Journal: Acta neuropathologica

Article Title: Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutations.

doi: 10.1007/s00401-012-1020-6

Figure Lengend Snippet: Fig. 2 Co-localization of Trn1 and FUS in all FTLD-FUS subtypes. Double-label immunofluorescence for FUS (red) and Trn1 (green), with DAPI staining of nuclei in the merged images. FUS-positive inclusions in all FTLD-FUS subtypes consistently showed co-localization of FUS and Trn1, as shown for neuronal cytoplasmic inclusions (NCI) and neuronal intranuclear inclusions (NII, arrow in a) in the dentate granule cells in aFTLD-U (a), NCI in the temporal cortex of NIFID (b) and NCI and glial cytoplasmic inclusions in the spinal cord of BIBD (c). Scale bar 10 lm

Article Snippet: Table 3 Trn1 cargo proteins with PY-NLS investigated in FTLD-FUS Protein name Antibody Physiological staining pattern Inclusions in FTLD-FUS Company Dilution Type FUS ProteinTech Group (60160-1-Ig) 1:1,000 MM nucl pos Sigma (HPA008784) 1:2,000 RP nucl pos TAF15 Bethyl Laboratories (IHC-00094-1) 1:200 RP nucl pos EWS Santa Cruz (clone G5) 1:200 MM nucl [ cyto pos Bethyl Laboratories (IHC-00086) 1:200 RP nucl [ cyto pos hnRNP A1 Santa Cruz (clone 4B10) 1:500 MM nucl neg hnRNP A0 Abcam (ab66661) 1:100 RP nucl neg hnRNP A2/B1 Sigma-Aldrich (clone DP3B3) 1:500 MM nucl neg hnRNP M3/M4 Santa Cruz (clone 2A6) 1:250 MM nucl neg hnRNP D ProteinTech Group (12770-1-AP) 1:500 RP nucl neg hnRNP H1 ProteinTech Group (14774-1-AP) 1:50 RP nucl [ cyto neg PQBP-1 ProteinTech Group (16264-1-AP) 1:250 RP nucl neg SAM68 ProteinTech Group (10222-1-AP) 1:250 RP nucl neg SLM-2 ProteinTech Group (13563-1-AP) 1:50 RP nucl neg HEXIM1 ProteinTech Group (15676-1-AP) 1:50 RP nucl neg RBM39 ProteinTech Group (21339-1-AP) 1:50 RP nucl [ cyto neg HuR Santa Cruz (clone 3A2) 1:250 MM nucl neg PABPN1 Abcam (EP3000Y) 1:1,000 RM nucl neg Cyto cytoplasmatic, MM mouse monoclonal, nucl nuclear, pos positive, RP rabbit polyclonal, RM rabbit monoclonal, neg negative Trn1 staining in neurological controls The normal and neurological control cases did not reveal Trn1 immunoreactive pathology with one exception (Table 2).

Techniques: Staining

Journal: Acta neuropathologica

Article Title: Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutations.

doi: 10.1007/s00401-012-1020-6

Figure Lengend Snippet: Fig. 3 Absence of Trn1 pathology in ALS-FUS. Double-label immuno- fluorescence for FUS (red) and Trn1 (green), with DAPI staining of nuclei in the merged images. FUS-positive inclusions in ALS-FUS were not labeled for Trn1 as shown for neuronal cytoplasmic inclusions in the spinal cord for three different FUS mutations (a–c). Note the physiological nuclear staining for Trn1 in inclusion bearing cells. FUS-positive glial cytoplasmic inclusions present in a subset of ALS-FUS cases also showed no co-labeling for Trn1 (arrow in a). Scale bar 10 lm

