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Mouse Anti Flag M2 Monoclonal Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Mouse Anti Flag Tag M2 Monoclonal Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Millipore mouse anti flag m2 antibody
Mouse Anti Flag M2 Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Mouse Anti Flag M2, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Millipore mouse anti flag m2
HDAC inhibition limited the reduction of histone acetylation in TDP-43 G348C -expressing motor neurons. After microinjection of plasmid encoding TDP-43 G348C or mCherry as control, cultures were treated with vehicle (DMSO), 4 µM arimoclomol, 4 µM SAHA, 1 µM RGFP963, alone and in combination for 3 days. Injected neurons were identified by double-labeling with rabbit <t>anti-flag</t> <t>M2</t> to visualize TDP-43 G348C or by mCherry epifluorescence. (a) Acetylation of histone 3 at lysine residues 9 and 14 (H3K9/K14Ac), evaluated by immunocytochemistry using an acetylation-specific antibody was categorized as: strong (H3K9/K14Ac+/+), weak (H3K9/K14Ac+/−) or absent (H3K9/K14Ac−/−). (b) Reduction in H3K9K14ac in motor neurons expressing TDP-43 G348C was prevented by the HDAC inhibitors (c) SAHA or (d) RGFP963 demonstrating target engagement, whereas arimoclomol had no impact. (e) No alteration of histone acetylation by wild-type TDP-43. Data are presented as mean ± SD. Each data point on the graph represents the mean % of neurons in each of 6–13 cultures (10–59 neurons/culture). Statistical significance was evaluated by one-way ANOVA followed by Bonferroni post hoc analysis. * P < 0.05, ** P < 0.01, *** P < 0.001. Scale bar = 20 µm. Abbreviations used: HDAC, histone deacetylase; SAHA, suberoylanilide hydroxamic acid; SD, standard deviation; TDP-43, TAR DNA binding protein 43 kDa. 43 kDa; DMSO dimethyl sulfoxide.
Mouse Anti Flag M2, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/mouse anti flag m2/product/Millipore
Average 86 stars, based on 1 article reviews
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mouse anti flag m2 - by Bioz Stars, 2024-05
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1) Product Images from "Impact of histone deacetylase inhibition and arimoclomol on heat shock protein expression and disease biomarkers in primary culture models of familial ALS"

Article Title: Impact of histone deacetylase inhibition and arimoclomol on heat shock protein expression and disease biomarkers in primary culture models of familial ALS

Journal: Cell Stress & Chaperones

doi: 10.1016/j.cstres.2024.03.010

HDAC inhibition limited the reduction of histone acetylation in TDP-43 G348C -expressing motor neurons. After microinjection of plasmid encoding TDP-43 G348C or mCherry as control, cultures were treated with vehicle (DMSO), 4 µM arimoclomol, 4 µM SAHA, 1 µM RGFP963, alone and in combination for 3 days. Injected neurons were identified by double-labeling with rabbit anti-flag M2 to visualize TDP-43 G348C or by mCherry epifluorescence. (a) Acetylation of histone 3 at lysine residues 9 and 14 (H3K9/K14Ac), evaluated by immunocytochemistry using an acetylation-specific antibody was categorized as: strong (H3K9/K14Ac+/+), weak (H3K9/K14Ac+/−) or absent (H3K9/K14Ac−/−). (b) Reduction in H3K9K14ac in motor neurons expressing TDP-43 G348C was prevented by the HDAC inhibitors (c) SAHA or (d) RGFP963 demonstrating target engagement, whereas arimoclomol had no impact. (e) No alteration of histone acetylation by wild-type TDP-43. Data are presented as mean ± SD. Each data point on the graph represents the mean % of neurons in each of 6–13 cultures (10–59 neurons/culture). Statistical significance was evaluated by one-way ANOVA followed by Bonferroni post hoc analysis. * P < 0.05, ** P < 0.01, *** P < 0.001. Scale bar = 20 µm. Abbreviations used: HDAC, histone deacetylase; SAHA, suberoylanilide hydroxamic acid; SD, standard deviation; TDP-43, TAR DNA binding protein 43 kDa. 43 kDa; DMSO dimethyl sulfoxide.
Figure Legend Snippet: HDAC inhibition limited the reduction of histone acetylation in TDP-43 G348C -expressing motor neurons. After microinjection of plasmid encoding TDP-43 G348C or mCherry as control, cultures were treated with vehicle (DMSO), 4 µM arimoclomol, 4 µM SAHA, 1 µM RGFP963, alone and in combination for 3 days. Injected neurons were identified by double-labeling with rabbit anti-flag M2 to visualize TDP-43 G348C or by mCherry epifluorescence. (a) Acetylation of histone 3 at lysine residues 9 and 14 (H3K9/K14Ac), evaluated by immunocytochemistry using an acetylation-specific antibody was categorized as: strong (H3K9/K14Ac+/+), weak (H3K9/K14Ac+/−) or absent (H3K9/K14Ac−/−). (b) Reduction in H3K9K14ac in motor neurons expressing TDP-43 G348C was prevented by the HDAC inhibitors (c) SAHA or (d) RGFP963 demonstrating target engagement, whereas arimoclomol had no impact. (e) No alteration of histone acetylation by wild-type TDP-43. Data are presented as mean ± SD. Each data point on the graph represents the mean % of neurons in each of 6–13 cultures (10–59 neurons/culture). Statistical significance was evaluated by one-way ANOVA followed by Bonferroni post hoc analysis. * P < 0.05, ** P < 0.01, *** P < 0.001. Scale bar = 20 µm. Abbreviations used: HDAC, histone deacetylase; SAHA, suberoylanilide hydroxamic acid; SD, standard deviation; TDP-43, TAR DNA binding protein 43 kDa. 43 kDa; DMSO dimethyl sulfoxide.

