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Bethyl rabbit anti rpa2 phospho s4 s8
PICH plays both catalytic and protein recruitment function in UFB resolution. ( A ) RPE1 PICH-AG cells expressing GFP-PICH constructs were treated with Dox and IAA for 72 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( B ) Clonogenic cell survival assays were carried out on RPE1 PICH-AG cells expressing different GFP-PICH constructs treated with Dox and IAA. ( C ) RPE1 PICH-AG expressing GFP-PICH WT or GFP-PICH K128A were treated with Dox and IAA for 24 h. GFP, histone H3 pS10 and DNA were visualized using anti-GFP (green), anti-histone H3 pS10 (red) antibodies and DAPI (blue), respectively. ( D ) Quantification of the number of PICH-coated UFBs and chromatin bridges per cells (90 cells per condition) as visualized in panel (C). ( E ) RPE1 PICH-AG expressing GFP-PICH WT , GFP-PICH K128A or GFP- PICH Δ791–1000 were treated with Dox and IAA for 24 h. Cells were then treated with ICRF-193 (25 nM, 2 h) before fixed. GFP, <t>RPA2</t> and DNA were visualized using anti-GFP (green), anti-RPA2 (red) antibodies and DAPI (blue), respectively. Scale bars, 10 μm. ( F ) Quantification of the number of PICH-coated and RPA2-coated UFBs per cells (90 cells per condition) as visualized in panel (E). ( G ) HeLa TOP3A-GFP cells were transfected with the indicated siRNAs for 48 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( H ) Cells in panel (G) were treated with ICRF-193 (50 nM) for 2 h. GFP, PICH and DNA were visualized using anti-GFP (green), anti-PICH (red) antibodies and DAPI (blue), respectively. ( I ) Quantification of the number of PICH-coated and TOP3A-coated UFBs per cells (>50 cells per condition) as visualized in panel (H). In all quantified data, bars represent the mean ± SD of n = 3 independent experiments. ** P < 0.01; **** P < 0.0001; ns (not significant) P > 0.05; statistical significance values were determined with unpaired two-tailed t -tests.
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1) Product Images from "The interplay of the translocase activity and protein recruitment function of PICH in ultrafine anaphase bridge resolution and genomic stability"

Article Title: The interplay of the translocase activity and protein recruitment function of PICH in ultrafine anaphase bridge resolution and genomic stability