Article Snippet: Table 3 Trn1 cargo proteins with PY-NLS investigated in FTLD-FUS Protein name Antibody Physiological staining pattern Inclusions in FTLD-FUS Company Dilution Type FUS ProteinTech Group (60160-1-Ig) 1:1,000 MM nucl pos Sigma (HPA008784) 1:2,000 RP nucl pos TAF15 Bethyl Laboratories (IHC-00094-1) 1:200 RP nucl pos EWS Santa Cruz (clone G5) 1:200 MM nucl [ cyto pos Bethyl Laboratories (IHC-00086) 1:200 RP nucl [ cyto pos hnRNP A1 Santa Cruz (clone 4B10) 1:500 MM nucl neg hnRNP A0 Abcam (ab66661) 1:100 RP nucl neg hnRNP A2/B1 Sigma-Aldrich (clone DP3B3) 1:500 MM nucl neg hnRNP M3/M4 Santa Cruz (clone 2A6) 1:250 MM nucl neg hnRNP D ProteinTech Group (12770-1-AP) 1:500 RP nucl neg hnRNP H1 ProteinTech Group (14774-1-AP) 1:50 RP nucl [ cyto neg PQBP-1 ProteinTech Group (16264-1-AP) 1:250 RP nucl neg SAM68 ProteinTech Group (10222-1-AP) 1:250 RP nucl neg SLM-2 ProteinTech Group (13563-1-AP) 1:50 RP nucl neg HEXIM1 ProteinTech Group (15676-1-AP) 1:50 RP nucl neg RBM39 ProteinTech Group (21339-1-AP) 1:50 RP nucl [ cyto neg HuR Santa Cruz (clone 3A2) 1:250 MM nucl neg PABPN1 Abcam (EP3000Y) 1:1,000 RM nucl neg Cyto cytoplasmatic, MM mouse monoclonal, nucl nuclear, pos positive, RP rabbit polyclonal, RM rabbit monoclonal, neg negative Trn1 staining in neurological controls The normal and neurological control cases did not reveal Trn1 immunoreactive pathology with one exception (Table 2).

Techniques: Staining, Labeling

Journal: Acta neuropathologica

Article Title: Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutations.

doi: 10.1007/s00401-012-1020-6

Figure Lengend Snippet: Fig. 5 Absence of selected other Trn1 cargos (hnRNP A1, SAM68 and PABPN1) in FTLD-FUS. Double-label immunofluorescence for FUS (red) and other Trn1 cargos with PY-NLS (hnRNP A1, SAM68 and PABPN1, respectively, green) with DAPI staining of nuclei in the merged images in FTLD-FUS. FUS-positive inclusions in FTLD-FUS as shown here in the dentate gyrus of aFTLD-U were not labeled for hnRNP A1 (a), SAM68 (b) and PABPN1 (c). Scale bar 10 lm

Article Snippet: Table 3 Trn1 cargo proteins with PY-NLS investigated in FTLD-FUS Protein name Antibody Physiological staining pattern Inclusions in FTLD-FUS Company Dilution Type FUS ProteinTech Group (60160-1-Ig) 1:1,000 MM nucl pos Sigma (HPA008784) 1:2,000 RP nucl pos TAF15 Bethyl Laboratories (IHC-00094-1) 1:200 RP nucl pos EWS Santa Cruz (clone G5) 1:200 MM nucl [ cyto pos Bethyl Laboratories (IHC-00086) 1:200 RP nucl [ cyto pos hnRNP A1 Santa Cruz (clone 4B10) 1:500 MM nucl neg hnRNP A0 Abcam (ab66661) 1:100 RP nucl neg hnRNP A2/B1 Sigma-Aldrich (clone DP3B3) 1:500 MM nucl neg hnRNP M3/M4 Santa Cruz (clone 2A6) 1:250 MM nucl neg hnRNP D ProteinTech Group (12770-1-AP) 1:500 RP nucl neg hnRNP H1 ProteinTech Group (14774-1-AP) 1:50 RP nucl [ cyto neg PQBP-1 ProteinTech Group (16264-1-AP) 1:250 RP nucl neg SAM68 ProteinTech Group (10222-1-AP) 1:250 RP nucl neg SLM-2 ProteinTech Group (13563-1-AP) 1:50 RP nucl neg HEXIM1 ProteinTech Group (15676-1-AP) 1:50 RP nucl neg RBM39 ProteinTech Group (21339-1-AP) 1:50 RP nucl [ cyto neg HuR Santa Cruz (clone 3A2) 1:250 MM nucl neg PABPN1 Abcam (EP3000Y) 1:1,000 RM nucl neg Cyto cytoplasmatic, MM mouse monoclonal, nucl nuclear, pos positive, RP rabbit polyclonal, RM rabbit monoclonal, neg negative Trn1 staining in neurological controls The normal and neurological control cases did not reveal Trn1 immunoreactive pathology with one exception (Table 2).

