egfr binding Affibody Search Results


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    Affibody egfr binding affibody molecule
    Specificity of 89 Zr-DFO-ZEGFR:2377 uptake in A431 xenografts and <t>EGFR-expressing</t> organs in mice at 3 h after injection. In the blocked group, receptors were saturated by pre-injection of large excess of non-labelled <t>affibody</t> molecules.
    Egfr Binding Affibody Molecule, supplied by Affibody, used in various techniques. Bioz Stars score: 90/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Affibody egfr binding affibody molecule zegfr
    PET images, summed 30–60 min, and TACs from a Balbc nu/nu mouse (prone) bearing tumors ( white arrows ): a one A431 xenograft (1 × 10 7 cells, 15 days) or b two A431 xenografts ( left : 1 × 10 7 cells, 28 days; right : 1 × 10 7 cells, 25 days). Comparison A shows a 7-times higher uptake with targeting [methyl- 11 C]-Z <t>EGFR:2377</t> -ST-CH 3 compared to the non-targeting [methyl- 11 C]-Z Taq:3638 -ST-CH 3 . Comparison B illustrates uptake of the targeting <t>Affibody</t> increasing as the tumors grow from time from inoculation
    Egfr Binding Affibody Molecule Zegfr, supplied by Affibody, used in various techniques. Bioz Stars score: 90/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Affibody non egfr binding affibody molecules
    PET images, summed 30–60 min, and TACs from a Balbc nu/nu mouse (prone) bearing tumors ( white arrows ): a one A431 xenograft (1 × 10 7 cells, 15 days) or b two A431 xenografts ( left : 1 × 10 7 cells, 28 days; right : 1 × 10 7 cells, 25 days). Comparison A shows a 7-times higher uptake with targeting [methyl- 11 C]-Z <t>EGFR:2377</t> -ST-CH 3 compared to the non-targeting [methyl- 11 C]-Z Taq:3638 -ST-CH 3 . Comparison B illustrates uptake of the targeting <t>Affibody</t> increasing as the tumors grow from time from inoculation
    Non Egfr Binding Affibody Molecules, supplied by Affibody, used in various techniques. Bioz Stars score: 84/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Affibody anti egfr binding affibody zegfr
    PET images, summed 30–60 min, and TACs from a Balbc nu/nu mouse (prone) bearing tumors ( white arrows ): a one A431 xenograft (1 × 10 7 cells, 15 days) or b two A431 xenografts ( left : 1 × 10 7 cells, 28 days; right : 1 × 10 7 cells, 25 days). Comparison A shows a 7-times higher uptake with targeting [methyl- 11 C]-Z <t>EGFR:2377</t> -ST-CH 3 compared to the non-targeting [methyl- 11 C]-Z Taq:3638 -ST-CH 3 . Comparison B illustrates uptake of the targeting <t>Affibody</t> increasing as the tumors grow from time from inoculation
    Anti Egfr Binding Affibody Zegfr, supplied by Affibody, used in various techniques. Bioz Stars score: 91/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Affibody compact egfr binding affibody zegfr
    Modular capacity of probes for labeling <t>EGFR</t> on the cell surface. (A) Structures of the fluorogens used. The synthetic and analytical details were shown in Supporting Information or described previously. 26 A431 cell labeled with <t>FAP–affibody</t> fusions and various malachite green derivatives were analyzed by flow cytometry (B) and live-cell fluorescence microscopy (C). 5 × 10 5 /mL of cells were labeled with 250 nM of AFA or F followed by incubation with 100 nM of fluorogens for 5 min. Cells were then either analyzed by flow cytometry for mean fluorescence measurement or cell imaging. Scale bar 20 μm.
    Compact Egfr Binding Affibody Zegfr, supplied by Affibody, used in various techniques. Bioz Stars score: 88/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Affibody dimeric egfr binding affibody
    Modular capacity of probes for labeling <t>EGFR</t> on the cell surface. (A) Structures of the fluorogens used. The synthetic and analytical details were shown in Supporting Information or described previously. 26 A431 cell labeled with <t>FAP–affibody</t> fusions and various malachite green derivatives were analyzed by flow cytometry (B) and live-cell fluorescence microscopy (C). 5 × 10 5 /mL of cells were labeled with 250 nM of AFA or F followed by incubation with 100 nM of fluorogens for 5 min. Cells were then either analyzed by flow cytometry for mean fluorescence measurement or cell imaging. Scale bar 20 μm.
    Dimeric Egfr Binding Affibody, supplied by Affibody, used in various techniques. Bioz Stars score: 85/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Specificity of 89 Zr-DFO-ZEGFR:2377 uptake in A431 xenografts and EGFR-expressing organs in mice at 3 h after injection. In the blocked group, receptors were saturated by pre-injection of large excess of non-labelled affibody molecules.

