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polyclonal rabbit anti mouse antibody against ckap4  (St Johns Laboratory)


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    St Johns Laboratory polyclonal rabbit anti mouse antibody against ckap4
    mGBP2 -/- MEFs were reconstituted with GFP-mGBP2 WT or one of the indicated mGBP2 truncation mutants as well as one of the N-terminal mCherry fusion proteins mCherry-mGBP2, mCherry-Gal9 or <t>mCherry-Ckap4.</t> Cells were stimulated with IFN-γ for 16 h and infected with of T. gondii ME49 for 4h. Cells were lysed and postnuclear supernatants were incubated o/n with either RFP-Trap ® beads or with GFP-Trap ® beads at 4°C. IP samples and appropriate cell lysate supernatants were subjected to Western Blotting. Blots were stained with α-GFP or α-mCherry antibodies. GTP-binding domain only (G), the G-domain and the middle domain (GM) or the C-terminal effector domain (E) .
    Polyclonal Rabbit Anti Mouse Antibody Against Ckap4, supplied by St Johns Laboratory, 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/result/polyclonal rabbit anti mouse antibody against ckap4/product/St Johns Laboratory
    Average 92 stars, based on 1 article reviews
    polyclonal rabbit anti mouse antibody against ckap4 - by Bioz Stars, 2026-02
    92/100 stars

    Images

    1) Product Images from "mGBP2 engages Galectin-9 and Cytoskeleton-associated Protein 4 for immunity against Toxoplasma gondii"

    Article Title: mGBP2 engages Galectin-9 and Cytoskeleton-associated Protein 4 for immunity against Toxoplasma gondii

    Journal: bioRxiv

    doi: 10.1101/2021.12.28.474342

    mGBP2 -/- MEFs were reconstituted with GFP-mGBP2 WT or one of the indicated mGBP2 truncation mutants as well as one of the N-terminal mCherry fusion proteins mCherry-mGBP2, mCherry-Gal9 or mCherry-Ckap4. Cells were stimulated with IFN-γ for 16 h and infected with of T. gondii ME49 for 4h. Cells were lysed and postnuclear supernatants were incubated o/n with either RFP-Trap ® beads or with GFP-Trap ® beads at 4°C. IP samples and appropriate cell lysate supernatants were subjected to Western Blotting. Blots were stained with α-GFP or α-mCherry antibodies. GTP-binding domain only (G), the G-domain and the middle domain (GM) or the C-terminal effector domain (E) .
    Figure Legend Snippet: mGBP2 -/- MEFs were reconstituted with GFP-mGBP2 WT or one of the indicated mGBP2 truncation mutants as well as one of the N-terminal mCherry fusion proteins mCherry-mGBP2, mCherry-Gal9 or mCherry-Ckap4. Cells were stimulated with IFN-γ for 16 h and infected with of T. gondii ME49 for 4h. Cells were lysed and postnuclear supernatants were incubated o/n with either RFP-Trap ® beads or with GFP-Trap ® beads at 4°C. IP samples and appropriate cell lysate supernatants were subjected to Western Blotting. Blots were stained with α-GFP or α-mCherry antibodies. GTP-binding domain only (G), the G-domain and the middle domain (GM) or the C-terminal effector domain (E) .

