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rabbit polyclonal anti sars cov 2 rbd antibody  (Sino Biological)


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    Sino Biological rabbit polyclonal anti sars cov 2 rbd antibody
    Rabbit Polyclonal Anti Sars Cov 2 Rbd Antibody, supplied by Sino Biological, used in various techniques. Bioz Stars score: 96/100, based on 201 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rbd+antigen/SARS-CoV-2+(2019-nCoV)+Spike+RBD+Antibody%2C+Rabbit+PAb%2C+Antigen+Affinity+Purified/pmc13016312-76-9-15
    Average 96 stars, based on 201 article reviews
    rabbit polyclonal anti sars cov 2 rbd antibody - by Bioz Stars, 2026-09
    96/100 stars

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    Article Title: Automated Cell-free Protein Synthesis for Distributed Biomanufacturing
    Article Snippet: Black 384-well plates were coated overnight at 4 °C with RBD antigen (SinoBiological [40592-VNAH], 1 μg/mL in PBS).



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    <t>Inhibition</t> <t>of</t> <t>SARS-CoV-2</t> Spike-mediated cell fusion and PsV infection by DBP. (A) DBP inhibits SARS-CoV-2 Spike-mediated cell membrane fusion. Seven different concentrations were tested. (B) Western blot analysis of Spike protein cleavage. As DBP concentration increases, the concentration of the S2’ subunit decreases compared to the Neg group. (C) Gray scale values of the S2’ subunit from three repeated experiments. The gray value of the S2’ protein strip was reported as mean ± SD. Statistical significance relative to the Neg group is denoted as follows: * P < 0.05, ** P < 0.01, *** P < 0.001. (D) DBP inhibits SARS-CoV-2 PsV infection but not VSVΔG/G PsV.
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    Image Search Results


    Inhibition of SARS-CoV-2 Spike-mediated cell fusion and PsV infection by DBP. (A) DBP inhibits SARS-CoV-2 Spike-mediated cell membrane fusion. Seven different concentrations were tested. (B) Western blot analysis of Spike protein cleavage. As DBP concentration increases, the concentration of the S2’ subunit decreases compared to the Neg group. (C) Gray scale values of the S2’ subunit from three repeated experiments. The gray value of the S2’ protein strip was reported as mean ± SD. Statistical significance relative to the Neg group is denoted as follows: * P < 0.05, ** P < 0.01, *** P < 0.001. (D) DBP inhibits SARS-CoV-2 PsV infection but not VSVΔG/G PsV.

    Journal: Frontiers in Microbiology

    Article Title: Broad-spectrum inhibition of SARS-CoV-2 variants by dibutyl phthalate through allosteric disruption of Spike-ACE2 interface

    doi: 10.3389/fmicb.2025.1610775

    Figure Lengend Snippet: Inhibition of SARS-CoV-2 Spike-mediated cell fusion and PsV infection by DBP. (A) DBP inhibits SARS-CoV-2 Spike-mediated cell membrane fusion. Seven different concentrations were tested. (B) Western blot analysis of Spike protein cleavage. As DBP concentration increases, the concentration of the S2’ subunit decreases compared to the Neg group. (C) Gray scale values of the S2’ subunit from three repeated experiments. The gray value of the S2’ protein strip was reported as mean ± SD. Statistical significance relative to the Neg group is denoted as follows: * P < 0.05, ** P < 0.01, *** P < 0.001. (D) DBP inhibits SARS-CoV-2 PsV infection but not VSVΔG/G PsV.

    Article Snippet: SARS-CoV-2 Spike trimer protein (40589-V08H4), ACE2 protein (10108-H08H), Recombinant Anti-ACE2 Antibody (10108-R003), SARS-CoV-2 (2019-nCoV) Spike Antibody (Rabbit PAb) (40592-T62) were purchased from sino biological (Beijing, China).

    Techniques: Inhibition, Infection, Membrane, Western Blot, Concentration Assay, Stripping Membranes

    Inhibition of SARS-CoV-2 Spike-mediated cell membrane fusion by DBP as assessed by fluorescence co-localization. (A) Fluorescent images were captured at 24 h after treatment with DBP to assess SARS-CoV-2 Spike-mediated cell-cell fusion. The green and red fluorescence signals are merged, and the yellow cells represent fused cells (red arrow). The blue fluorescence signal represents the nucleus. (B) Percentage of SARS-CoV-2 Spike-mediated cell-cell fusion. The ratio of yellow (fusion cells) to blue (total cells) areas was calculated from the fluorescent images. The membrane fusion percentage was reported as mean ± SD. Statistical significance is denoted as follows: * P < 0.05, ** P < 0.01, *** P < 0.001 versus the Mock group. (C) Statistical analysis of the membrane fusion inhibition rate. Three randomly selected fields per sample were analyzed from each sample.

