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anti-feline coronavirus nucleocapsid (n) antibody fipv3-70  (MyBiosource Biotechnology)

 
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    MyBiosource Biotechnology anti-feline coronavirus nucleocapsid (n) antibody fipv3-70
    Anti Feline Coronavirus Nucleocapsid (N) Antibody Fipv3 70, supplied by MyBiosource Biotechnology, 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/fipv3+70/anti+feline+coronavirus+nucleocapsid++n++antibody+fipv3+70/pmc03403912-50-21-27
    Average 90 stars, based on 1 article reviews
    anti-feline coronavirus nucleocapsid (n) antibody fipv3-70 - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    Protein Binding:

    Article Title: Suppression of feline coronavirus replication in vitro by cyclosporin A
    Article Snippet: Non-specific protein binding was blocked with 5 % non-fat dry milk for 1 h and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA) or anti-β-actin (Sigma-Aldrich) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Scientific, Tokyo, Japan) according to the manufacturer’s protocol.

    Article Title: Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk, and then the membranes were incubated with the primary antibodies [anti-FCoV nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA), anti-c-Myc antibody (Santa Cruz Biotechnology, CA, USA), anti-Pin1 antibody (Cell Signaling Technology, Tokyo, Japan), anti-Cyp B (Thermo Fisher Scientific, Yokohama, Japan), and anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH; Calbiochem, CA, USA)] for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) and/or anti-rabbit IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Fisher Scientific) according to the manufacturer's protocol.

    Article Title: Ionophore Antibiotics Inhibit Type II Feline Coronavirus Proliferation In Vitro
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk for 1 h, and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, San Diego, CA, USA) or anti-glyceraldehyde-3-phosphate dehydrogenase antibody (GAPDH, 6c5 clone; Calbiochem, Tokyo, Japan) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega Corporation, Madison, WI, USA), followed by an enhanced chemiluminescence substrate (ImmunoStar LD; Fujifilm WAKO Pure Chemical Corporation, Tokyo, Japan), according to the manufacturer’s protocol.

    Incubation:

    Article Title: Suppression of feline coronavirus replication in vitro by cyclosporin A
    Article Snippet: Non-specific protein binding was blocked with 5 % non-fat dry milk for 1 h and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA) or anti-β-actin (Sigma-Aldrich) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Scientific, Tokyo, Japan) according to the manufacturer’s protocol.

    Article Title: Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk, and then the membranes were incubated with the primary antibodies [anti-FCoV nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA), anti-c-Myc antibody (Santa Cruz Biotechnology, CA, USA), anti-Pin1 antibody (Cell Signaling Technology, Tokyo, Japan), anti-Cyp B (Thermo Fisher Scientific, Yokohama, Japan), and anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH; Calbiochem, CA, USA)] for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) and/or anti-rabbit IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Fisher Scientific) according to the manufacturer's protocol.

    Article Title: Ionophore Antibiotics Inhibit Type II Feline Coronavirus Proliferation In Vitro
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk for 1 h, and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, San Diego, CA, USA) or anti-glyceraldehyde-3-phosphate dehydrogenase antibody (GAPDH, 6c5 clone; Calbiochem, Tokyo, Japan) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega Corporation, Madison, WI, USA), followed by an enhanced chemiluminescence substrate (ImmunoStar LD; Fujifilm WAKO Pure Chemical Corporation, Tokyo, Japan), according to the manufacturer’s protocol.

    Western Blot:

    Article Title: Suppression of feline coronavirus replication in vitro by cyclosporin A
    Article Snippet: Non-specific protein binding was blocked with 5 % non-fat dry milk for 1 h and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA) or anti-β-actin (Sigma-Aldrich) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Scientific, Tokyo, Japan) according to the manufacturer’s protocol.

    Article Title: Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk, and then the membranes were incubated with the primary antibodies [anti-FCoV nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA), anti-c-Myc antibody (Santa Cruz Biotechnology, CA, USA), anti-Pin1 antibody (Cell Signaling Technology, Tokyo, Japan), anti-Cyp B (Thermo Fisher Scientific, Yokohama, Japan), and anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH; Calbiochem, CA, USA)] for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) and/or anti-rabbit IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Fisher Scientific) according to the manufacturer's protocol.