    Techniques Used: Infection, Incubation, Western Blot, Staining, Binding Assay

    Recruitment and colocalization of mGBP2, Gal9, and Ckpap4 was analyzed after transduction of a GFP-mGBP2 fusion construct in mGBP2 -/- MEFs and additional transduction of either mCherry-Gal9 or mCherry-Ckap4. MEFs were seeded and incubated on glass slides, stimulated with IFN-γ for 16 h and subsequently infected with T. gondii ME49 for 2 h. After fixation, infected cells were treated with an α-RFP V H H nanobody conjugated to eGFPBoosterAtto647N and with an α-GFP V H H nanobody conjugated to eGFPBoosterAtto488 for enhancement of the immunofluorescence of mCherry and GFP, respectively. Glass slides were analyzed by STED microscopy. Bars 2 μm. The graphs in the right panel depict a fluorescence intensity analysis of STED images on the far right with the ImageJ software (Fiji) for Atto488 and Atto647 fluorescence signals along the cross sections of PVMs as indicated.
    Figure Legend Snippet: Recruitment and colocalization of mGBP2, Gal9, and Ckpap4 was analyzed after transduction of a GFP-mGBP2 fusion construct in mGBP2 -/- MEFs and additional transduction of either mCherry-Gal9 or mCherry-Ckap4. MEFs were seeded and incubated on glass slides, stimulated with IFN-γ for 16 h and subsequently infected with T. gondii ME49 for 2 h. After fixation, infected cells were treated with an α-RFP V H H nanobody conjugated to eGFPBoosterAtto647N and with an α-GFP V H H nanobody conjugated to eGFPBoosterAtto488 for enhancement of the immunofluorescence of mCherry and GFP, respectively. Glass slides were analyzed by STED microscopy. Bars 2 μm. The graphs in the right panel depict a fluorescence intensity analysis of STED images on the far right with the ImageJ software (Fiji) for Atto488 and Atto647 fluorescence signals along the cross sections of PVMs as indicated.

    Techniques Used: Transduction, Construct, Incubation, Infection, Immunofluorescence, Microscopy, Fluorescence, Software

    Recruitment of mGBP2 to the PVM was analyzed by transduction of a GFP-mGBP2 fusion construct in WT and independent NIH 3T3 cell line clones with verified CRISPR/Cas9 mediated inactivation of Gal9 or Ckap4 (see main text and Figs.S5/S6). Cells were stimulated with IFN-γ for 16 h and subsequently infected with T. gondii ME49 for 2 h. The recruitment rate of GFP-mGBP2 in WT cells was set as 100% and the recruitment rate of mGBP2 in the respective knock-out cells was calculated to this reference. The percentage values are plotted on the y-axis. Also, Gal9 and Ckap4 recruitment to the T. gondii PV was analyzed in mGBP2 -/- vs. WT MEFs transduced either with mCherry-Gal9 or mCherry-Ckap4. The rate of either Gal9 positive or Ckap4 positive PVMs in WT cells was set as 100% and related to the respective rates in mGBP2 knock out cells. The percentage values are plotted on the y-axis. After fixation, T. gondii were stained with an α-SAGI antibody and the nuclei were labeled with DAPI. Glass slides were analyzed by confocal microscopy. In each cell line more than 100 PVs were counted. Mean values ± SD are shown.
    Figure Legend Snippet: Recruitment of mGBP2 to the PVM was analyzed by transduction of a GFP-mGBP2 fusion construct in WT and independent NIH 3T3 cell line clones with verified CRISPR/Cas9 mediated inactivation of Gal9 or Ckap4 (see main text and Figs.S5/S6). Cells were stimulated with IFN-γ for 16 h and subsequently infected with T. gondii ME49 for 2 h. The recruitment rate of GFP-mGBP2 in WT cells was set as 100% and the recruitment rate of mGBP2 in the respective knock-out cells was calculated to this reference. The percentage values are plotted on the y-axis. Also, Gal9 and Ckap4 recruitment to the T. gondii PV was analyzed in mGBP2 -/- vs. WT MEFs transduced either with mCherry-Gal9 or mCherry-Ckap4. The rate of either Gal9 positive or Ckap4 positive PVMs in WT cells was set as 100% and related to the respective rates in mGBP2 knock out cells. The percentage values are plotted on the y-axis. After fixation, T. gondii were stained with an α-SAGI antibody and the nuclei were labeled with DAPI. Glass slides were analyzed by confocal microscopy. In each cell line more than 100 PVs were counted. Mean values ± SD are shown.

