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siglec f  (Mimotopes)

 
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    Structured Review

    Mimotopes siglec f
    Interaction between Co4B and Siglec F. ( A ) Similarity between the Co4B and VAP-1 amino acid sequences. ( B ) EGFP and EGFP-Co4B were incubated on plates coated with recombinant Siglec F, and binding was detected using ELISA. ( C ) Binding of recombinant <t>Siglec</t> <t>F</t> to immobilized EGFP–Co4B was quantified by ELISA. ( D ) Binding of Siglec F to immobilized Co4B peptides was assessed by ELISA using serial dilutions of Siglec F. ( E ) NALTs were collected and sectioned after administration of EGFP-Co4B. Colocalization of EGFP-Co4B and Siglec F on M cells (identified using NKM 16-2-4, red) in NALT was assessed based on fluorescence signal overlap. Scale bars represent 50 μm. ( F ) The expression of Siglec F (purple) on M cells (green) in a Peyer’s patch (PP) was visualized by confocal laser-scanning microscopy, demonstrating colocalization of EGFP-Co4B with Siglec F on M cells. Scale bar represents 10 μm. Data represent the mean ± SDs of at least two independent experiments. Statistical significance in ( B , C ) was determined using an unpaired t -test, and in ( D ) using two-way ANOVA (* p < 0.05, *** p < 0.001, **** p < 0.0001).
    Siglec F, supplied by Mimotopes, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/siglec+f/f+siglec/pmc13211405-88-6-16
    Average 86 stars, based on 1 article reviews
    siglec f - by Bioz Stars, 2026-11
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    Images

    1) Product Images from "Mucosal Delivery of Recombinant SARS-CoV-2 Spike Receptor-Binding Domain Antigen Containing Immune-Stimulating Peptides Induces Protective Immune Responses Against Viral Infection in huACE2 Mice"

    Article Title: Mucosal Delivery of Recombinant SARS-CoV-2 Spike Receptor-Binding Domain Antigen Containing Immune-Stimulating Peptides Induces Protective Immune Responses Against Viral Infection in huACE2 Mice

    Journal: Vaccines

    doi: 10.3390/vaccines14050421

    Interaction between Co4B and Siglec F. ( A ) Similarity between the Co4B and VAP-1 amino acid sequences. ( B ) EGFP and EGFP-Co4B were incubated on plates coated with recombinant Siglec F, and binding was detected using ELISA. ( C ) Binding of recombinant Siglec F to immobilized EGFP–Co4B was quantified by ELISA. ( D ) Binding of Siglec F to immobilized Co4B peptides was assessed by ELISA using serial dilutions of Siglec F. ( E ) NALTs were collected and sectioned after administration of EGFP-Co4B. Colocalization of EGFP-Co4B and Siglec F on M cells (identified using NKM 16-2-4, red) in NALT was assessed based on fluorescence signal overlap. Scale bars represent 50 μm. ( F ) The expression of Siglec F (purple) on M cells (green) in a Peyer’s patch (PP) was visualized by confocal laser-scanning microscopy, demonstrating colocalization of EGFP-Co4B with Siglec F on M cells. Scale bar represents 10 μm. Data represent the mean ± SDs of at least two independent experiments. Statistical significance in ( B , C ) was determined using an unpaired t -test, and in ( D ) using two-way ANOVA (* p < 0.05, *** p < 0.001, **** p < 0.0001).
    Figure Legend Snippet: Interaction between Co4B and Siglec F. ( A ) Similarity between the Co4B and VAP-1 amino acid sequences. ( B ) EGFP and EGFP-Co4B were incubated on plates coated with recombinant Siglec F, and binding was detected using ELISA. ( C ) Binding of recombinant Siglec F to immobilized EGFP–Co4B was quantified by ELISA. ( D ) Binding of Siglec F to immobilized Co4B peptides was assessed by ELISA using serial dilutions of Siglec F. ( E ) NALTs were collected and sectioned after administration of EGFP-Co4B. Colocalization of EGFP-Co4B and Siglec F on M cells (identified using NKM 16-2-4, red) in NALT was assessed based on fluorescence signal overlap. Scale bars represent 50 μm. ( F ) The expression of Siglec F (purple) on M cells (green) in a Peyer’s patch (PP) was visualized by confocal laser-scanning microscopy, demonstrating colocalization of EGFP-Co4B with Siglec F on M cells. Scale bar represents 10 μm. Data represent the mean ± SDs of at least two independent experiments. Statistical significance in ( B , C ) was determined using an unpaired t -test, and in ( D ) using two-way ANOVA (* p < 0.05, *** p < 0.001, **** p < 0.0001).