    Article Title: Ionophore Antibiotics Inhibit Type II Feline Coronavirus Proliferation In Vitro
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk for 1 h, and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, San Diego, CA, USA) or anti-glyceraldehyde-3-phosphate dehydrogenase antibody (GAPDH, 6c5 clone; Calbiochem, Tokyo, Japan) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega Corporation, Madison, WI, USA), followed by an enhanced chemiluminescence substrate (ImmunoStar LD; Fujifilm WAKO Pure Chemical Corporation, Tokyo, Japan), according to the manufacturer’s protocol.

    Solvent:

    Article Title: Suppression of feline coronavirus replication in vitro by cyclosporin A
    Article Snippet: Non-specific protein binding was blocked with 5 % non-fat dry milk for 1 h and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA) or anti-β-actin (Sigma-Aldrich) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Scientific, Tokyo, Japan) according to the manufacturer’s protocol.

    Article Title: Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk, and then the membranes were incubated with the primary antibodies [anti-FCoV nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA), anti-c-Myc antibody (Santa Cruz Biotechnology, CA, USA), anti-Pin1 antibody (Cell Signaling Technology, Tokyo, Japan), anti-Cyp B (Thermo Fisher Scientific, Yokohama, Japan), and anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH; Calbiochem, CA, USA)] for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) and/or anti-rabbit IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Fisher Scientific) according to the manufacturer's protocol.

    Article Title: Ionophore Antibiotics Inhibit Type II Feline Coronavirus Proliferation In Vitro
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk for 1 h, and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, San Diego, CA, USA) or anti-glyceraldehyde-3-phosphate dehydrogenase antibody (GAPDH, 6c5 clone; Calbiochem, Tokyo, Japan) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega Corporation, Madison, WI, USA), followed by an enhanced chemiluminescence substrate (ImmunoStar LD; Fujifilm WAKO Pure Chemical Corporation, Tokyo, Japan), according to the manufacturer’s protocol.

    Infection:

    Article Title: Suppression of feline coronavirus replication in vitro by cyclosporin A
    Article Snippet: Non-specific protein binding was blocked with 5 % non-fat dry milk for 1 h and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA) or anti-β-actin (Sigma-Aldrich) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Scientific, Tokyo, Japan) according to the manufacturer’s protocol.

    Article Title: Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk, and then the membranes were incubated with the primary antibodies [anti-FCoV nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA), anti-c-Myc antibody (Santa Cruz Biotechnology, CA, USA), anti-Pin1 antibody (Cell Signaling Technology, Tokyo, Japan), anti-Cyp B (Thermo Fisher Scientific, Yokohama, Japan), and anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH; Calbiochem, CA, USA)] for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) and/or anti-rabbit IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Fisher Scientific) according to the manufacturer's protocol.

    Article Title: Ionophore Antibiotics Inhibit Type II Feline Coronavirus Proliferation In Vitro
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk for 1 h, and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, San Diego, CA, USA) or anti-glyceraldehyde-3-phosphate dehydrogenase antibody (GAPDH, 6c5 clone; Calbiochem, Tokyo, Japan) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega Corporation, Madison, WI, USA), followed by an enhanced chemiluminescence substrate (ImmunoStar LD; Fujifilm WAKO Pure Chemical Corporation, Tokyo, Japan), according to the manufacturer’s protocol.

    Lysis:

    Article Title: Suppression of feline coronavirus replication in vitro by cyclosporin A
    Article Snippet: Non-specific protein binding was blocked with 5 % non-fat dry milk for 1 h and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA) or anti-β-actin (Sigma-Aldrich) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Scientific, Tokyo, Japan) according to the manufacturer’s protocol.

