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polyclonal rabbit anti tdp 43 antibody  (Proteintech)


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    Proteintech polyclonal rabbit anti tdp 43 antibody
    a , Immunofluorescence of H4 cells overexpressing TDP-43venus (green) via lentivirus transduction were after 3 days, infected with HSV-1 (MOI 0.3). Cells were fixed after 17 h. ICP27 (red), DAPI (blue), actin (white). Scale bar, 10 µm. b , Analysis of nuclear TDP-43venus foci area in ( a ) using foci analyzer. Lines represent mean±SEM, n = 101-110, three independent biological replicates. ***p<0.001, t test. c , Representative immunofluorescence of H4 cells transduced with AAV expressing TDP-43venus (green). 3 days post-transduction, cells were infected with HSV-1 (MOI 0.3). 17 h post-HSV-1 infection, cells were fixed. DAPI (blue). White squares indicate origin of inset. Scale bar, 200 µm. d , Quantification of the total cytosolic TDP-43venus signal divided by the cell number per image as assessed by DAPI count, using Imaris software. Dots represent individual replicates. n = 9, three independent biological replicates. **p<0.01, paired t test. e , Representative immunofluorescent images of H4 cells transduced with lentiviruses expressing TDP-43venus (green) and 3 days later, infected with HSV-1 (MOI 0.3). Cells were fixed 17 h post-HSV-1 infection and stained for pTDP-43 (red), ICP27 (orange), and DAPI (blue). Scale bar, 10 µm. f , Quantification of the pTDP-43 area after thresholding for pTDP-43 dots (ImageJ). Lines represent mean±SEM, n = 60, three independent biological replicates. ***p<0.001, t test. g , Representative immunoblot <t>of</t> <t>TDP-43</t> and GAPDH in H4 cells transduced with AAV expressing TDP-43venus for 3 days and infected with HSV-1 for 17 h. Cells were harvested and separated into whole cell lysate (WCL), nuclear (N) and cytosolic (C) fractions. Stained with anti-TDP-43, anti-Lamin, and anti-GAPDH. h , Quantification of the 35 kDa C-terminal fragment (CTF35) WCL band intensity in ( g ). Normalized to respective GAPDH band. n = 4, *p<0.05, paired t test. i , Representative immunoblots of HEK293T cells transduced with AAV-TDP-43venus (3 d) and infected with HSV-1 (MOI 0.3, 17 h). Fractions of the whole cell lysate (WCL) were separated into soluble (S) and insoluble (I) components. j , Western blot band intensities of soluble and insoluble TDP-43venus in ( i ) displayed as ratio. n = 6, *p<0.05, paired t test. k , Schematic representation of the TDP-43 split luciferase system. Upon TDP-43 oligomerization the fusion of L1 and L2 results in a functional luciferase. l , Quantification of luciferase activity in HEK293T cells co-transfected with split luciferase: TDP43-L1 and TDP43-L2. 24 h post-transfection cells were infected with HSV-1 (MOI 0.3). After 48 h post-infection cells were lysed and luciferase activity was analyzed. Bars represent mean±SEM of n = 4. *p<0.05, t test, m , Fluorescence recovery after photobleaching (FRAP) of H4 cells transduced with lentiviruses expressing TDP-43halo (red) and infected with HSV-1 GFP. 17 h post-infection, GFP positive cells with TDP-43halo delocalization were selected and analyzed. High laser intensity (100%) was applied to the region of interest (ROI) for 5 s. Subsequently, 10 images were acquired every 5 s. Scale bar, 20 µm. n , Quantification of the fluorescence recovery in ROIs as shown in ( m ). Pre-bleaching mean fluorescence intensity (MFI) was set to 100% and post-bleaching MFI was set to 0%. n = 12 individual cells. A linear mixed model with time and treatment as fixed effects and replicate (n = 9) as a random effect demonstrates a significant (**p=0.00272) effect for treatment and treatment:timepoint interaction (***p=2.45 x 10 -8 ).
    Polyclonal Rabbit Anti Tdp 43 Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 896 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+tdp+43/TDP-43+Polyclonal+antibody/bio_rxiv__64898__2026__03__27__714707-459-12-16
    Average 96 stars, based on 896 article reviews
    polyclonal rabbit anti tdp 43 antibody - by Bioz Stars, 2026-09
    96/100 stars

    Images

    1) Product Images from "Herpes simplex virus infection promotes ALS pathology through ICP0-mediated PML body disruption"

    Article Title: Herpes simplex virus infection promotes ALS pathology through ICP0-mediated PML body disruption

    Journal: bioRxiv

    doi: 10.64898/2026.03.27.714707

    a , Immunofluorescence of H4 cells overexpressing TDP-43venus (green) via lentivirus transduction were after 3 days, infected with HSV-1 (MOI 0.3). Cells were fixed after 17 h. ICP27 (red), DAPI (blue), actin (white). Scale bar, 10 µm. b , Analysis of nuclear TDP-43venus foci area in ( a ) using foci analyzer. Lines represent mean±SEM, n = 101-110, three independent biological replicates. ***p<0.001, t test. c , Representative immunofluorescence of H4 cells transduced with AAV expressing TDP-43venus (green). 3 days post-transduction, cells were infected with HSV-1 (MOI 0.3). 17 h post-HSV-1 infection, cells were fixed. DAPI (blue). White squares indicate origin of inset. Scale bar, 200 µm. d , Quantification of the total cytosolic TDP-43venus signal divided by the cell number per image as assessed by DAPI count, using Imaris software. Dots represent individual replicates. n = 9, three independent biological replicates. **p<0.01, paired t test. e , Representative immunofluorescent images of H4 cells transduced with lentiviruses expressing TDP-43venus (green) and 3 days later, infected with HSV-1 (MOI 0.3). Cells were fixed 17 h post-HSV-1 infection and stained for pTDP-43 (red), ICP27 (orange), and DAPI (blue). Scale bar, 10 µm. f , Quantification of the pTDP-43 area after thresholding for pTDP-43 dots (ImageJ). Lines represent mean±SEM, n = 60, three independent biological replicates. ***p<0.001, t test. g , Representative immunoblot of TDP-43 and GAPDH in H4 cells transduced with AAV expressing TDP-43venus for 3 days and infected with HSV-1 for 17 h. Cells were harvested and separated into whole cell lysate (WCL), nuclear (N) and cytosolic (C) fractions. Stained with anti-TDP-43, anti-Lamin, and anti-GAPDH. h , Quantification of the 35 kDa C-terminal fragment (CTF35) WCL band intensity in ( g ). Normalized to respective GAPDH band. n = 4, *p<0.05, paired t test. i , Representative immunoblots of HEK293T cells transduced with AAV-TDP-43venus (3 d) and infected with HSV-1 (MOI 0.3, 17 h). Fractions of the whole cell lysate (WCL) were separated into soluble (S) and insoluble (I) components. j , Western blot band intensities of soluble and insoluble TDP-43venus in ( i ) displayed as ratio. n = 6, *p<0.05, paired t test. k , Schematic representation of the TDP-43 split luciferase system. Upon TDP-43 oligomerization the fusion of L1 and L2 results in a functional luciferase. l , Quantification of luciferase activity in HEK293T cells co-transfected with split luciferase: TDP43-L1 and TDP43-L2. 24 h post-transfection cells were infected with HSV-1 (MOI 0.3). After 48 h post-infection cells were lysed and luciferase activity was analyzed. Bars represent mean±SEM of n = 4. *p<0.05, t test, m , Fluorescence recovery after photobleaching (FRAP) of H4 cells transduced with lentiviruses expressing TDP-43halo (red) and infected with HSV-1 GFP. 17 h post-infection, GFP positive cells with TDP-43halo delocalization were selected and analyzed. High laser intensity (100%) was applied to the region of interest (ROI) for 5 s. Subsequently, 10 images were acquired every 5 s. Scale bar, 20 µm. n , Quantification of the fluorescence recovery in ROIs as shown in ( m ). Pre-bleaching mean fluorescence intensity (MFI) was set to 100% and post-bleaching MFI was set to 0%. n = 12 individual cells. A linear mixed model with time and treatment as fixed effects and replicate (n = 9) as a random effect demonstrates a significant (**p=0.00272) effect for treatment and treatment:timepoint interaction (***p=2.45 x 10 -8 ).
    Figure Legend Snippet: a , Immunofluorescence of H4 cells overexpressing TDP-43venus (green) via lentivirus transduction were after 3 days, infected with HSV-1 (MOI 0.3). Cells were fixed after 17 h. ICP27 (red), DAPI (blue), actin (white). Scale bar, 10 µm. b , Analysis of nuclear TDP-43venus foci area in ( a ) using foci analyzer. Lines represent mean±SEM, n = 101-110, three independent biological replicates. ***p<0.001, t test. c , Representative immunofluorescence of H4 cells transduced with AAV expressing TDP-43venus (green). 3 days post-transduction, cells were infected with HSV-1 (MOI 0.3). 17 h post-HSV-1 infection, cells were fixed. DAPI (blue). White squares indicate origin of inset. Scale bar, 200 µm. d , Quantification of the total cytosolic TDP-43venus signal divided by the cell number per image as assessed by DAPI count, using Imaris software. Dots represent individual replicates. n = 9, three independent biological replicates. **p<0.01, paired t test. e , Representative immunofluorescent images of H4 cells transduced with lentiviruses expressing TDP-43venus (green) and 3 days later, infected with HSV-1 (MOI 0.3). Cells were fixed 17 h post-HSV-1 infection and stained for pTDP-43 (red), ICP27 (orange), and DAPI (blue). Scale bar, 10 µm. f , Quantification of the pTDP-43 area after thresholding for pTDP-43 dots (ImageJ). Lines represent mean±SEM, n = 60, three independent biological replicates. ***p<0.001, t test. g , Representative immunoblot of TDP-43 and GAPDH in H4 cells transduced with AAV expressing TDP-43venus for 3 days and infected with HSV-1 for 17 h. Cells were harvested and separated into whole cell lysate (WCL), nuclear (N) and cytosolic (C) fractions. Stained with anti-TDP-43, anti-Lamin, and anti-GAPDH. h , Quantification of the 35 kDa C-terminal fragment (CTF35) WCL band intensity in ( g ). Normalized to respective GAPDH band. n = 4, *p<0.05, paired t test. i , Representative immunoblots of HEK293T cells transduced with AAV-TDP-43venus (3 d) and infected with HSV-1 (MOI 0.3, 17 h). Fractions of the whole cell lysate (WCL) were separated into soluble (S) and insoluble (I) components. j , Western blot band intensities of soluble and insoluble TDP-43venus in ( i ) displayed as ratio. n = 6, *p<0.05, paired t test. k , Schematic representation of the TDP-43 split luciferase system. Upon TDP-43 oligomerization the fusion of L1 and L2 results in a functional luciferase. l , Quantification of luciferase activity in HEK293T cells co-transfected with split luciferase: TDP43-L1 and TDP43-L2. 24 h post-transfection cells were infected with HSV-1 (MOI 0.3). After 48 h post-infection cells were lysed and luciferase activity was analyzed. Bars represent mean±SEM of n = 4. *p<0.05, t test, m , Fluorescence recovery after photobleaching (FRAP) of H4 cells transduced with lentiviruses expressing TDP-43halo (red) and infected with HSV-1 GFP. 17 h post-infection, GFP positive cells with TDP-43halo delocalization were selected and analyzed. High laser intensity (100%) was applied to the region of interest (ROI) for 5 s. Subsequently, 10 images were acquired every 5 s. Scale bar, 20 µm. n , Quantification of the fluorescence recovery in ROIs as shown in ( m ). Pre-bleaching mean fluorescence intensity (MFI) was set to 100% and post-bleaching MFI was set to 0%. n = 12 individual cells. A linear mixed model with time and treatment as fixed effects and replicate (n = 9) as a random effect demonstrates a significant (**p=0.00272) effect for treatment and treatment:timepoint interaction (***p=2.45 x 10 -8 ).