    Techniques Used: Incubation, Recombinant, Binding Assay, Enzyme-linked Immunosorbent Assay, Fluorescence, Expressing, Confocal Laser Scanning Microscopy

    Related Articles

    Recombinant:

    Article Title: Mucosal Delivery of Recombinant SARS-CoV-2 Spike Receptor-Binding Domain Antigen Containing Immune-Stimulating Peptides Induces Protective Immune Responses Against Viral Infection in huACE2 Mice
    Article Snippet: Colorimetric development was performed by adding the appropriate substrate, and absorbance was measured with a SPECTROstar Nano microplate reader (BMG LABTECH, Ortenberg, Germany). .. To investigate interactions between Co4B and Siglec F, recombinant EGFP-Co4B, EGFP alone, and Co4B peptide alone (Mimotopes, Mulgrave, VIC, Australia) were individually coated onto ELISA plates. .. After the plates were blocked, Siglec F protein (R&D Systems, Minneapolis, MN, USA) was incubated with the coated proteins or peptides for 2 h. The wells were then treated with anti-CD170 (Siglec F) Ab (eBioscience, San Diego, CA, USA) or anti-His Ab (Qiagen) for 2 h at room temperature, followed by treatment with AP-conjugated secondary Abs.

    Enzyme-linked Immunosorbent Assay:

    Article Title: Mucosal Delivery of Recombinant SARS-CoV-2 Spike Receptor-Binding Domain Antigen Containing Immune-Stimulating Peptides Induces Protective Immune Responses Against Viral Infection in huACE2 Mice
    Article Snippet: Colorimetric development was performed by adding the appropriate substrate, and absorbance was measured with a SPECTROstar Nano microplate reader (BMG LABTECH, Ortenberg, Germany). .. To investigate interactions between Co4B and Siglec F, recombinant EGFP-Co4B, EGFP alone, and Co4B peptide alone (Mimotopes, Mulgrave, VIC, Australia) were individually coated onto ELISA plates. .. After the plates were blocked, Siglec F protein (R&D Systems, Minneapolis, MN, USA) was incubated with the coated proteins or peptides for 2 h. The wells were then treated with anti-CD170 (Siglec F) Ab (eBioscience, San Diego, CA, USA) or anti-His Ab (Qiagen) for 2 h at room temperature, followed by treatment with AP-conjugated secondary Abs.



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    Interaction between Co4B and Siglec F. ( A ) Similarity between the Co4B and VAP-1 amino acid sequences. ( B ) EGFP and EGFP-Co4B were incubated on plates coated with recombinant Siglec F, and binding was detected using ELISA. ( C ) Binding of recombinant <t>Siglec</t> <t>F</t> to immobilized EGFP–Co4B was quantified by ELISA. ( D ) Binding of Siglec F to immobilized Co4B peptides was assessed by ELISA using serial dilutions of Siglec F. ( E ) NALTs were collected and sectioned after administration of EGFP-Co4B. Colocalization of EGFP-Co4B and Siglec F on M cells (identified using NKM 16-2-4, red) in NALT was assessed based on fluorescence signal overlap. Scale bars represent 50 μm. ( F ) The expression of Siglec F (purple) on M cells (green) in a Peyer’s patch (PP) was visualized by confocal laser-scanning microscopy, demonstrating colocalization of EGFP-Co4B with Siglec F on M cells. Scale bar represents 10 μm. Data represent the mean ± SDs of at least two independent experiments. Statistical significance in ( B , C ) was determined using an unpaired t -test, and in ( D ) using two-way ANOVA (* p < 0.05, *** p < 0.001, **** p < 0.0001).
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    Interaction between Co4B and Siglec F. ( A ) Similarity between the Co4B and VAP-1 amino acid sequences. ( B ) EGFP and EGFP-Co4B were incubated on plates coated with recombinant Siglec F, and binding was detected using ELISA. ( C ) Binding of recombinant <t>Siglec</t> <t>F</t> to immobilized EGFP–Co4B was quantified by ELISA. ( D ) Binding of Siglec F to immobilized Co4B peptides was assessed by ELISA using serial dilutions of Siglec F. ( E ) NALTs were collected and sectioned after administration of EGFP-Co4B. Colocalization of EGFP-Co4B and Siglec F on M cells (identified using NKM 16-2-4, red) in NALT was assessed based on fluorescence signal overlap. Scale bars represent 50 μm. ( F ) The expression of Siglec F (purple) on M cells (green) in a Peyer’s patch (PP) was visualized by confocal laser-scanning microscopy, demonstrating colocalization of EGFP-Co4B with Siglec F on M cells. Scale bar represents 10 μm. Data represent the mean ± SDs of at least two independent experiments. Statistical significance in ( B , C ) was determined using an unpaired t -test, and in ( D ) using two-way ANOVA (* p < 0.05, *** p < 0.001, **** p < 0.0001).
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    Interaction between Co4B and Siglec F. ( A ) Similarity between the Co4B and VAP-1 amino acid sequences. ( B ) EGFP and EGFP-Co4B were incubated on plates coated with recombinant Siglec F, and binding was detected using ELISA. ( C ) Binding of recombinant <t>Siglec</t> <t>F</t> to immobilized EGFP–Co4B was quantified by ELISA. ( D ) Binding of Siglec F to immobilized Co4B peptides was assessed by ELISA using serial dilutions of Siglec F. ( E ) NALTs were collected and sectioned after administration of EGFP-Co4B. Colocalization of EGFP-Co4B and Siglec F on M cells (identified using NKM 16-2-4, red) in NALT was assessed based on fluorescence signal overlap. Scale bars represent 50 μm. ( F ) The expression of Siglec F (purple) on M cells (green) in a Peyer’s patch (PP) was visualized by confocal laser-scanning microscopy, demonstrating colocalization of EGFP-Co4B with Siglec F on M cells. Scale bar represents 10 μm. Data represent the mean ± SDs of at least two independent experiments. Statistical significance in ( B , C ) was determined using an unpaired t -test, and in ( D ) using two-way ANOVA (* p < 0.05, *** p < 0.001, **** p < 0.0001).
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    Interaction between Co4B and Siglec F. ( A ) Similarity between the Co4B and VAP-1 amino acid sequences. ( B ) EGFP and EGFP-Co4B were incubated on plates coated with recombinant Siglec F, and binding was detected using ELISA. ( C ) Binding of recombinant <t>Siglec</t> <t>F</t> to immobilized EGFP–Co4B was quantified by ELISA. ( D ) Binding of Siglec F to immobilized Co4B peptides was assessed by ELISA using serial dilutions of Siglec F. ( E ) NALTs were collected and sectioned after administration of EGFP-Co4B. Colocalization of EGFP-Co4B and Siglec F on M cells (identified using NKM 16-2-4, red) in NALT was assessed based on fluorescence signal overlap. Scale bars represent 50 μm. ( F ) The expression of Siglec F (purple) on M cells (green) in a Peyer’s patch (PP) was visualized by confocal laser-scanning microscopy, demonstrating colocalization of EGFP-Co4B with Siglec F on M cells. Scale bar represents 10 μm. Data represent the mean ± SDs of at least two independent experiments. Statistical significance in ( B , C ) was determined using an unpaired t -test, and in ( D ) using two-way ANOVA (* p < 0.05, *** p < 0.001, **** p < 0.0001).
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    Image Search Results