Journal: Nucleic Acids Research

doi: 10.1093/nar/gkae1249

PICH plays both catalytic and protein recruitment function in UFB resolution. ( A ) RPE1 PICH-AG cells expressing GFP-PICH constructs were treated with Dox and IAA for 72 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( B ) Clonogenic cell survival assays were carried out on RPE1 PICH-AG cells expressing different GFP-PICH constructs treated with Dox and IAA. ( C ) RPE1 PICH-AG expressing GFP-PICH WT or GFP-PICH K128A were treated with Dox and IAA for 24 h. GFP, histone H3 pS10 and DNA were visualized using anti-GFP (green), anti-histone H3 pS10 (red) antibodies and DAPI (blue), respectively. ( D ) Quantification of the number of PICH-coated UFBs and chromatin bridges per cells (90 cells per condition) as visualized in panel (C). ( E ) RPE1 PICH-AG expressing GFP-PICH WT , GFP-PICH K128A or GFP- PICH Δ791–1000 were treated with Dox and IAA for 24 h. Cells were then treated with ICRF-193 (25 nM, 2 h) before fixed. GFP, RPA2 and DNA were visualized using anti-GFP (green), anti-RPA2 (red) antibodies and DAPI (blue), respectively. Scale bars, 10 μm. ( F ) Quantification of the number of PICH-coated and RPA2-coated UFBs per cells (90 cells per condition) as visualized in panel (E). ( G ) HeLa TOP3A-GFP cells were transfected with the indicated siRNAs for 48 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( H ) Cells in panel (G) were treated with ICRF-193 (50 nM) for 2 h. GFP, PICH and DNA were visualized using anti-GFP (green), anti-PICH (red) antibodies and DAPI (blue), respectively. ( I ) Quantification of the number of PICH-coated and TOP3A-coated UFBs per cells (>50 cells per condition) as visualized in panel (H). In all quantified data, bars represent the mean ± SD of n = 3 independent experiments. ** P < 0.01; **** P < 0.0001; ns (not significant) P > 0.05; statistical significance values were determined with unpaired two-tailed t -tests.
Figure Legend Snippet: PICH plays both catalytic and protein recruitment function in UFB resolution. ( A ) RPE1 PICH-AG cells expressing GFP-PICH constructs were treated with Dox and IAA for 72 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( B ) Clonogenic cell survival assays were carried out on RPE1 PICH-AG cells expressing different GFP-PICH constructs treated with Dox and IAA. ( C ) RPE1 PICH-AG expressing GFP-PICH WT or GFP-PICH K128A were treated with Dox and IAA for 24 h. GFP, histone H3 pS10 and DNA were visualized using anti-GFP (green), anti-histone H3 pS10 (red) antibodies and DAPI (blue), respectively. ( D ) Quantification of the number of PICH-coated UFBs and chromatin bridges per cells (90 cells per condition) as visualized in panel (C). ( E ) RPE1 PICH-AG expressing GFP-PICH WT , GFP-PICH K128A or GFP- PICH Δ791–1000 were treated with Dox and IAA for 24 h. Cells were then treated with ICRF-193 (25 nM, 2 h) before fixed. GFP, RPA2 and DNA were visualized using anti-GFP (green), anti-RPA2 (red) antibodies and DAPI (blue), respectively. Scale bars, 10 μm. ( F ) Quantification of the number of PICH-coated and RPA2-coated UFBs per cells (90 cells per condition) as visualized in panel (E). ( G ) HeLa TOP3A-GFP cells were transfected with the indicated siRNAs for 48 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( H ) Cells in panel (G) were treated with ICRF-193 (50 nM) for 2 h. GFP, PICH and DNA were visualized using anti-GFP (green), anti-PICH (red) antibodies and DAPI (blue), respectively. ( I ) Quantification of the number of PICH-coated and TOP3A-coated UFBs per cells (>50 cells per condition) as visualized in panel (H). In all quantified data, bars represent the mean ± SD of n = 3 independent experiments. ** P < 0.01; **** P < 0.0001; ns (not significant) P > 0.05; statistical significance values were determined with unpaired two-tailed t -tests.

Techniques Used: Expressing, Construct, Western Blot, Transfection, Two Tailed Test