    Journal: Frontiers in Microbiology

    Article Title: Broad-spectrum inhibition of SARS-CoV-2 variants by dibutyl phthalate through allosteric disruption of Spike-ACE2 interface

    doi: 10.3389/fmicb.2025.1610775

    Figure Lengend Snippet: Inhibition of SARS-CoV-2 Spike-mediated cell membrane fusion by DBP as assessed by fluorescence co-localization. (A) Fluorescent images were captured at 24 h after treatment with DBP to assess SARS-CoV-2 Spike-mediated cell-cell fusion. The green and red fluorescence signals are merged, and the yellow cells represent fused cells (red arrow). The blue fluorescence signal represents the nucleus. (B) Percentage of SARS-CoV-2 Spike-mediated cell-cell fusion. The ratio of yellow (fusion cells) to blue (total cells) areas was calculated from the fluorescent images. The membrane fusion percentage was reported as mean ± SD. Statistical significance is denoted as follows: * P < 0.05, ** P < 0.01, *** P < 0.001 versus the Mock group. (C) Statistical analysis of the membrane fusion inhibition rate. Three randomly selected fields per sample were analyzed from each sample.

    Article Snippet: SARS-CoV-2 Spike trimer protein (40589-V08H4), ACE2 protein (10108-H08H), Recombinant Anti-ACE2 Antibody (10108-R003), SARS-CoV-2 (2019-nCoV) Spike Antibody (Rabbit PAb) (40592-T62) were purchased from sino biological (Beijing, China).

    Techniques: Inhibition, Membrane, Fluorescence

    SPR Analysis of DBP Binding to ACE2 and SARS-CoV-2 Spike Trimer, and Its Inhibition of Spike-ACE2 Interaction. (A,B) The response curves of DBP (0.0122–3.1250 μM) with ACE2 (40 μg/mL, optimized for DBP-ACE2 binding detection) and S trimer (40 μg/mL, optimized for DBP-S trimer binding detection). (C) Concentration-dependent binding of ACE2 (15.625–250 nM) to S trimer (20 μg/mL, optimized for ACE2-S trimer binding detection). (D) Inhibitory effect of DBP on S trimer-ACE2 interaction. K D : Equilibrium dissociation constant. (E) Proposed mechanism of action of DBP.

    Journal: Frontiers in Microbiology

    Article Title: Broad-spectrum inhibition of SARS-CoV-2 variants by dibutyl phthalate through allosteric disruption of Spike-ACE2 interface

    doi: 10.3389/fmicb.2025.1610775

    Figure Lengend Snippet: SPR Analysis of DBP Binding to ACE2 and SARS-CoV-2 Spike Trimer, and Its Inhibition of Spike-ACE2 Interaction. (A,B) The response curves of DBP (0.0122–3.1250 μM) with ACE2 (40 μg/mL, optimized for DBP-ACE2 binding detection) and S trimer (40 μg/mL, optimized for DBP-S trimer binding detection). (C) Concentration-dependent binding of ACE2 (15.625–250 nM) to S trimer (20 μg/mL, optimized for ACE2-S trimer binding detection). (D) Inhibitory effect of DBP on S trimer-ACE2 interaction. K D : Equilibrium dissociation constant. (E) Proposed mechanism of action of DBP.

    Article Snippet: SARS-CoV-2 Spike trimer protein (40589-V08H4), ACE2 protein (10108-H08H), Recombinant Anti-ACE2 Antibody (10108-R003), SARS-CoV-2 (2019-nCoV) Spike Antibody (Rabbit PAb) (40592-T62) were purchased from sino biological (Beijing, China).

    Techniques: Binding Assay, Inhibition, Concentration Assay

    Inhibition of SARS-CoV-2 RBD-ACE2 interaction by DBP and its effect on ACE2 enzymatic activity. (A) Schematic illustration of ELISA assays under three experimental conditions: DBP No Premix, DBP-ACE2 Premix, and DBP-Spike Premix. (B) ELISA showing the inhibitory effect of DBP on the binding of SARS-CoV-2 RBD to ACE2. (C) Bar graph depicting the inhibition rate of ACE2/RBD binding by DBP under varied preincubation conditions. DBP at concentrations of 100 μM (blue) and 200 μM (orange) was evaluated in three conditions: no preincubation (DBP No Premix), preincubation with ACE2 (DBP-ACE2 Premix, 1 h), and preincubation with RBD (DBP-RBD Premix, 1 h). (D) Assessment of DBP’s effect on ACE2 enzymatic activity within a concentration range of 12.5–200 μM. Relative Fluorescence units were reported as mean ± SD. Significant differences were observed in the MLN-4760 group compared to the Neg group (*** P < 0.001), while no statistically significant differences (ns) were detected in the other experimental groups. (E) Molecular docking analysis showing that DBP stably binds at the RBD (Cyan). (F) Structural representation of the ACE2-RBD interface (Red) before DBP binding, showing the formation of 18 hydrogen bonds (Yellow) and one salt bridge (Orange). ACE2 inter-action residues are shown in yellow, RBD residues in salmon. (G) Structural representation of the ACE2-RBD interface (Red) after DBP binding, with only 7 hydrogen bonds remaining.