    Journal: International Journal of Oncology

    Article Title: PET imaging of epidermal growth factor receptor expression in tumours using 89Zr-labelled ZEGFR:2377 affibody molecules

    doi: 10.3892/ijo.2016.3369

    Figure Lengend Snippet: Specificity of 89 Zr-DFO-ZEGFR:2377 uptake in A431 xenografts and EGFR-expressing organs in mice at 3 h after injection. In the blocked group, receptors were saturated by pre-injection of large excess of non-labelled affibody molecules.

    Article Snippet: In the present study, an EGFR-binding affibody molecule (ZEGFR:2377) was site-specifically conjugated with a deferoxamine (DFO) chelator and labelled under mild conditions (room temperature and neutral pH) with a positron-emitting radionuclide 89 Zr.

    Techniques: Expressing, Mouse Assay, Injection

    (A) Denaturing polyacrylamide gel electrophoresis (SDS-PAGE) showing photo-cross-linking products of the affibody as indicated. All samples were treated with PNGase to degloycosylate and visualize EGFR extracellular domain (∼70 kDa) as a distinct band. Each sample contained both an affibody and EGFR fragment unless otherwise indicated. Note that only the N23BP mutant gave a photoproduct, which corresponded to a mass increase of 10 kDa. Ladder proteins are (top to bottom) 100, 75, and 50 kDa. (B) N23BP and EGFR mixed as in (A) or with the equimolar concentration (260 nM) bovine serum albumin (BSA) as indicated and irradiated for the time listed. A band corresponding to the EGFR-affibody conjugate appears at 5, 15, and 30 min (red arrows). Ladder proteins are (top to bottom) 100, 75, and 50 kDa.

    Journal: Journal of the American Chemical Society

    Article Title: Anti-EGFR Affibodies with Site-Specific Photo-Cross-Linker Incorporation Show Both Directed Target-Specific Photoconjugation and Increased Retention in Tumors

    doi: 10.1021/jacs.8b07601

    Figure Lengend Snippet: (A) Denaturing polyacrylamide gel electrophoresis (SDS-PAGE) showing photo-cross-linking products of the affibody as indicated. All samples were treated with PNGase to degloycosylate and visualize EGFR extracellular domain (∼70 kDa) as a distinct band. Each sample contained both an affibody and EGFR fragment unless otherwise indicated. Note that only the N23BP mutant gave a photoproduct, which corresponded to a mass increase of 10 kDa. Ladder proteins are (top to bottom) 100, 75, and 50 kDa. (B) N23BP and EGFR mixed as in (A) or with the equimolar concentration (260 nM) bovine serum albumin (BSA) as indicated and irradiated for the time listed. A band corresponding to the EGFR-affibody conjugate appears at 5, 15, and 30 min (red arrows). Ladder proteins are (top to bottom) 100, 75, and 50 kDa.

    Article Snippet: The coding sequence for the EGFR binding affibody designated as ZEGFR:1907 or the nonbinding parent Z domain was synthesized by Integrated DNA Technologies and ligated into the pET21b+ vector, attaching an N-terminal T7 epitope tag and C-terminal 6xHis tag.

    Techniques: Polyacrylamide Gel Electrophoresis, SDS Page, Mutagenesis, Concentration Assay, Irradiation

    (A) Denaturing polyacrylamide gel electrophoresis (SDS-PAGE) showing photo-cross-linking products of either N23BP or WT to EGFR, with or without irradiation at 980 nm. Note that only 980 nm irradiation of N23BP produced a photoproduct significantly different than free EGFR (right lane). Ladder proteins are (top to bottom) 100, 75, and 50 kDa. (B) Retention of fluorescently labeled affibodies (left, N23BP; right, WT) in 3D tumor spheroids grown from transfected 4T1 cells either induced with 15 μ g/mL cumate. Concentrations of retained affibodies were calculated by comparing spheroid lysate fluorescence to standard curves prepared for each labeled affibody. “20 IR” designates that this sample was irradiated at 980 nm after 3 h incubation, then left to grow to a total of 20 h. Lanes without an IR designation were not irradiated.

