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human ace 2 fc chimera protein  (R&D Systems)


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    Structured Review

    R&D Systems human ace 2 fc chimera protein
    Human Ace 2 Fc Chimera Protein, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human ace 2 fc chimera protein/product/R&D Systems
    Average 93 stars, based on 7 article reviews
    human ace 2 fc chimera protein - by Bioz Stars, 2026-03
    93/100 stars

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    R&D Systems biotinylated recombinant human ace2
    Inhibitory effects of different polyphenols on the interaction between SARS-CoV-2 spike protein receptor binding domain (RBD (N501Y)) and human angiotensin-converting enzyme 2 <t>(ACE2).</t> ( A ) 10 µM of pelargonidin-3-O-glucoside (Pel-3-O-G), malvidin-3-O-glucoside (Mal-3-O-G), cyanidin-3-O-glucoside (Cya-3-O-G), peonidin, tannic acid (TA), 1,3,6-tri-O-galloyl-β-D-glucose (TGG), and corilagin were tested to evaluate their ability to inhibit the binding of immobilized spike protein (0.5 µg/mL) to human, biotin-labeled ACE2 (0.25 µg/mL) by using an enzyme-linked immunosorbent assay (ELISA). Dose effect inhibition of 0.1, 1, and 5 µM ( B ) TA, ( C ) TGG, and ( D ) corilagin. The absorbance of ACE2 (0.25 µg/mL) at 450 nm was set to 100%. Results are expressed as mean ± SD (n = 3). Statistical analysis was performed using one-way ANOVA followed by the Tukey post hoc test with * p < 0.05, ** p < 0.01, *** p < 0.001 compared to ACE2 (0.25 µg/mL).
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    SARS-CoV-2 neutralization potency of the pre-pandemic hCoV antibodies. Individual sera ( n = 10) positive (grey columns) or negative (white columns) for SARS-CoV-2 receptor-binding domain (RBD) and/or spike-specific antibodies were used to block spike (a) or RBD (b) proteins binding to immobilized human angiotensin-converting enzyme 2 <t>(ACE-2)</t> in a surrogate neutralization assay. RBD-specific monoclonal antibody (mAb) was used as positive blocking control (black columns). The columns represent the binding inhibition percent (%) for each sample was calculated as 100% - (optical density [OD] of ACE-2 binding in the presence of serum/OD of ACE-2 maximum binding × 100%). The numerical values above/inside columns illustrate the OD-values obtained from spike (a) or RBD (b) -specific IgG ELISAs.
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    R&D Systems human ace 2 fc
    SARS-CoV-2 neutralization potency of the pre-pandemic hCoV antibodies. Individual sera ( n = 10) positive (grey columns) or negative (white columns) for SARS-CoV-2 receptor-binding domain (RBD) and/or spike-specific antibodies were used to block spike (a) or RBD (b) proteins binding to immobilized human angiotensin-converting enzyme 2 <t>(ACE-2)</t> in a surrogate neutralization assay. RBD-specific monoclonal antibody (mAb) was used as positive blocking control (black columns). The columns represent the binding inhibition percent (%) for each sample was calculated as 100% - (optical density [OD] of ACE-2 binding in the presence of serum/OD of ACE-2 maximum binding × 100%). The numerical values above/inside columns illustrate the OD-values obtained from spike (a) or RBD (b) -specific IgG ELISAs.
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    Inhibitory effects of different polyphenols on the interaction between SARS-CoV-2 spike protein receptor binding domain (RBD (N501Y)) and human angiotensin-converting enzyme 2 (ACE2). ( A ) 10 µM of pelargonidin-3-O-glucoside (Pel-3-O-G), malvidin-3-O-glucoside (Mal-3-O-G), cyanidin-3-O-glucoside (Cya-3-O-G), peonidin, tannic acid (TA), 1,3,6-tri-O-galloyl-β-D-glucose (TGG), and corilagin were tested to evaluate their ability to inhibit the binding of immobilized spike protein (0.5 µg/mL) to human, biotin-labeled ACE2 (0.25 µg/mL) by using an enzyme-linked immunosorbent assay (ELISA). Dose effect inhibition of 0.1, 1, and 5 µM ( B ) TA, ( C ) TGG, and ( D ) corilagin. The absorbance of ACE2 (0.25 µg/mL) at 450 nm was set to 100%. Results are expressed as mean ± SD (n = 3). Statistical analysis was performed using one-way ANOVA followed by the Tukey post hoc test with * p < 0.05, ** p < 0.01, *** p < 0.001 compared to ACE2 (0.25 µg/mL).