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PICH plays both catalytic and protein recruitment function in UFB resolution. ( A ) RPE1 PICH-AG cells expressing GFP-PICH constructs were treated with Dox and IAA for 72 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( B ) Clonogenic cell survival assays were carried out on RPE1 PICH-AG cells expressing different GFP-PICH constructs treated with Dox and IAA. ( C ) RPE1 PICH-AG expressing GFP-PICH WT or GFP-PICH K128A were treated with Dox and IAA for 24 h. GFP, histone H3 pS10 and DNA were visualized using anti-GFP (green), anti-histone H3 pS10 (red) antibodies and DAPI (blue), respectively. ( D ) Quantification of the number of PICH-coated UFBs and chromatin bridges per cells (90 cells per condition) as visualized in panel (C). ( E ) RPE1 PICH-AG expressing GFP-PICH WT , GFP-PICH K128A or GFP- PICH Δ791–1000 were treated with Dox and IAA for 24 h. Cells were then treated with ICRF-193 (25 nM, 2 h) before fixed. GFP, <t>RPA2</t> and DNA were visualized using anti-GFP (green), anti-RPA2 (red) antibodies and DAPI (blue), respectively. Scale bars, 10 μm. ( F ) Quantification of the number of PICH-coated and RPA2-coated UFBs per cells (90 cells per condition) as visualized in panel (E). ( G ) HeLa TOP3A-GFP cells were transfected with the indicated siRNAs for 48 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( H ) Cells in panel (G) were treated with ICRF-193 (50 nM) for 2 h. GFP, PICH and DNA were visualized using anti-GFP (green), anti-PICH (red) antibodies and DAPI (blue), respectively. ( I ) Quantification of the number of PICH-coated and TOP3A-coated UFBs per cells (>50 cells per condition) as visualized in panel (H). In all quantified data, bars represent the mean ± SD of n = 3 independent experiments. ** P < 0.01; **** P < 0.0001; ns (not significant) P > 0.05; statistical significance values were determined with unpaired two-tailed t -tests.
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PICH plays both catalytic and protein recruitment function in UFB resolution. ( A ) RPE1 PICH-AG cells expressing GFP-PICH constructs were treated with Dox and IAA for 72 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( B ) Clonogenic cell survival assays were carried out on RPE1 PICH-AG cells expressing different GFP-PICH constructs treated with Dox and IAA. ( C ) RPE1 PICH-AG expressing GFP-PICH WT or GFP-PICH K128A were treated with Dox and IAA for 24 h. GFP, histone H3 pS10 and DNA were visualized using anti-GFP (green), anti-histone H3 pS10 (red) antibodies and DAPI (blue), respectively. ( D ) Quantification of the number of PICH-coated UFBs and chromatin bridges per cells (90 cells per condition) as visualized in panel (C). ( E ) RPE1 PICH-AG expressing GFP-PICH WT , GFP-PICH K128A or GFP- PICH Δ791–1000 were treated with Dox and IAA for 24 h. Cells were then treated with ICRF-193 (25 nM, 2 h) before fixed. GFP, <t>RPA2</t> and DNA were visualized using anti-GFP (green), anti-RPA2 (red) antibodies and DAPI (blue), respectively. Scale bars, 10 μm. ( F ) Quantification of the number of PICH-coated and RPA2-coated UFBs per cells (90 cells per condition) as visualized in panel (E). ( G ) HeLa TOP3A-GFP cells were transfected with the indicated siRNAs for 48 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( H ) Cells in panel (G) were treated with ICRF-193 (50 nM) for 2 h. GFP, PICH and DNA were visualized using anti-GFP (green), anti-PICH (red) antibodies and DAPI (blue), respectively. ( I ) Quantification of the number of PICH-coated and TOP3A-coated UFBs per cells (>50 cells per condition) as visualized in panel (H). In all quantified data, bars represent the mean ± SD of n = 3 independent experiments. ** P < 0.01; **** P < 0.0001; ns (not significant) P > 0.05; statistical significance values were determined with unpaired two-tailed t -tests.
