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ACROBiosystems recombinant human egfr- his protein
Recombinant Human Egfr His Protein, supplied by ACROBiosystems, 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 egfr- his protein/product/ACROBiosystems
Average 90 stars, based on 1 article reviews
recombinant human egfr- his protein - by Bioz Stars, 2026-02
90/100 stars

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(A) shows the ELISA signal (reflecting <t>EGFR</t> binding) normalized by nanoparticle concentration. Both C225 and VHH-122 have high binding, while PEG has almost none. Differences in binding between all three nanoparticle types are statistically significant. (B) shows the ELISA signal normalized by antibody concentration. Here, C225 has much higher signal than VHH-122, consistent with its higher binding affinity and lower number of antibodies per nanoparticle.
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(A) shows the ELISA signal (reflecting <t>EGFR</t> binding) normalized by nanoparticle concentration. Both C225 and VHH-122 have high binding, while PEG has almost none. Differences in binding between all three nanoparticle types are statistically significant. (B) shows the ELISA signal normalized by antibody concentration. Here, C225 has much higher signal than VHH-122, consistent with its higher binding affinity and lower number of antibodies per nanoparticle.
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(A) shows the ELISA signal (reflecting EGFR binding) normalized by nanoparticle concentration. Both C225 and VHH-122 have high binding, while PEG has almost none. Differences in binding between all three nanoparticle types are statistically significant. (B) shows the ELISA signal normalized by antibody concentration. Here, C225 has much higher signal than VHH-122, consistent with its higher binding affinity and lower number of antibodies per nanoparticle.

Journal: PLoS ONE

Article Title: A comparative analysis of EGFR-targeting antibodies for gold nanoparticle CT imaging of lung cancer

doi: 10.1371/journal.pone.0206950

Figure Lengend Snippet: (A) shows the ELISA signal (reflecting EGFR binding) normalized by nanoparticle concentration. Both C225 and VHH-122 have high binding, while PEG has almost none. Differences in binding between all three nanoparticle types are statistically significant. (B) shows the ELISA signal normalized by antibody concentration. Here, C225 has much higher signal than VHH-122, consistent with its higher binding affinity and lower number of antibodies per nanoparticle.

Article Snippet: Antibody-conjugated AuNPs were blocked with 10% donkey serum in PBS, then incubated with a soluble recombinant human EGFR extracellular domain-Fc chimera (Sino Biological) at 10 nM in blocking buffer for 2 hours.

Techniques: Enzyme-linked Immunosorbent Assay, Binding Assay, Concentration Assay

AuNPs appear as bright yellow-orange dots in the dark field images. PEG-AuNPs (A) showed little to no cell binding, VHH-AuNPs (B) showed a moderate level of cell binding, while C225-AuNPs (C) had a high number of nanoparticles bound to the cells in culture. This demonstrates effective EGFR-targeting, particularly for the C225-AuNPs. Scale bars are 30 μ m.

Journal: PLoS ONE

Article Title: A comparative analysis of EGFR-targeting antibodies for gold nanoparticle CT imaging of lung cancer

doi: 10.1371/journal.pone.0206950

Figure Lengend Snippet: AuNPs appear as bright yellow-orange dots in the dark field images. PEG-AuNPs (A) showed little to no cell binding, VHH-AuNPs (B) showed a moderate level of cell binding, while C225-AuNPs (C) had a high number of nanoparticles bound to the cells in culture. This demonstrates effective EGFR-targeting, particularly for the C225-AuNPs. Scale bars are 30 μ m.

Article Snippet: Antibody-conjugated AuNPs were blocked with 10% donkey serum in PBS, then incubated with a soluble recombinant human EGFR extracellular domain-Fc chimera (Sino Biological) at 10 nM in blocking buffer for 2 hours.

Techniques: Binding Assay