    Journal: International Journal of Molecular Sciences

    Article Title: Molecular Interactions of Tannic Acid with Proteins Associated with SARS-CoV-2 Infectivity

    doi: 10.3390/ijms23052643

    Figure Lengend Snippet: Inhibitory effects of different polyphenols on the interaction between SARS-CoV-2 spike protein receptor binding domain (RBD (N501Y)) and human angiotensin-converting enzyme 2 (ACE2). ( A ) 10 µM of pelargonidin-3-O-glucoside (Pel-3-O-G), malvidin-3-O-glucoside (Mal-3-O-G), cyanidin-3-O-glucoside (Cya-3-O-G), peonidin, tannic acid (TA), 1,3,6-tri-O-galloyl-β-D-glucose (TGG), and corilagin were tested to evaluate their ability to inhibit the binding of immobilized spike protein (0.5 µg/mL) to human, biotin-labeled ACE2 (0.25 µg/mL) by using an enzyme-linked immunosorbent assay (ELISA). Dose effect inhibition of 0.1, 1, and 5 µM ( B ) TA, ( C ) TGG, and ( D ) corilagin. The absorbance of ACE2 (0.25 µg/mL) at 450 nm was set to 100%. Results are expressed as mean ± SD (n = 3). Statistical analysis was performed using one-way ANOVA followed by the Tukey post hoc test with * p < 0.05, ** p < 0.01, *** p < 0.001 compared to ACE2 (0.25 µg/mL).

    Article Snippet: Biotinylated recombinant human ACE2 with purity >95% and camostat mesylate compound were both purchased from R&D Systems (Minneapolis, MN, USA).

    Techniques: Binding Assay, Labeling, Enzyme-linked Immunosorbent Assay, Inhibition

    SARS-CoV-2 neutralization potency of the pre-pandemic hCoV antibodies. Individual sera ( n = 10) positive (grey columns) or negative (white columns) for SARS-CoV-2 receptor-binding domain (RBD) and/or spike-specific antibodies were used to block spike (a) or RBD (b) proteins binding to immobilized human angiotensin-converting enzyme 2 (ACE-2) in a surrogate neutralization assay. RBD-specific monoclonal antibody (mAb) was used as positive blocking control (black columns). The columns represent the binding inhibition percent (%) for each sample was calculated as 100% - (optical density [OD] of ACE-2 binding in the presence of serum/OD of ACE-2 maximum binding × 100%). The numerical values above/inside columns illustrate the OD-values obtained from spike (a) or RBD (b) -specific IgG ELISAs.

    Journal: Clinical Immunology (Orlando, Fla.)

    Article Title: Seroprevalence and SARS-CoV-2 cross-reactivity of endemic coronavirus OC43 and 229E antibodies in Finnish children and adults

    doi: 10.1016/j.clim.2021.108782

    Figure Lengend Snippet: SARS-CoV-2 neutralization potency of the pre-pandemic hCoV antibodies. Individual sera ( n = 10) positive (grey columns) or negative (white columns) for SARS-CoV-2 receptor-binding domain (RBD) and/or spike-specific antibodies were used to block spike (a) or RBD (b) proteins binding to immobilized human angiotensin-converting enzyme 2 (ACE-2) in a surrogate neutralization assay. RBD-specific monoclonal antibody (mAb) was used as positive blocking control (black columns). The columns represent the binding inhibition percent (%) for each sample was calculated as 100% - (optical density [OD] of ACE-2 binding in the presence of serum/OD of ACE-2 maximum binding × 100%). The numerical values above/inside columns illustrate the OD-values obtained from spike (a) or RBD (b) -specific IgG ELISAs.

    Article Snippet: Ninety-six well plates (Corning) were coated overnight with human ACE-2 (hACE-2, aa18–740) Fc chimera recombinant protein (1 μg/ml in PBS, Invitrogen) and the plates were blocked with 5% milk in PBS for one hour at RT.

    Techniques: Neutralization, Binding Assay, Blocking Assay, Inhibition