    Techniques Used: Transduction, Construct, Clone Assay, CRISPR, Infection, Knock-Out, Staining, Labeling, Confocal Microscopy

    WT and independent NIH 3T3 cell line clones with verified CRISPR/Cas9 mediated inactivation of Gal9 or Ckap4 (see main text and Figs.S5/S6) were stimulated with IFN-γ for 16 h and subsequently infected with T. gondii ME49. After fixation, T. gondii were stained with an α-SAGI antibody and the cell nuclei were labeled with DAPI. Glass slides were analyzed by confocal microscopy. Bars, 5 μm. The amounts of rosettes (replicative units) and single parasites inside the PV were determined in WT, Gal9- and Ckap4-deficient NIH 3T3 fibroblasts 22 h after infection. In each cell line more than 100 PVs were counted. Mean values ± SD are shown (lower panel).
    Figure Legend Snippet: WT and independent NIH 3T3 cell line clones with verified CRISPR/Cas9 mediated inactivation of Gal9 or Ckap4 (see main text and Figs.S5/S6) were stimulated with IFN-γ for 16 h and subsequently infected with T. gondii ME49. After fixation, T. gondii were stained with an α-SAGI antibody and the cell nuclei were labeled with DAPI. Glass slides were analyzed by confocal microscopy. Bars, 5 μm. The amounts of rosettes (replicative units) and single parasites inside the PV were determined in WT, Gal9- and Ckap4-deficient NIH 3T3 fibroblasts 22 h after infection. In each cell line more than 100 PVs were counted. Mean values ± SD are shown (lower panel).

    Techniques Used: Clone Assay, CRISPR, Infection, Staining, Labeling, Confocal Microscopy

    WT and independent NIH 3T3 cell line clones with verified CRISPR/Cas9 mediated inactivation of Gal9 or Ckap4 (see main text and Figs.S5/S6) and NIH 3T3 cell line clones with verified CRISPR/Cas9 mediated inactivation of Gal9 or Ckap4 reconstituted with mCherry-Gal9 or mCherry-Ckap4 were stimulated with IFN-γ for 16 h and subsequently infected with T. gondii ME49 for 22 h. After fixation, T. gondii were stained with an α-SAGI antibody and the cell nuclei were labeled with DAPI. Glass slides were analyzed by confocal microscopy. The amounts of rosettes (replicative units) and single parasites inside the PV were determined in WT, Gal9- and Ckap4-deficient and Gal9 or Ckap4 reconstituted NIH 3T3 fibroblasts 22 h after infection. In each cell line more than 100 PVs were counted. Mean values ± SD are shown.
    Figure Legend Snippet: WT and independent NIH 3T3 cell line clones with verified CRISPR/Cas9 mediated inactivation of Gal9 or Ckap4 (see main text and Figs.S5/S6) and NIH 3T3 cell line clones with verified CRISPR/Cas9 mediated inactivation of Gal9 or Ckap4 reconstituted with mCherry-Gal9 or mCherry-Ckap4 were stimulated with IFN-γ for 16 h and subsequently infected with T. gondii ME49 for 22 h. After fixation, T. gondii were stained with an α-SAGI antibody and the cell nuclei were labeled with DAPI. Glass slides were analyzed by confocal microscopy. The amounts of rosettes (replicative units) and single parasites inside the PV were determined in WT, Gal9- and Ckap4-deficient and Gal9 or Ckap4 reconstituted NIH 3T3 fibroblasts 22 h after infection. In each cell line more than 100 PVs were counted. Mean values ± SD are shown.

    Techniques Used: Clone Assay, CRISPR, Infection, Staining, Labeling, Confocal Microscopy



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    polyclonal rabbit anti mouse antibody against ckap4  (St Johns Laboratory)
    92
    St Johns Laboratory polyclonal rabbit anti mouse antibody against ckap4
    mGBP2 -/- MEFs were reconstituted with GFP-mGBP2 WT or one of the indicated mGBP2 truncation mutants as well as one of the N-terminal mCherry fusion proteins mCherry-mGBP2, mCherry-Gal9 or <t>mCherry-Ckap4.</t> Cells were stimulated with IFN-γ for 16 h and infected with of T. gondii ME49 for 4h. Cells were lysed and postnuclear supernatants were incubated o/n with either RFP-Trap ® beads or with GFP-Trap ® beads at 4°C. IP samples and appropriate cell lysate supernatants were subjected to Western Blotting. Blots were stained with α-GFP or α-mCherry antibodies. GTP-binding domain only (G), the G-domain and the middle domain (GM) or the C-terminal effector domain (E) .
    Polyclonal Rabbit Anti Mouse Antibody Against Ckap4, supplied by St Johns Laboratory, 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/result/polyclonal rabbit anti mouse antibody against ckap4/product/St Johns Laboratory
    Average 92 stars, based on 1 article reviews
    polyclonal rabbit anti mouse antibody against ckap4 - by Bioz Stars, 2026-02
    92/100 stars
    		  Buy from Supplier

