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R&D Systems mouse egfr fc chimera protein

Figure 1. Cell labeling efficiency of the bispecific B10–B11 Nanofitin and its cytotoxic effect on the A431 on tumor cell line. (A) Cell labeling efficiency evaluation by flow cytometry of B10, B11, and bispecific <t>B10–B11</t> <t>Nanofitins</t> on A431 cell line. Dotted lines represent alignment with the isotype control. (B) Expression level of programmed death-ligand 1 (PD-L1) (left) and Epithelial Growth Factor Receptor <t>(EGFR)</t> (right) on the A431 cell line. In grey: isotype control; in black: anti-PD-L1 or anti-EGFR antibody. (C) The real-time proliferation of A431 cells co-cultured with Jurkat cells exhibiting background activity. In black: A431 cells co-cultured with a mix of Jurkat cells and anti-EpCAM x CD3 BiTE without Nanofitin treatment; in red: A431 cells co-cultured with a mix of Jurkat cells and anti-EpCAM x CD3 BiTE and treated by the B11 Nanofitin (10 µM); in purple: A431 cells co-cultured with a mix of Jurkat cells and anti-EpCAM x CD3 BiTE and treated by the B10–B11 Nanofitin (10 µM). Significance was assessed by two-way ANOVA using 6 Prism software (GraphPad). **** p < 0.0001 (n = 3). (D) The real-time proliferation of A431 cells. In black: A431 cells alone; in red: A431 cells treated by the B11 Nanofitin (10 µM); in purple: A431 cells treated by the B10–B11 Nanofitin (10 µM). Significance was assessed by two-way ANOVA using 6 Prism software (GraphPad). NS: not significant (n = 3).

Mouse Egfr Fc Chimera Protein, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 4 article reviews

mouse egfr fc chimera protein - by Bioz Stars, 2026-07

93/100 stars

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1) Product Images from "A Multispecific Checkpoint Inhibitor Nanofitin with a Fast Tumor Accumulation Property and Anti-Tumor Activity in Immune Competent Mice."

Article Title: A Multispecific Checkpoint Inhibitor Nanofitin with a Fast Tumor Accumulation Property and Anti-Tumor Activity in Immune Competent Mice.

Journal: Biomolecules

doi: 10.3390/biom15040471

Figure Legend Snippet: Figure 1. Cell labeling efficiency of the bispecific B10–B11 Nanofitin and its cytotoxic effect on the A431 on tumor cell line. (A) Cell labeling efficiency evaluation by flow cytometry of B10, B11, and bispecific B10–B11 Nanofitins on A431 cell line. Dotted lines represent alignment with the isotype control. (B) Expression level of programmed death-ligand 1 (PD-L1) (left) and Epithelial Growth Factor Receptor (EGFR) (right) on the A431 cell line. In grey: isotype control; in black: anti-PD-L1 or anti-EGFR antibody. (C) The real-time proliferation of A431 cells co-cultured with Jurkat cells exhibiting background activity. In black: A431 cells co-cultured with a mix of Jurkat cells and anti-EpCAM x CD3 BiTE without Nanofitin treatment; in red: A431 cells co-cultured with a mix of Jurkat cells and anti-EpCAM x CD3 BiTE and treated by the B11 Nanofitin (10 µM); in purple: A431 cells co-cultured with a mix of Jurkat cells and anti-EpCAM x CD3 BiTE and treated by the B10–B11 Nanofitin (10 µM). Significance was assessed by two-way ANOVA using 6 Prism software (GraphPad). **** p < 0.0001 (n = 3). (D) The real-time proliferation of A431 cells. In black: A431 cells alone; in red: A431 cells treated by the B11 Nanofitin (10 µM); in purple: A431 cells treated by the B10–B11 Nanofitin (10 µM). Significance was assessed by two-way ANOVA using 6 Prism software (GraphPad). NS: not significant (n = 3).

Techniques Used: Labeling, Flow Cytometry, Control, Expressing, Cell Culture, Activity Assay, Software

Figure 3. Mouse cross-reactivity of the bispecific B10–B11 Nanofitin. (A) Expression level of PD-L1 (left) and EGFR (right) on CT26 cell line. In grey: isotype control; in black: anti-PD-L1 or EGFR antibody. (B) Biolayer interferometry sensorgrams and binding kinetic parameters of monomeric B10 and B11 Nanofitins and bispecific B10–B11 Nanofitin on mouse EGFR and PD-L1. Fittings (1:1 model) are represented as solid gray lines. (C) CT26 cell labeling efficiency evaluation by flow cytometry of monomeric B10 and B11 and bispecific B10–B11 Nanofitins. Dotted lines represent alignment with the isotype control.

