from Supplier

    94
    R&D Systems recombinant human integrin α5β1 protein
    F4 binds to αvβ3 and <t>α5β1</t> <t>integrins</t> on HUVEC . (a) HUVECs were analyzed by flow cytometry for the expression of αvβ3 and α5β1 integrins. (b) HUVEC extracts were submitted to F4 affinity chromatography. Bound proteins were eluted with increasing concentrations of NaCl (0.15, 0.6 and 1 M) and the elution profile was checked by recording the absorbance at 280 nm. (c) Eluted samples were then analyzed by SDS-PAGE and western blot HUVEC total extracts and recombinant αvβ3 and α5β1 integrins were used as positive controls. The 0.6 M eluted sample revealed bands which matched the molecular weight of the α5, β1, αv and β3 recombinant integrin subunits. The experiment was repeated twice (N = 2)
    Recombinant Human Integrin α5β1 Protein, 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 human integrin α5β1 protein/product/R&D Systems
    Average 94 stars, based on 1 article reviews
    recombinant human integrin α5β1 protein - by Bioz Stars, 2026-03
    94/100 stars
      Buy from Supplier

    90
    R&D Systems recombinant human integrin α5β1 heterodimer
    F4 binds to αvβ3 and <t>α5β1</t> <t>integrins</t> on HUVEC . (a) HUVECs were analyzed by flow cytometry for the expression of αvβ3 and α5β1 integrins. (b) HUVEC extracts were submitted to F4 affinity chromatography. Bound proteins were eluted with increasing concentrations of NaCl (0.15, 0.6 and 1 M) and the elution profile was checked by recording the absorbance at 280 nm. (c) Eluted samples were then analyzed by SDS-PAGE and western blot HUVEC total extracts and recombinant αvβ3 and α5β1 integrins were used as positive controls. The 0.6 M eluted sample revealed bands which matched the molecular weight of the α5, β1, αv and β3 recombinant integrin subunits. The experiment was repeated twice (N = 2)
    Recombinant Human Integrin α5β1 Heterodimer, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant human integrin α5β1 heterodimer/product/R&D Systems
    Average 90 stars, based on 1 article reviews
    recombinant human integrin α5β1 heterodimer - by Bioz Stars, 2026-03
    90/100 stars
      Buy from Supplier

    Image Search Results


    (A) Strategies for modification of GS, including amino acid mutation, covalent modification, cyclization, and multivalency. (B) SPR sensorgrams demonstrating the binding affinity of GS and GR for human integrin α5β1 in a concentration-dependent manner. The equilibrium dissociation constant (K D ) of each peptide was calculated based on SPR measurements. The K D values of each precursor are shown. (C) Molecular docking of GR and GS binding integrin a5b1 protein (grey; PDB: 7NWL) showing the selected possible ligation residues. (D-F) Analysis of integrin α5β1 expression in U87MG cells and tumor tissues by western blot ( D ), and immunohistochemistry ( E-F ) analysis. The band for integrin α5 was approximately 150 kDa. M, marker. C, cell. T, tumor. For immunofluorescence images, green is for integrin α5, red for integrin β1, and blue for nucleus. Scale bar, 50□μm ( E-F ). (G) In vitro cellular uptake of [ 68 Ga]GS and [ 68 Ga]GR in U87MG cell lines. All results are expressed as means ± SEM, as indicated in at least three independent experiments. “*” represents differences compared with the [ 68 Ga]GS. * p < 0.05.

    Journal: bioRxiv

    Article Title: Development of Integrin α5β1-targeted PET/NIR imaging probes for glioblastoma intraoperative navigation and intracavity targeted radionuclide therapy

    doi: 10.64898/2026.01.09.698741

    Figure Lengend Snippet: (A) Strategies for modification of GS, including amino acid mutation, covalent modification, cyclization, and multivalency. (B) SPR sensorgrams demonstrating the binding affinity of GS and GR for human integrin α5β1 in a concentration-dependent manner. The equilibrium dissociation constant (K D ) of each peptide was calculated based on SPR measurements. The K D values of each precursor are shown. (C) Molecular docking of GR and GS binding integrin a5b1 protein (grey; PDB: 7NWL) showing the selected possible ligation residues. (D-F) Analysis of integrin α5β1 expression in U87MG cells and tumor tissues by western blot ( D ), and immunohistochemistry ( E-F ) analysis. The band for integrin α5 was approximately 150 kDa. M, marker. C, cell. T, tumor. For immunofluorescence images, green is for integrin α5, red for integrin β1, and blue for nucleus. Scale bar, 50□μm ( E-F ). (G) In vitro cellular uptake of [ 68 Ga]GS and [ 68 Ga]GR in U87MG cell lines. All results are expressed as means ± SEM, as indicated in at least three independent experiments. “*” represents differences compared with the [ 68 Ga]GS. * p < 0.05.

