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ctip 61141 antibody  (Active Motif)


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    Structured Review

    Active Motif ctip 61141 antibody
    a , b U2OS cells stably <t>expressing</t> <t>GFP,</t> GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3 and treated with CPT for 24 h followed by CCK8 assay (a), or Olaparib for 48 h followed by colony formation assay (b). c U2OS-DR-GFP stably expressing Flag, Flag-SART3, or Flag-SART3-YA1 were transfected with siSART3, then infected with I-SceI lentivirus. The percentage of GFP-positive cells was quantitated by FACS (left). The specified proteins were examined by immunoblotting (right). d U2OS cells stably expressing GFP, GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3, treated with ETO (RPA32, BRCA1 and BARD1) or CPT (DDX1) and further recovery for 2 h. Immunostainings was performed. The percentages of cells with more than 10 or 20 foci were quantified (bottom). Representative images are shown (top). Scale bars for overall and magnified images are respectively 50 and 10 µm. e U2OS-ER-AsiSI cells stably expressing GFP, GFP-SART3 or GFP-SART3-YA1 were transfected with the indicated siRNAs and treated with 4-OHT, followed by qPCR to measure DNA end resection (top). Immunoblotting verifies the knockdown of SART3 and <t>CtIP</t> (bottom). f HEK293T cells transfected with the indicated constructs were treated with CPT (5 µM, 2 h). Chromatin fractions were isolated for immunoprecipitation with anti-GFP beads, followed by immunoblotting with indicated antibodies. Asterisks indicate none-specific bands. CF-IP stands for Chromatin Fractions-IP. g U2OS-GFP-MMEJ cells stably expressing Flag, Flag-SART3, Flag-SART3-R836W, or Flag-SART3-YA1 were transfected with the indicated siRNAs followed by infection with I-SceI lentivirus. The percentage of GFP-positive cells was quantified by FACS analysis (top). The specified proteins were examined by immunoblotting (bottom). h U2OS cells stably expressing GFP, GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3 for 48 h. Cells were then exposed to 15 J/m 2 UVC and repaired for 4 h. The TIF and WCL were harvested and analyzed with the indicated antibodies. i Working model of how SART3 regulates HR repair. In ( a – e ), and ( g ) error bars represent mean ± SEM ( N = 3 independent experiments), and p values were calculated using one-way ANOVA analysis with Tukey test ( a , b ) or unpaired two-tailed Student’s t test ( c – e , g ). Source data are provided as a Source Data file.
    Ctip 61141 Antibody, supplied by Active Motif, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ctip+antibody+61141/ctip+61141+antibody/pmc11885473-346-83-85
    Average 90 stars, based on 1 article reviews
    ctip 61141 antibody - by Bioz Stars, 2026-09
    90/100 stars

    Images

    1) Product Images from "SART3 promotes homologous recombination repair by stimulating DNA-RNA hybrids removal and DNA end resection"

    Article Title: SART3 promotes homologous recombination repair by stimulating DNA-RNA hybrids removal and DNA end resection