Techniques: Staining, Labeling

Journal: bioRxiv

Article Title: Differential TDP-43 interactomes between the cortex and cerebellum in the mouse

doi: 10.64898/2026.01.16.699854

Figure Lengend Snippet: TDP-43 differentially interacts with core paraspeckle proteins FUS, PSPC1, SFPQ and NONO in the cortex and cerebellum (a) Representative examples of co-immunoprecipitation of FUS, PSPC1, SFPQ and NONO following TDP-43 pull-down in the cortex and cerebellum of 3-month-old C57Bl/6J mice with both the N (Abcam, #ab225710) and C (Proteintech #12892-1-AP) terminal TDP-43 antibodies. All four proteins were detected in the IP fraction of the cortex with both antibodies, with no band present with IgG alone. In contrast, PSPC1 was absent from the cerebellar samples following pull down with either antibody. IP: immunoprecipitation, FT: flow through. (b) Representative examples of western blot detection of total, nuclear and cytoplasmic FUS, PSPC1, SFPQ and NONO expression levels in the cortex and cerebellum of 3-month-old C57Bl/6J mice. (c-e) Quantification of FUS, PSPC1, SFPQ and NONO total (c), nuclear (d) and cytoplasmic (e) expression levels in the cortex and cerebellum of 3-month-old C57Bl/6J mice. PSPC1 levels were significantly reduced in the nuclear fraction of the cerebellum compared to the cortex. No other significant changes were observed. cx: cortex, cb: cerebellum, n=3 *p<0.05 Welch’s t-test

Article Snippet: Mouse anti FUS (1:500, Santa Cruz: sc-373698), rabbit anti-PSPC1 (1:1000, Abcam: ab133574), mouse anti-SFPQ (1:500, Invitrogen: MA1-25325) and rabbit anti-NONO (1:500, Abcam: ab133574) antibodies were used with loading controls and secondary antibodies as before.

Techniques: Immunoprecipitation, Western Blot, Expressing

Journal: bioRxiv

Article Title: Differential TDP-43 interactomes between the cortex and cerebellum in the mouse

doi: 10.64898/2026.01.16.699854

Figure Lengend Snippet: NONO shows differential cellular distribution between the cortex and cerebellum. (a-d) Representative examples of paraspeckle proteins (PSPr), FUS (a), PSPC1 (b), SFPQ (c) and NONO (d) distribution and colocalisation with TDP-43 in the motor cortex and Crus 1 region of the cerebellum. Scale bar is 20μm. All four paraspeckle proteins show abundant staining in the nucleus, with minimal evidence of expression within the cytoplasm with the exception of NONO within the cerebellum, which shows a distinct punctate pattern of staining within the nucleus and cytoplasm. TDP-43 shows abundant nuclear colocalisation with all four paraspeckle proteins in both the cortex and cerebellum, but no robust evidence of colocalization in the cytoplasm

Article Snippet: Mouse anti FUS (1:500, Santa Cruz: sc-373698), rabbit anti-PSPC1 (1:1000, Abcam: ab133574), mouse anti-SFPQ (1:500, Invitrogen: MA1-25325) and rabbit anti-NONO (1:500, Abcam: ab133574) antibodies were used with loading controls and secondary antibodies as before.

Techniques: Staining, Expressing

Journal: bioRxiv

Article Title: Differential TDP-43 interactomes between the cortex and cerebellum in the mouse

doi: 10.64898/2026.01.16.699854

Figure Lengend Snippet: TDP-43 interactions with FUS, PSPC1, SFPQ and NONO show distinct differences between different cortical and cerebellar cell populations (a) Representative examples of proximity ligation assay (PLA) assessment of TDP-43 with FUS, PSPC1, SFPQ and NONO. (b) Quantitative analysis of PLA spot counts in the large cells of the motor cortex (MC; layer V), and the large (Purkinje cells; PC) and small (Granule cells; GC) of the cerebellum. n=3, *p<0.05; **p<0.01 cytoplasm vs. nucleus; †p<0.05 nucleus vs. motor cortex nucleus #p<0.05; ##p<0.01 cytoplasm vs. motor cortex cytoplasm. Two-way ANOVA with Fisher LSD post hoc. (c) Quantitative analysis of mean PLA spot size in large cells of the motor cortex (MC) and large (PC) and small (GC) cells of the cerebellum. n=3, *p<0.05 vs motor cortex. One way ANOVA with Tukey post hoc

Article Snippet: Mouse anti FUS (1:500, Santa Cruz: sc-373698), rabbit anti-PSPC1 (1:1000, Abcam: ab133574), mouse anti-SFPQ (1:500, Invitrogen: MA1-25325) and rabbit anti-NONO (1:500, Abcam: ab133574) antibodies were used with loading controls and secondary antibodies as before.