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PICH plays both catalytic and protein recruitment function in UFB resolution. ( A ) RPE1 PICH-AG cells expressing GFP-PICH constructs were treated with Dox and IAA for 72 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( B ) Clonogenic cell survival assays were carried out on RPE1 PICH-AG cells expressing different GFP-PICH constructs treated with Dox and IAA. ( C ) RPE1 PICH-AG expressing GFP-PICH WT or GFP-PICH K128A were treated with Dox and IAA for 24 h. GFP, histone H3 pS10 and DNA were visualized using anti-GFP (green), anti-histone H3 pS10 (red) antibodies and DAPI (blue), respectively. ( D ) Quantification of the number of PICH-coated UFBs and chromatin bridges per cells (90 cells per condition) as visualized in panel (C). ( E ) RPE1 PICH-AG expressing GFP-PICH WT , GFP-PICH K128A or GFP- PICH Δ791–1000 were treated with Dox and IAA for 24 h. Cells were then treated with ICRF-193 (25 nM, 2 h) before fixed. GFP, <t>RPA2</t> and DNA were visualized using anti-GFP (green), anti-RPA2 (red) antibodies and DAPI (blue), respectively. Scale bars, 10 μm. ( F ) Quantification of the number of PICH-coated and RPA2-coated UFBs per cells (90 cells per condition) as visualized in panel (E). ( G ) HeLa TOP3A-GFP cells were transfected with the indicated siRNAs for 48 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( H ) Cells in panel (G) were treated with ICRF-193 (50 nM) for 2 h. GFP, PICH and DNA were visualized using anti-GFP (green), anti-PICH (red) antibodies and DAPI (blue), respectively. ( I ) Quantification of the number of PICH-coated and TOP3A-coated UFBs per cells (>50 cells per condition) as visualized in panel (H). In all quantified data, bars represent the mean ± SD of n = 3 independent experiments. ** P < 0.01; **** P < 0.0001; ns (not significant) P > 0.05; statistical significance values were determined with unpaired two-tailed t -tests.
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PICH plays both catalytic and protein recruitment function in UFB resolution. ( A ) RPE1 PICH-AG cells expressing GFP-PICH constructs were treated with Dox and IAA for 72 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( B ) Clonogenic cell survival assays were carried out on RPE1 PICH-AG cells expressing different GFP-PICH constructs treated with Dox and IAA. ( C ) RPE1 PICH-AG expressing GFP-PICH WT or GFP-PICH K128A were treated with Dox and IAA for 24 h. GFP, histone H3 pS10 and DNA were visualized using anti-GFP (green), anti-histone H3 pS10 (red) antibodies and DAPI (blue), respectively. ( D ) Quantification of the number of PICH-coated UFBs and chromatin bridges per cells (90 cells per condition) as visualized in panel (C). ( E ) RPE1 PICH-AG expressing GFP-PICH WT , GFP-PICH K128A or GFP- PICH Δ791–1000 were treated with Dox and IAA for 24 h. Cells were then treated with ICRF-193 (25 nM, 2 h) before fixed. GFP, <t>RPA2</t> and DNA were visualized using anti-GFP (green), anti-RPA2 (red) antibodies and DAPI (blue), respectively. Scale bars, 10 μm. ( F ) Quantification of the number of PICH-coated and RPA2-coated UFBs per cells (90 cells per condition) as visualized in panel (E). ( G ) HeLa TOP3A-GFP cells were transfected with the indicated siRNAs for 48 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( H ) Cells in panel (G) were treated with ICRF-193 (50 nM) for 2 h. GFP, PICH and DNA were visualized using anti-GFP (green), anti-PICH (red) antibodies and DAPI (blue), respectively. ( I ) Quantification of the number of PICH-coated and TOP3A-coated UFBs per cells (>50 cells per condition) as visualized in panel (H). In all quantified data, bars represent the mean ± SD of n = 3 independent experiments. ** P < 0.01; **** P < 0.0001; ns (not significant) P > 0.05; statistical significance values were determined with unpaired two-tailed t -tests.
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PICH plays both catalytic and protein recruitment function in UFB resolution. ( A ) RPE1 PICH-AG cells expressing GFP-PICH constructs were treated with Dox and IAA for 72 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( B ) Clonogenic cell survival assays were carried out on RPE1 PICH-AG cells expressing different GFP-PICH constructs treated with Dox and IAA. ( C ) RPE1 PICH-AG expressing GFP-PICH WT or GFP-PICH K128A were treated with Dox and IAA for 24 h. GFP, histone H3 pS10 and DNA were visualized using anti-GFP (green), anti-histone H3 pS10 (red) antibodies and DAPI (blue), respectively. ( D ) Quantification of the number of PICH-coated UFBs and chromatin bridges per cells (90 cells per condition) as visualized in panel (C). ( E ) RPE1 PICH-AG expressing GFP-PICH WT , GFP-PICH K128A or GFP- PICH Δ791–1000 were treated with Dox and IAA for 24 h. Cells were then treated with ICRF-193 (25 nM, 2 h) before fixed. GFP, <t>RPA2</t> and DNA were visualized using anti-GFP (green), anti-RPA2 (red) antibodies and DAPI (blue), respectively. Scale bars, 10 μm. ( F ) Quantification of the number of PICH-coated and RPA2-coated UFBs per cells (90 cells per condition) as visualized in panel (E). ( G ) HeLa TOP3A-GFP cells were transfected with the indicated siRNAs for 48 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( H ) Cells in panel (G) were treated with ICRF-193 (50 nM) for 2 h. GFP, PICH and DNA were visualized using anti-GFP (green), anti-PICH (red) antibodies and DAPI (blue), respectively. ( I ) Quantification of the number of PICH-coated and TOP3A-coated UFBs per cells (>50 cells per condition) as visualized in panel (H). In all quantified data, bars represent the mean ± SD of n = 3 independent experiments. ** P < 0.01; **** P < 0.0001; ns (not significant) P > 0.05; statistical significance values were determined with unpaired two-tailed t -tests.
