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human egfr protein with fc tag  (ACROBiosystems)


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    ACROBiosystems human egfr protein with fc tag
    Human Egfr Protein With Fc Tag, 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/product/human+egfr+protein+with+an+fc+tag/human+egfr/pm40384482-63-4-6
    Average 90 stars, based on 1 article reviews
    human egfr protein with fc tag - by Bioz Stars, 2026-10
    90/100 stars

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    Related Articles

    Blocking Assay:

    Article Title: Discovery and Design of Novel Cyclic Peptides as Specific Inhibitors Targeting CCN2 and Disrupting CCN2/EGFR Interaction for Kidney Fibrosis Treatment.
    Article Snippet: Kidney fibrosis is a serious consequence of chronic kidney disease (CKD), and currently, there is no effective pharmacological treatment available.. Cellular communication network-2 (CCN2/CTGF) is an extracellular matrix (ECM) protein that regulates the fibrotic process by activating the epidermal growth factor receptor (EGFR) signaling pathway.. We herein present the discovery and structure−activity relationship study of novel peptides targeting CCN2 to develop potent and stable specific inhibitors of the CCN2/EGFR interaction.



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    human egfr protein with fc tag  (ACROBiosystems)
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    Human Egfr Protein With Fc Tag, 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
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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 ) EGFRvIII antigen expression level on mutant GBM cell line U87MG.ΔEGFR and wild-type GBM cell line U87MG. ( b ) A binding activity comparison of EGFRvIII-BsAb and CD3 mAb with Jurkat cells (CD3-positive) (upper), as well as a binding activity comparison of the EGFRvIII-BsAb and the EGFRvIII mAb with U87MG.ΔEGFR cells (EGFRvIII-positive) (lower). ( c ) Photographs of the redirection of T cells to cancer cells by 0.01 ng/mL EGFRvIII-BsAb or EGFRvIII mAb. ( d ) FACS analysis of the redirection of CD3+ Jurkat cells to cancer cells by EGFRvIII-BsAb. Jurkat (CD3+) cells labeled by PKH26 (PE-A), as well as U87MG.ΔEGFR cells labeled by CFSE (FITC-A).

    Journal: Biomedicines

    Article Title: A Rational Designed Novel Bispecific Antibody for the Treatment of GBM

    doi: 10.3390/biomedicines9060640

    Figure Lengend Snippet: ( a ) EGFRvIII antigen expression level on mutant GBM cell line U87MG.ΔEGFR and wild-type GBM cell line U87MG. ( b ) A binding activity comparison of EGFRvIII-BsAb and CD3 mAb with Jurkat cells (CD3-positive) (upper), as well as a binding activity comparison of the EGFRvIII-BsAb and the EGFRvIII mAb with U87MG.ΔEGFR cells (EGFRvIII-positive) (lower). ( c ) Photographs of the redirection of T cells to cancer cells by 0.01 ng/mL EGFRvIII-BsAb or EGFRvIII mAb. ( d ) FACS analysis of the redirection of CD3+ Jurkat cells to cancer cells by EGFRvIII-BsAb. Jurkat (CD3+) cells labeled by PKH26 (PE-A), as well as U87MG.ΔEGFR cells labeled by CFSE (FITC-A).

    Article Snippet: The EGFRvIII antigen (AVI10494; R&D System, Minneapolis, MN, USA) and extracellular domain of human CD3D/CD3E heterodimer (CT038-H2508H; Sino Biological, Beijing, China) were immobilized to a CM5 chip (29149603; GE Healthcare, Chicago, IL, USA) surface using standard protocols with 1-ethyl-3 (3-dimethylaminopropyl) carbodiimide (EDC)/N-hydroxysuccinimide (NHS) amine.

    Techniques: Expressing, Mutagenesis, Binding Assay, Activity Assay, Comparison, Labeling

    (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