    Journal: Nature Communications

    doi: 10.1038/s41467-025-57599-8

    a , b U2OS cells stably expressing GFP, GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3 and treated with CPT for 24 h followed by CCK8 assay (a), or Olaparib for 48 h followed by colony formation assay (b). c U2OS-DR-GFP stably expressing Flag, Flag-SART3, or Flag-SART3-YA1 were transfected with siSART3, then infected with I-SceI lentivirus. The percentage of GFP-positive cells was quantitated by FACS (left). The specified proteins were examined by immunoblotting (right). d U2OS cells stably expressing GFP, GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3, treated with ETO (RPA32, BRCA1 and BARD1) or CPT (DDX1) and further recovery for 2 h. Immunostainings was performed. The percentages of cells with more than 10 or 20 foci were quantified (bottom). Representative images are shown (top). Scale bars for overall and magnified images are respectively 50 and 10 µm. e U2OS-ER-AsiSI cells stably expressing GFP, GFP-SART3 or GFP-SART3-YA1 were transfected with the indicated siRNAs and treated with 4-OHT, followed by qPCR to measure DNA end resection (top). Immunoblotting verifies the knockdown of SART3 and CtIP (bottom). f HEK293T cells transfected with the indicated constructs were treated with CPT (5 µM, 2 h). Chromatin fractions were isolated for immunoprecipitation with anti-GFP beads, followed by immunoblotting with indicated antibodies. Asterisks indicate none-specific bands. CF-IP stands for Chromatin Fractions-IP. g U2OS-GFP-MMEJ cells stably expressing Flag, Flag-SART3, Flag-SART3-R836W, or Flag-SART3-YA1 were transfected with the indicated siRNAs followed by infection with I-SceI lentivirus. The percentage of GFP-positive cells was quantified by FACS analysis (top). The specified proteins were examined by immunoblotting (bottom). h U2OS cells stably expressing GFP, GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3 for 48 h. Cells were then exposed to 15 J/m 2 UVC and repaired for 4 h. The TIF and WCL were harvested and analyzed with the indicated antibodies. i Working model of how SART3 regulates HR repair. In ( a – e ), and ( g ) error bars represent mean ± SEM ( N = 3 independent experiments), and p values were calculated using one-way ANOVA analysis with Tukey test ( a , b ) or unpaired two-tailed Student’s t test ( c – e , g ). Source data are provided as a Source Data file.
    Figure Legend Snippet: a , b U2OS cells stably expressing GFP, GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3 and treated with CPT for 24 h followed by CCK8 assay (a), or Olaparib for 48 h followed by colony formation assay (b). c U2OS-DR-GFP stably expressing Flag, Flag-SART3, or Flag-SART3-YA1 were transfected with siSART3, then infected with I-SceI lentivirus. The percentage of GFP-positive cells was quantitated by FACS (left). The specified proteins were examined by immunoblotting (right). d U2OS cells stably expressing GFP, GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3, treated with ETO (RPA32, BRCA1 and BARD1) or CPT (DDX1) and further recovery for 2 h. Immunostainings was performed. The percentages of cells with more than 10 or 20 foci were quantified (bottom). Representative images are shown (top). Scale bars for overall and magnified images are respectively 50 and 10 µm. e U2OS-ER-AsiSI cells stably expressing GFP, GFP-SART3 or GFP-SART3-YA1 were transfected with the indicated siRNAs and treated with 4-OHT, followed by qPCR to measure DNA end resection (top). Immunoblotting verifies the knockdown of SART3 and CtIP (bottom). f HEK293T cells transfected with the indicated constructs were treated with CPT (5 µM, 2 h). Chromatin fractions were isolated for immunoprecipitation with anti-GFP beads, followed by immunoblotting with indicated antibodies. Asterisks indicate none-specific bands. CF-IP stands for Chromatin Fractions-IP. g U2OS-GFP-MMEJ cells stably expressing Flag, Flag-SART3, Flag-SART3-R836W, or Flag-SART3-YA1 were transfected with the indicated siRNAs followed by infection with I-SceI lentivirus. The percentage of GFP-positive cells was quantified by FACS analysis (top). The specified proteins were examined by immunoblotting (bottom). h U2OS cells stably expressing GFP, GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3 for 48 h. Cells were then exposed to 15 J/m 2 UVC and repaired for 4 h. The TIF and WCL were harvested and analyzed with the indicated antibodies. i Working model of how SART3 regulates HR repair. In ( a – e ), and ( g ) error bars represent mean ± SEM ( N = 3 independent experiments), and p values were calculated using one-way ANOVA analysis with Tukey test ( a , b ) or unpaired two-tailed Student’s t test ( c – e , g ). Source data are provided as a Source Data file.

    Techniques Used: Stable Transfection, Expressing, Transfection, CCK-8 Assay, Colony Assay, Infection, Western Blot, Knockdown, Construct, Isolation, Immunoprecipitation, Two Tailed Test

    Related Articles

    other:

    Article Title: UFL1 promotes histone H4 ufmylation and ATM activation.
    Article Snippet: CTIP antibody (61141, 1:1000 for IF) was purchased from Active Motif.