    Journal: Frontiers in Microbiology

    Article Title: Broad-spectrum inhibition of SARS-CoV-2 variants by dibutyl phthalate through allosteric disruption of Spike-ACE2 interface

    doi: 10.3389/fmicb.2025.1610775

    Figure Lengend Snippet: Inhibition of SARS-CoV-2 RBD-ACE2 interaction by DBP and its effect on ACE2 enzymatic activity. (A) Schematic illustration of ELISA assays under three experimental conditions: DBP No Premix, DBP-ACE2 Premix, and DBP-Spike Premix. (B) ELISA showing the inhibitory effect of DBP on the binding of SARS-CoV-2 RBD to ACE2. (C) Bar graph depicting the inhibition rate of ACE2/RBD binding by DBP under varied preincubation conditions. DBP at concentrations of 100 μM (blue) and 200 μM (orange) was evaluated in three conditions: no preincubation (DBP No Premix), preincubation with ACE2 (DBP-ACE2 Premix, 1 h), and preincubation with RBD (DBP-RBD Premix, 1 h). (D) Assessment of DBP’s effect on ACE2 enzymatic activity within a concentration range of 12.5–200 μM. Relative Fluorescence units were reported as mean ± SD. Significant differences were observed in the MLN-4760 group compared to the Neg group (*** P < 0.001), while no statistically significant differences (ns) were detected in the other experimental groups. (E) Molecular docking analysis showing that DBP stably binds at the RBD (Cyan). (F) Structural representation of the ACE2-RBD interface (Red) before DBP binding, showing the formation of 18 hydrogen bonds (Yellow) and one salt bridge (Orange). ACE2 inter-action residues are shown in yellow, RBD residues in salmon. (G) Structural representation of the ACE2-RBD interface (Red) after DBP binding, with only 7 hydrogen bonds remaining.

    Article Snippet: SARS-CoV-2 Spike trimer protein (40589-V08H4), ACE2 protein (10108-H08H), Recombinant Anti-ACE2 Antibody (10108-R003), SARS-CoV-2 (2019-nCoV) Spike Antibody (Rabbit PAb) (40592-T62) were purchased from sino biological (Beijing, China).

    Techniques: Inhibition, Activity Assay, Enzyme-linked Immunosorbent Assay, Binding Assay, Concentration Assay, Fluorescence, Stable Transfection

    Inhibition of Spike-mediated membrane fusion by DBP in SARS-CoV-2 WT, Delta and Omicron XBB1.5 variants. (A–C) The luciferase expression after cell membrane fusion. Membrane fusion activity in cell lysates was quantified using a luciferase reporter assay. Data are presented as mean ± SD. Statistical significance is denoted as follows: * P < 0.05, ** P < 0.01, *** P < 0.001, versus the Neg group. (D) Dose-response curve showing the IC 50 of DBP. (E–G) Western blot analysis showing the inhibition of Spike-mediated membrane fusion.

    Journal: Frontiers in Microbiology

    Article Title: Broad-spectrum inhibition of SARS-CoV-2 variants by dibutyl phthalate through allosteric disruption of Spike-ACE2 interface

    doi: 10.3389/fmicb.2025.1610775

    Figure Lengend Snippet: Inhibition of Spike-mediated membrane fusion by DBP in SARS-CoV-2 WT, Delta and Omicron XBB1.5 variants. (A–C) The luciferase expression after cell membrane fusion. Membrane fusion activity in cell lysates was quantified using a luciferase reporter assay. Data are presented as mean ± SD. Statistical significance is denoted as follows: * P < 0.05, ** P < 0.01, *** P < 0.001, versus the Neg group. (D) Dose-response curve showing the IC 50 of DBP. (E–G) Western blot analysis showing the inhibition of Spike-mediated membrane fusion.

    Article Snippet: SARS-CoV-2 Spike trimer protein (40589-V08H4), ACE2 protein (10108-H08H), Recombinant Anti-ACE2 Antibody (10108-R003), SARS-CoV-2 (2019-nCoV) Spike Antibody (Rabbit PAb) (40592-T62) were purchased from sino biological (Beijing, China).

    Techniques: Inhibition, Membrane, Luciferase, Expressing, Activity Assay, Reporter Assay, Western Blot