    Article Snippet: Recombinant human integrin α5β1 (alpha 5 beta 1, HY-P77718, MCE, NJ, USA) was immobilized on a CM5 sensor chip at 25 □ following a standard amine coupling kit.

    Techniques: Modification, Mutagenesis, Binding Assay, Concentration Assay, Ligation, Expressing, Western Blot, Immunohistochemistry, Marker, Immunofluorescence, In Vitro

    (A) Immunofluorescence images show the expression of integrin α5β1, GFAP, and NEUN of U87MG tumors in orthotopic glioblastoma tumor-bearing mice. Green indicates integrin α5, Red for NEUN, yellow for GFAP, and blue for nucleus. Scale bar, 1 mm. (B-C) Representative fluorescence imaging of mice bearing in orthotopic U87MG tumors ( B ) and ex vivo brains ( C ). Cy5-GS and Cy5-GR were intravenously injected with a dose of 5 mg/kg. (D) Quantification of fluorescence intensity in tumors corresponding to ( C ). (E) Immunohistochemical analysis of integrin α5β1 expression in brain tissue sections from orthotopic glioblastoma tumor-bearing mice. Scale bar, 1 mm. (F-G) Immunofluorescence images of brain tissue sections from orthotopic glioblastoma tumor-bearing mice treated with Cy5-GS ( F ) and Cy5-GR ( G ). Green indicates integrin α5, Red for GS or GR, and blue for nucleus. Scale bar, 1 mm. (H-I) Magnific imaging of brain tissue sections from orthotopic glioblastoma tumor-bearing mice treated with GS-Cy5. Scale bar, 50 μm. All results are expressed as means ± SEM, as indicated in at least three independent experiments. A multiple t-test was used when two groups were compared. The symbol “*” represents differences compared with the Cy5-GS. *** p < 0.001.

    Journal: bioRxiv

    Article Title: Development of Integrin α5β1-targeted PET/NIR imaging probes for glioblastoma intraoperative navigation and intracavity targeted radionuclide therapy

    doi: 10.64898/2026.01.09.698741

    Figure Lengend Snippet: (A) Immunofluorescence images show the expression of integrin α5β1, GFAP, and NEUN of U87MG tumors in orthotopic glioblastoma tumor-bearing mice. Green indicates integrin α5, Red for NEUN, yellow for GFAP, and blue for nucleus. Scale bar, 1 mm. (B-C) Representative fluorescence imaging of mice bearing in orthotopic U87MG tumors ( B ) and ex vivo brains ( C ). Cy5-GS and Cy5-GR were intravenously injected with a dose of 5 mg/kg. (D) Quantification of fluorescence intensity in tumors corresponding to ( C ). (E) Immunohistochemical analysis of integrin α5β1 expression in brain tissue sections from orthotopic glioblastoma tumor-bearing mice. Scale bar, 1 mm. (F-G) Immunofluorescence images of brain tissue sections from orthotopic glioblastoma tumor-bearing mice treated with Cy5-GS ( F ) and Cy5-GR ( G ). Green indicates integrin α5, Red for GS or GR, and blue for nucleus. Scale bar, 1 mm. (H-I) Magnific imaging of brain tissue sections from orthotopic glioblastoma tumor-bearing mice treated with GS-Cy5. Scale bar, 50 μm. All results are expressed as means ± SEM, as indicated in at least three independent experiments. A multiple t-test was used when two groups were compared. The symbol “*” represents differences compared with the Cy5-GS. *** p < 0.001.

    Article Snippet: Recombinant human integrin α5β1 (alpha 5 beta 1, HY-P77718, MCE, NJ, USA) was immobilized on a CM5 sensor chip at 25 □ following a standard amine coupling kit.