Figure Legend Snippet: Figure 3. Mouse cross-reactivity of the bispecific B10–B11 Nanofitin. (A) Expression level of PD-L1 (left) and EGFR (right) on CT26 cell line. In grey: isotype control; in black: anti-PD-L1 or EGFR antibody. (B) Biolayer interferometry sensorgrams and binding kinetic parameters of monomeric B10 and B11 Nanofitins and bispecific B10–B11 Nanofitin on mouse EGFR and PD-L1. Fittings (1:1 model) are represented as solid gray lines. (C) CT26 cell labeling efficiency evaluation by flow cytometry of monomeric B10 and B11 and bispecific B10–B11 Nanofitins. Dotted lines represent alignment with the isotype control.

Techniques Used: Expressing, Control, Binding Assay, Labeling, Flow Cytometry

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Journal: Biomolecules

Article Title: A Multispecific Checkpoint Inhibitor Nanofitin with a Fast Tumor Accumulation Property and Anti-Tumor Activity in Immune Competent Mice.

doi: 10.3390/biom15040471

Figure Lengend Snippet: Figure 1. Cell labeling efficiency of the bispecific B10–B11 Nanofitin and its cytotoxic effect on the A431 on tumor cell line. (A) Cell labeling efficiency evaluation by flow cytometry of B10, B11, and bispecific B10–B11 Nanofitins on A431 cell line. Dotted lines represent alignment with the isotype control. (B) Expression level of programmed death-ligand 1 (PD-L1) (left) and Epithelial Growth Factor Receptor (EGFR) (right) on the A431 cell line. In grey: isotype control; in black: anti-PD-L1 or anti-EGFR antibody. (C) The real-time proliferation of A431 cells co-cultured with Jurkat cells exhibiting background activity. In black: A431 cells co-cultured with a mix of Jurkat cells and anti-EpCAM x CD3 BiTE without Nanofitin treatment; in red: A431 cells co-cultured with a mix of Jurkat cells and anti-EpCAM x CD3 BiTE and treated by the B11 Nanofitin (10 µM); in purple: A431 cells co-cultured with a mix of Jurkat cells and anti-EpCAM x CD3 BiTE and treated by the B10–B11 Nanofitin (10 µM). Significance was assessed by two-way ANOVA using 6 Prism software (GraphPad). **** p < 0.0001 (n = 3). (D) The real-time proliferation of A431 cells. In black: A431 cells alone; in red: A431 cells treated by the B11 Nanofitin (10 µM); in purple: A431 cells treated by the B10–B11 Nanofitin (10 µM). Significance was assessed by two-way ANOVA using 6 Prism software (GraphPad). NS: not significant (n = 3).

Article Snippet: The binding kinetic parameters of Nanofitins were defined by loading of 10 μg/mL mouse EGFR Fc chimera protein (#1280-ER-050, R&D Systems, Minneapolis, MN, USA) and 5 μg/mL recombinant mouse PDL1/B7-H1 Fc chimera protein (#1019-B7-100, R&D Systems) at 2 nm on protein A biosensors (#18-5012, Sartorius).

Techniques: Labeling, Flow Cytometry, Control, Expressing, Cell Culture, Activity Assay, Software

Journal: Biomolecules

Article Title: A Multispecific Checkpoint Inhibitor Nanofitin with a Fast Tumor Accumulation Property and Anti-Tumor Activity in Immune Competent Mice.

doi: 10.3390/biom15040471

Figure Lengend Snippet: Figure 3. Mouse cross-reactivity of the bispecific B10–B11 Nanofitin. (A) Expression level of PD-L1 (left) and EGFR (right) on CT26 cell line. In grey: isotype control; in black: anti-PD-L1 or EGFR antibody. (B) Biolayer interferometry sensorgrams and binding kinetic parameters of monomeric B10 and B11 Nanofitins and bispecific B10–B11 Nanofitin on mouse EGFR and PD-L1. Fittings (1:1 model) are represented as solid gray lines. (C) CT26 cell labeling efficiency evaluation by flow cytometry of monomeric B10 and B11 and bispecific B10–B11 Nanofitins. Dotted lines represent alignment with the isotype control.