    Image Search Results


    mGBP2 -/- MEFs were reconstituted with GFP-mGBP2 WT or one of the indicated mGBP2 truncation mutants as well as one of the N-terminal mCherry fusion proteins mCherry-mGBP2, mCherry-Gal9 or mCherry-Ckap4. Cells were stimulated with IFN-γ for 16 h and infected with of T. gondii ME49 for 4h. Cells were lysed and postnuclear supernatants were incubated o/n with either RFP-Trap ® beads or with GFP-Trap ® beads at 4°C. IP samples and appropriate cell lysate supernatants were subjected to Western Blotting. Blots were stained with α-GFP or α-mCherry antibodies. GTP-binding domain only (G), the G-domain and the middle domain (GM) or the C-terminal effector domain (E) .

    Journal: bioRxiv

    Article Title: mGBP2 engages Galectin-9 and Cytoskeleton-associated Protein 4 for immunity against Toxoplasma gondii

    doi: 10.1101/2021.12.28.474342

    Figure Lengend Snippet: mGBP2 -/- MEFs were reconstituted with GFP-mGBP2 WT or one of the indicated mGBP2 truncation mutants as well as one of the N-terminal mCherry fusion proteins mCherry-mGBP2, mCherry-Gal9 or mCherry-Ckap4. Cells were stimulated with IFN-γ for 16 h and infected with of T. gondii ME49 for 4h. Cells were lysed and postnuclear supernatants were incubated o/n with either RFP-Trap ® beads or with GFP-Trap ® beads at 4°C. IP samples and appropriate cell lysate supernatants were subjected to Western Blotting. Blots were stained with α-GFP or α-mCherry antibodies. GTP-binding domain only (G), the G-domain and the middle domain (GM) or the C-terminal effector domain (E) .

    Article Snippet: Additionally, WB analysis was performed with a polyclonal rabbit anti-mouse antibody against Ckap4 (STJ110088, St John’s Laboratory Ltd, UK) and a polyclonal rabbit anti-mouse antibody against Gal9 (ARP54821_P050, Aviva Systems Biology).

    Techniques: Infection, Incubation, Western Blot, Staining, Binding Assay

    Recruitment and colocalization of mGBP2, Gal9, and Ckpap4 was analyzed after transduction of a GFP-mGBP2 fusion construct in mGBP2 -/- MEFs and additional transduction of either mCherry-Gal9 or mCherry-Ckap4. MEFs were seeded and incubated on glass slides, stimulated with IFN-γ for 16 h and subsequently infected with T. gondii ME49 for 2 h. After fixation, infected cells were treated with an α-RFP V H H nanobody conjugated to eGFPBoosterAtto647N and with an α-GFP V H H nanobody conjugated to eGFPBoosterAtto488 for enhancement of the immunofluorescence of mCherry and GFP, respectively. Glass slides were analyzed by STED microscopy. Bars 2 μm. The graphs in the right panel depict a fluorescence intensity analysis of STED images on the far right with the ImageJ software (Fiji) for Atto488 and Atto647 fluorescence signals along the cross sections of PVMs as indicated.

    Journal: bioRxiv

    Article Title: mGBP2 engages Galectin-9 and Cytoskeleton-associated Protein 4 for immunity against Toxoplasma gondii

    doi: 10.1101/2021.12.28.474342

    Figure Lengend Snippet: Recruitment and colocalization of mGBP2, Gal9, and Ckpap4 was analyzed after transduction of a GFP-mGBP2 fusion construct in mGBP2 -/- MEFs and additional transduction of either mCherry-Gal9 or mCherry-Ckap4. MEFs were seeded and incubated on glass slides, stimulated with IFN-γ for 16 h and subsequently infected with T. gondii ME49 for 2 h. After fixation, infected cells were treated with an α-RFP V H H nanobody conjugated to eGFPBoosterAtto647N and with an α-GFP V H H nanobody conjugated to eGFPBoosterAtto488 for enhancement of the immunofluorescence of mCherry and GFP, respectively. Glass slides were analyzed by STED microscopy. Bars 2 μm. The graphs in the right panel depict a fluorescence intensity analysis of STED images on the far right with the ImageJ software (Fiji) for Atto488 and Atto647 fluorescence signals along the cross sections of PVMs as indicated.