    Techniques: Immunofluorescence, Expressing, Fluorescence, Imaging, Ex Vivo, Injection, Immunohistochemical staining

    F4 binds to αvβ3 and α5β1 integrins on HUVEC . (a) HUVECs were analyzed by flow cytometry for the expression of αvβ3 and α5β1 integrins. (b) HUVEC extracts were submitted to F4 affinity chromatography. Bound proteins were eluted with increasing concentrations of NaCl (0.15, 0.6 and 1 M) and the elution profile was checked by recording the absorbance at 280 nm. (c) Eluted samples were then analyzed by SDS-PAGE and western blot HUVEC total extracts and recombinant αvβ3 and α5β1 integrins were used as positive controls. The 0.6 M eluted sample revealed bands which matched the molecular weight of the α5, β1, αv and β3 recombinant integrin subunits. The experiment was repeated twice (N = 2)

    Journal: Cell Adhesion & Migration

    Article Title: F4, a collagen XIX-derived peptide, inhibits tumor angiogenesis through αvβ3 and α5β1 integrin interaction

    doi: 10.1080/19336918.2021.1951425

    Figure Lengend Snippet: F4 binds to αvβ3 and α5β1 integrins on HUVEC . (a) HUVECs were analyzed by flow cytometry for the expression of αvβ3 and α5β1 integrins. (b) HUVEC extracts were submitted to F4 affinity chromatography. Bound proteins were eluted with increasing concentrations of NaCl (0.15, 0.6 and 1 M) and the elution profile was checked by recording the absorbance at 280 nm. (c) Eluted samples were then analyzed by SDS-PAGE and western blot HUVEC total extracts and recombinant αvβ3 and α5β1 integrins were used as positive controls. The 0.6 M eluted sample revealed bands which matched the molecular weight of the α5, β1, αv and β3 recombinant integrin subunits. The experiment was repeated twice (N = 2)

    Article Snippet: HUVEC extracts and recombinant human αvβ3 and α5β1 integrins (3230-A5-050 and 3050-AV-050, R&D systems) were used as positive controls.

    Techniques: Flow Cytometry, Expressing, Affinity Chromatography, SDS Page, Western Blot, Recombinant, Molecular Weight

    F4 directly binds to αvβ3 and α5β1 integrins . Direct interaction between αvβ3 or α5β1 integrin and F4 was studied using solid phase assays as described in the material and method section. The F4 peptide was biotinylated to allow its detection using the streptavidin-peroxidase complex. Different conditions were used. (a-b) The amounts of coated αvβ3 (a) or α5β1 integrin (b) were increased while biotinylated F4 peptide was kept constant. (c-d) The concentration of biotinylated F4 peptide was increased while coated amounts of αvβ3 (c) or α5β1 (d) integrins were kept constant. (e-f) Competitive assays were performed using increasing concentrations of F4 peptide while biotinylated-F4 peptide and αvβ3 (e) or α5β1 (f) integrins were kept constant. The solid phase assays were repeated twice (N = 2; n = 2)

    Journal: Cell Adhesion & Migration

    Article Title: F4, a collagen XIX-derived peptide, inhibits tumor angiogenesis through αvβ3 and α5β1 integrin interaction

    doi: 10.1080/19336918.2021.1951425

    Figure Lengend Snippet: F4 directly binds to αvβ3 and α5β1 integrins . Direct interaction between αvβ3 or α5β1 integrin and F4 was studied using solid phase assays as described in the material and method section. The F4 peptide was biotinylated to allow its detection using the streptavidin-peroxidase complex. Different conditions were used. (a-b) The amounts of coated αvβ3 (a) or α5β1 integrin (b) were increased while biotinylated F4 peptide was kept constant. (c-d) The concentration of biotinylated F4 peptide was increased while coated amounts of αvβ3 (c) or α5β1 (d) integrins were kept constant. (e-f) Competitive assays were performed using increasing concentrations of F4 peptide while biotinylated-F4 peptide and αvβ3 (e) or α5β1 (f) integrins were kept constant. The solid phase assays were repeated twice (N = 2; n = 2)

    Article Snippet: HUVEC extracts and recombinant human αvβ3 and α5β1 integrins (3230-A5-050 and 3050-AV-050, R&D systems) were used as positive controls.

    Techniques: Concentration Assay