Techniques: Expressing, Control, Binding Assay, Labeling, Flow Cytometry

Figure 1. Discovery of allosteric antibodies. A: workflow overview. After camelid immunization with rhEGFR (1), a yeast surface display library was generated (2) and subsequently incubated with EGFR and EGF fc and their respective detection antibodies (3). Non-egf-competitive binders were selected via FACS using a three-color staining strategy (4), reformatted as heavy-chain antibodies (5) and expressed in mammalian cells (6). Antibodies were characterized using various biochemical and functional assays (7). Created with BioRender.com. B: FACS-based selection of non-egf-competitive antibodies. A three-color based sorting approach was applied, first a two-dimensional gate to identify functional VHH display in combination to EGFR binding (upper panel). Then, a second two-dimensional gate was applied to select EGFR binders that did not compete with EGF fc (lower panel). For the final round a more stringent sorting gate was designed to select antibodies that were better negatively modulating EGFR affinity for EGF fc. Applied sorting gates and corresponding cell population (as % of total cells) are shown. Plots were generated using FlowJo. C: sequence homology of egfr-binders. Green bars highlight 100% sequence identity at a particular residue, olive bars indicate an intermediate sequence conservation, and red bars represent a high sequence diversity. Alignment generated with geneious prime.

Journal: mAbs

Article Title: Discovery of potent allosteric antibodies inhibiting EGFR.

doi: 10.1080/19420862.2024.2406548

Figure Lengend Snippet: Figure 1. Discovery of allosteric antibodies. A: workflow overview. After camelid immunization with rhEGFR (1), a yeast surface display library was generated (2) and subsequently incubated with EGFR and EGF fc and their respective detection antibodies (3). Non-egf-competitive binders were selected via FACS using a three-color staining strategy (4), reformatted as heavy-chain antibodies (5) and expressed in mammalian cells (6). Antibodies were characterized using various biochemical and functional assays (7). Created with BioRender.com. B: FACS-based selection of non-egf-competitive antibodies. A three-color based sorting approach was applied, first a two-dimensional gate to identify functional VHH display in combination to EGFR binding (upper panel). Then, a second two-dimensional gate was applied to select EGFR binders that did not compete with EGF fc (lower panel). For the final round a more stringent sorting gate was designed to select antibodies that were better negatively modulating EGFR affinity for EGF fc. Applied sorting gates and corresponding cell population (as % of total cells) are shown. Plots were generated using FlowJo. C: sequence homology of egfr-binders. Green bars highlight 100% sequence identity at a particular residue, olive bars indicate an intermediate sequence conservation, and red bars represent a high sequence diversity. Alignment generated with geneious prime.

Article Snippet: Lastly, cross reactivity binding assays were performed using rhHER2 (Sino Biological 10,004- H08H), rhHER3 (10368-RB-050), rhHER4 (1131-ER-050), recombinant cynomolgus monkey EGFR (10405-ER-050) and recombinant mouse EGFR (1280-ER-050) all from R&D Systems.

Techniques: Generated, Incubation, Staining, Functional Assay, Selection, Binding Assay, Sequencing, Residue

Figure 2. Impact of antibodies on EGFR:EGF equilibrium determined by fluorescence polarization. Atto-488 labeled EGF (100 nM) was incubated with EGFR (400 nM) until equilibrium. Subsequently, antibodies were added. Cetuximab was used a control as it fully competes with EGF. Fluorescence polarization values were monitored using a plate reader with adequate FP module. Graphs show means ± SD. The experiment was run twice in duplicate, data shown for one representative experiment.

Journal: mAbs

Article Title: Discovery of potent allosteric antibodies inhibiting EGFR.

doi: 10.1080/19420862.2024.2406548

Figure Lengend Snippet: Figure 2. Impact of antibodies on EGFR:EGF equilibrium determined by fluorescence polarization. Atto-488 labeled EGF (100 nM) was incubated with EGFR (400 nM) until equilibrium. Subsequently, antibodies were added. Cetuximab was used a control as it fully competes with EGF. Fluorescence polarization values were monitored using a plate reader with adequate FP module. Graphs show means ± SD. The experiment was run twice in duplicate, data shown for one representative experiment.

