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10g11  (OriGene)


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    Structured Review

    OriGene 10g11
    Investigated <t> DSG2-variants. </t>
    10g11, supplied by OriGene, used in various techniques. Bioz Stars score: 94/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/10g11/product/OriGene
    Average 94 stars, based on 6 article reviews
    10g11 - by Bioz Stars, 2026-02
    94/100 stars

    Images

    1) Product Images from "In Vitro Functional Analyses of Arrhythmogenic Right Ventricular Cardiomyopathy-Associated Desmoglein-2-Missense Variations"

    Article Title: In Vitro Functional Analyses of Arrhythmogenic Right Ventricular Cardiomyopathy-Associated Desmoglein-2-Missense Variations

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0047097

    Investigated  DSG2-variants.
    Figure Legend Snippet: Investigated DSG2-variants.

    Techniques Used: Variant Assay

    Schematic view of the rECD with analysed ARVC-associated variations. The dotted line shows the predicted PC cleavage site. SS = signal sequence, Pro = prodomain, EC1-EC4 = DSG2 extracellular cadherin subdomains 1-4. B Recombinantly expressed proteins were identified as DSG2-ECD with anti-DSG2-10G11 by Western blot analysis. The calculated apparent molecular weights were 67.5±1.5, 72.5±3.5, 70.0±3.0, 70.0±3.0, 70.5±2.5, and 69.0±4.0 (mean±SEM; n = 2) for the proteins in the traces in 1, 2, 3, 4, 5 and 6, respectively. C Coomassie-R-250 staining revealed the purity of the proteins. 1 = rECD-wt, 2-6 = rECDs as labelled in A .
    Figure Legend Snippet: Schematic view of the rECD with analysed ARVC-associated variations. The dotted line shows the predicted PC cleavage site. SS = signal sequence, Pro = prodomain, EC1-EC4 = DSG2 extracellular cadherin subdomains 1-4. B Recombinantly expressed proteins were identified as DSG2-ECD with anti-DSG2-10G11 by Western blot analysis. The calculated apparent molecular weights were 67.5±1.5, 72.5±3.5, 70.0±3.0, 70.0±3.0, 70.5±2.5, and 69.0±4.0 (mean±SEM; n = 2) for the proteins in the traces in 1, 2, 3, 4, 5 and 6, respectively. C Coomassie-R-250 staining revealed the purity of the proteins. 1 = rECD-wt, 2-6 = rECDs as labelled in A .

    Techniques Used: Sequencing, Western Blot, Staining

    A+B Flow cytometry-based assay for the binding of 0.8 µM rECD-wt or -variants to HT1080. A Representative histograms of FITC- fluorescence for binding of rECD-wt- and rECD-R46Q (as indicated). Bound rECD was detected with anti-HisFITC. As a negative control, HT1080 cells were incubated with only anti-HisFITC (grey filled area). B Column plots representing the ratio of rECD-binding related to the negative control (ratio rECD-bound ) as detected by flow cytometry. Ratios rECD-bound are indicated as mean± SEM of 7 independent measurements for rECD-variants and 9 independent measurements for rECD-wt with rECDs from at least 3 different purifications. Statistical analysis was performed by one-way ANOVA with Dunnett’s posttest using rECD-wt as a control (GraphPad Prism 5.01). rECD-R46Q-binding to HT1080 is increased 1.8-fold as compared to rECD-wt. Other ARVC-associated variants have no influence on rECD-binding to HT1080. C Representative Western blot (with anti-DSG2-10G11) of rECDs crosslinked in a 5 mM CaCl 2 containing buffer with BS 3 (+) or of controls (-) reveals that rECD wild-type and variants exist in solution as monomers (m), dimers (d), and oligomers (o).
    Figure Legend Snippet: A+B Flow cytometry-based assay for the binding of 0.8 µM rECD-wt or -variants to HT1080. A Representative histograms of FITC- fluorescence for binding of rECD-wt- and rECD-R46Q (as indicated). Bound rECD was detected with anti-HisFITC. As a negative control, HT1080 cells were incubated with only anti-HisFITC (grey filled area). B Column plots representing the ratio of rECD-binding related to the negative control (ratio rECD-bound ) as detected by flow cytometry. Ratios rECD-bound are indicated as mean± SEM of 7 independent measurements for rECD-variants and 9 independent measurements for rECD-wt with rECDs from at least 3 different purifications. Statistical analysis was performed by one-way ANOVA with Dunnett’s posttest using rECD-wt as a control (GraphPad Prism 5.01). rECD-R46Q-binding to HT1080 is increased 1.8-fold as compared to rECD-wt. Other ARVC-associated variants have no influence on rECD-binding to HT1080. C Representative Western blot (with anti-DSG2-10G11) of rECDs crosslinked in a 5 mM CaCl 2 containing buffer with BS 3 (+) or of controls (-) reveals that rECD wild-type and variants exist in solution as monomers (m), dimers (d), and oligomers (o).