    Article Title: Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk, and then the membranes were incubated with the primary antibodies [anti-FCoV nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA), anti-c-Myc antibody (Santa Cruz Biotechnology, CA, USA), anti-Pin1 antibody (Cell Signaling Technology, Tokyo, Japan), anti-Cyp B (Thermo Fisher Scientific, Yokohama, Japan), and anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH; Calbiochem, CA, USA)] for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) and/or anti-rabbit IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Fisher Scientific) according to the manufacturer's protocol.

    Article Title: Ionophore Antibiotics Inhibit Type II Feline Coronavirus Proliferation In Vitro
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk for 1 h, and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, San Diego, CA, USA) or anti-glyceraldehyde-3-phosphate dehydrogenase antibody (GAPDH, 6c5 clone; Calbiochem, Tokyo, Japan) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega Corporation, Madison, WI, USA), followed by an enhanced chemiluminescence substrate (ImmunoStar LD; Fujifilm WAKO Pure Chemical Corporation, Tokyo, Japan), according to the manufacturer’s protocol.

    Quantitative RT-PCR:

    Article Title: Suppression of feline coronavirus replication in vitro by cyclosporin A
    Article Snippet: Non-specific protein binding was blocked with 5 % non-fat dry milk for 1 h and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA) or anti-β-actin (Sigma-Aldrich) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Scientific, Tokyo, Japan) according to the manufacturer’s protocol.

    Article Title: Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk, and then the membranes were incubated with the primary antibodies [anti-FCoV nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA), anti-c-Myc antibody (Santa Cruz Biotechnology, CA, USA), anti-Pin1 antibody (Cell Signaling Technology, Tokyo, Japan), anti-Cyp B (Thermo Fisher Scientific, Yokohama, Japan), and anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH; Calbiochem, CA, USA)] for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) and/or anti-rabbit IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Fisher Scientific) according to the manufacturer's protocol.

    Article Title: Ionophore Antibiotics Inhibit Type II Feline Coronavirus Proliferation In Vitro
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk for 1 h, and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, San Diego, CA, USA) or anti-glyceraldehyde-3-phosphate dehydrogenase antibody (GAPDH, 6c5 clone; Calbiochem, Tokyo, Japan) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega Corporation, Madison, WI, USA), followed by an enhanced chemiluminescence substrate (ImmunoStar LD; Fujifilm WAKO Pure Chemical Corporation, Tokyo, Japan), according to the manufacturer’s protocol.

    Comparison:

    Article Title: Suppression of feline coronavirus replication in vitro by cyclosporin A
    Article Snippet: Non-specific protein binding was blocked with 5 % non-fat dry milk for 1 h and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA) or anti-β-actin (Sigma-Aldrich) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Scientific, Tokyo, Japan) according to the manufacturer’s protocol.

    Article Title: Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk, and then the membranes were incubated with the primary antibodies [anti-FCoV nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA), anti-c-Myc antibody (Santa Cruz Biotechnology, CA, USA), anti-Pin1 antibody (Cell Signaling Technology, Tokyo, Japan), anti-Cyp B (Thermo Fisher Scientific, Yokohama, Japan), and anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH; Calbiochem, CA, USA)] for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) and/or anti-rabbit IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Fisher Scientific) according to the manufacturer's protocol.

    Article Title: Ionophore Antibiotics Inhibit Type II Feline Coronavirus Proliferation In Vitro
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk for 1 h, and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, San Diego, CA, USA) or anti-glyceraldehyde-3-phosphate dehydrogenase antibody (GAPDH, 6c5 clone; Calbiochem, Tokyo, Japan) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega Corporation, Madison, WI, USA), followed by an enhanced chemiluminescence substrate (ImmunoStar LD; Fujifilm WAKO Pure Chemical Corporation, Tokyo, Japan), according to the manufacturer’s protocol.

    Reverse Transcription:

    Article Title: Suppression of feline coronavirus replication in vitro by cyclosporin A
    Article Snippet: Non-specific protein binding was blocked with 5 % non-fat dry milk for 1 h and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA) or anti-β-actin (Sigma-Aldrich) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Scientific, Tokyo, Japan) according to the manufacturer’s protocol.