    Article Snippet: Additionally, WB analysis was performed with a polyclonal rabbit anti-mouse antibody against Ckap4 (STJ110088, St John’s Laboratory Ltd, UK) and a polyclonal rabbit anti-mouse antibody against Gal9 (ARP54821_P050, Aviva Systems Biology).

    Techniques: Transduction, Construct, Incubation, Infection, Immunofluorescence, Microscopy, Fluorescence, Software

    Recruitment of mGBP2 to the PVM was analyzed by transduction of a GFP-mGBP2 fusion construct in WT and independent NIH 3T3 cell line clones with verified CRISPR/Cas9 mediated inactivation of Gal9 or Ckap4 (see main text and Figs.S5/S6). Cells were stimulated with IFN-γ for 16 h and subsequently infected with T. gondii ME49 for 2 h. The recruitment rate of GFP-mGBP2 in WT cells was set as 100% and the recruitment rate of mGBP2 in the respective knock-out cells was calculated to this reference. The percentage values are plotted on the y-axis. Also, Gal9 and Ckap4 recruitment to the T. gondii PV was analyzed in mGBP2 -/- vs. WT MEFs transduced either with mCherry-Gal9 or mCherry-Ckap4. The rate of either Gal9 positive or Ckap4 positive PVMs in WT cells was set as 100% and related to the respective rates in mGBP2 knock out cells. The percentage values are plotted on the y-axis. After fixation, T. gondii were stained with an α-SAGI antibody and the nuclei were labeled with DAPI. Glass slides were analyzed by confocal microscopy. In each cell line more than 100 PVs were counted. Mean values ± SD are shown.

    Journal: bioRxiv

    Article Title: mGBP2 engages Galectin-9 and Cytoskeleton-associated Protein 4 for immunity against Toxoplasma gondii

    doi: 10.1101/2021.12.28.474342

    Figure Lengend Snippet: Recruitment of mGBP2 to the PVM was analyzed by transduction of a GFP-mGBP2 fusion construct in WT and independent NIH 3T3 cell line clones with verified CRISPR/Cas9 mediated inactivation of Gal9 or Ckap4 (see main text and Figs.S5/S6). Cells were stimulated with IFN-γ for 16 h and subsequently infected with T. gondii ME49 for 2 h. The recruitment rate of GFP-mGBP2 in WT cells was set as 100% and the recruitment rate of mGBP2 in the respective knock-out cells was calculated to this reference. The percentage values are plotted on the y-axis. Also, Gal9 and Ckap4 recruitment to the T. gondii PV was analyzed in mGBP2 -/- vs. WT MEFs transduced either with mCherry-Gal9 or mCherry-Ckap4. The rate of either Gal9 positive or Ckap4 positive PVMs in WT cells was set as 100% and related to the respective rates in mGBP2 knock out cells. The percentage values are plotted on the y-axis. After fixation, T. gondii were stained with an α-SAGI antibody and the nuclei were labeled with DAPI. Glass slides were analyzed by confocal microscopy. In each cell line more than 100 PVs were counted. Mean values ± SD are shown.

    Article Snippet: Additionally, WB analysis was performed with a polyclonal rabbit anti-mouse antibody against Ckap4 (STJ110088, St John’s Laboratory Ltd, UK) and a polyclonal rabbit anti-mouse antibody against Gal9 (ARP54821_P050, Aviva Systems Biology).

    Techniques: Transduction, Construct, Clone Assay, CRISPR, Infection, Knock-Out, Staining, Labeling, Confocal Microscopy

    WT and independent NIH 3T3 cell line clones with verified CRISPR/Cas9 mediated inactivation of Gal9 or Ckap4 (see main text and Figs.S5/S6) were stimulated with IFN-γ for 16 h and subsequently infected with T. gondii ME49. After fixation, T. gondii were stained with an α-SAGI antibody and the cell nuclei were labeled with DAPI. Glass slides were analyzed by confocal microscopy. Bars, 5 μm. The amounts of rosettes (replicative units) and single parasites inside the PV were determined in WT, Gal9- and Ckap4-deficient NIH 3T3 fibroblasts 22 h after infection. In each cell line more than 100 PVs were counted. Mean values ± SD are shown (lower panel).