    Techniques Used: Immunofluorescence, Transduction, Infection, Expressing, Software, Staining, Western Blot, Luciferase, Functional Assay, Activity Assay, Transfection, Fluorescence

    a , Primary murine neurons were isolated from C57BL/6J mice at postnatal day 0–1. Neurons were transduced with AAV expressing TDP-43venus (green). After 3 days, cells were infected with HSV-1 and 17 h later fixed. Neurotracer (red), DAPI (blue). Scale bar, 10 µm. b , Analysis of TDP-43venus puncta per cell in ( a ). n = 31-43, three biological replicates. ***p<0.001, t test. c, Three-week-old human iPSC derived motoneurons (MNs) were HSV-1 GFP (green) infected and 17 h later stained for TDP-43 (red). DAPI (blue). Scale bar, 10 µm. d , Quantification of TDP-43 puncta in HSV-1 or mock infected MNs in ( c ). n = 64-68, two biological replicates. ***p<0.001, t test. e , Human iPSC derived brain organoids infected with HSV-1 GFP (green) for 48 h. Organoid slices were stained for TDP-43 (magenta), DAPI (blue). White arrows indicate TDP-43 delocalization in HSV-1 GFP positive cells. White squares indicate origin of inset. Scale bar, 50 µm. f , Zoom-in of representative cells in either condition in ( e ), white arrow indicate perinuclear TDP-43. Nuclei are framed by the dotted line. Scale bar, 5 µm. g , Quantification of TDP-43 puncta per cell in infected (HSV-1) and uninfected (mock) organoids (left) in ( e , f ), and analysis of TDP-43 puncta per cell per image in HSV-1 GFP infected organoids in GFP negative (HSV-1 −) or GFP positive (HSV-1 +) cells (right). n = 21-24, two independent replicates of two donors, ***p<0.001, t test. h , Representative immunofluorescence staining of C57BL/6J mice (10-week-old) that were intracerebrally infected with HSV-1 (1 x 10 5 PFU/mice) or inoculated with PBS (mock). At day 3 post-infection, mid-sagittal sections were prepared and stained for phosphorylated TDP-43 (pTDP-43, magenta), HSV-1 (green), and nuclei (DAPI, blue). White squares indicate origin of inset. Scale bar, 20 µm. i , Quantification of pTDP-43 mean fluorescence intensity (MFI) in 8-10 unbiasedly selected brain areas for each mouse. n = 3 mice per group, *p<0.05, t test. j , Scatter plot of pTDP-43 MFI/image (y-axis) against HSV-1 MFI/image (x-axis). Each dot represents one corresponding measurement from HSV-1 infected mice in ( i ). Grey areas represent averaged MFI in mock infected mice (background signal). The line indicates the linear regression including 95% confidence intervals. Spearman’s rank correlation test (r = 0.8661, ***p<0.001, n = 25). k , NF-L serum levels of C57BL/6J mice (16-week-old) at day 4 post-intracerebral HSV-1 infection (5 x 10 5 PFU/mice) or mock treatment, determined by ELISA. n = 6 mice per group, *p<0.05, t test. l , Representative immunohistochemistry of human liver section from an HSV-1 hepatitis patient. HSV-1 stained in brown, pTDP43 stained in magenta. Scale bar, 500 µm. Insets are indicated of infected (HSV-1 positive cells, brown) and non-infected areas. Arrows indicate pTDP-43 accumulations.
    Figure Legend Snippet: a , Primary murine neurons were isolated from C57BL/6J mice at postnatal day 0–1. Neurons were transduced with AAV expressing TDP-43venus (green). After 3 days, cells were infected with HSV-1 and 17 h later fixed. Neurotracer (red), DAPI (blue). Scale bar, 10 µm. b , Analysis of TDP-43venus puncta per cell in ( a ). n = 31-43, three biological replicates. ***p<0.001, t test. c, Three-week-old human iPSC derived motoneurons (MNs) were HSV-1 GFP (green) infected and 17 h later stained for TDP-43 (red). DAPI (blue). Scale bar, 10 µm. d , Quantification of TDP-43 puncta in HSV-1 or mock infected MNs in ( c ). n = 64-68, two biological replicates. ***p<0.001, t test. e , Human iPSC derived brain organoids infected with HSV-1 GFP (green) for 48 h. Organoid slices were stained for TDP-43 (magenta), DAPI (blue). White arrows indicate TDP-43 delocalization in HSV-1 GFP positive cells. White squares indicate origin of inset. Scale bar, 50 µm. f , Zoom-in of representative cells in either condition in ( e ), white arrow indicate perinuclear TDP-43. Nuclei are framed by the dotted line. Scale bar, 5 µm. g , Quantification of TDP-43 puncta per cell in infected (HSV-1) and uninfected (mock) organoids (left) in ( e , f ), and analysis of TDP-43 puncta per cell per image in HSV-1 GFP infected organoids in GFP negative (HSV-1 −) or GFP positive (HSV-1 +) cells (right). n = 21-24, two independent replicates of two donors, ***p<0.001, t test. h , Representative immunofluorescence staining of C57BL/6J mice (10-week-old) that were intracerebrally infected with HSV-1 (1 x 10 5 PFU/mice) or inoculated with PBS (mock). At day 3 post-infection, mid-sagittal sections were prepared and stained for phosphorylated TDP-43 (pTDP-43, magenta), HSV-1 (green), and nuclei (DAPI, blue). White squares indicate origin of inset. Scale bar, 20 µm. i , Quantification of pTDP-43 mean fluorescence intensity (MFI) in 8-10 unbiasedly selected brain areas for each mouse. n = 3 mice per group, *p<0.05, t test. j , Scatter plot of pTDP-43 MFI/image (y-axis) against HSV-1 MFI/image (x-axis). Each dot represents one corresponding measurement from HSV-1 infected mice in ( i ). Grey areas represent averaged MFI in mock infected mice (background signal). The line indicates the linear regression including 95% confidence intervals. Spearman’s rank correlation test (r = 0.8661, ***p<0.001, n = 25). k , NF-L serum levels of C57BL/6J mice (16-week-old) at day 4 post-intracerebral HSV-1 infection (5 x 10 5 PFU/mice) or mock treatment, determined by ELISA. n = 6 mice per group, *p<0.05, t test. l , Representative immunohistochemistry of human liver section from an HSV-1 hepatitis patient. HSV-1 stained in brown, pTDP43 stained in magenta. Scale bar, 500 µm. Insets are indicated of infected (HSV-1 positive cells, brown) and non-infected areas. Arrows indicate pTDP-43 accumulations.

    Techniques Used: Isolation, Transduction, Expressing, Infection, Derivative Assay, Staining, Immunofluorescence, Fluorescence, Enzyme-linked Immunosorbent Assay, Immunohistochemistry

    a , Schematic overview of the HSV-1 ICP0 gene with mutations to disrupt either RNF8 binding site (T67A), E3 ligase function (C116G/C156A), Cyclin D3 binding site (D199A) or CoREST interaction (D671A/E673A). b , Representative immunofluorescence images of H4 cells co-transfected with TDP-43venus (green) and either vector, wild-type (WT) ICP0 or indicated ICP0 mutant. Cells were fixed 24 h post-transfection and stained for PML (white), ICP0 (red) and DAPI (blue). Scale bar, 10 µm. c , Quantification of nuclear TDP-43venus foci area (µm 2 ) (top) and PML foci count (bottom) of co-transfected cells in (b) using Foci Analyzer (ImageJ). Lines represent mean±SEM, dots represent individual cells (n = 37-74) of three independent biological replicates. *p<0.05, ***p<0.001 Kruskal-Wallis test followed by Dunn’s multiple comparisons test. d , Scatter plot of total nuclear TDP-43venus foci size (y-axis) against the nuclear PML dot count (x-axis). Each dot represents one corresponding measurement from (c). Blue dots represent cells overexpressing ICP0 WT, black dots represent cells transfected with vector. For association testing, all events were taken together in Spearman’s rank correlation test (r = –0.54, ***p<0.001, n = 118). e , Representative immunofluorescence images of H4 cells transduced with lentiviruses encoding TDP-43venus (green). After 3 days, cells were infected with HSV-1 and 1 h post-infection treated with proteasome inhibitor MG132 or DMSO, respectively. Cells were fixed 17 h post-infection and stained for PML (white), ICP27 (red) and DAPI (blue). Scale bar, 10 µm. f , Quantification of PML foci (top) and total nuclear TDP-43venus foci area (µm 2 ) (bottom) in (e). Lines represent mean±SEM. Dots represent individual cells, n = 58-362, three independent biological replicates, ***p<0.001 Kruskal-Wallis test followed by Dunn’s multiple comparisons test. g , Representative immunoblots showing SUMOylation status of FLAG-tagged TDP-43 purified by anti-FLAG immunoprecipitation (IP) from whole cell lysates (WCL) of HEK293T cells at 40 h post-transfection. Cells were co-transfected with HSV-1 ICP0 and/or stimulated with arsenite (500 µM, 1 h), as indicated. IP and WCL was analyzed by immunoblotting. Blots were stained with anti-SUMO2, anti-FLAG, anti-HSV-1 ICP0 and anti-GAPDH. h , Quantification of the full SUMO-2 lane in the TDP-43 IP of ( g ) normalized to the vector control. n = 3, **p<0.01 paired t test.
    Figure Legend Snippet: a , Schematic overview of the HSV-1 ICP0 gene with mutations to disrupt either RNF8 binding site (T67A), E3 ligase function (C116G/C156A), Cyclin D3 binding site (D199A) or CoREST interaction (D671A/E673A). b , Representative immunofluorescence images of H4 cells co-transfected with TDP-43venus (green) and either vector, wild-type (WT) ICP0 or indicated ICP0 mutant. Cells were fixed 24 h post-transfection and stained for PML (white), ICP0 (red) and DAPI (blue). Scale bar, 10 µm. c , Quantification of nuclear TDP-43venus foci area (µm 2 ) (top) and PML foci count (bottom) of co-transfected cells in (b) using Foci Analyzer (ImageJ). Lines represent mean±SEM, dots represent individual cells (n = 37-74) of three independent biological replicates. *p<0.05, ***p<0.001 Kruskal-Wallis test followed by Dunn’s multiple comparisons test. d , Scatter plot of total nuclear TDP-43venus foci size (y-axis) against the nuclear PML dot count (x-axis). Each dot represents one corresponding measurement from (c). Blue dots represent cells overexpressing ICP0 WT, black dots represent cells transfected with vector. For association testing, all events were taken together in Spearman’s rank correlation test (r = –0.54, ***p<0.001, n = 118). e , Representative immunofluorescence images of H4 cells transduced with lentiviruses encoding TDP-43venus (green). After 3 days, cells were infected with HSV-1 and 1 h post-infection treated with proteasome inhibitor MG132 or DMSO, respectively. Cells were fixed 17 h post-infection and stained for PML (white), ICP27 (red) and DAPI (blue). Scale bar, 10 µm. f , Quantification of PML foci (top) and total nuclear TDP-43venus foci area (µm 2 ) (bottom) in (e). Lines represent mean±SEM. Dots represent individual cells, n = 58-362, three independent biological replicates, ***p<0.001 Kruskal-Wallis test followed by Dunn’s multiple comparisons test. g , Representative immunoblots showing SUMOylation status of FLAG-tagged TDP-43 purified by anti-FLAG immunoprecipitation (IP) from whole cell lysates (WCL) of HEK293T cells at 40 h post-transfection. Cells were co-transfected with HSV-1 ICP0 and/or stimulated with arsenite (500 µM, 1 h), as indicated. IP and WCL was analyzed by immunoblotting. Blots were stained with anti-SUMO2, anti-FLAG, anti-HSV-1 ICP0 and anti-GAPDH. h , Quantification of the full SUMO-2 lane in the TDP-43 IP of ( g ) normalized to the vector control. n = 3, **p<0.01 paired t test.