Techniques: Proximity Ligation Assay

Journal: Molecular cell

Article Title: ULK1/2 Regulates Stress Granule Disassembly Through Phosphorylation and Activation of VCP/p97

doi: 10.1016/j.molcel.2019.03.027

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: The following primary antibodies were used: mouse anti-SQSTM1/p62 (Abnova; H00008878-M01), rabbit anti-ubiquitin (DAKO; Z0458), rabbit anti-LC3B (MBL; PM036), rat anti-LAMP1 (Developmental Studies Hybridoma Bank; 1D4B), mouse anti–SMI-31 (Covance; SMI-31R), rabbit anti–β-amyloid 1–42 (Millipore; AB5078P), rabbit anti-FUS (Bethyl Laboratories; IHC-00074), rabbit anti–TDP-43 (Proteintech; 10782–2-AP), goat anti-TIA1 (Santa Cruz Biotechnology; sc-1751), and mouse anti–hnRNP A2B1 (Santa Cruz Biotechnology; sc-53531).

Techniques: Recombinant, Western Blot, Software

Journal: Frontiers in Cell and Developmental Biology

Article Title: CREB1 and ATF1 Negatively Regulate Glutathione Biosynthesis Sensitizing Cells to Oxidative Stress

doi: 10.3389/fcell.2021.698264

Figure Lengend Snippet: CREB1 and ATF1 repress the expression of GCLM and GSS. (A) Schematic depicting the GSH synthesis pathway and its associated hypotaurine synthesis pathway. (B,C) Relative mRNA levels of enzymes of GSH synthesis pathway in U2OS cells (B) and U87 cells (C) transfected with CREB1 siRNA or control siRNA. (D,E) Relative mRNA levels of GSH synthesis enzymes in U2OS cells (D) and U87 cells (E) transfected with control siRNA or ATF1 siRNA as indicated. (F) U2OS and U87 cells expressing control siRNA, or siRNAs against CREB1, ATF1, or both (CREB1/ATF1) as indicated. Protein expression was analyzed by Western blot. Data are means ± SD. ( n = 3), * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.00001.

Article Snippet: Antibodies against the following proteins/epitopes were used for immunoblot with the sources, catalog numbers, and dilutions indicated: Actin (Easy Bio, BE0037-10, 1:5000), Flag (Sigma-Aldrich, F3165, 1:5000), GCLM (Proteintech, 14241-1-AP, 1:1000), GSS (Santa Cruz Biotechnology, sc-166882, 1:1000), CREB1 (Proteintech, 12208-1-AP, 1:1000), and ATF1 (Proteintech, 11946-1-AP, 1:1000).

Techniques: Expressing, Transfection, Control, Western Blot

Journal: Frontiers in Cell and Developmental Biology

Article Title: CREB1 and ATF1 Negatively Regulate Glutathione Biosynthesis Sensitizing Cells to Oxidative Stress

doi: 10.3389/fcell.2021.698264

Figure Lengend Snippet: GCLM and GSS are transcriptional targets of CREB1 and ATF1. (A) Schematic representation of human GCLM and GSS genomic structure. The sequences of potential CREB1 and ATF1 response elements GCLM -RE13, GSS -RE20, GCLM -RE1, and GSS -RE6 are shown. (B,C) 293T cells were transfected with Flag-CREB1 (B) , Flag-ATF1 (C) or vector control plasmid. Cell lysates were used for ChIP assay using anti-Flag antibody. Bound DNA was amplified by PCR. Results are representative of three independent experiments. (D,E) Luciferase constructs containing indicated responsive elements (REs) were transfected into 293T cells together with Flag-CREB1 (D) , Flag-ATF1 (E) and vector control, respectively. Renilla vector pRL-CMV was used as a transfection internal control. The relative luciferase activity was normalized to the co-transfected Renilla activity. Data are means ± SD. ( n = 3), ** p < 0.01, *** p < 0.001, **** p < 0.0001.

Article Snippet: Antibodies against the following proteins/epitopes were used for immunoblot with the sources, catalog numbers, and dilutions indicated: Actin (Easy Bio, BE0037-10, 1:5000), Flag (Sigma-Aldrich, F3165, 1:5000), GCLM (Proteintech, 14241-1-AP, 1:1000), GSS (Santa Cruz Biotechnology, sc-166882, 1:1000), CREB1 (Proteintech, 12208-1-AP, 1:1000), and ATF1 (Proteintech, 11946-1-AP, 1:1000).