    Article Title: Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk, and then the membranes were incubated with the primary antibodies [anti-FCoV nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA), anti-c-Myc antibody (Santa Cruz Biotechnology, CA, USA), anti-Pin1 antibody (Cell Signaling Technology, Tokyo, Japan), anti-Cyp B (Thermo Fisher Scientific, Yokohama, Japan), and anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH; Calbiochem, CA, USA)] for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) and/or anti-rabbit IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Fisher Scientific) according to the manufacturer's protocol.

    Article Title: Ionophore Antibiotics Inhibit Type II Feline Coronavirus Proliferation In Vitro
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk for 1 h, and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, San Diego, CA, USA) or anti-glyceraldehyde-3-phosphate dehydrogenase antibody (GAPDH, 6c5 clone; Calbiochem, Tokyo, Japan) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega Corporation, Madison, WI, USA), followed by an enhanced chemiluminescence substrate (ImmunoStar LD; Fujifilm WAKO Pure Chemical Corporation, Tokyo, Japan), according to the manufacturer’s protocol.

    Real-time Polymerase Chain Reaction:

    Article Title: Suppression of feline coronavirus replication in vitro by cyclosporin A
    Article Snippet: Non-specific protein binding was blocked with 5 % non-fat dry milk for 1 h and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA) or anti-β-actin (Sigma-Aldrich) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Scientific, Tokyo, Japan) according to the manufacturer’s protocol.

    Article Title: Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk, and then the membranes were incubated with the primary antibodies [anti-FCoV nucleocapsid (N) antibody (FIPV3-70; MyBioSource, CA, USA), anti-c-Myc antibody (Santa Cruz Biotechnology, CA, USA), anti-Pin1 antibody (Cell Signaling Technology, Tokyo, Japan), anti-Cyp B (Thermo Fisher Scientific, Yokohama, Japan), and anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH; Calbiochem, CA, USA)] for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega) and/or anti-rabbit IgG antibody (Promega) followed by an enhanced chemiluminescence substrate (SuperSignal West Femto Maximum Sensitivity Substrate; Thermo Fisher Scientific) according to the manufacturer's protocol.

    Article Title: Ionophore Antibiotics Inhibit Type II Feline Coronavirus Proliferation In Vitro
    Article Snippet: Non-specific protein binding was blocked with 5% non-fat dry milk for 1 h, and then the membranes were incubated with anti-feline coronavirus nucleocapsid (N) antibody (FIPV3-70; MyBioSource, San Diego, CA, USA) or anti-glyceraldehyde-3-phosphate dehydrogenase antibody (GAPDH, 6c5 clone; Calbiochem, Tokyo, Japan) for 1 h. Antigen signals were visualized by reacting proteins on the membranes with horseradish peroxidase-conjugated anti-mouse IgG antibody (Promega Corporation, Madison, WI, USA), followed by an enhanced chemiluminescence substrate (ImmunoStar LD; Fujifilm WAKO Pure Chemical Corporation, Tokyo, Japan), according to the manufacturer’s protocol.