    Chromatin Immunoprecipitation:

    Article Title: Genome-wide analysis of DNA-PK-bound MRN cleavage products supports a sequential model of DSB repair pathway choice.
    Article Snippet: .. For CtIP GLASS ChIP experiments, methods were identical except that CtIP antibody (Active Motif, 61141) was used. ..



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    Active Motif ctip 61141 antibody
    a , b U2OS cells stably <t>expressing</t> <t>GFP,</t> GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3 and treated with CPT for 24 h followed by CCK8 assay (a), or Olaparib for 48 h followed by colony formation assay (b). c U2OS-DR-GFP stably expressing Flag, Flag-SART3, or Flag-SART3-YA1 were transfected with siSART3, then infected with I-SceI lentivirus. The percentage of GFP-positive cells was quantitated by FACS (left). The specified proteins were examined by immunoblotting (right). d U2OS cells stably expressing GFP, GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3, treated with ETO (RPA32, BRCA1 and BARD1) or CPT (DDX1) and further recovery for 2 h. Immunostainings was performed. The percentages of cells with more than 10 or 20 foci were quantified (bottom). Representative images are shown (top). Scale bars for overall and magnified images are respectively 50 and 10 µm. e U2OS-ER-AsiSI cells stably expressing GFP, GFP-SART3 or GFP-SART3-YA1 were transfected with the indicated siRNAs and treated with 4-OHT, followed by qPCR to measure DNA end resection (top). Immunoblotting verifies the knockdown of SART3 and <t>CtIP</t> (bottom). f HEK293T cells transfected with the indicated constructs were treated with CPT (5 µM, 2 h). Chromatin fractions were isolated for immunoprecipitation with anti-GFP beads, followed by immunoblotting with indicated antibodies. Asterisks indicate none-specific bands. CF-IP stands for Chromatin Fractions-IP. g U2OS-GFP-MMEJ cells stably expressing Flag, Flag-SART3, Flag-SART3-R836W, or Flag-SART3-YA1 were transfected with the indicated siRNAs followed by infection with I-SceI lentivirus. The percentage of GFP-positive cells was quantified by FACS analysis (top). The specified proteins were examined by immunoblotting (bottom). h U2OS cells stably expressing GFP, GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3 for 48 h. Cells were then exposed to 15 J/m 2 UVC and repaired for 4 h. The TIF and WCL were harvested and analyzed with the indicated antibodies. i Working model of how SART3 regulates HR repair. In ( a – e ), and ( g ) error bars represent mean ± SEM ( N = 3 independent experiments), and p values were calculated using one-way ANOVA analysis with Tukey test ( a , b ) or unpaired two-tailed Student’s t test ( c – e , g ). Source data are provided as a Source Data file.
    Ctip 61141 Antibody, supplied by Active Motif, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Active Motif ctip (61141) antibody
    a RNF25 +/+ and RNF25 -/- H1299 cells were transfected with indicated siRNAs for 48 h before conducting the DNA fiber fork degradation assay. 150 fibers were analyzed per condition with means shown using bars. This figure is a representative experiment from two biological replicates. Statistics: two-tailed Mann-Whitney test. b Schematic depicting the role of RNF25 in basal replication and following replication stress. Under basal conditions, RNF25 promotes fork movement. Under replication stress conditions, RNF25 protects reversed forks by <t>recruiting</t> <t>REV7.</t> REV1 and REV3L also function in the same fork protection pathway. However, in RNF25 deficient cells, fork degradation is mediated by nucleases MRE11 and <t>CtIP.</t>
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    Active Motif ctip antibody 61141
    a RNF25 +/+ and RNF25 -/- H1299 cells were transfected with indicated siRNAs for 48 h before conducting the DNA fiber fork degradation assay. 150 fibers were analyzed per condition with means shown using bars. This figure is a representative experiment from two biological replicates. Statistics: two-tailed Mann-Whitney test. b Schematic depicting the role of RNF25 in basal replication and following replication stress. Under basal conditions, RNF25 promotes fork movement. Under replication stress conditions, RNF25 protects reversed forks by <t>recruiting</t> <t>REV7.</t> REV1 and REV3L also function in the same fork protection pathway. However, in RNF25 deficient cells, fork degradation is mediated by nucleases MRE11 and <t>CtIP.</t>
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    Active Motif anti-ctip antibody #61141
    a RNF25 +/+ and RNF25 -/- H1299 cells were transfected with indicated siRNAs for 48 h before conducting the DNA fiber fork degradation assay. 150 fibers were analyzed per condition with means shown using bars. This figure is a representative experiment from two biological replicates. Statistics: two-tailed Mann-Whitney test. b Schematic depicting the role of RNF25 in basal replication and following replication stress. Under basal conditions, RNF25 promotes fork movement. Under replication stress conditions, RNF25 protects reversed forks by <t>recruiting</t> <t>REV7.</t> REV1 and REV3L also function in the same fork protection pathway. However, in RNF25 deficient cells, fork degradation is mediated by nucleases MRE11 and <t>CtIP.</t>
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    Active Motif anti-ctip monoclonal antibody 61141
    a RNF25 +/+ and RNF25 -/- H1299 cells were transfected with indicated siRNAs for 48 h before conducting the DNA fiber fork degradation assay. 150 fibers were analyzed per condition with means shown using bars. This figure is a representative experiment from two biological replicates. Statistics: two-tailed Mann-Whitney test. b Schematic depicting the role of RNF25 in basal replication and following replication stress. Under basal conditions, RNF25 promotes fork movement. Under replication stress conditions, RNF25 protects reversed forks by <t>recruiting</t> <t>REV7.</t> REV1 and REV3L also function in the same fork protection pathway. However, in RNF25 deficient cells, fork degradation is mediated by nucleases MRE11 and <t>CtIP.</t>
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    Active Motif anti-ctip antibody 61141
    a RNF25 +/+ and RNF25 -/- H1299 cells were transfected with indicated siRNAs for 48 h before conducting the DNA fiber fork degradation assay. 150 fibers were analyzed per condition with means shown using bars. This figure is a representative experiment from two biological replicates. Statistics: two-tailed Mann-Whitney test. b Schematic depicting the role of RNF25 in basal replication and following replication stress. Under basal conditions, RNF25 promotes fork movement. Under replication stress conditions, RNF25 protects reversed forks by <t>recruiting</t> <t>REV7.</t> REV1 and REV3L also function in the same fork protection pathway. However, in RNF25 deficient cells, fork degradation is mediated by nucleases MRE11 and <t>CtIP.</t>
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    Image Search Results