Techniques: Transfection, Plasmid Preparation, Control, Amplification, Luciferase, Construct, Activity Assay

Journal: Frontiers in Cell and Developmental Biology

Article Title: CREB1 and ATF1 Negatively Regulate Glutathione Biosynthesis Sensitizing Cells to Oxidative Stress

doi: 10.3389/fcell.2021.698264

Figure Lengend Snippet: CREB1 and ATF1 inhibit intracellular ROS. (A,B) U2OS cells transfected with control siRNA, or CREB1 siRNA together with ATF1 siRNA (siCREB1/ATF1) were assayed for intracellular GSH production by LC-MS. (C) Relative ROS level in U2OS cells transfected with CREB1 and ATF1 siRNAs (siCREB1/ATF1), or control siRNA was determined by flow cytometry analysis. Protein expression was analyzed by Western blot. (D) U2OS cells were transfected with control, CREB1, ATF1 and/or GCLM siRNA as indicated. Relative ROS level was analyzed by flow cytometry. Protein expression was analyzed by Western blot. Data are means ± SD. ( n = 3), * p < 0.05, ** p < 0.01, *** p < 0.001.

Article Snippet: Antibodies against the following proteins/epitopes were used for immunoblot with the sources, catalog numbers, and dilutions indicated: Actin (Easy Bio, BE0037-10, 1:5000), Flag (Sigma-Aldrich, F3165, 1:5000), GCLM (Proteintech, 14241-1-AP, 1:1000), GSS (Santa Cruz Biotechnology, sc-166882, 1:1000), CREB1 (Proteintech, 12208-1-AP, 1:1000), and ATF1 (Proteintech, 11946-1-AP, 1:1000).

Techniques: Transfection, Control, Liquid Chromatography with Mass Spectroscopy, Flow Cytometry, Expressing, Western Blot

Journal: Frontiers in Cell and Developmental Biology

Article Title: CREB1 and ATF1 Negatively Regulate Glutathione Biosynthesis Sensitizing Cells to Oxidative Stress

doi: 10.3389/fcell.2021.698264

Figure Lengend Snippet: CREB1 and ATF1 inhibit cell survival under oxidative stress. (A) U2OS cells transfected with control, or CREB1 and ATF1 siRNAs (siCREB1/ATF1) were treated with 100 μM H 2 O 2 for 24 h. Protein expression was measured by Western blot analysis. Cell death was analyzed by flow cytometry after PI staining. (B,C) U2OS cells treated with control, CREB1, ATF1, GCLM, and/or GSS siRNAs as indicated. Protein expression was analyzed by Western blot (B) , and cell survival was assayed by crystal violet staining (C) . (D) U87 cells transfected with control siRNA, or siRNAs against CREB1 and ATF1 as indicated were treated with 100 μM H 2 O 2 for 24 h. Protein expression was analyzed by Western blot. (E) U87 cells were transfected with control, CREB1, ATF1, GCLM, and/or GSS siRNAs for colony formation assay. Numbers of colonies with a diameter greater than 20 μm were quantified. Data are means ± SD. ( n = 3), ** p < 0.01, *** p < 0.001, **** p < 0.0001.

Article Snippet: Antibodies against the following proteins/epitopes were used for immunoblot with the sources, catalog numbers, and dilutions indicated: Actin (Easy Bio, BE0037-10, 1:5000), Flag (Sigma-Aldrich, F3165, 1:5000), GCLM (Proteintech, 14241-1-AP, 1:1000), GSS (Santa Cruz Biotechnology, sc-166882, 1:1000), CREB1 (Proteintech, 12208-1-AP, 1:1000), and ATF1 (Proteintech, 11946-1-AP, 1:1000).