    Techniques Used: Binding Assay, Immunofluorescence, Transfection, Plasmid Preparation, Mutagenesis, Staining, Transduction, Infection, Western Blot, Purification, Immunoprecipitation, Control

    Related Articles

    Immunofluorescence:

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    Article Title: Imbalanced chromatin distribution in cellular senescence specifies paraspeckle dynamics
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    Article Title: ALS-linked mutant TDP-43 in oligodendrocytes induces oligodendrocyte damage and exacerbates motor dysfunction in mice
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    Article Title: ALS-linked mutant TDP-43 in oligodendrocytes induces oligodendrocyte damage and exacerbates motor dysfunction in mice.
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    Incubation:

    Article Title: Imbalanced chromatin distribution in cellular senescence specifies paraspeckle dynamics.
    Article Snippet: After a brief rinse with RNase-free PBS, cells were blocked with RNase-free PBS containing 1% bovine serum albumin (BSA) (GeneDepot) for 30 min at room temperature. .. For sequential immunofluorescence of NONO or TDP-43, cells were incubated overnight at 4 °C with the following primary antibodies diluted in RNase-free PBS containing 1% BSA: mouse monoclonal anti-NONO (1:300; Santa Cruz, sc-376804) or rabbit polyclonal anti-TDP-43 (1:300; Proteintech, 10,782–2-AP). .. After three 5-min washes with RNase-free PBS, cells were incubated for 1 h at room temperature with the corresponding secondary antibodies diluted in RNase-free PBS containing 1% BSA: Alexa Fluor 488-conjugated goat anti-mouse IgG (H + L) or Alexa Fluor 647-conjugated goat anti-rabbit IgG (1:300; Invitrogen).

    Article Title: Imbalanced chromatin distribution in cellular senescence specifies paraspeckle dynamics
    Article Snippet: After a brief rinse with RNase-free PBS, cells were blocked with RNase-free PBS containing 1% bovine serum albumin (BSA) (GeneDepot) for 30 min at room temperature. .. For sequential immunofluorescence of NONO or TDP-43, cells were incubated overnight at 4 °C with the following primary antibodies diluted in RNase-free PBS containing 1% BSA: mouse monoclonal anti-NONO (1:300; Santa Cruz, sc-376804) or rabbit polyclonal anti-TDP-43 (1:300; Proteintech, 10,782–2-AP). .. After three 5-min washes with RNase-free PBS, cells were incubated for 1 h at room temperature with the corresponding secondary antibodies diluted in RNase-free PBS containing 1% BSA: Alexa Fluor 488-conjugated goat anti-mouse IgG (H + L) or Alexa Fluor 647-conjugated goat anti-rabbit IgG (1:300; Invitrogen).

    Western Blot:

    Article Title: HIV-1 Vpu induces neurotoxicity by promoting Caspase 3-dependent cleavage of TDP-43
    Article Snippet: Mouse monoclonal anti-TDP-43 (WB:1/5000,IF:1/500) , Abcam , Cat#ab104223. .. Rabbit polyclonal anti-TDP-43 (WB:1/2000,IF:1/3000) , Proteintech , Cat#10782-2-AP. .. Rabbit polyclonal anti-TDP-43 (C-terminal) (WB:1/500, IF:1/2000) , Proteintech , Cat#12892-1-AP.

    Article Title: TBK1 eliminates aggregation-prone monomeric TDP-43 through the IFNβ-immunoproteasome pathway
    Article Snippet: .. The antibodies used in this study were as follows: rabbit monoclonal anti-TBK1 (D1B4) (1:1000; #3504S, Cell Signaling Technology, Danvers, MA, USA), rabbit polyclonal anti-DDDDK-tag (1:4000 for immunoblotting (IB), 1:2500 for immunofluorescence (IF); #PM020, Medical & Biological Laboratories, Tokyo, Japan), mouse monoclonal anti-phosphorylated TDP-43 Ser409/410 (11-9) (1:2000 for IB, 1:2500 for IF; #TIP-PTD-M01, Cosmo Bio, Tokyo, Japan), mouse monoclonal anti-β-actin (1:5000; #A5441, Sigma-Aldrich, St. Louis, MO, USA), rat monoclonal anti-phosphorylated-p62 Ser403 (4F6) (1:500; #D343-3, Medical & Biological Laboratories), rabbit polyclonal anti-LC3 (1:1000; #PM020, Medical & Biological Laboratories), mouse monoclonal anti-Myc-tag (9B11) (1:1000; #2276S, Cell Signaling Technology), rabbit polyclonal anti-RFP (1:1000; #PM005, Medical & Biological Laboratories), mouse monoclonal anti-NeuN (A60) (1:500; #MAB377, Merck Millipore, Burlington, MA, USA), goat polyclonal anti-Choline Acetyltransferase (1:100; #AB144P, Merck Millipore), mouse monoclonal anti-IFNAR1 (H-11) (1:50; #sc-7391, Santa Cruz Biotechnology, Santa Cruz, CA, USA), rat monoclonal anti-CTIP2 (25B6) (1:500; #ab18465, abcam, Cambridge, UK), rabbit polyclonal anti-TDP-43 (1:1000; #10782-2-AP, Proteintech, Rosemont, IL, USA), mouse monoclonal anti-ISG15 (F-9) (1:250; #sc-166755, Santa Cruz Biotechnology), mouse monoclonal anti-PSMB8 (D-2) (1:500 for IB; #sc374089, Santa Cruz Biotechnology), mouse monoclonal anti-PSMB9 (G-2) (1:500; #sc373971, Santa Cruz Biotechnology), rabbit monoclonal anti-PSMB8 (D1K7X) (1:250 for IF; #13635S, Cell Signaling Technology), rabbit polyclonal anti-human SOD1 (raised in our laboratory against a recombinant human SOD1 peptide (aa 24-36)), rabbit polyclonal anti-p62 (1:1000; #PM045, Medical & Biological Laboratories), mouse monoclonal anti-Multi Ubiquitin (FK2) (1:1000; #D058-3, Medical & Biological Laboratories), and rabbit polyclonal anti-phosphorylated STING Ser366 (1:100; #AF7416, Affinity Biosciences, Cincinnati, OH, USA). .. Alexa Fluor– conjugated and horseradish peroxidase (HRP)-conjugated secondary antibodies were purchased from Thermo Fisher Scientific (Waltham, MA, USA) and Jackson ImmunoResearch Laboratories (West Grove, PA, USA).

    Article Title: ALS-linked mutant TDP-43 in oligodendrocytes induces oligodendrocyte damage and exacerbates motor dysfunction in mice
    Article Snippet: .. The antibodies used in this study were as follows: mouse monoclonal anti-Myc-Tag (9B11) (1:1000 for immunoblotting, 1:500 for immunofluorescence; #2276S, Cell Signaling Technology, Danvers, MA, USA), mouse monoclonal anti-TDP-43 (3H8) (1:1000; #MABN45, Merck Millipore, Burlington, MA, USA), mouse monoclonal anti-β-actin (1:5000; #A5441, Sigma-Aldrich, St. Louis, MO, USA), goat polyclonal anti-PDGFRα (1:200; #AF1062, R&D Systems, Minneapolis, MN, USA), mouse monoclonal anti-APC (cc-1) (1:500; #OP80, Merck Millipore), rabbit polyclonal anti-Myc-Tag (1:500; #562, Medical & Biological Laboratories, Tokyo, Japan), goat polyclonal anti-AIF-1/Iba1 (1:250; #NB100-1028, Novus Biologicals, Littleton, CO, USA), mouse monoclonal anti-GFAP (1:500; #G3893, Sigma-Aldrich), rabbit polyclonal anti-Iba1 (1:500; #019-19741, Wako, Osaka, Japan), rabbit polyclonal anti-GFAP (1:200; #MSFR101830, Nittobo Medical, Tokyo, Japan), rabbit polyclonal anti-TDP-43 (1:500; #10782-2-AP, Proteintech, Rosemont, IL, USA), goat polyclonal anti-Choline Acetyltransferase (1:100; #AB144P, Sigma-Aldrich), rabbit polyclonal anti-Cleaved Caspase-3 (Asp175) (1:200; #9661, Cell Signaling Technology), rat monoclonal anti-Mac2 (1:500; #CL8942AP, Cedarlane Laboratories, Burlington, Canada), mouse monoclonal anti-b-Galactosidase (1:300; #Z3781, Promega, Madison, WI, USA), rabbit polyclonal anti-Olig2 (1:500; #AB9610, Merck Millipore), rabbit monoclonal anti-Mbp (1:1000; #ab218011, Abcam), rabbit polyclonal anti-Mbp (1:200; #AB980, Merck Millipore), rat monoclonal anti-CD16/CD32 (1:250; #14-0161-82, Thermo Fisher Scientific, Waltham, MA, USA), and mouse monoclonal anti-O1 (1:50; #MAB344, Merck Millipore). .. Alexa Fluor–conjugated and horseradish peroxidase (HRP)-conjugated secondary antibodies were purchased from Thermo Fisher Scientific and Jackson ImmunoResearch Laboratories (West Grove, PA, USA).