    Journal: Journal of the American Chemical Society

    Article Title: Anti-EGFR Affibodies with Site-Specific Photo-Cross-Linker Incorporation Show Both Directed Target-Specific Photoconjugation and Increased Retention in Tumors

    doi: 10.1021/jacs.8b07601

    Figure Lengend Snippet: (A) Denaturing polyacrylamide gel electrophoresis (SDS-PAGE) showing photo-cross-linking products of either N23BP or WT to EGFR, with or without irradiation at 980 nm. Note that only 980 nm irradiation of N23BP produced a photoproduct significantly different than free EGFR (right lane). Ladder proteins are (top to bottom) 100, 75, and 50 kDa. (B) Retention of fluorescently labeled affibodies (left, N23BP; right, WT) in 3D tumor spheroids grown from transfected 4T1 cells either induced with 15 μ g/mL cumate. Concentrations of retained affibodies were calculated by comparing spheroid lysate fluorescence to standard curves prepared for each labeled affibody. “20 IR” designates that this sample was irradiated at 980 nm after 3 h incubation, then left to grow to a total of 20 h. Lanes without an IR designation were not irradiated.

    Article Snippet: The coding sequence for the EGFR binding affibody designated as ZEGFR:1907 or the nonbinding parent Z domain was synthesized by Integrated DNA Technologies and ligated into the pET21b+ vector, attaching an N-terminal T7 epitope tag and C-terminal 6xHis tag.

    Techniques: Polyacrylamide Gel Electrophoresis, SDS Page, Irradiation, Produced, Labeling, Transfection, Fluorescence, Incubation

    Left: Spheroids were treated with 1 μ M N23BP (top) or WT (bottom) affibody for a total of 4 h (left column) and 20 h (middle and right columns) and additionally irradiated with 365 nm light for 30 min after 3.5 h incubation (right column). These spheroids were sectioned at approximately the same depth and imaged for Rhodamine and GFP distribution. Micrographs show Rhodamine signal within each section normalized by the average GFP intensity. Scale bars are 200 μ m. Right: Five spheroids were grown and irradiated for 1 h with the indicated N23BP affibody concentration in growth media. Affibody containing media was removed, and spheroids were lysed and loaded onto a PAGE gel and probed for affibody conjugates using an anti-T7 antibody. High molecular weight bands around the expected molecular weight of EGFR were observed only when the spheroid-affibody mixtures were irradiated, indicating photo-cross-linking.

    Journal: Journal of the American Chemical Society

    Article Title: Anti-EGFR Affibodies with Site-Specific Photo-Cross-Linker Incorporation Show Both Directed Target-Specific Photoconjugation and Increased Retention in Tumors

    doi: 10.1021/jacs.8b07601

    Figure Lengend Snippet: Left: Spheroids were treated with 1 μ M N23BP (top) or WT (bottom) affibody for a total of 4 h (left column) and 20 h (middle and right columns) and additionally irradiated with 365 nm light for 30 min after 3.5 h incubation (right column). These spheroids were sectioned at approximately the same depth and imaged for Rhodamine and GFP distribution. Micrographs show Rhodamine signal within each section normalized by the average GFP intensity. Scale bars are 200 μ m. Right: Five spheroids were grown and irradiated for 1 h with the indicated N23BP affibody concentration in growth media. Affibody containing media was removed, and spheroids were lysed and loaded onto a PAGE gel and probed for affibody conjugates using an anti-T7 antibody. High molecular weight bands around the expected molecular weight of EGFR were observed only when the spheroid-affibody mixtures were irradiated, indicating photo-cross-linking.

    Article Snippet: The coding sequence for the EGFR binding affibody designated as ZEGFR:1907 or the nonbinding parent Z domain was synthesized by Integrated DNA Technologies and ligated into the pET21b+ vector, attaching an N-terminal T7 epitope tag and C-terminal 6xHis tag.