    Journal: bioRxiv

    Article Title: mGBP2 engages Galectin-9 and Cytoskeleton-associated Protein 4 for immunity against Toxoplasma gondii

    doi: 10.1101/2021.12.28.474342

    Figure Lengend Snippet: WT and independent NIH 3T3 cell line clones with verified CRISPR/Cas9 mediated inactivation of Gal9 or Ckap4 (see main text and Figs.S5/S6) were stimulated with IFN-γ for 16 h and subsequently infected with T. gondii ME49. After fixation, T. gondii were stained with an α-SAGI antibody and the cell nuclei were labeled with DAPI. Glass slides were analyzed by confocal microscopy. Bars, 5 μm. The amounts of rosettes (replicative units) and single parasites inside the PV were determined in WT, Gal9- and Ckap4-deficient NIH 3T3 fibroblasts 22 h after infection. In each cell line more than 100 PVs were counted. Mean values ± SD are shown (lower panel).

    Article Snippet: Additionally, WB analysis was performed with a polyclonal rabbit anti-mouse antibody against Ckap4 (STJ110088, St John’s Laboratory Ltd, UK) and a polyclonal rabbit anti-mouse antibody against Gal9 (ARP54821_P050, Aviva Systems Biology).

    Techniques: Clone Assay, CRISPR, Infection, Staining, Labeling, Confocal Microscopy

    WT and independent NIH 3T3 cell line clones with verified CRISPR/Cas9 mediated inactivation of Gal9 or Ckap4 (see main text and Figs.S5/S6) and NIH 3T3 cell line clones with verified CRISPR/Cas9 mediated inactivation of Gal9 or Ckap4 reconstituted with mCherry-Gal9 or mCherry-Ckap4 were stimulated with IFN-γ for 16 h and subsequently infected with T. gondii ME49 for 22 h. After fixation, T. gondii were stained with an α-SAGI antibody and the cell nuclei were labeled with DAPI. Glass slides were analyzed by confocal microscopy. The amounts of rosettes (replicative units) and single parasites inside the PV were determined in WT, Gal9- and Ckap4-deficient and Gal9 or Ckap4 reconstituted NIH 3T3 fibroblasts 22 h after infection. In each cell line more than 100 PVs were counted. Mean values ± SD are shown.

    Journal: bioRxiv

    Article Title: mGBP2 engages Galectin-9 and Cytoskeleton-associated Protein 4 for immunity against Toxoplasma gondii

    doi: 10.1101/2021.12.28.474342

    Figure Lengend Snippet: WT and independent NIH 3T3 cell line clones with verified CRISPR/Cas9 mediated inactivation of Gal9 or Ckap4 (see main text and Figs.S5/S6) and NIH 3T3 cell line clones with verified CRISPR/Cas9 mediated inactivation of Gal9 or Ckap4 reconstituted with mCherry-Gal9 or mCherry-Ckap4 were stimulated with IFN-γ for 16 h and subsequently infected with T. gondii ME49 for 22 h. After fixation, T. gondii were stained with an α-SAGI antibody and the cell nuclei were labeled with DAPI. Glass slides were analyzed by confocal microscopy. The amounts of rosettes (replicative units) and single parasites inside the PV were determined in WT, Gal9- and Ckap4-deficient and Gal9 or Ckap4 reconstituted NIH 3T3 fibroblasts 22 h after infection. In each cell line more than 100 PVs were counted. Mean values ± SD are shown.

    Article Snippet: Additionally, WB analysis was performed with a polyclonal rabbit anti-mouse antibody against Ckap4 (STJ110088, St John’s Laboratory Ltd, UK) and a polyclonal rabbit anti-mouse antibody against Gal9 (ARP54821_P050, Aviva Systems Biology).

    Techniques: Clone Assay, CRISPR, Infection, Staining, Labeling, Confocal Microscopy