    Article Title: ALS-linked mutant TDP-43 in oligodendrocytes induces oligodendrocyte damage and exacerbates motor dysfunction in mice.
    Article Snippet: .. The antibodies used in this study were as follows: mouse monoclonal anti-Myc-Tag (9B11) (1:1000 for immunoblotting, 1:500 for immunofluorescence; #2276S, Cell Signaling Technology, Danvers, MA, USA), mouse monoclonal anti-TDP-43 (3H8) (1:1000; #MABN45, Merck Millipore, Burlington, MA, USA), mouse monoclonal anti-β-actin (1:5000; #A5441, Sigma-Aldrich, St. Louis, MO, USA), goat polyclonal anti-PDGFRα (1:200; #AF1062, R&D Systems, Minneapolis, MN, USA), mouse monoclonal anti-APC (cc-1) (1:500; #OP80, Merck Millipore), rabbit polyclonal anti-Myc-Tag (1:500; #562, Medical & Biological Laboratories, Tokyo, Japan), goat polyclonal anti-AIF-1/Iba1 (1:250; #NB100-1028, Novus Biologicals, Littleton, CO, USA), mouse monoclonal antiGFAP (1:500; #G3893, Sigma-Aldrich), rabbit polyclonal anti-Iba1 (1:500; #019-19741, Wako, Osaka, Japan), rabbit polyclonal anti-GFAP (1:200; #MSFR101830, Nittobo Medical, Tokyo, Japan), rabbit polyclonal anti-TDP-43 (1:500; #10782-2-AP, Proteintech, Rosemont, IL, USA), goat polyclonal anti-Choline Acetyltransferase (1:100; #AB144P, Sigma-Aldrich), rabbit polyclonal anti-Cleaved Caspase-3 (Asp175) (1:200; #9661, Cell Signaling Technology), rat monoclonal anti-Mac2 (1:500; #CL8942AP, Cedarlane Laboratories, Burlington, Canada), mouse monoclonal anti-b-Galactosidase (1:300; #Z3781, Promega, Madison, WI, USA), rabbit polyclonal anti-Olig2 (1:500; #AB9610, Merck Millipore), rabbit monoclonal anti-Mbp (1:1000; #ab218011, Abcam), rabbit polyclonal anti-Mbp (1:200; #AB980, Merck Millipore), rat monoclonal anti-CD16/CD32 (1:250; #14-0161-82, Thermo Fisher Scientific, Waltham, MA, USA), and mouse monoclonal anti-O1 (1:50; #MAB344, Merck Millipore). .. Alexa Fluor–conjugated and horseradish peroxidase (HRP)conjugated secondary antibodies were purchased from Thermo Fisher Scientific and Jackson ImmunoResearch Laboratories (West Grove, PA, USA).

    Recombinant:

    Article Title: TBK1 eliminates aggregation-prone monomeric TDP-43 through the IFNβ-immunoproteasome pathway
    Article Snippet: .. The antibodies used in this study were as follows: rabbit monoclonal anti-TBK1 (D1B4) (1:1000; #3504S, Cell Signaling Technology, Danvers, MA, USA), rabbit polyclonal anti-DDDDK-tag (1:4000 for immunoblotting (IB), 1:2500 for immunofluorescence (IF); #PM020, Medical & Biological Laboratories, Tokyo, Japan), mouse monoclonal anti-phosphorylated TDP-43 Ser409/410 (11-9) (1:2000 for IB, 1:2500 for IF; #TIP-PTD-M01, Cosmo Bio, Tokyo, Japan), mouse monoclonal anti-β-actin (1:5000; #A5441, Sigma-Aldrich, St. Louis, MO, USA), rat monoclonal anti-phosphorylated-p62 Ser403 (4F6) (1:500; #D343-3, Medical & Biological Laboratories), rabbit polyclonal anti-LC3 (1:1000; #PM020, Medical & Biological Laboratories), mouse monoclonal anti-Myc-tag (9B11) (1:1000; #2276S, Cell Signaling Technology), rabbit polyclonal anti-RFP (1:1000; #PM005, Medical & Biological Laboratories), mouse monoclonal anti-NeuN (A60) (1:500; #MAB377, Merck Millipore, Burlington, MA, USA), goat polyclonal anti-Choline Acetyltransferase (1:100; #AB144P, Merck Millipore), mouse monoclonal anti-IFNAR1 (H-11) (1:50; #sc-7391, Santa Cruz Biotechnology, Santa Cruz, CA, USA), rat monoclonal anti-CTIP2 (25B6) (1:500; #ab18465, abcam, Cambridge, UK), rabbit polyclonal anti-TDP-43 (1:1000; #10782-2-AP, Proteintech, Rosemont, IL, USA), mouse monoclonal anti-ISG15 (F-9) (1:250; #sc-166755, Santa Cruz Biotechnology), mouse monoclonal anti-PSMB8 (D-2) (1:500 for IB; #sc374089, Santa Cruz Biotechnology), mouse monoclonal anti-PSMB9 (G-2) (1:500; #sc373971, Santa Cruz Biotechnology), rabbit monoclonal anti-PSMB8 (D1K7X) (1:250 for IF; #13635S, Cell Signaling Technology), rabbit polyclonal anti-human SOD1 (raised in our laboratory against a recombinant human SOD1 peptide (aa 24-36)), rabbit polyclonal anti-p62 (1:1000; #PM045, Medical & Biological Laboratories), mouse monoclonal anti-Multi Ubiquitin (FK2) (1:1000; #D058-3, Medical & Biological Laboratories), and rabbit polyclonal anti-phosphorylated STING Ser366 (1:100; #AF7416, Affinity Biosciences, Cincinnati, OH, USA). .. Alexa Fluor– conjugated and horseradish peroxidase (HRP)-conjugated secondary antibodies were purchased from Thermo Fisher Scientific (Waltham, MA, USA) and Jackson ImmunoResearch Laboratories (West Grove, PA, USA).

    Ubiquitin Proteomics:

    Article Title: TBK1 eliminates aggregation-prone monomeric TDP-43 through the IFNβ-immunoproteasome pathway
    Article Snippet: .. The antibodies used in this study were as follows: rabbit monoclonal anti-TBK1 (D1B4) (1:1000; #3504S, Cell Signaling Technology, Danvers, MA, USA), rabbit polyclonal anti-DDDDK-tag (1:4000 for immunoblotting (IB), 1:2500 for immunofluorescence (IF); #PM020, Medical & Biological Laboratories, Tokyo, Japan), mouse monoclonal anti-phosphorylated TDP-43 Ser409/410 (11-9) (1:2000 for IB, 1:2500 for IF; #TIP-PTD-M01, Cosmo Bio, Tokyo, Japan), mouse monoclonal anti-β-actin (1:5000; #A5441, Sigma-Aldrich, St. Louis, MO, USA), rat monoclonal anti-phosphorylated-p62 Ser403 (4F6) (1:500; #D343-3, Medical & Biological Laboratories), rabbit polyclonal anti-LC3 (1:1000; #PM020, Medical & Biological Laboratories), mouse monoclonal anti-Myc-tag (9B11) (1:1000; #2276S, Cell Signaling Technology), rabbit polyclonal anti-RFP (1:1000; #PM005, Medical & Biological Laboratories), mouse monoclonal anti-NeuN (A60) (1:500; #MAB377, Merck Millipore, Burlington, MA, USA), goat polyclonal anti-Choline Acetyltransferase (1:100; #AB144P, Merck Millipore), mouse monoclonal anti-IFNAR1 (H-11) (1:50; #sc-7391, Santa Cruz Biotechnology, Santa Cruz, CA, USA), rat monoclonal anti-CTIP2 (25B6) (1:500; #ab18465, abcam, Cambridge, UK), rabbit polyclonal anti-TDP-43 (1:1000; #10782-2-AP, Proteintech, Rosemont, IL, USA), mouse monoclonal anti-ISG15 (F-9) (1:250; #sc-166755, Santa Cruz Biotechnology), mouse monoclonal anti-PSMB8 (D-2) (1:500 for IB; #sc374089, Santa Cruz Biotechnology), mouse monoclonal anti-PSMB9 (G-2) (1:500; #sc373971, Santa Cruz Biotechnology), rabbit monoclonal anti-PSMB8 (D1K7X) (1:250 for IF; #13635S, Cell Signaling Technology), rabbit polyclonal anti-human SOD1 (raised in our laboratory against a recombinant human SOD1 peptide (aa 24-36)), rabbit polyclonal anti-p62 (1:1000; #PM045, Medical & Biological Laboratories), mouse monoclonal anti-Multi Ubiquitin (FK2) (1:1000; #D058-3, Medical & Biological Laboratories), and rabbit polyclonal anti-phosphorylated STING Ser366 (1:100; #AF7416, Affinity Biosciences, Cincinnati, OH, USA). .. Alexa Fluor– conjugated and horseradish peroxidase (HRP)-conjugated secondary antibodies were purchased from Thermo Fisher Scientific (Waltham, MA, USA) and Jackson ImmunoResearch Laboratories (West Grove, PA, USA).

    other:

    Article Title: Long noncoding RNAs heat shock RNA omega nucleates TBPH and promotes intestinal stem cell differentiation upon heat shock
    Article Snippet: The following antibodies were used: rabbit polyclonal anti-TDP-43 (1:100; Proteintech #10782-2-AP); rabbit polyclonal anti-Pdm1 (1:100; Bioworlde #NCP0381P); Goat anti-Rabbit IgG, Alexa Fluor 568 (1:1000; Invitrogen #A-21124); Goat anti-Rabbit IgG, Alexa Fluor 647 (1:1000; Invitrogen #A-21244).