    Techniques: Irradiation, Incubation, Concentration Assay, Polyacrylamide Gel Electrophoresis, Molecular Weight

    PET images, summed 30–60 min, and TACs from a Balbc nu/nu mouse (prone) bearing tumors ( white arrows ): a one A431 xenograft (1 × 10 7 cells, 15 days) or b two A431 xenografts ( left : 1 × 10 7 cells, 28 days; right : 1 × 10 7 cells, 25 days). Comparison A shows a 7-times higher uptake with targeting [methyl- 11 C]-Z EGFR:2377 -ST-CH 3 compared to the non-targeting [methyl- 11 C]-Z Taq:3638 -ST-CH 3 . Comparison B illustrates uptake of the targeting Affibody increasing as the tumors grow from time from inoculation

    Journal: EJNMMI Research

    Article Title: Preclinical PET imaging of EGFR levels: pairing a targeting with a non-targeting Sel-tagged Affibody-based tracer to estimate the specific uptake

    doi: 10.1186/s13550-016-0213-8

    Figure Lengend Snippet: PET images, summed 30–60 min, and TACs from a Balbc nu/nu mouse (prone) bearing tumors ( white arrows ): a one A431 xenograft (1 × 10 7 cells, 15 days) or b two A431 xenografts ( left : 1 × 10 7 cells, 28 days; right : 1 × 10 7 cells, 25 days). Comparison A shows a 7-times higher uptake with targeting [methyl- 11 C]-Z EGFR:2377 -ST-CH 3 compared to the non-targeting [methyl- 11 C]-Z Taq:3638 -ST-CH 3 . Comparison B illustrates uptake of the targeting Affibody increasing as the tumors grow from time from inoculation

    Article Snippet: The EGFR-binding Affibody molecule ZEGFR:2377 and its size-matched non-binding control ZTaq:3638 were recombinantly fused with a C-terminal selenocysteine-containing Sel-tag (ZEGFR:2377 -ST and ZTaq:3638 -ST).

    Techniques: Positron Emission Tomography

    PET images, summed 30–60 min, and TACs from a SCID mouse (prone) bearing tumors ( white arrows ): a one FaDu xenograft (1 × 10 6 cells, 12 days) or b two FaDu xenografts ( left : (1 × 10 6 cells, 12 days); right : (0.5 × 10 6 cells, 12 days). Comparison A illustrates the higher uptake with targeting [methyl- 11 C]-Z EGFR:2377 -ST-CH 3 but with a ≈60 % non-targeting uptake of [methyl- 11 C]-Z Taq:3638 -ST-CH 3 . Comparison B illustrates the visually discernable heterogeneous uptake of the targeting Affibody in the larger tumor on the left. SUV mean is affected by whether the entire (1) or only central ROI (2) of the left tumor is used

    Journal: EJNMMI Research

    Article Title: Preclinical PET imaging of EGFR levels: pairing a targeting with a non-targeting Sel-tagged Affibody-based tracer to estimate the specific uptake

    doi: 10.1186/s13550-016-0213-8

    Figure Lengend Snippet: PET images, summed 30–60 min, and TACs from a SCID mouse (prone) bearing tumors ( white arrows ): a one FaDu xenograft (1 × 10 6 cells, 12 days) or b two FaDu xenografts ( left : (1 × 10 6 cells, 12 days); right : (0.5 × 10 6 cells, 12 days). Comparison A illustrates the higher uptake with targeting [methyl- 11 C]-Z EGFR:2377 -ST-CH 3 but with a ≈60 % non-targeting uptake of [methyl- 11 C]-Z Taq:3638 -ST-CH 3 . Comparison B illustrates the visually discernable heterogeneous uptake of the targeting Affibody in the larger tumor on the left. SUV mean is affected by whether the entire (1) or only central ROI (2) of the left tumor is used

    Article Snippet: The EGFR-binding Affibody molecule ZEGFR:2377 and its size-matched non-binding control ZTaq:3638 were recombinantly fused with a C-terminal selenocysteine-containing Sel-tag (ZEGFR:2377 -ST and ZTaq:3638 -ST).

    Techniques: Positron Emission Tomography

    Modular capacity of probes for labeling EGFR on the cell surface. (A) Structures of the fluorogens used. The synthetic and analytical details were shown in Supporting Information or described previously. 26 A431 cell labeled with FAP–affibody fusions and various malachite green derivatives were analyzed by flow cytometry (B) and live-cell fluorescence microscopy (C). 5 × 10 5 /mL of cells were labeled with 250 nM of AFA or F followed by incubation with 100 nM of fluorogens for 5 min. Cells were then either analyzed by flow cytometry for mean fluorescence measurement or cell imaging. Scale bar 20 μm.