Techniques: Fluorescence, Labeling, Incubation, Control

Figure 3. Functional assays on triple-negative egfr-expressing breast cancer cells (MDA-MB-468). a: cellular binding of antibodies on cells detected by secondary- labeled detection antibody and recorded by FACS. The experiment was run twice in duplicate, data shown for one representative experiment. Graphs show means ± SD. b. EC50 values were determined after data fitting on GraphPad prism. c: displacement of bEGF affinity by anti-egfr antibodies. The experiment was run twice in duplicate, data shown for one representative experiment. Graphs show normalized means ± SD. d IC50 and EC50 values were determined after data fitting on GraphPad prism.

Journal: mAbs

Article Title: Discovery of potent allosteric antibodies inhibiting EGFR.

doi: 10.1080/19420862.2024.2406548

Figure Lengend Snippet: Figure 3. Functional assays on triple-negative egfr-expressing breast cancer cells (MDA-MB-468). a: cellular binding of antibodies on cells detected by secondary- labeled detection antibody and recorded by FACS. The experiment was run twice in duplicate, data shown for one representative experiment. Graphs show means ± SD. b. EC50 values were determined after data fitting on GraphPad prism. c: displacement of bEGF affinity by anti-egfr antibodies. The experiment was run twice in duplicate, data shown for one representative experiment. Graphs show normalized means ± SD. d IC50 and EC50 values were determined after data fitting on GraphPad prism.

Techniques: Functional Assay, Expressing, Binding Assay, Labeling

Figure 4. Inhibition of egf-induced MAPK/ERK and PI3K/AKT pathways by anti-egfr antibodies. a: inhibition of MAPK/ERK pathway using BPS bioscience reporter cells. Cells were seeded, after adherence and overnight serum starvation, incubated with the respective antibodies for 24 h. Cells were stimulated with EGF at its EC80 for 6 h before reading of luminescence via a plate reader. Graphs show normalized means ± SD. The experiment was run three times in duplicate, data shown for one representative experiment (left panel). b: IC50 values were obtained after data fitting on GraphPad software (right panel). c: inhibition of PI3K/AKT pathway using HTRF kit from revvity to monitor AKT phosphorylation. After seeding of MDA-MB-468 cells, adherence and overnight serum-starvation, cells were treated with 250 nM of the respective antibodies for 1 h, subsequently cells were activated with 20 ng/mL of EGF for 10 min. Homogeneous time-resolved fluorescence ratio (HTRF ratio) was calculated according to the manufacturer’s instructions as follows: acceptor (665 nm)/donor (620 nm) × 10,000. Graphs show means ± SD. ****p-value < 0.0001. The experiment was run three times in triplicate.

Journal: mAbs

Article Title: Discovery of potent allosteric antibodies inhibiting EGFR.

doi: 10.1080/19420862.2024.2406548

Figure Lengend Snippet: Figure 4. Inhibition of egf-induced MAPK/ERK and PI3K/AKT pathways by anti-egfr antibodies. a: inhibition of MAPK/ERK pathway using BPS bioscience reporter cells. Cells were seeded, after adherence and overnight serum starvation, incubated with the respective antibodies for 24 h. Cells were stimulated with EGF at its EC80 for 6 h before reading of luminescence via a plate reader. Graphs show normalized means ± SD. The experiment was run three times in duplicate, data shown for one representative experiment (left panel). b: IC50 values were obtained after data fitting on GraphPad software (right panel). c: inhibition of PI3K/AKT pathway using HTRF kit from revvity to monitor AKT phosphorylation. After seeding of MDA-MB-468 cells, adherence and overnight serum-starvation, cells were treated with 250 nM of the respective antibodies for 1 h, subsequently cells were activated with 20 ng/mL of EGF for 10 min. Homogeneous time-resolved fluorescence ratio (HTRF ratio) was calculated according to the manufacturer’s instructions as follows: acceptor (665 nm)/donor (620 nm) × 10,000. Graphs show means ± SD. ****p-value < 0.0001. The experiment was run three times in triplicate.

Techniques: Inhibition, Incubation, Software, Phospho-proteomics, Fluorescence

Intratumoral infiltration 90 minutres after systemic administration. A, Intratumoral infiltration of antiEGFR Nanofitins or Cetuximab, revealed by anti-HA and anti-IgG IHC, respectively. Host vasculature is revealed by anti-CD31 staining of consecutive slice sections. Zoom of selected regions illustrates EGFR labeling at the vessel proximity. B, Labeling index, on the basis of cells positively labeled, in the whole tumor. C, Labeling index relative to the distance from the closest blood vessel. ****, P < 0.0001; ***, P < 0.0005.