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    96
    Proteintech rabbit polyclonal anti tbph
    a , Immunofluorescence of H4 cells overexpressing TDP-43venus (green) via lentivirus transduction were after 3 days, infected with HSV-1 (MOI 0.3). Cells were fixed after 17 h. ICP27 (red), DAPI (blue), actin (white). Scale bar, 10 µm. b , Analysis of nuclear TDP-43venus foci area in ( a ) using foci analyzer. Lines represent mean±SEM, n = 101-110, three independent biological replicates. ***p<0.001, t test. c , Representative immunofluorescence of H4 cells transduced with AAV expressing TDP-43venus (green). 3 days post-transduction, cells were infected with HSV-1 (MOI 0.3). 17 h post-HSV-1 infection, cells were fixed. DAPI (blue). White squares indicate origin of inset. Scale bar, 200 µm. d , Quantification of the total cytosolic TDP-43venus signal divided by the cell number per image as assessed by DAPI count, using Imaris software. Dots represent individual replicates. n = 9, three independent biological replicates. **p<0.01, paired t test. e , Representative immunofluorescent images of H4 cells transduced with lentiviruses expressing TDP-43venus (green) and 3 days later, infected with HSV-1 (MOI 0.3). Cells were fixed 17 h post-HSV-1 infection and stained for pTDP-43 (red), ICP27 (orange), and DAPI (blue). Scale bar, 10 µm. f , Quantification of the pTDP-43 area after thresholding for pTDP-43 dots (ImageJ). Lines represent mean±SEM, n = 60, three independent biological replicates. ***p<0.001, t test. g , Representative immunoblot <t>of</t> <t>TDP-43</t> and GAPDH in H4 cells transduced with AAV expressing TDP-43venus for 3 days and infected with HSV-1 for 17 h. Cells were harvested and separated into whole cell lysate (WCL), nuclear (N) and cytosolic (C) fractions. Stained with anti-TDP-43, anti-Lamin, and anti-GAPDH. h , Quantification of the 35 kDa C-terminal fragment (CTF35) WCL band intensity in ( g ). Normalized to respective GAPDH band. n = 4, *p<0.05, paired t test. i , Representative immunoblots of HEK293T cells transduced with AAV-TDP-43venus (3 d) and infected with HSV-1 (MOI 0.3, 17 h). Fractions of the whole cell lysate (WCL) were separated into soluble (S) and insoluble (I) components. j , Western blot band intensities of soluble and insoluble TDP-43venus in ( i ) displayed as ratio. n = 6, *p<0.05, paired t test. k , Schematic representation of the TDP-43 split luciferase system. Upon TDP-43 oligomerization the fusion of L1 and L2 results in a functional luciferase. l , Quantification of luciferase activity in HEK293T cells co-transfected with split luciferase: TDP43-L1 and TDP43-L2. 24 h post-transfection cells were infected with HSV-1 (MOI 0.3). After 48 h post-infection cells were lysed and luciferase activity was analyzed. Bars represent mean±SEM of n = 4. *p<0.05, t test, m , Fluorescence recovery after photobleaching (FRAP) of H4 cells transduced with lentiviruses expressing TDP-43halo (red) and infected with HSV-1 GFP. 17 h post-infection, GFP positive cells with TDP-43halo delocalization were selected and analyzed. High laser intensity (100%) was applied to the region of interest (ROI) for 5 s. Subsequently, 10 images were acquired every 5 s. Scale bar, 20 µm. n , Quantification of the fluorescence recovery in ROIs as shown in ( m ). Pre-bleaching mean fluorescence intensity (MFI) was set to 100% and post-bleaching MFI was set to 0%. n = 12 individual cells. A linear mixed model with time and treatment as fixed effects and replicate (n = 9) as a random effect demonstrates a significant (**p=0.00272) effect for treatment and treatment:timepoint interaction (***p=2.45 x 10 -8 ).
    Rabbit Polyclonal Anti Tbph, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+tdp+43/TDP-43+Polyclonal+antibody/bio_rxiv__64898__2026__02__27__708457-24-12-16
    Average 96 stars, based on 1 article reviews
    rabbit polyclonal anti tbph - by Bioz Stars, 2026-09
    96/100 stars
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    rabbit  (Proteintech)
    96
    Proteintech rabbit
    a , Immunofluorescence of H4 cells overexpressing TDP-43venus (green) via lentivirus transduction were after 3 days, infected with HSV-1 (MOI 0.3). Cells were fixed after 17 h. ICP27 (red), DAPI (blue), actin (white). Scale bar, 10 µm. b , Analysis of nuclear TDP-43venus foci area in ( a ) using foci analyzer. Lines represent mean±SEM, n = 101-110, three independent biological replicates. ***p<0.001, t test. c , Representative immunofluorescence of H4 cells transduced with AAV expressing TDP-43venus (green). 3 days post-transduction, cells were infected with HSV-1 (MOI 0.3). 17 h post-HSV-1 infection, cells were fixed. DAPI (blue). White squares indicate origin of inset. Scale bar, 200 µm. d , Quantification of the total cytosolic TDP-43venus signal divided by the cell number per image as assessed by DAPI count, using Imaris software. Dots represent individual replicates. n = 9, three independent biological replicates. **p<0.01, paired t test. e , Representative immunofluorescent images of H4 cells transduced with lentiviruses expressing TDP-43venus (green) and 3 days later, infected with HSV-1 (MOI 0.3). Cells were fixed 17 h post-HSV-1 infection and stained for pTDP-43 (red), ICP27 (orange), and DAPI (blue). Scale bar, 10 µm. f , Quantification of the pTDP-43 area after thresholding for pTDP-43 dots (ImageJ). Lines represent mean±SEM, n = 60, three independent biological replicates. ***p<0.001, t test. g , Representative immunoblot <t>of</t> <t>TDP-43</t> and GAPDH in H4 cells transduced with AAV expressing TDP-43venus for 3 days and infected with HSV-1 for 17 h. Cells were harvested and separated into whole cell lysate (WCL), nuclear (N) and cytosolic (C) fractions. Stained with anti-TDP-43, anti-Lamin, and anti-GAPDH. h , Quantification of the 35 kDa C-terminal fragment (CTF35) WCL band intensity in ( g ). Normalized to respective GAPDH band. n = 4, *p<0.05, paired t test. i , Representative immunoblots of HEK293T cells transduced with AAV-TDP-43venus (3 d) and infected with HSV-1 (MOI 0.3, 17 h). Fractions of the whole cell lysate (WCL) were separated into soluble (S) and insoluble (I) components. j , Western blot band intensities of soluble and insoluble TDP-43venus in ( i ) displayed as ratio. n = 6, *p<0.05, paired t test. k , Schematic representation of the TDP-43 split luciferase system. Upon TDP-43 oligomerization the fusion of L1 and L2 results in a functional luciferase. l , Quantification of luciferase activity in HEK293T cells co-transfected with split luciferase: TDP43-L1 and TDP43-L2. 24 h post-transfection cells were infected with HSV-1 (MOI 0.3). After 48 h post-infection cells were lysed and luciferase activity was analyzed. Bars represent mean±SEM of n = 4. *p<0.05, t test, m , Fluorescence recovery after photobleaching (FRAP) of H4 cells transduced with lentiviruses expressing TDP-43halo (red) and infected with HSV-1 GFP. 17 h post-infection, GFP positive cells with TDP-43halo delocalization were selected and analyzed. High laser intensity (100%) was applied to the region of interest (ROI) for 5 s. Subsequently, 10 images were acquired every 5 s. Scale bar, 20 µm. n , Quantification of the fluorescence recovery in ROIs as shown in ( m ). Pre-bleaching mean fluorescence intensity (MFI) was set to 100% and post-bleaching MFI was set to 0%. n = 12 individual cells. A linear mixed model with time and treatment as fixed effects and replicate (n = 9) as a random effect demonstrates a significant (**p=0.00272) effect for treatment and treatment:timepoint interaction (***p=2.45 x 10 -8 ).
    Rabbit, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+tdp+43/TDP-43+Polyclonal+antibody/pmc12922372-8-7-2
    Average 96 stars, based on 1 article reviews
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    rabbit polyclonal anti tdp 43 antibody  (Cell Signaling Technology Inc)
    93
    Cell Signaling Technology Inc rabbit polyclonal anti tdp 43 antibody
    Oxidative stress induced the conformational change of G4s. ( A ) Flowchart of the cellular oxidative stress experiment. Twelve hours after the addition of hydrogen peroxide, the GOTO neuroblastoma cells were fixed and immunostained. Then, total RNA was purified from the cells and used for the TO1B turn-on assay. ( B ) Representative immunofluorescence images <t>showing</t> <t>TDP-43</t> and G4 signals detected using anti-TDP-43 and anti-G4 antibodies. Single-channel images and DAPI staining are shown, along with merged views. For quantification (bottom panels), the fluorescence intensities of TDP-43 and G4 were measured in ten cells per condition; values are normalized to untreated cells. Data represent mean ± SEM. Statistical significance was assessed using a two-tailed Student’s t-test (* P < 0.05). ( C ) Binding model of G4BPs. The proteins are classified into two groups: those that bind to prevent G4 formation (group 1) and those that stabilize G4 structures (group 2). ( D ) Measurement of G4 levels using the G4-specific fluorescent sensor TO1B. The fluorescence emission spectra of TO1B were measured after adding RNA extracted from untreated cells and cells oxidatively stressed with 20, 40, and 80 µM hydrogen peroxide. The G4-independent fluorescence intensity is also shown as a control. The graph on the right displays the average fluorescence intensity at 530 nm. The experiments were performed in triplicate, and the values on the y-axis represent the mean ± SEM. Statistical significance was determined using a two-tailed Student’s t -test. * P < 0.05.
    Rabbit Polyclonal Anti Tdp 43 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+tdp+43/TDP43+(A260)+Antibody/pmc12982756-229-13-17
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    rabbit polyclonal anti tdp 43 antibody 16  (Proteintech)
    94
    Proteintech rabbit polyclonal anti tdp 43 antibody 16
    Oxidative stress induced the conformational change of G4s. ( A ) Flowchart of the cellular oxidative stress experiment. Twelve hours after the addition of hydrogen peroxide, the GOTO neuroblastoma cells were fixed and immunostained. Then, total RNA was purified from the cells and used for the TO1B turn-on assay. ( B ) Representative immunofluorescence images <t>showing</t> <t>TDP-43</t> and G4 signals detected using anti-TDP-43 and anti-G4 antibodies. Single-channel images and DAPI staining are shown, along with merged views. For quantification (bottom panels), the fluorescence intensities of TDP-43 and G4 were measured in ten cells per condition; values are normalized to untreated cells. Data represent mean ± SEM. Statistical significance was assessed using a two-tailed Student’s t-test (* P < 0.05). ( C ) Binding model of G4BPs. The proteins are classified into two groups: those that bind to prevent G4 formation (group 1) and those that stabilize G4 structures (group 2). ( D ) Measurement of G4 levels using the G4-specific fluorescent sensor TO1B. The fluorescence emission spectra of TO1B were measured after adding RNA extracted from untreated cells and cells oxidatively stressed with 20, 40, and 80 µM hydrogen peroxide. The G4-independent fluorescence intensity is also shown as a control. The graph on the right displays the average fluorescence intensity at 530 nm. The experiments were performed in triplicate, and the values on the y-axis represent the mean ± SEM. Statistical significance was determined using a two-tailed Student’s t -test. * P < 0.05.
    Rabbit Polyclonal Anti Tdp 43 Antibody 16, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+tdp+43/TDP-43+Antibody/pm41678358-67-8-14
    Average 94 stars, based on 1 article reviews
    rabbit polyclonal anti tdp 43 antibody 16 - by Bioz Stars, 2026-09
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    Image Search Results