    Journal: Bioconjugate Chemistry

    Article Title: Fluorogen Activating Protein–Affibody Probes: Modular, No-Wash Measurement of Epidermal Growth Factor Receptors

    doi: 10.1021/bc500525b

    Figure Lengend Snippet: Modular capacity of probes for labeling EGFR on the cell surface. (A) Structures of the fluorogens used. The synthetic and analytical details were shown in Supporting Information or described previously. 26 A431 cell labeled with FAP–affibody fusions and various malachite green derivatives were analyzed by flow cytometry (B) and live-cell fluorescence microscopy (C). 5 × 10 5 /mL of cells were labeled with 250 nM of AFA or F followed by incubation with 100 nM of fluorogens for 5 min. Cells were then either analyzed by flow cytometry for mean fluorescence measurement or cell imaging. Scale bar 20 μm.

    Article Snippet: A protein domain (FAP dL5** ) that binds to malachite-green (MG) derivatives for fluorescence activation was expressed as a recombinant fusion to one or two copies of the compact EGFR binding affibody ZEGFR:1907 .

    Techniques: Labeling, Flow Cytometry, Cytometry, Fluorescence, Microscopy, Incubation, Imaging

    Characterization of probes binding on A431 cell surface. (A) Dissociation constant analysis of probes on cell surface. 5 × 10 5 /mL quantities of cells were incubated with probes for 1 h at 37 °C followed by 2 μM MG-B-tau for 5 min. Then cells were kept on ice for flow cytometry. The mean fluorescence intensity was corrected with background of cells incubating with F/MG and then normalized to mean fluorescence at 250 nM of probes. (B) Competition assay of nonfluorescent affibody A binding to the cell surface. Cells were labeled with 250 nM AFA or F and a serial dilution of A followed by 100 nM of MG-B-tau added prior to measurement. (C) Detection of receptor activation by Western blots. Starved cells were labeled with 250 nM probes followed by 100 nM of MG-B-tau and then cells were treated with 100 ng/mL EGF. Then cells were lysed for Western blot in order to detect phosphorylated EGFR and total EGFR. (D) Live-cell fluorescence microscopy of A431 cells labeled by various probes. Cells were labeled with 250 nM of probe and 100 nM of MG-B-tau prior to imaging or 100 nM of Cy5 conjugated affibody dimer. Scale bar 20 μm.

    Journal: Bioconjugate Chemistry

    Article Title: Fluorogen Activating Protein–Affibody Probes: Modular, No-Wash Measurement of Epidermal Growth Factor Receptors

    doi: 10.1021/bc500525b

    Figure Lengend Snippet: Characterization of probes binding on A431 cell surface. (A) Dissociation constant analysis of probes on cell surface. 5 × 10 5 /mL quantities of cells were incubated with probes for 1 h at 37 °C followed by 2 μM MG-B-tau for 5 min. Then cells were kept on ice for flow cytometry. The mean fluorescence intensity was corrected with background of cells incubating with F/MG and then normalized to mean fluorescence at 250 nM of probes. (B) Competition assay of nonfluorescent affibody A binding to the cell surface. Cells were labeled with 250 nM AFA or F and a serial dilution of A followed by 100 nM of MG-B-tau added prior to measurement. (C) Detection of receptor activation by Western blots. Starved cells were labeled with 250 nM probes followed by 100 nM of MG-B-tau and then cells were treated with 100 ng/mL EGF. Then cells were lysed for Western blot in order to detect phosphorylated EGFR and total EGFR. (D) Live-cell fluorescence microscopy of A431 cells labeled by various probes. Cells were labeled with 250 nM of probe and 100 nM of MG-B-tau prior to imaging or 100 nM of Cy5 conjugated affibody dimer. Scale bar 20 μm.

    Article Snippet: A protein domain (FAP dL5** ) that binds to malachite-green (MG) derivatives for fluorescence activation was expressed as a recombinant fusion to one or two copies of the compact EGFR binding affibody ZEGFR:1907 .

    Techniques: Binding Assay, Incubation, Flow Cytometry, Cytometry, Fluorescence, Competitive Binding Assay, Labeling, Serial Dilution, Activation Assay, Western Blot, Microscopy, Imaging