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    The overexpression of the bovine miRNA16a inhibited <t>BCoV</t> replication on the viral genome copy numbers and the viral infectivity levels. ( A ) In silico prediction of miRNA16atargeting the BCoV spike gene at two different sites. The folding energy represents the binding energy of the miRNA with the target region. ( B ) Multiple sequence alignment shows that the miRNA16a/Spike binding region (indicated in red box) is conserved among nine different BCoV/Ent and BCoV/Resp isolates. ( C ) qRT-PCR analysis demonstrating the genome viral load of BCoV in scrambled- and miRNA16a-transfected MDBK cells. ( D ) qRT-PCR analysis illustrating the genome viral load of BCoV in scrambled- and miRNA16a-transfected BEC cells. ( E ) Viral plaque assay indicating the infectivity level of the BCoV enteric isolate in scrambled- and miRNA16a-transfected MDBK cells. ( F ) Western blot analysis of <t>BCoV-nucleocapsid</t> (BCoV-N) and BCoV-spike (BCoV-S) in the MDBK cells transfected with scrambled or miRNA16a. ( G ) Western blot band density of the BCoV-N protein normalized to that of β-actin in the MDBK cells. ( H ) Western blot band density of the BCoV-S protein normalized to that of β-actin in the MDBK cells. ( I ) BEC cells were transfected with miRNA-Scr and miRNA16a, and western blot analysis was used to assess the protein expression of BCoV-N and BCoV-S. ( J ) Western blot band density of BCoV-N protein normalized to that of β-actin in BEC cells. ( K ) Western blot band density of BCoV-S protein normalized to that of β-actin in BEC cells. All the experiments were performed in triplicate. The significance of the data was determined by one-way ANOVA with Dunnett’s multiple comparison test and indicated as * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.
    Anti 229e N, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/fipv3+70/Coronavirus+Antibody+(FIPV3-70)+-+BSA+Free/pmc11543989-488-4-7
    Average 92 stars, based on 1 article reviews
    anti 229e n - by Bioz Stars, 2026-09
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    bcov-nucleocapsid mouse anti-bovine monoclonal (clone: fipv3-70; cat. no. ma1-82189)  (Thermo Fisher)
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    Thermo Fisher bcov-nucleocapsid mouse anti-bovine monoclonal (clone: fipv3-70; cat. no. ma1-82189)
    The overexpression of the bovine miRNA16a inhibited <t>BCoV</t> replication on the viral genome copy numbers and the viral infectivity levels. ( A ) In silico prediction of miRNA16atargeting the BCoV spike gene at two different sites. The folding energy represents the binding energy of the miRNA with the target region. ( B ) Multiple sequence alignment shows that the miRNA16a/Spike binding region (indicated in red box) is conserved among nine different BCoV/Ent and BCoV/Resp isolates. ( C ) qRT-PCR analysis demonstrating the genome viral load of BCoV in scrambled- and miRNA16a-transfected MDBK cells. ( D ) qRT-PCR analysis illustrating the genome viral load of BCoV in scrambled- and miRNA16a-transfected BEC cells. ( E ) Viral plaque assay indicating the infectivity level of the BCoV enteric isolate in scrambled- and miRNA16a-transfected MDBK cells. ( F ) Western blot analysis of <t>BCoV-nucleocapsid</t> (BCoV-N) and BCoV-spike (BCoV-S) in the MDBK cells transfected with scrambled or miRNA16a. ( G ) Western blot band density of the BCoV-N protein normalized to that of β-actin in the MDBK cells. ( H ) Western blot band density of the BCoV-S protein normalized to that of β-actin in the MDBK cells. ( I ) BEC cells were transfected with miRNA-Scr and miRNA16a, and western blot analysis was used to assess the protein expression of BCoV-N and BCoV-S. ( J ) Western blot band density of BCoV-N protein normalized to that of β-actin in BEC cells. ( K ) Western blot band density of BCoV-S protein normalized to that of β-actin in BEC cells. All the experiments were performed in triplicate. The significance of the data was determined by one-way ANOVA with Dunnett’s multiple comparison test and indicated as * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.
    Bcov Nucleocapsid Mouse Anti Bovine Monoclonal (Clone: Fipv3 70; Cat. No. Ma1 82189), supplied by Thermo Fisher, 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/fipv3+70/pm39490206-107-8-20
    Average 90 stars, based on 1 article reviews
    bcov-nucleocapsid mouse anti-bovine monoclonal (clone: fipv3-70; cat. no. ma1-82189) - by Bioz Stars, 2026-09
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    The overexpression of the bovine miRNA16a inhibited BCoV replication on the viral genome copy numbers and the viral infectivity levels. ( A ) In silico prediction of miRNA16atargeting the BCoV spike gene at two different sites. The folding energy represents the binding energy of the miRNA with the target region. ( B ) Multiple sequence alignment shows that the miRNA16a/Spike binding region (indicated in red box) is conserved among nine different BCoV/Ent and BCoV/Resp isolates. ( C ) qRT-PCR analysis demonstrating the genome viral load of BCoV in scrambled- and miRNA16a-transfected MDBK cells. ( D ) qRT-PCR analysis illustrating the genome viral load of BCoV in scrambled- and miRNA16a-transfected BEC cells. ( E ) Viral plaque assay indicating the infectivity level of the BCoV enteric isolate in scrambled- and miRNA16a-transfected MDBK cells. ( F ) Western blot analysis of BCoV-nucleocapsid (BCoV-N) and BCoV-spike (BCoV-S) in the MDBK cells transfected with scrambled or miRNA16a. ( G ) Western blot band density of the BCoV-N protein normalized to that of β-actin in the MDBK cells. ( H ) Western blot band density of the BCoV-S protein normalized to that of β-actin in the MDBK cells. ( I ) BEC cells were transfected with miRNA-Scr and miRNA16a, and western blot analysis was used to assess the protein expression of BCoV-N and BCoV-S. ( J ) Western blot band density of BCoV-N protein normalized to that of β-actin in BEC cells. ( K ) Western blot band density of BCoV-S protein normalized to that of β-actin in BEC cells. All the experiments were performed in triplicate. The significance of the data was determined by one-way ANOVA with Dunnett’s multiple comparison test and indicated as * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