Techniques: Transfection, Control, Expressing, Western Blot, Flow Cytometry, Staining, Colony Assay

Journal:

Article Title: Extensive FUS-immunoreactive Pathology in Juvenile Amyotrophic Lateral Sclerosis with Basophilic Inclusions

doi: 10.1111/j.1750-3639.2010.00413.x

Figure Lengend Snippet: Histopathology of juvenile ALS with basophilic inclusions in comparison with that of late-onset sporadic ALS. (A, E) H&E sections of the spinal cord show the presence of basophilic inclusions in the remaining motor neurons in Cases 1 and 2. (B, F) Immunohistochemical staining shows that the basophilic inclusions are positive for FUS proteins. (C, G) Furthermore, these inclusions are only weakly positive for ubiquitin, but negative for TDP-43 (D, H). (I) In contrast, spinal motor neurons in patients with late-onset sporadic ALS show no evidence of basophilic inclusions on H&E-stained section. (J) Furthermore, immunohistochemistry shows the presence of FUS protein in the nucleus of remaining spinal motor neurons. (K–L) Many of the spinal motor neurons in late-onset sporadic ALS patients show abnormal accumulation of ubiquitinated proteins (K) and TDP-43 proteins (L). Scale bar in L is 25 µm and applies to all panels.

Article Snippet: The tissues were then incubated with a primary antibody for FUS (1:20, Novus Biologicals) or ubiquitin (1:10, Abcam), and the goat anti-rabbit secondary antibody conjugated with 15-nm gold particles (1:20, Ted Pella, Redding, CA, USA).

Techniques: Histopathology, Comparison, Immunohistochemical staining, Staining, Ubiquitin Proteomics, Immunohistochemistry

Journal:

Article Title: Extensive FUS-immunoreactive Pathology in Juvenile Amyotrophic Lateral Sclerosis with Basophilic Inclusions

doi: 10.1111/j.1750-3639.2010.00413.x

Figure Lengend Snippet: Ultrastructural analyses of basophilic inclusions in juvenile ALS. (A) A low magnification electron micrograph of the intracytoplasmic inclusion in a spinal motor neuron. The three rectangles in panel A highlight areas of higher magnifications shown in panels B, C and D. (B–D) Higher magnification image at the edge and the center of the inclusion. Both panels B and D show aggregates of disorganized endoplasmic reticulum (ER) and mitochondria (M). (C) In contrast, the center of the inclusion contains filamentous structures that measure 15–20 nm in diameter. (E,F) Immunogold EM using FUS-specific antibody shows that the majority of FUS proteins are associated with the filamentous structures (E), whereas the immunogold staining for ubiquitin show very few positive gold particles.

Article Snippet: The tissues were then incubated with a primary antibody for FUS (1:20, Novus Biologicals) or ubiquitin (1:10, Abcam), and the goat anti-rabbit secondary antibody conjugated with 15-nm gold particles (1:20, Ted Pella, Redding, CA, USA).

Techniques: Staining, Ubiquitin Proteomics

Journal:

Article Title: Extensive FUS-immunoreactive Pathology in Juvenile Amyotrophic Lateral Sclerosis with Basophilic Inclusions

doi: 10.1111/j.1750-3639.2010.00413.x

Figure Lengend Snippet: Basophilic inclusions can be detected in cerebral cortex and brainstem nuclei in patients with juvenile ALS. (A–B) An H&E section shows the presence of basophilic inclusion in the cytoplasm of a neuron in the cingulate gyrus (A). IHC using FUS antibody confirms that these inclusions are positive for FUS protein (B). (C–E) The basophilic and FUS-positive inclusions can also be identified in neurons in the reticular formation in the medulla oblongata (C and D) and the red nucleus (E). (F) In contrast, neurons in the hypoglossal nucleus in both juvenile ALS patients show staining of FUS proteins in the nuclei.

Article Snippet: The tissues were then incubated with a primary antibody for FUS (1:20, Novus Biologicals) or ubiquitin (1:10, Abcam), and the goat anti-rabbit secondary antibody conjugated with 15-nm gold particles (1:20, Ted Pella, Redding, CA, USA).

Techniques: Staining

Journal:

Article Title: Extensive FUS-immunoreactive Pathology in Juvenile Amyotrophic Lateral Sclerosis with Basophilic Inclusions

doi: 10.1111/j.1750-3639.2010.00413.x

Figure Lengend Snippet: Comparisons of age onset and neuropathological features of FUS-immunostaining in familial ALS cases with FUS/TLS mutations.

Article Snippet: The tissues were then incubated with a primary antibody for FUS (1:20, Novus Biologicals) or ubiquitin (1:10, Abcam), and the goat anti-rabbit secondary antibody conjugated with 15-nm gold particles (1:20, Ted Pella, Redding, CA, USA).

Techniques: Immunohistochemistry, Ubiquitin Proteomics