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PICH plays both catalytic and protein recruitment function in UFB resolution. ( A ) RPE1 PICH-AG cells expressing GFP-PICH constructs were treated with Dox and IAA for 72 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( B ) Clonogenic cell survival assays were carried out on RPE1 PICH-AG cells expressing different GFP-PICH constructs treated with Dox and IAA. ( C ) RPE1 PICH-AG expressing GFP-PICH WT or GFP-PICH K128A were treated with Dox and IAA for 24 h. GFP, histone H3 pS10 and DNA were visualized using anti-GFP (green), anti-histone H3 pS10 (red) antibodies and DAPI (blue), respectively. ( D ) Quantification of the number of PICH-coated UFBs and chromatin bridges per cells (90 cells per condition) as visualized in panel (C). ( E ) RPE1 PICH-AG expressing GFP-PICH WT , GFP-PICH K128A or GFP- PICH Δ791–1000 were treated with Dox and IAA for 24 h. Cells were then treated with ICRF-193 (25 nM, 2 h) before fixed. GFP, <t>RPA2</t> and DNA were visualized using anti-GFP (green), anti-RPA2 (red) antibodies and DAPI (blue), respectively. Scale bars, 10 μm. ( F ) Quantification of the number of PICH-coated and RPA2-coated UFBs per cells (90 cells per condition) as visualized in panel (E). ( G ) HeLa TOP3A-GFP cells were transfected with the indicated siRNAs for 48 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( H ) Cells in panel (G) were treated with ICRF-193 (50 nM) for 2 h. GFP, PICH and DNA were visualized using anti-GFP (green), anti-PICH (red) antibodies and DAPI (blue), respectively. ( I ) Quantification of the number of PICH-coated and TOP3A-coated UFBs per cells (>50 cells per condition) as visualized in panel (H). In all quantified data, bars represent the mean ± SD of n = 3 independent experiments. ** P < 0.01; **** P < 0.0001; ns (not significant) P > 0.05; statistical significance values were determined with unpaired two-tailed t -tests.
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PICH plays both catalytic and protein recruitment function in UFB resolution. ( A ) RPE1 PICH-AG cells expressing GFP-PICH constructs were treated with Dox and IAA for 72 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( B ) Clonogenic cell survival assays were carried out on RPE1 PICH-AG cells expressing different GFP-PICH constructs treated with Dox and IAA. ( C ) RPE1 PICH-AG expressing GFP-PICH WT or GFP-PICH K128A were treated with Dox and IAA for 24 h. GFP, histone H3 pS10 and DNA were visualized using anti-GFP (green), anti-histone H3 pS10 (red) antibodies and DAPI (blue), respectively. ( D ) Quantification of the number of PICH-coated UFBs and chromatin bridges per cells (90 cells per condition) as visualized in panel (C). ( E ) RPE1 PICH-AG expressing GFP-PICH WT , GFP-PICH K128A or GFP- PICH Δ791–1000 were treated with Dox and IAA for 24 h. Cells were then treated with ICRF-193 (25 nM, 2 h) before fixed. GFP, <t>RPA2</t> and DNA were visualized using anti-GFP (green), anti-RPA2 (red) antibodies and DAPI (blue), respectively. Scale bars, 10 μm. ( F ) Quantification of the number of PICH-coated and RPA2-coated UFBs per cells (90 cells per condition) as visualized in panel (E). ( G ) HeLa TOP3A-GFP cells were transfected with the indicated siRNAs for 48 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( H ) Cells in panel (G) were treated with ICRF-193 (50 nM) for 2 h. GFP, PICH and DNA were visualized using anti-GFP (green), anti-PICH (red) antibodies and DAPI (blue), respectively. ( I ) Quantification of the number of PICH-coated and TOP3A-coated UFBs per cells (>50 cells per condition) as visualized in panel (H). In all quantified data, bars represent the mean ± SD of n = 3 independent experiments. ** P < 0.01; **** P < 0.0001; ns (not significant) P > 0.05; statistical significance values were determined with unpaired two-tailed t -tests.
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Image Search Results


