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GenScript corporation human egfr-fc fusion protein
Human Egfr Fc Fusion Protein, supplied by GenScript corporation, 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/human egfr-fc fusion protein/product/GenScript corporation
Average 90 stars, based on 1 article reviews
human egfr-fc fusion protein - by Bioz Stars, 2026-02
90/100 stars

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R&D Systems human egfr fc fusion protein
Human Egfr Fc Fusion 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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GenScript corporation human egfr-fc fusion protein
Human Egfr Fc Fusion Protein, supplied by GenScript corporation, 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/human egfr-fc fusion protein/product/GenScript corporation
Average 90 stars, based on 1 article reviews
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R&D Systems recombinant egfr fc fusion protein
Recombinant Egfr Fc Fusion 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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R&D Systems pmoles recombinant human egfr fc hegfr fusion protein
The N62 pool and aptamers E03, E04, and E07 were assayed in triplicate by filtration for binding to <t>hEGFR,</t> mEGFR, hErbB2, and hIgG1. Average values and standard deviations are shown. Binding assays were carried out either in the absence (left) or presence (right) of DTT. A no protein control was also carried through the procedure. Percent binding was relative to the total RNA added.
Pmoles Recombinant Human Egfr Fc Hegfr Fusion 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/pmoles recombinant human egfr fc hegfr fusion protein/product/R&D Systems
Average 94 stars, based on 1 article reviews
pmoles recombinant human egfr fc hegfr fusion protein - by Bioz Stars, 2026-02
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The N62 pool and aptamers E03, E04, and E07 were assayed in triplicate by filtration for binding to hEGFR, mEGFR, hErbB2, and hIgG1. Average values and standard deviations are shown. Binding assays were carried out either in the absence (left) or presence (right) of DTT. A no protein control was also carried through the procedure. Percent binding was relative to the total RNA added.

Journal: PLoS ONE

Article Title: Inhibition of Cell Proliferation by an Anti-EGFR Aptamer

doi: 10.1371/journal.pone.0020299

Figure Lengend Snippet: The N62 pool and aptamers E03, E04, and E07 were assayed in triplicate by filtration for binding to hEGFR, mEGFR, hErbB2, and hIgG1. Average values and standard deviations are shown. Binding assays were carried out either in the absence (left) or presence (right) of DTT. A no protein control was also carried through the procedure. Percent binding was relative to the total RNA added.

Article Snippet: About 2 nmoles RNA and 90 pmoles recombinant human EGFR-Fc (hEGFR) fusion protein (R&D Systems, Minneapolis, MN) were used for each round of selection in a reaction volume of 100 μL.

Techniques: Filtration, Binding Assay, Control

Binding isotherms were constructed using 0.1 nM aptamer and varying amounts of hEGFR or mEGFR. Binding assays were carried out in triplicate and the average value and standard deviation are shown. The fact that binding does not reach 100% is a function of the filtration assay, and is commonly observed. Dissociation constants were calculated following curve-fitting, as described in .

Journal: PLoS ONE

Article Title: Inhibition of Cell Proliferation by an Anti-EGFR Aptamer

doi: 10.1371/journal.pone.0020299

Figure Lengend Snippet: Binding isotherms were constructed using 0.1 nM aptamer and varying amounts of hEGFR or mEGFR. Binding assays were carried out in triplicate and the average value and standard deviation are shown. The fact that binding does not reach 100% is a function of the filtration assay, and is commonly observed. Dissociation constants were calculated following curve-fitting, as described in .

Article Snippet: About 2 nmoles RNA and 90 pmoles recombinant human EGFR-Fc (hEGFR) fusion protein (R&D Systems, Minneapolis, MN) were used for each round of selection in a reaction volume of 100 μL.

Techniques: Binding Assay, Construct, Standard Deviation, Filtration