    a , Immunofluorescence of H4 cells overexpressing TDP-43venus (green) via lentivirus transduction were after 3 days, infected with HSV-1 (MOI 0.3). Cells were fixed after 17 h. ICP27 (red), DAPI (blue), actin (white). Scale bar, 10 µm. b , Analysis of nuclear TDP-43venus foci area in ( a ) using foci analyzer. Lines represent mean±SEM, n = 101-110, three independent biological replicates. ***p<0.001, t test. c , Representative immunofluorescence of H4 cells transduced with AAV expressing TDP-43venus (green). 3 days post-transduction, cells were infected with HSV-1 (MOI 0.3). 17 h post-HSV-1 infection, cells were fixed. DAPI (blue). White squares indicate origin of inset. Scale bar, 200 µm. d , Quantification of the total cytosolic TDP-43venus signal divided by the cell number per image as assessed by DAPI count, using Imaris software. Dots represent individual replicates. n = 9, three independent biological replicates. **p<0.01, paired t test. e , Representative immunofluorescent images of H4 cells transduced with lentiviruses expressing TDP-43venus (green) and 3 days later, infected with HSV-1 (MOI 0.3). Cells were fixed 17 h post-HSV-1 infection and stained for pTDP-43 (red), ICP27 (orange), and DAPI (blue). Scale bar, 10 µm. f , Quantification of the pTDP-43 area after thresholding for pTDP-43 dots (ImageJ). Lines represent mean±SEM, n = 60, three independent biological replicates. ***p<0.001, t test. g , Representative immunoblot of TDP-43 and GAPDH in H4 cells transduced with AAV expressing TDP-43venus for 3 days and infected with HSV-1 for 17 h. Cells were harvested and separated into whole cell lysate (WCL), nuclear (N) and cytosolic (C) fractions. Stained with anti-TDP-43, anti-Lamin, and anti-GAPDH. h , Quantification of the 35 kDa C-terminal fragment (CTF35) WCL band intensity in ( g ). Normalized to respective GAPDH band. n = 4, *p<0.05, paired t test. i , Representative immunoblots of HEK293T cells transduced with AAV-TDP-43venus (3 d) and infected with HSV-1 (MOI 0.3, 17 h). Fractions of the whole cell lysate (WCL) were separated into soluble (S) and insoluble (I) components. j , Western blot band intensities of soluble and insoluble TDP-43venus in ( i ) displayed as ratio. n = 6, *p<0.05, paired t test. k , Schematic representation of the TDP-43 split luciferase system. Upon TDP-43 oligomerization the fusion of L1 and L2 results in a functional luciferase. l , Quantification of luciferase activity in HEK293T cells co-transfected with split luciferase: TDP43-L1 and TDP43-L2. 24 h post-transfection cells were infected with HSV-1 (MOI 0.3). After 48 h post-infection cells were lysed and luciferase activity was analyzed. Bars represent mean±SEM of n = 4. *p<0.05, t test, m , Fluorescence recovery after photobleaching (FRAP) of H4 cells transduced with lentiviruses expressing TDP-43halo (red) and infected with HSV-1 GFP. 17 h post-infection, GFP positive cells with TDP-43halo delocalization were selected and analyzed. High laser intensity (100%) was applied to the region of interest (ROI) for 5 s. Subsequently, 10 images were acquired every 5 s. Scale bar, 20 µm. n , Quantification of the fluorescence recovery in ROIs as shown in ( m ). Pre-bleaching mean fluorescence intensity (MFI) was set to 100% and post-bleaching MFI was set to 0%. n = 12 individual cells. A linear mixed model with time and treatment as fixed effects and replicate (n = 9) as a random effect demonstrates a significant (**p=0.00272) effect for treatment and treatment:timepoint interaction (***p=2.45 x 10 -8 ).

    Journal: bioRxiv

    Article Title: Herpes simplex virus infection promotes ALS pathology through ICP0-mediated PML body disruption

    doi: 10.64898/2026.03.27.714707

    Figure Lengend Snippet: a , Immunofluorescence of H4 cells overexpressing TDP-43venus (green) via lentivirus transduction were after 3 days, infected with HSV-1 (MOI 0.3). Cells were fixed after 17 h. ICP27 (red), DAPI (blue), actin (white). Scale bar, 10 µm. b , Analysis of nuclear TDP-43venus foci area in ( a ) using foci analyzer. Lines represent mean±SEM, n = 101-110, three independent biological replicates. ***p<0.001, t test. c , Representative immunofluorescence of H4 cells transduced with AAV expressing TDP-43venus (green). 3 days post-transduction, cells were infected with HSV-1 (MOI 0.3). 17 h post-HSV-1 infection, cells were fixed. DAPI (blue). White squares indicate origin of inset. Scale bar, 200 µm. d , Quantification of the total cytosolic TDP-43venus signal divided by the cell number per image as assessed by DAPI count, using Imaris software. Dots represent individual replicates. n = 9, three independent biological replicates. **p<0.01, paired t test. e , Representative immunofluorescent images of H4 cells transduced with lentiviruses expressing TDP-43venus (green) and 3 days later, infected with HSV-1 (MOI 0.3). Cells were fixed 17 h post-HSV-1 infection and stained for pTDP-43 (red), ICP27 (orange), and DAPI (blue). Scale bar, 10 µm. f , Quantification of the pTDP-43 area after thresholding for pTDP-43 dots (ImageJ). Lines represent mean±SEM, n = 60, three independent biological replicates. ***p<0.001, t test. g , Representative immunoblot of TDP-43 and GAPDH in H4 cells transduced with AAV expressing TDP-43venus for 3 days and infected with HSV-1 for 17 h. Cells were harvested and separated into whole cell lysate (WCL), nuclear (N) and cytosolic (C) fractions. Stained with anti-TDP-43, anti-Lamin, and anti-GAPDH. h , Quantification of the 35 kDa C-terminal fragment (CTF35) WCL band intensity in ( g ). Normalized to respective GAPDH band. n = 4, *p<0.05, paired t test. i , Representative immunoblots of HEK293T cells transduced with AAV-TDP-43venus (3 d) and infected with HSV-1 (MOI 0.3, 17 h). Fractions of the whole cell lysate (WCL) were separated into soluble (S) and insoluble (I) components. j , Western blot band intensities of soluble and insoluble TDP-43venus in ( i ) displayed as ratio. n = 6, *p<0.05, paired t test. k , Schematic representation of the TDP-43 split luciferase system. Upon TDP-43 oligomerization the fusion of L1 and L2 results in a functional luciferase. l , Quantification of luciferase activity in HEK293T cells co-transfected with split luciferase: TDP43-L1 and TDP43-L2. 24 h post-transfection cells were infected with HSV-1 (MOI 0.3). After 48 h post-infection cells were lysed and luciferase activity was analyzed. Bars represent mean±SEM of n = 4. *p<0.05, t test, m , Fluorescence recovery after photobleaching (FRAP) of H4 cells transduced with lentiviruses expressing TDP-43halo (red) and infected with HSV-1 GFP. 17 h post-infection, GFP positive cells with TDP-43halo delocalization were selected and analyzed. High laser intensity (100%) was applied to the region of interest (ROI) for 5 s. Subsequently, 10 images were acquired every 5 s. Scale bar, 20 µm. n , Quantification of the fluorescence recovery in ROIs as shown in ( m ). Pre-bleaching mean fluorescence intensity (MFI) was set to 100% and post-bleaching MFI was set to 0%. n = 12 individual cells. A linear mixed model with time and treatment as fixed effects and replicate (n = 9) as a random effect demonstrates a significant (**p=0.00272) effect for treatment and treatment:timepoint interaction (***p=2.45 x 10 -8 ).

    Article Snippet: Monoclonal mouse anti-FLAG-tag antibody, M2 (1:5,000), Sigma-Aldrich, F1804), anti-GAPDH (BioLegend, 607902; 1:1,000), Polyclonal rabbit anti-TDP-43 antibody (proteintech, 10782-2-AP, 1:2,000), mouse anti-lamin B (proteintech, 66095-1, 1:1,000), mouse anti-HSV-1 ICP0 (abcam, AB6513, 1:7,500), anti-SUMO2 (novus biologicals, NBP1-77163, 1:1,000) Secondary Antibodies: anti-rabbit IgG HRP (Promega, W401B, 1:10,000), anti-mouse IgG HRP (Promega, W402B, 1:10,000), Veriblot HRP (abcam, ab131366, 1:1,000)

    Techniques: Immunofluorescence, Transduction, Infection, Expressing, Software, Staining, Western Blot, Luciferase, Functional Assay, Activity Assay, Transfection, Fluorescence

    a , Primary murine neurons were isolated from C57BL/6J mice at postnatal day 0–1. Neurons were transduced with AAV expressing TDP-43venus (green). After 3 days, cells were infected with HSV-1 and 17 h later fixed. Neurotracer (red), DAPI (blue). Scale bar, 10 µm. b , Analysis of TDP-43venus puncta per cell in ( a ). n = 31-43, three biological replicates. ***p<0.001, t test. c, Three-week-old human iPSC derived motoneurons (MNs) were HSV-1 GFP (green) infected and 17 h later stained for TDP-43 (red). DAPI (blue). Scale bar, 10 µm. d , Quantification of TDP-43 puncta in HSV-1 or mock infected MNs in ( c ). n = 64-68, two biological replicates. ***p<0.001, t test. e , Human iPSC derived brain organoids infected with HSV-1 GFP (green) for 48 h. Organoid slices were stained for TDP-43 (magenta), DAPI (blue). White arrows indicate TDP-43 delocalization in HSV-1 GFP positive cells. White squares indicate origin of inset. Scale bar, 50 µm. f , Zoom-in of representative cells in either condition in ( e ), white arrow indicate perinuclear TDP-43. Nuclei are framed by the dotted line. Scale bar, 5 µm. g , Quantification of TDP-43 puncta per cell in infected (HSV-1) and uninfected (mock) organoids (left) in ( e , f ), and analysis of TDP-43 puncta per cell per image in HSV-1 GFP infected organoids in GFP negative (HSV-1 −) or GFP positive (HSV-1 +) cells (right). n = 21-24, two independent replicates of two donors, ***p<0.001, t test. h , Representative immunofluorescence staining of C57BL/6J mice (10-week-old) that were intracerebrally infected with HSV-1 (1 x 10 5 PFU/mice) or inoculated with PBS (mock). At day 3 post-infection, mid-sagittal sections were prepared and stained for phosphorylated TDP-43 (pTDP-43, magenta), HSV-1 (green), and nuclei (DAPI, blue). White squares indicate origin of inset. Scale bar, 20 µm. i , Quantification of pTDP-43 mean fluorescence intensity (MFI) in 8-10 unbiasedly selected brain areas for each mouse. n = 3 mice per group, *p<0.05, t test. j , Scatter plot of pTDP-43 MFI/image (y-axis) against HSV-1 MFI/image (x-axis). Each dot represents one corresponding measurement from HSV-1 infected mice in ( i ). Grey areas represent averaged MFI in mock infected mice (background signal). The line indicates the linear regression including 95% confidence intervals. Spearman’s rank correlation test (r = 0.8661, ***p<0.001, n = 25). k , NF-L serum levels of C57BL/6J mice (16-week-old) at day 4 post-intracerebral HSV-1 infection (5 x 10 5 PFU/mice) or mock treatment, determined by ELISA. n = 6 mice per group, *p<0.05, t test. l , Representative immunohistochemistry of human liver section from an HSV-1 hepatitis patient. HSV-1 stained in brown, pTDP43 stained in magenta. Scale bar, 500 µm. Insets are indicated of infected (HSV-1 positive cells, brown) and non-infected areas. Arrows indicate pTDP-43 accumulations.