PICH plays both catalytic and protein recruitment function in UFB resolution. ( A ) RPE1 PICH-AG cells expressing GFP-PICH constructs were treated with Dox and IAA for 72 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( B ) Clonogenic cell survival assays were carried out on RPE1 PICH-AG cells expressing different GFP-PICH constructs treated with Dox and IAA. ( C ) RPE1 PICH-AG expressing GFP-PICH WT or GFP-PICH K128A were treated with Dox and IAA for 24 h. GFP, histone H3 pS10 and DNA were visualized using anti-GFP (green), anti-histone H3 pS10 (red) antibodies and DAPI (blue), respectively. ( D ) Quantification of the number of PICH-coated UFBs and chromatin bridges per cells (90 cells per condition) as visualized in panel (C). ( E ) RPE1 PICH-AG expressing GFP-PICH WT , GFP-PICH K128A or GFP- PICH Δ791–1000 were treated with Dox and IAA for 24 h. Cells were then treated with ICRF-193 (25 nM, 2 h) before fixed. GFP, RPA2 and DNA were visualized using anti-GFP (green), anti-RPA2 (red) antibodies and DAPI (blue), respectively. Scale bars, 10 μm. ( F ) Quantification of the number of PICH-coated and RPA2-coated UFBs per cells (90 cells per condition) as visualized in panel (E). ( G ) HeLa TOP3A-GFP cells were transfected with the indicated siRNAs for 48 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( H ) Cells in panel (G) were treated with ICRF-193 (50 nM) for 2 h. GFP, PICH and DNA were visualized using anti-GFP (green), anti-PICH (red) antibodies and DAPI (blue), respectively. ( I ) Quantification of the number of PICH-coated and TOP3A-coated UFBs per cells (>50 cells per condition) as visualized in panel (H). In all quantified data, bars represent the mean ± SD of n = 3 independent experiments. ** P < 0.01; **** P < 0.0001; ns (not significant) P > 0.05; statistical significance values were determined with unpaired two-tailed t -tests.