    Techniques Used: Flow Cytometry, Binding Assay, Fluorescence, Negative Control, Incubation, Western Blot

    DSC2b-HT1080 cells were transfected with full-length(fl)-DSG2-pEYFP; live cells were analysed with a fluorescence miscroscope one day after transfection. R46Q, D154E, D187G, K294E and V392I indicate the sequence variant in fl-DSG2-EYFP, wt fl-DSG2-wt-pEYFP, and C the LFA mock transfected control. Chimeric DSG2-proteins localised preferentially to the cell borders. ARVC-associated variations had no detectable influence on the localisation of fl-DSG2-EYFP in DSC2b-HT1080. Images were acquired through YFP and phase-contrast filters. Scale (red bar) = 10 µm.
    Figure Legend Snippet: DSC2b-HT1080 cells were transfected with full-length(fl)-DSG2-pEYFP; live cells were analysed with a fluorescence miscroscope one day after transfection. R46Q, D154E, D187G, K294E and V392I indicate the sequence variant in fl-DSG2-EYFP, wt fl-DSG2-wt-pEYFP, and C the LFA mock transfected control. Chimeric DSG2-proteins localised preferentially to the cell borders. ARVC-associated variations had no detectable influence on the localisation of fl-DSG2-EYFP in DSC2b-HT1080. Images were acquired through YFP and phase-contrast filters. Scale (red bar) = 10 µm.

    Techniques Used: Transfection, Fluorescence, Sequencing, Variant Assay



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    Image Search Results


    Investigated  DSG2-variants.

    Journal: PLoS ONE

    Article Title: In Vitro Functional Analyses of Arrhythmogenic Right Ventricular Cardiomyopathy-Associated Desmoglein-2-Missense Variations

    doi: 10.1371/journal.pone.0047097

    Figure Lengend Snippet: Investigated DSG2-variants.

    Article Snippet: For Western blotting a murine IgG1 antibody against the extracellular domain of DSG2 clone 10G11 (anti-DSG2-10G11; BM5016, Acris Antibodies GmbH), a murine IgG1 antibody clone DG3.10 against the intracellular domain of DSG1+2 (anti-DSG1+2-DG3.10; BM370, Acris Antibodies GmbH) and a rabbit polyclonal antibody to PDI IgG (anti-PDI; ab31811, Abcam) as an endoplasmatic reticulum marker were used.

    Techniques: Variant Assay

    Schematic view of the rECD with analysed ARVC-associated variations. The dotted line shows the predicted PC cleavage site. SS = signal sequence, Pro = prodomain, EC1-EC4 = DSG2 extracellular cadherin subdomains 1-4. B Recombinantly expressed proteins were identified as DSG2-ECD with anti-DSG2-10G11 by Western blot analysis. The calculated apparent molecular weights were 67.5±1.5, 72.5±3.5, 70.0±3.0, 70.0±3.0, 70.5±2.5, and 69.0±4.0 (mean±SEM; n = 2) for the proteins in the traces in 1, 2, 3, 4, 5 and 6, respectively. C Coomassie-R-250 staining revealed the purity of the proteins. 1 = rECD-wt, 2-6 = rECDs as labelled in A .

    Journal: PLoS ONE

    Article Title: In Vitro Functional Analyses of Arrhythmogenic Right Ventricular Cardiomyopathy-Associated Desmoglein-2-Missense Variations

    doi: 10.1371/journal.pone.0047097

    Figure Lengend Snippet: Schematic view of the rECD with analysed ARVC-associated variations. The dotted line shows the predicted PC cleavage site. SS = signal sequence, Pro = prodomain, EC1-EC4 = DSG2 extracellular cadherin subdomains 1-4. B Recombinantly expressed proteins were identified as DSG2-ECD with anti-DSG2-10G11 by Western blot analysis. The calculated apparent molecular weights were 67.5±1.5, 72.5±3.5, 70.0±3.0, 70.0±3.0, 70.5±2.5, and 69.0±4.0 (mean±SEM; n = 2) for the proteins in the traces in 1, 2, 3, 4, 5 and 6, respectively. C Coomassie-R-250 staining revealed the purity of the proteins. 1 = rECD-wt, 2-6 = rECDs as labelled in A .

    Article Snippet: For Western blotting a murine IgG1 antibody against the extracellular domain of DSG2 clone 10G11 (anti-DSG2-10G11; BM5016, Acris Antibodies GmbH), a murine IgG1 antibody clone DG3.10 against the intracellular domain of DSG1+2 (anti-DSG1+2-DG3.10; BM370, Acris Antibodies GmbH) and a rabbit polyclonal antibody to PDI IgG (anti-PDI; ab31811, Abcam) as an endoplasmatic reticulum marker were used.