Journal: Molecular Cancer Therapeutics

Article Title: Targeted Nanofitin-drug Conjugates Achieve Efficient Tumor Delivery and Therapeutic Effect in an EGFR pos Mouse Xenograft Model

doi: 10.1158/1535-7163.MCT-22-0805

Figure Lengend Snippet: Intratumoral infiltration 90 minutres after systemic administration. A, Intratumoral infiltration of antiEGFR Nanofitins or Cetuximab, revealed by anti-HA and anti-IgG IHC, respectively. Host vasculature is revealed by anti-CD31 staining of consecutive slice sections. Zoom of selected regions illustrates EGFR labeling at the vessel proximity. B, Labeling index, on the basis of cells positively labeled, in the whole tumor. C, Labeling index relative to the distance from the closest blood vessel. ****, P < 0.0001; ***, P < 0.0005.

Article Snippet: Affinities were also determined for cysteine-free and HA-tagged ( ) Nanofitins (500, 250, 125, 62.5, 31.25, 15.63, 7.81, and 0 nmol/L), either on human EGFR as described above, or on murine EGFR by using Recombinant Mouse EGFR Fc chimera protein (1280-ER, R&D Systems) for the loading step.

Techniques: Staining, Labeling

Biochemical profiles of Nanofitin-drug conjugates. A, Schematic representation of a Nanofitin-drug conjugate. The single chain of the Nanofitin scaffold (rainbow cartoon) is engineered to target EGFR by randomizing up to 14 amino acids (spheres in lieu of carbon alpha). Each Nanofitin is genetically fused to a C-terminal cysteine (gray/yellow stick) to allow the regioselective chemistry on the only thiol group. The vc-MMAE payload (structural formula) is coupled via its maleimide-based moiety (black) and releases the MMAE toxin (red) after proteolytic cleavage of the valine-citrulline linker (orange). B, UPLC-RP/MS profiles. Peaks were identified by ESI-MS spectral deconvolution to determine their mass. Percentages of corresponding species were determined from the area under the absorbance curves. C, Determination of the binding characteristics of the antiEGFR Nanofitin-drug conjugates D8-vc-MMAE (left) and B10-vc-MMAE (right) by biolayer interferometry on human EGFR, using the antiEGFR Nanofitin at concentrations of 500, 125, 31.25, and 7.81 nmol/L. Fittings are represented as solid red lines.

Journal: Molecular Cancer Therapeutics

Article Title: Targeted Nanofitin-drug Conjugates Achieve Efficient Tumor Delivery and Therapeutic Effect in an EGFR pos Mouse Xenograft Model

doi: 10.1158/1535-7163.MCT-22-0805

Figure Lengend Snippet: Biochemical profiles of Nanofitin-drug conjugates. A, Schematic representation of a Nanofitin-drug conjugate. The single chain of the Nanofitin scaffold (rainbow cartoon) is engineered to target EGFR by randomizing up to 14 amino acids (spheres in lieu of carbon alpha). Each Nanofitin is genetically fused to a C-terminal cysteine (gray/yellow stick) to allow the regioselective chemistry on the only thiol group. The vc-MMAE payload (structural formula) is coupled via its maleimide-based moiety (black) and releases the MMAE toxin (red) after proteolytic cleavage of the valine-citrulline linker (orange). B, UPLC-RP/MS profiles. Peaks were identified by ESI-MS spectral deconvolution to determine their mass. Percentages of corresponding species were determined from the area under the absorbance curves. C, Determination of the binding characteristics of the antiEGFR Nanofitin-drug conjugates D8-vc-MMAE (left) and B10-vc-MMAE (right) by biolayer interferometry on human EGFR, using the antiEGFR Nanofitin at concentrations of 500, 125, 31.25, and 7.81 nmol/L. Fittings are represented as solid red lines.

Techniques: Binding Assay

Affinity determination against human and mouse EGFR.

Journal: Molecular Cancer Therapeutics

Article Title: Targeted Nanofitin-drug Conjugates Achieve Efficient Tumor Delivery and Therapeutic Effect in an EGFR pos Mouse Xenograft Model

doi: 10.1158/1535-7163.MCT-22-0805

Figure Lengend Snippet: Affinity determination against human and mouse EGFR.

Techniques:

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1) Product Images from "A Multispecific Checkpoint Inhibitor Nanofitin with a Fast Tumor Accumulation Property and Anti-Tumor Activity in Immune Competent Mice."

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