    Journal: Scientific Reports

    Article Title: The dual actions of miRNA16a in restricting Bovine Coronavirus replication through downregulation of Furin and enhancing the host immune response

    doi: 10.1038/s41598-024-80708-4

    Figure Lengend Snippet: The overexpression of the bovine miRNA16a inhibited BCoV replication on the viral genome copy numbers and the viral infectivity levels. ( A ) In silico prediction of miRNA16atargeting the BCoV spike gene at two different sites. The folding energy represents the binding energy of the miRNA with the target region. ( B ) Multiple sequence alignment shows that the miRNA16a/Spike binding region (indicated in red box) is conserved among nine different BCoV/Ent and BCoV/Resp isolates. ( C ) qRT-PCR analysis demonstrating the genome viral load of BCoV in scrambled- and miRNA16a-transfected MDBK cells. ( D ) qRT-PCR analysis illustrating the genome viral load of BCoV in scrambled- and miRNA16a-transfected BEC cells. ( E ) Viral plaque assay indicating the infectivity level of the BCoV enteric isolate in scrambled- and miRNA16a-transfected MDBK cells. ( F ) Western blot analysis of BCoV-nucleocapsid (BCoV-N) and BCoV-spike (BCoV-S) in the MDBK cells transfected with scrambled or miRNA16a. ( G ) Western blot band density of the BCoV-N protein normalized to that of β-actin in the MDBK cells. ( H ) Western blot band density of the BCoV-S protein normalized to that of β-actin in the MDBK cells. ( I ) BEC cells were transfected with miRNA-Scr and miRNA16a, and western blot analysis was used to assess the protein expression of BCoV-N and BCoV-S. ( J ) Western blot band density of BCoV-N protein normalized to that of β-actin in BEC cells. ( K ) Western blot band density of BCoV-S protein normalized to that of β-actin in BEC cells. All the experiments were performed in triplicate. The significance of the data was determined by one-way ANOVA with Dunnett’s multiple comparison test and indicated as * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

    Article Snippet: The primary antibodies were used to detect the expression levels of the BCoV-nucleocapsid mouse anti-bovine monoclonal (clone: FIPV3-70; Cat. No. MA1-82,189), BCoV-spike rabbit anti-bovine polyclonal (cat. no. PA5-117562), and β-actin rabbit anti-bovine polyclonal (Catalogue number: PA1-46296) antibodies were purchased from Invitrogen.

    Techniques: Over Expression, Infection, In Silico, Binding Assay, Sequencing, Quantitative RT-PCR, Transfection, Viral Plaque Assay, Western Blot, Expressing, Comparison