    Journal: bioRxiv

    Article Title: Herpes simplex virus infection promotes ALS pathology through ICP0-mediated PML body disruption

    doi: 10.64898/2026.03.27.714707

    Figure Lengend Snippet: a , Primary murine neurons were isolated from C57BL/6J mice at postnatal day 0–1. Neurons were transduced with AAV expressing TDP-43venus (green). After 3 days, cells were infected with HSV-1 and 17 h later fixed. Neurotracer (red), DAPI (blue). Scale bar, 10 µm. b , Analysis of TDP-43venus puncta per cell in ( a ). n = 31-43, three biological replicates. ***p<0.001, t test. c, Three-week-old human iPSC derived motoneurons (MNs) were HSV-1 GFP (green) infected and 17 h later stained for TDP-43 (red). DAPI (blue). Scale bar, 10 µm. d , Quantification of TDP-43 puncta in HSV-1 or mock infected MNs in ( c ). n = 64-68, two biological replicates. ***p<0.001, t test. e , Human iPSC derived brain organoids infected with HSV-1 GFP (green) for 48 h. Organoid slices were stained for TDP-43 (magenta), DAPI (blue). White arrows indicate TDP-43 delocalization in HSV-1 GFP positive cells. White squares indicate origin of inset. Scale bar, 50 µm. f , Zoom-in of representative cells in either condition in ( e ), white arrow indicate perinuclear TDP-43. Nuclei are framed by the dotted line. Scale bar, 5 µm. g , Quantification of TDP-43 puncta per cell in infected (HSV-1) and uninfected (mock) organoids (left) in ( e , f ), and analysis of TDP-43 puncta per cell per image in HSV-1 GFP infected organoids in GFP negative (HSV-1 −) or GFP positive (HSV-1 +) cells (right). n = 21-24, two independent replicates of two donors, ***p<0.001, t test. h , Representative immunofluorescence staining of C57BL/6J mice (10-week-old) that were intracerebrally infected with HSV-1 (1 x 10 5 PFU/mice) or inoculated with PBS (mock). At day 3 post-infection, mid-sagittal sections were prepared and stained for phosphorylated TDP-43 (pTDP-43, magenta), HSV-1 (green), and nuclei (DAPI, blue). White squares indicate origin of inset. Scale bar, 20 µm. i , Quantification of pTDP-43 mean fluorescence intensity (MFI) in 8-10 unbiasedly selected brain areas for each mouse. n = 3 mice per group, *p<0.05, t test. j , Scatter plot of pTDP-43 MFI/image (y-axis) against HSV-1 MFI/image (x-axis). Each dot represents one corresponding measurement from HSV-1 infected mice in ( i ). Grey areas represent averaged MFI in mock infected mice (background signal). The line indicates the linear regression including 95% confidence intervals. Spearman’s rank correlation test (r = 0.8661, ***p<0.001, n = 25). k , NF-L serum levels of C57BL/6J mice (16-week-old) at day 4 post-intracerebral HSV-1 infection (5 x 10 5 PFU/mice) or mock treatment, determined by ELISA. n = 6 mice per group, *p<0.05, t test. l , Representative immunohistochemistry of human liver section from an HSV-1 hepatitis patient. HSV-1 stained in brown, pTDP43 stained in magenta. Scale bar, 500 µm. Insets are indicated of infected (HSV-1 positive cells, brown) and non-infected areas. Arrows indicate pTDP-43 accumulations.

    Article Snippet: Monoclonal mouse anti-FLAG-tag antibody, M2 (1:5,000), Sigma-Aldrich, F1804), anti-GAPDH (BioLegend, 607902; 1:1,000), Polyclonal rabbit anti-TDP-43 antibody (proteintech, 10782-2-AP, 1:2,000), mouse anti-lamin B (proteintech, 66095-1, 1:1,000), mouse anti-HSV-1 ICP0 (abcam, AB6513, 1:7,500), anti-SUMO2 (novus biologicals, NBP1-77163, 1:1,000) Secondary Antibodies: anti-rabbit IgG HRP (Promega, W401B, 1:10,000), anti-mouse IgG HRP (Promega, W402B, 1:10,000), Veriblot HRP (abcam, ab131366, 1:1,000)

    Techniques: Isolation, Transduction, Expressing, Infection, Derivative Assay, Staining, Immunofluorescence, Fluorescence, Enzyme-linked Immunosorbent Assay, Immunohistochemistry

    a , Schematic overview of the HSV-1 ICP0 gene with mutations to disrupt either RNF8 binding site (T67A), E3 ligase function (C116G/C156A), Cyclin D3 binding site (D199A) or CoREST interaction (D671A/E673A). b , Representative immunofluorescence images of H4 cells co-transfected with TDP-43venus (green) and either vector, wild-type (WT) ICP0 or indicated ICP0 mutant. Cells were fixed 24 h post-transfection and stained for PML (white), ICP0 (red) and DAPI (blue). Scale bar, 10 µm. c , Quantification of nuclear TDP-43venus foci area (µm 2 ) (top) and PML foci count (bottom) of co-transfected cells in (b) using Foci Analyzer (ImageJ). Lines represent mean±SEM, dots represent individual cells (n = 37-74) of three independent biological replicates. *p<0.05, ***p<0.001 Kruskal-Wallis test followed by Dunn’s multiple comparisons test. d , Scatter plot of total nuclear TDP-43venus foci size (y-axis) against the nuclear PML dot count (x-axis). Each dot represents one corresponding measurement from (c). Blue dots represent cells overexpressing ICP0 WT, black dots represent cells transfected with vector. For association testing, all events were taken together in Spearman’s rank correlation test (r = –0.54, ***p<0.001, n = 118). e , Representative immunofluorescence images of H4 cells transduced with lentiviruses encoding TDP-43venus (green). After 3 days, cells were infected with HSV-1 and 1 h post-infection treated with proteasome inhibitor MG132 or DMSO, respectively. Cells were fixed 17 h post-infection and stained for PML (white), ICP27 (red) and DAPI (blue). Scale bar, 10 µm. f , Quantification of PML foci (top) and total nuclear TDP-43venus foci area (µm 2 ) (bottom) in (e). Lines represent mean±SEM. Dots represent individual cells, n = 58-362, three independent biological replicates, ***p<0.001 Kruskal-Wallis test followed by Dunn’s multiple comparisons test. g , Representative immunoblots showing SUMOylation status of FLAG-tagged TDP-43 purified by anti-FLAG immunoprecipitation (IP) from whole cell lysates (WCL) of HEK293T cells at 40 h post-transfection. Cells were co-transfected with HSV-1 ICP0 and/or stimulated with arsenite (500 µM, 1 h), as indicated. IP and WCL was analyzed by immunoblotting. Blots were stained with anti-SUMO2, anti-FLAG, anti-HSV-1 ICP0 and anti-GAPDH. h , Quantification of the full SUMO-2 lane in the TDP-43 IP of ( g ) normalized to the vector control. n = 3, **p<0.01 paired t test.

    Journal: bioRxiv

    Article Title: Herpes simplex virus infection promotes ALS pathology through ICP0-mediated PML body disruption

    doi: 10.64898/2026.03.27.714707

    Figure Lengend Snippet: a , Schematic overview of the HSV-1 ICP0 gene with mutations to disrupt either RNF8 binding site (T67A), E3 ligase function (C116G/C156A), Cyclin D3 binding site (D199A) or CoREST interaction (D671A/E673A). b , Representative immunofluorescence images of H4 cells co-transfected with TDP-43venus (green) and either vector, wild-type (WT) ICP0 or indicated ICP0 mutant. Cells were fixed 24 h post-transfection and stained for PML (white), ICP0 (red) and DAPI (blue). Scale bar, 10 µm. c , Quantification of nuclear TDP-43venus foci area (µm 2 ) (top) and PML foci count (bottom) of co-transfected cells in (b) using Foci Analyzer (ImageJ). Lines represent mean±SEM, dots represent individual cells (n = 37-74) of three independent biological replicates. *p<0.05, ***p<0.001 Kruskal-Wallis test followed by Dunn’s multiple comparisons test. d , Scatter plot of total nuclear TDP-43venus foci size (y-axis) against the nuclear PML dot count (x-axis). Each dot represents one corresponding measurement from (c). Blue dots represent cells overexpressing ICP0 WT, black dots represent cells transfected with vector. For association testing, all events were taken together in Spearman’s rank correlation test (r = –0.54, ***p<0.001, n = 118). e , Representative immunofluorescence images of H4 cells transduced with lentiviruses encoding TDP-43venus (green). After 3 days, cells were infected with HSV-1 and 1 h post-infection treated with proteasome inhibitor MG132 or DMSO, respectively. Cells were fixed 17 h post-infection and stained for PML (white), ICP27 (red) and DAPI (blue). Scale bar, 10 µm. f , Quantification of PML foci (top) and total nuclear TDP-43venus foci area (µm 2 ) (bottom) in (e). Lines represent mean±SEM. Dots represent individual cells, n = 58-362, three independent biological replicates, ***p<0.001 Kruskal-Wallis test followed by Dunn’s multiple comparisons test. g , Representative immunoblots showing SUMOylation status of FLAG-tagged TDP-43 purified by anti-FLAG immunoprecipitation (IP) from whole cell lysates (WCL) of HEK293T cells at 40 h post-transfection. Cells were co-transfected with HSV-1 ICP0 and/or stimulated with arsenite (500 µM, 1 h), as indicated. IP and WCL was analyzed by immunoblotting. Blots were stained with anti-SUMO2, anti-FLAG, anti-HSV-1 ICP0 and anti-GAPDH. h , Quantification of the full SUMO-2 lane in the TDP-43 IP of ( g ) normalized to the vector control. n = 3, **p<0.01 paired t test.