Techniques Used: Inhibition, Expressing, Plasmid Preparation, Injection, Labeling, Immunocytochemistry, Histone Deacetylase Assay, Standard Deviation, Binding Assay

HDAC inhibitors and arimoclomol preserve Brg1, the ATPase component of nBAF chromatin remodeling complexes, in TDP-43 G348C -expressing motor neurons. Three days after microinjection, cultures were immunolabeled with rabbit anti-Brg1 and mouse anti-flag M2 to visualize TDP-43 G348C . (a) Intensity of Brg1 immunolabeling in the nucleus was categorized as: strong (+/+), (+/−), or none (−/−). (b) Compared to controls (mCherry), expression of TDP-43 G348C significantly reduced the percentage of motor neurons displaying strong Brg1 labeling. This percentage was maintained similar to controls by (c) SAHA and (d) RGFP963 treatments. Arimoclomol also maintained nuclear Brg1 expression, although slightly less efficiently than HDAC inhibitors. When SAHA or RGFP963 was combined with arimoclomol, a modest enhancement occurred. (e) Brg1 distribution was not significantly affected by overexpression of wild-type TDP-43. Data are presented as mean ± SD. Each data point on the graph represents the mean % of neurons in each of 4–15 cultures (13–39 neurons/culture). Statistical significance was evaluated through one-way ANOVA followed by Bonferroni post hoc analysis. * P < 0.05, ** P < 0.01, *** P < 0.001. Scale bar = 20 µm. Abbreviations used: HDAC, histone deacetylase; nBAF, neuronal Brm/Brg-associated factor; SAHA, suberoylanilide hydroxamic acid; SD, standard deviation; TDP-43, TAR DNA binding protein 43 kDa.
Figure Legend Snippet: HDAC inhibitors and arimoclomol preserve Brg1, the ATPase component of nBAF chromatin remodeling complexes, in TDP-43 G348C -expressing motor neurons. Three days after microinjection, cultures were immunolabeled with rabbit anti-Brg1 and mouse anti-flag M2 to visualize TDP-43 G348C . (a) Intensity of Brg1 immunolabeling in the nucleus was categorized as: strong (+/+), (+/−), or none (−/−). (b) Compared to controls (mCherry), expression of TDP-43 G348C significantly reduced the percentage of motor neurons displaying strong Brg1 labeling. This percentage was maintained similar to controls by (c) SAHA and (d) RGFP963 treatments. Arimoclomol also maintained nuclear Brg1 expression, although slightly less efficiently than HDAC inhibitors. When SAHA or RGFP963 was combined with arimoclomol, a modest enhancement occurred. (e) Brg1 distribution was not significantly affected by overexpression of wild-type TDP-43. Data are presented as mean ± SD. Each data point on the graph represents the mean % of neurons in each of 4–15 cultures (13–39 neurons/culture). Statistical significance was evaluated through one-way ANOVA followed by Bonferroni post hoc analysis. * P < 0.05, ** P < 0.01, *** P < 0.001. Scale bar = 20 µm. Abbreviations used: HDAC, histone deacetylase; nBAF, neuronal Brm/Brg-associated factor; SAHA, suberoylanilide hydroxamic acid; SD, standard deviation; TDP-43, TAR DNA binding protein 43 kDa.

Techniques Used: Expressing, Immunolabeling, Labeling, Over Expression, Histone Deacetylase Assay, Standard Deviation, Binding Assay


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Millipore mouse anti flag m2 ab
Mouse Anti Flag M2 Ab, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Millipore mouse m2 flag ab
Mouse M2 Flag Ab, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Millipore mouse m2 flag ab
Mouse M2 Flag Ab, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore mouse anti flag m2 monoclonal antibody
    Mouse Anti Flag M2 Monoclonal Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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