recombinant human integrin α5β1 Search Results


94
R&D Systems recombinant human integrin α5β1 protein
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
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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
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90
R&D Systems recombinant human integrin α5β1 heterodimer
(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 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
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92
R&D Systems integrin ecd
(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.
Integrin Ecd, 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
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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
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95
R&D Systems α5β1 function purified human fibronectin
(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.
α5β1 Function Purified Human Fibronectin, 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
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93
Selleck Chemicals atn 161
(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.
Atn 161, supplied by Selleck Chemicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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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
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α5β1 integrins - by Bioz Stars, 2026-03
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93
Sino Biological human α5β1 ct 014 h2508h
Anti-integrin antibodies apparent affinities to different integrin subunits investigated by ELISA.
Human α5β1 Ct 014 H2508h, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
Millipore human α5β1 integrin
Anti-integrin antibodies apparent affinities to different integrin subunits investigated by ELISA.
Human α5β1 Integrin, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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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

Anti-integrin antibodies apparent affinities to different integrin subunits investigated by ELISA.

Journal: PLoS ONE

Article Title: An innovative strategy to identify new targets for delivering antibodies to the brain has led to the exploration of the integrin family

doi: 10.1371/journal.pone.0274667

Figure Lengend Snippet: Anti-integrin antibodies apparent affinities to different integrin subunits investigated by ELISA.

Article Snippet: Recombinant integrin proteins were purchased from OriGene for human monomer α3, α5 and β1 (tp320975, tp301151 and tp303818), from GeneTex for human monomer α4 (GTX48181), from R&D Systems for human and mouse dimer α3β1, α4β1 and α5β1 (2840-a3, 3230-a5, 5668-a4, 7728-a5, 9374-a3) for human ALCAM 656-AL, from Sino Biological for human α5β1 (CT-014-H2508H), from Abcam for Striatin3 (ab162295) Antibodies were purchased from antibodies-online (natalizumab ABIN5668196), from Abcam (Anti-VE Cadherin ab33168), from BD Biosciences (553715), from BioLegend (343802 and MFR5 103801), from Interchim (DCABH-8217), from Invitrogen (14-0299-82, MA5-17103, MA1-25298), from Millipore (MABT409, MABT199, MAB2079Z) from Novus Biological (NBP2-52708), from Proteintech (66070-1-Ig), from R&DSystems (MAB1345), from Sigma-Aldrich (MAB1965), from ThermoFisher Scientific (Anti-ZO-1 #61–7300; Anti-Occludin #33–1500; all other antibodies were produced in-house by Sanofi Biological Research. hCMEC/D3 cells were obtained from Cedarlane.

Techniques: Enzyme-linked Immunosorbent Assay