recombinant human integrin α5β1 (MedChemExpress)
Structured Review
![(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.](https://bio-rxiv-images-cdn.bioz.com/dois_ending_with_41/10__64898_slash_2026__01__09__698741/10__64898_slash_2026__01__09__698741___F1.large.jpg)
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
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
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
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
![In vitro binding affinity and stability studies of [ 64 Cu]QM-2301, [ 64 Cu]QM-2302, and [ 64 Cu]QM-2303. (A) SPR sensorgrams demonstrating the binding affinity of QM-2301, QM-2302, and QM-2303 for human <t>integrin</t> α 5 β 1 in a concentration-dependent manner. (B) The equilibrium dissociation constant ( Κ D ) of each peptide was calculated based on SPR measurements. The K D values of each precursor are shown. (C, D) Schematic diagram of the binding patterns of [ 64 Cu]QM-2301, [ 64 Cu]QM-2302 (C), and [ 64 Cu]QM-2303 (D) to integrin α 5 β 1. Monomeric [ 64 Cu]QM-2301, and [ 64 Cu]QM-2302 bind to receptors in a single-network pattern. For [ 64 Cu]QM-2303, the PEGibody-based radiotracer, one PEGibody can bind to more than two integrin α 5 β 1 receptors, exhibiting better binding affinity. (E, F) The expression of integrin α 5 β 1 in B16F10 cells was analyzed by flow cytometry (E) and Western blotting (F). For flow cytometry assays, an anti-integrin α 5 + β 1 antibody was used. For Western blot assays, integrin α 5 (∼150 kDa) and integrin β 1 (∼138 kDa) were examined using two antibodies. (G) The stability of [ 64 Cu]QM-2301, [ 64 Cu]QM-2302, and [ 64 Cu]QM-2303 after coincubation with mouse serum within 1 h, as indicated by radio-HPLC. (H) I n vitro cell uptake of [ 64 Cu]QM-2301, [ 64 Cu]QM-2302, and [ 64 Cu]QM-2303 (750 KBq/mL) when incubated with B16F10 cells for different time period. (I) IC 50 of [ 64 Cu]QM-2301, [ 64 Cu]QM-2302, and [ 64 Cu]QM-2303 when inhibited with antibodies at different concentrations. ∗ P < 0.05, ∗∗ P < 0.01. All the quantitative experiments were performed independently at least three times (data are the mean ± SD, n = 3).](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_9959/pmc11959959/pmc11959959__gr2.jpg)