Journal: Nucleic Acids Research

Article Title: The interplay of the translocase activity and protein recruitment function of PICH in ultrafine anaphase bridge resolution and genomic stability

doi: 10.1093/nar/gkae1249

Figure Lengend Snippet: PICH plays both catalytic and protein recruitment function in UFB resolution. ( A ) RPE1 PICH-AG cells expressing GFP-PICH constructs were treated with Dox and IAA for 72 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( B ) Clonogenic cell survival assays were carried out on RPE1 PICH-AG cells expressing different GFP-PICH constructs treated with Dox and IAA. ( C ) RPE1 PICH-AG expressing GFP-PICH WT or GFP-PICH K128A were treated with Dox and IAA for 24 h. GFP, histone H3 pS10 and DNA were visualized using anti-GFP (green), anti-histone H3 pS10 (red) antibodies and DAPI (blue), respectively. ( D ) Quantification of the number of PICH-coated UFBs and chromatin bridges per cells (90 cells per condition) as visualized in panel (C). ( E ) RPE1 PICH-AG expressing GFP-PICH WT , GFP-PICH K128A or GFP- PICH Δ791–1000 were treated with Dox and IAA for 24 h. Cells were then treated with ICRF-193 (25 nM, 2 h) before fixed. GFP, RPA2 and DNA were visualized using anti-GFP (green), anti-RPA2 (red) antibodies and DAPI (blue), respectively. Scale bars, 10 μm. ( F ) Quantification of the number of PICH-coated and RPA2-coated UFBs per cells (90 cells per condition) as visualized in panel (E). ( G ) HeLa TOP3A-GFP cells were transfected with the indicated siRNAs for 48 h. Cell extracts were analyzed by western blotting with the indicated antibodies. ( H ) Cells in panel (G) were treated with ICRF-193 (50 nM) for 2 h. GFP, PICH and DNA were visualized using anti-GFP (green), anti-PICH (red) antibodies and DAPI (blue), respectively. ( I ) Quantification of the number of PICH-coated and TOP3A-coated UFBs per cells (>50 cells per condition) as visualized in panel (H). In all quantified data, bars represent the mean ± SD of n = 3 independent experiments. ** P < 0.01; **** P < 0.0001; ns (not significant) P > 0.05; statistical significance values were determined with unpaired two-tailed t -tests.

Article Snippet: Proteins were detected by western blotting or immunofluorescence using the following primary antibodies: rabbit anti-GFP (1:5000, Abcam, #ab290), mouse anti-GFP (1:1000, Roche, #11814460001), rabbit anti-PICH (1:1000, Cell Signaling, #8886), mouse anti-PICH (1:1000, Millipore, #04–1540), rabbit anti-OsTIR1 (1:1000, MBL, #PD048), rabbit anti-53BP1 (1:2000, Abcam, #ab36823), mouse anti-cyclin A (1:200, Santa Cruz, #sc-271682), rabbit anti-Rb phosphor-S807/811 (1:1000, Cell Signaling, #8516), mouse anti-p53 (1:1000, Santa Cruz, #sc-126), rabbit anti-p53 phospho-S15 (1:1000, Cell Signaling, #9284), mouse anti-p21 (1:1000, Santa Cruz, #sc-6246), rabbit anti-cGAS (1:1000, Cell Signaling, #15102), rabbit anti-IRF3 (1:1000, Abcam, #ab68481), rabbit anti-IRF3 phospho-S386 (1:1000, Abcam, #ab76493), rabbit anti-BLM (1:1000, Abcam, #ab2179), rabbit anti-TOP3A (1:1000, Proteintech, #14525–1-AP), rabbit anti-RMI1 (1:1000, Abcam, #ab70525), mouse anti-PLK1 (1:1000, Santa Cruz, #sc-17783), mouse anti-histone H3 phospho-S10 (1:5000, Abcam, #ab14955), mouse anti-α-tubulin (1:1000, Sigma–Aldrich, #00020911), mouse anti-CHK1 (1:1000, Sigma–Aldrich, #C9358), rabbit-anti-CHK1 phospho-S317 (1:1000, Cell Signaling, #2344), mouse anti-CHK2 (1:1000, Millipore, #05–649), rabbit anti-CHK2 phospho-T68 (1:1000, Cell Signaling, #2661), rabbit anti-KAP1 phospho-S824 (1:1000, Abcam, #ab70369), mouse anti-RPA2 (1:1000, Abcam, #ab2175), rabbit anti-RPA2 phospho-S4/S8 (1:1000, Bethyl, #A300-245A), rabbit anti-SMC2 (1:1000, Bethyl, #A300-058A), rabbit anti-STING phospho-S366 (1:1000, Cell Signaling, #19781), rabbit anti-TBK1 phospho-S172 (1:1000, Cell Signaling, #5483) and rabbit anti-RIF1 (1:1000, Bethyl, #A300-568A).

Techniques: Expressing, Construct, Western Blot, Transfection, Two Tailed Test