    Techniques: Sequencing, Western Blot, Staining

    A+B Flow cytometry-based assay for the binding of 0.8 µM rECD-wt or -variants to HT1080. A Representative histograms of FITC- fluorescence for binding of rECD-wt- and rECD-R46Q (as indicated). Bound rECD was detected with anti-HisFITC. As a negative control, HT1080 cells were incubated with only anti-HisFITC (grey filled area). B Column plots representing the ratio of rECD-binding related to the negative control (ratio rECD-bound ) as detected by flow cytometry. Ratios rECD-bound are indicated as mean± SEM of 7 independent measurements for rECD-variants and 9 independent measurements for rECD-wt with rECDs from at least 3 different purifications. Statistical analysis was performed by one-way ANOVA with Dunnett’s posttest using rECD-wt as a control (GraphPad Prism 5.01). rECD-R46Q-binding to HT1080 is increased 1.8-fold as compared to rECD-wt. Other ARVC-associated variants have no influence on rECD-binding to HT1080. C Representative Western blot (with anti-DSG2-10G11) of rECDs crosslinked in a 5 mM CaCl 2 containing buffer with BS 3 (+) or of controls (-) reveals that rECD wild-type and variants exist in solution as monomers (m), dimers (d), and oligomers (o).

    Journal: PLoS ONE

    Article Title: In Vitro Functional Analyses of Arrhythmogenic Right Ventricular Cardiomyopathy-Associated Desmoglein-2-Missense Variations

    doi: 10.1371/journal.pone.0047097

    Figure Lengend Snippet: A+B Flow cytometry-based assay for the binding of 0.8 µM rECD-wt or -variants to HT1080. A Representative histograms of FITC- fluorescence for binding of rECD-wt- and rECD-R46Q (as indicated). Bound rECD was detected with anti-HisFITC. As a negative control, HT1080 cells were incubated with only anti-HisFITC (grey filled area). B Column plots representing the ratio of rECD-binding related to the negative control (ratio rECD-bound ) as detected by flow cytometry. Ratios rECD-bound are indicated as mean± SEM of 7 independent measurements for rECD-variants and 9 independent measurements for rECD-wt with rECDs from at least 3 different purifications. Statistical analysis was performed by one-way ANOVA with Dunnett’s posttest using rECD-wt as a control (GraphPad Prism 5.01). rECD-R46Q-binding to HT1080 is increased 1.8-fold as compared to rECD-wt. Other ARVC-associated variants have no influence on rECD-binding to HT1080. C Representative Western blot (with anti-DSG2-10G11) of rECDs crosslinked in a 5 mM CaCl 2 containing buffer with BS 3 (+) or of controls (-) reveals that rECD wild-type and variants exist in solution as monomers (m), dimers (d), and oligomers (o).

    Article Snippet: For Western blotting a murine IgG1 antibody against the extracellular domain of DSG2 clone 10G11 (anti-DSG2-10G11; BM5016, Acris Antibodies GmbH), a murine IgG1 antibody clone DG3.10 against the intracellular domain of DSG1+2 (anti-DSG1+2-DG3.10; BM370, Acris Antibodies GmbH) and a rabbit polyclonal antibody to PDI IgG (anti-PDI; ab31811, Abcam) as an endoplasmatic reticulum marker were used.

    Techniques: Flow Cytometry, Binding Assay, Fluorescence, Negative Control, Incubation, Western Blot

    DSC2b-HT1080 cells were transfected with full-length(fl)-DSG2-pEYFP; live cells were analysed with a fluorescence miscroscope one day after transfection. R46Q, D154E, D187G, K294E and V392I indicate the sequence variant in fl-DSG2-EYFP, wt fl-DSG2-wt-pEYFP, and C the LFA mock transfected control. Chimeric DSG2-proteins localised preferentially to the cell borders. ARVC-associated variations had no detectable influence on the localisation of fl-DSG2-EYFP in DSC2b-HT1080. Images were acquired through YFP and phase-contrast filters. Scale (red bar) = 10 µm.

    Journal: PLoS ONE

    Article Title: In Vitro Functional Analyses of Arrhythmogenic Right Ventricular Cardiomyopathy-Associated Desmoglein-2-Missense Variations

    doi: 10.1371/journal.pone.0047097

    Figure Lengend Snippet: DSC2b-HT1080 cells were transfected with full-length(fl)-DSG2-pEYFP; live cells were analysed with a fluorescence miscroscope one day after transfection. R46Q, D154E, D187G, K294E and V392I indicate the sequence variant in fl-DSG2-EYFP, wt fl-DSG2-wt-pEYFP, and C the LFA mock transfected control. Chimeric DSG2-proteins localised preferentially to the cell borders. ARVC-associated variations had no detectable influence on the localisation of fl-DSG2-EYFP in DSC2b-HT1080. Images were acquired through YFP and phase-contrast filters. Scale (red bar) = 10 µm.

    Article Snippet: For Western blotting a murine IgG1 antibody against the extracellular domain of DSG2 clone 10G11 (anti-DSG2-10G11; BM5016, Acris Antibodies GmbH), a murine IgG1 antibody clone DG3.10 against the intracellular domain of DSG1+2 (anti-DSG1+2-DG3.10; BM370, Acris Antibodies GmbH) and a rabbit polyclonal antibody to PDI IgG (anti-PDI; ab31811, Abcam) as an endoplasmatic reticulum marker were used.

    Techniques: Transfection, Fluorescence, Sequencing, Variant Assay