    Interaction between Co4B and Siglec F. ( A ) Similarity between the Co4B and VAP-1 amino acid sequences. ( B ) EGFP and EGFP-Co4B were incubated on plates coated with recombinant Siglec F, and binding was detected using ELISA. ( C ) Binding of recombinant Siglec F to immobilized EGFP–Co4B was quantified by ELISA. ( D ) Binding of Siglec F to immobilized Co4B peptides was assessed by ELISA using serial dilutions of Siglec F. ( E ) NALTs were collected and sectioned after administration of EGFP-Co4B. Colocalization of EGFP-Co4B and Siglec F on M cells (identified using NKM 16-2-4, red) in NALT was assessed based on fluorescence signal overlap. Scale bars represent 50 μm. ( F ) The expression of Siglec F (purple) on M cells (green) in a Peyer’s patch (PP) was visualized by confocal laser-scanning microscopy, demonstrating colocalization of EGFP-Co4B with Siglec F on M cells. Scale bar represents 10 μm. Data represent the mean ± SDs of at least two independent experiments. Statistical significance in ( B , C ) was determined using an unpaired t -test, and in ( D ) using two-way ANOVA (* p < 0.05, *** p < 0.001, **** p < 0.0001).

    Journal: Vaccines

    Article Title: Mucosal Delivery of Recombinant SARS-CoV-2 Spike Receptor-Binding Domain Antigen Containing Immune-Stimulating Peptides Induces Protective Immune Responses Against Viral Infection in huACE2 Mice

    doi: 10.3390/vaccines14050421

    Figure Lengend Snippet: Interaction between Co4B and Siglec F. ( A ) Similarity between the Co4B and VAP-1 amino acid sequences. ( B ) EGFP and EGFP-Co4B were incubated on plates coated with recombinant Siglec F, and binding was detected using ELISA. ( C ) Binding of recombinant Siglec F to immobilized EGFP–Co4B was quantified by ELISA. ( D ) Binding of Siglec F to immobilized Co4B peptides was assessed by ELISA using serial dilutions of Siglec F. ( E ) NALTs were collected and sectioned after administration of EGFP-Co4B. Colocalization of EGFP-Co4B and Siglec F on M cells (identified using NKM 16-2-4, red) in NALT was assessed based on fluorescence signal overlap. Scale bars represent 50 μm. ( F ) The expression of Siglec F (purple) on M cells (green) in a Peyer’s patch (PP) was visualized by confocal laser-scanning microscopy, demonstrating colocalization of EGFP-Co4B with Siglec F on M cells. Scale bar represents 10 μm. Data represent the mean ± SDs of at least two independent experiments. Statistical significance in ( B , C ) was determined using an unpaired t -test, and in ( D ) using two-way ANOVA (* p < 0.05, *** p < 0.001, **** p < 0.0001).

    Article Snippet: To investigate interactions between Co4B and Siglec F, recombinant EGFP-Co4B, EGFP alone, and Co4B peptide alone (Mimotopes, Mulgrave, VIC, Australia) were individually coated onto ELISA plates.

    Techniques: Incubation, Recombinant, Binding Assay, Enzyme-linked Immunosorbent Assay, Fluorescence, Expressing, Confocal Laser Scanning Microscopy