    Article Snippet: Monoclonal mouse anti-FLAG-tag antibody, M2 (1:5,000), Sigma-Aldrich, F1804), anti-GAPDH (BioLegend, 607902; 1:1,000), Polyclonal rabbit anti-TDP-43 antibody (proteintech, 10782-2-AP, 1:2,000), mouse anti-lamin B (proteintech, 66095-1, 1:1,000), mouse anti-HSV-1 ICP0 (abcam, AB6513, 1:7,500), anti-SUMO2 (novus biologicals, NBP1-77163, 1:1,000) Secondary Antibodies: anti-rabbit IgG HRP (Promega, W401B, 1:10,000), anti-mouse IgG HRP (Promega, W402B, 1:10,000), Veriblot HRP (abcam, ab131366, 1:1,000)

    Techniques: Binding Assay, Immunofluorescence, Transfection, Plasmid Preparation, Mutagenesis, Staining, Transduction, Infection, Western Blot, Purification, Immunoprecipitation, Control

    Oxidative stress induced the conformational change of G4s. ( A ) Flowchart of the cellular oxidative stress experiment. Twelve hours after the addition of hydrogen peroxide, the GOTO neuroblastoma cells were fixed and immunostained. Then, total RNA was purified from the cells and used for the TO1B turn-on assay. ( B ) Representative immunofluorescence images showing TDP-43 and G4 signals detected using anti-TDP-43 and anti-G4 antibodies. Single-channel images and DAPI staining are shown, along with merged views. For quantification (bottom panels), the fluorescence intensities of TDP-43 and G4 were measured in ten cells per condition; values are normalized to untreated cells. Data represent mean ± SEM. Statistical significance was assessed using a two-tailed Student’s t-test (* P < 0.05). ( C ) Binding model of G4BPs. The proteins are classified into two groups: those that bind to prevent G4 formation (group 1) and those that stabilize G4 structures (group 2). ( D ) Measurement of G4 levels using the G4-specific fluorescent sensor TO1B. The fluorescence emission spectra of TO1B were measured after adding RNA extracted from untreated cells and cells oxidatively stressed with 20, 40, and 80 µM hydrogen peroxide. The G4-independent fluorescence intensity is also shown as a control. The graph on the right displays the average fluorescence intensity at 530 nm. The experiments were performed in triplicate, and the values on the y-axis represent the mean ± SEM. Statistical significance was determined using a two-tailed Student’s t -test. * P < 0.05.

    Journal: Scientific Reports

    Article Title: Impact of G-quadruplex RNA oxidation on its conformational dynamics and interaction with ALS-associated TDP-43

    doi: 10.1038/s41598-026-39767-y

    Figure Lengend Snippet: Oxidative stress induced the conformational change of G4s. ( A ) Flowchart of the cellular oxidative stress experiment. Twelve hours after the addition of hydrogen peroxide, the GOTO neuroblastoma cells were fixed and immunostained. Then, total RNA was purified from the cells and used for the TO1B turn-on assay. ( B ) Representative immunofluorescence images showing TDP-43 and G4 signals detected using anti-TDP-43 and anti-G4 antibodies. Single-channel images and DAPI staining are shown, along with merged views. For quantification (bottom panels), the fluorescence intensities of TDP-43 and G4 were measured in ten cells per condition; values are normalized to untreated cells. Data represent mean ± SEM. Statistical significance was assessed using a two-tailed Student’s t-test (* P < 0.05). ( C ) Binding model of G4BPs. The proteins are classified into two groups: those that bind to prevent G4 formation (group 1) and those that stabilize G4 structures (group 2). ( D ) Measurement of G4 levels using the G4-specific fluorescent sensor TO1B. The fluorescence emission spectra of TO1B were measured after adding RNA extracted from untreated cells and cells oxidatively stressed with 20, 40, and 80 µM hydrogen peroxide. The G4-independent fluorescence intensity is also shown as a control. The graph on the right displays the average fluorescence intensity at 530 nm. The experiments were performed in triplicate, and the values on the y-axis represent the mean ± SEM. Statistical significance was determined using a two-tailed Student’s t -test. * P < 0.05.

    Article Snippet: Immunofluorescence staining of cultured cells was performed as previously described , using a rabbit polyclonal anti-TDP-43 antibody (Cell Signaling Technology Inc., #3449 Danvers, Massachusetts, USA) and the mouse monoclonal anti-G-quadruplex antibody BG4 (Absolute Antibody Ltd., Ab00174-1.1 Redcar, UK).

    Techniques: Purification, Immunofluorescence, Staining, Fluorescence, Two Tailed Test, Binding Assay, Control

    G4 oxidation reduces its interaction with TDP-43. ( A , B ) Agarose gel mobility shift assay. Fifty nanograms (0.5 pmol) of fluorescently labeled G4 probes ( Ax647 PSD-95-G4 or Ax647 CaMKIIα-G4) was mixed with two pmol of TDP-43 and the indicated unlabeled RNA competitors (threefold or 10-fold molar excess relative to the probe) and then electrophoresed under nondenaturing conditions. The shifted bands were quantified, and the mean and standard error of the mean (± SEM) were calculated from three independent experiments and displayed in the graph. The y-axis represents the mean ± SEM. Statistical significance was determined by two-tailed Student’s t -test. * P < 0.05, ** P < 0.01, *** P < 0.001. The red arrow indicates unexpected inhibition by the oxidized form of CaMKIIα-G4 (40% 8OG). These smear signals, indicated by dagger (†), have been confirmed to be the result of dissociation during electrophoresis . ( C ) CD spectra of PSD-95-G4 and oxidized RNAs (2 µM) in the absence and presence of TDP-43 (2 µM). The scans were repeated five times, and the protein spectra were subtracted; the mean values are shown. The CD spectrum of TDP-43 without RNA is also included. ( D ) Schematic illustration of G4 stabilization by TDP-43. The CD spectra of the oxidized RNA showed a decrease in the positive peak in the presence of TDP-43, indicating the stabilization of the transition intermediate G4 conformation.

    Journal: Scientific Reports

    Article Title: Impact of G-quadruplex RNA oxidation on its conformational dynamics and interaction with ALS-associated TDP-43

    doi: 10.1038/s41598-026-39767-y

    Figure Lengend Snippet: G4 oxidation reduces its interaction with TDP-43. ( A , B ) Agarose gel mobility shift assay. Fifty nanograms (0.5 pmol) of fluorescently labeled G4 probes ( Ax647 PSD-95-G4 or Ax647 CaMKIIα-G4) was mixed with two pmol of TDP-43 and the indicated unlabeled RNA competitors (threefold or 10-fold molar excess relative to the probe) and then electrophoresed under nondenaturing conditions. The shifted bands were quantified, and the mean and standard error of the mean (± SEM) were calculated from three independent experiments and displayed in the graph. The y-axis represents the mean ± SEM. Statistical significance was determined by two-tailed Student’s t -test. * P < 0.05, ** P < 0.01, *** P < 0.001. The red arrow indicates unexpected inhibition by the oxidized form of CaMKIIα-G4 (40% 8OG). These smear signals, indicated by dagger (†), have been confirmed to be the result of dissociation during electrophoresis . ( C ) CD spectra of PSD-95-G4 and oxidized RNAs (2 µM) in the absence and presence of TDP-43 (2 µM). The scans were repeated five times, and the protein spectra were subtracted; the mean values are shown. The CD spectrum of TDP-43 without RNA is also included. ( D ) Schematic illustration of G4 stabilization by TDP-43. The CD spectra of the oxidized RNA showed a decrease in the positive peak in the presence of TDP-43, indicating the stabilization of the transition intermediate G4 conformation.

    Article Snippet: Immunofluorescence staining of cultured cells was performed as previously described , using a rabbit polyclonal anti-TDP-43 antibody (Cell Signaling Technology Inc., #3449 Danvers, Massachusetts, USA) and the mouse monoclonal anti-G-quadruplex antibody BG4 (Absolute Antibody Ltd., Ab00174-1.1 Redcar, UK).

    Techniques: Agarose Gel Electrophoresis, Mobility Shift, Labeling, Two Tailed Test, Inhibition, Electrophoresis, Circular Dichroism

    Vulnerability of ALS mutant proteins to G4 oxidation. ( A ) TDP-43, which is encoded by the TARDBP gene, consists of two RRM with strong RNA-binding properties and a glycine-rich domain that regulates specific interactions. Ten mutations associated with patients with ALS, which were used in this study, are shown. The order/disorder propensity of TDP-43 was predicted using the Protein DisOrder prediction System (PrDOS) algorithm . ( B ) Purified TDP-43 wild-type and 10 mutant proteins used in this study. One microgram each of proteins was separated by 12.5% SDS-PAGE and detected by Coomassie brilliant blue staining. ( C ) Agarose gel mobility shift assay with Ax647 PSD-95-G4. Wild-type TDP-43 and the 10 mutant proteins were reacted with the probe in the presence or absence of competitor RNA (10% 8OG, 10-fold for probe). ( D ) Each overshifted band was quantified, and the mean and standard error (± SEM) obtained from three independent experiments were calculated and shown in the graph. E , Graph showing the average binding with and without competitor RNA. The ± SEM from three independent experiments is displayed. Statistical significance was assessed using a two-tailed Student’s t -test. * P < 0.05.

    Journal: Scientific Reports

    Article Title: Impact of G-quadruplex RNA oxidation on its conformational dynamics and interaction with ALS-associated TDP-43

    doi: 10.1038/s41598-026-39767-y

    Figure Lengend Snippet: Vulnerability of ALS mutant proteins to G4 oxidation. ( A ) TDP-43, which is encoded by the TARDBP gene, consists of two RRM with strong RNA-binding properties and a glycine-rich domain that regulates specific interactions. Ten mutations associated with patients with ALS, which were used in this study, are shown. The order/disorder propensity of TDP-43 was predicted using the Protein DisOrder prediction System (PrDOS) algorithm . ( B ) Purified TDP-43 wild-type and 10 mutant proteins used in this study. One microgram each of proteins was separated by 12.5% SDS-PAGE and detected by Coomassie brilliant blue staining. ( C ) Agarose gel mobility shift assay with Ax647 PSD-95-G4. Wild-type TDP-43 and the 10 mutant proteins were reacted with the probe in the presence or absence of competitor RNA (10% 8OG, 10-fold for probe). ( D ) Each overshifted band was quantified, and the mean and standard error (± SEM) obtained from three independent experiments were calculated and shown in the graph. E , Graph showing the average binding with and without competitor RNA. The ± SEM from three independent experiments is displayed. Statistical significance was assessed using a two-tailed Student’s t -test. * P < 0.05.

    Article Snippet: Immunofluorescence staining of cultured cells was performed as previously described , using a rabbit polyclonal anti-TDP-43 antibody (Cell Signaling Technology Inc., #3449 Danvers, Massachusetts, USA) and the mouse monoclonal anti-G-quadruplex antibody BG4 (Absolute Antibody Ltd., Ab00174-1.1 Redcar, UK).

    Techniques: Mutagenesis, RNA Binding Assay, Purification, SDS Page, Staining, Agarose Gel Electrophoresis, Mobility Shift, Binding Assay, Two Tailed Test