    a , b U2OS cells stably expressing GFP, GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3 and treated with CPT for 24 h followed by CCK8 assay (a), or Olaparib for 48 h followed by colony formation assay (b). c U2OS-DR-GFP stably expressing Flag, Flag-SART3, or Flag-SART3-YA1 were transfected with siSART3, then infected with I-SceI lentivirus. The percentage of GFP-positive cells was quantitated by FACS (left). The specified proteins were examined by immunoblotting (right). d U2OS cells stably expressing GFP, GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3, treated with ETO (RPA32, BRCA1 and BARD1) or CPT (DDX1) and further recovery for 2 h. Immunostainings was performed. The percentages of cells with more than 10 or 20 foci were quantified (bottom). Representative images are shown (top). Scale bars for overall and magnified images are respectively 50 and 10 µm. e U2OS-ER-AsiSI cells stably expressing GFP, GFP-SART3 or GFP-SART3-YA1 were transfected with the indicated siRNAs and treated with 4-OHT, followed by qPCR to measure DNA end resection (top). Immunoblotting verifies the knockdown of SART3 and CtIP (bottom). f HEK293T cells transfected with the indicated constructs were treated with CPT (5 µM, 2 h). Chromatin fractions were isolated for immunoprecipitation with anti-GFP beads, followed by immunoblotting with indicated antibodies. Asterisks indicate none-specific bands. CF-IP stands for Chromatin Fractions-IP. g U2OS-GFP-MMEJ cells stably expressing Flag, Flag-SART3, Flag-SART3-R836W, or Flag-SART3-YA1 were transfected with the indicated siRNAs followed by infection with I-SceI lentivirus. The percentage of GFP-positive cells was quantified by FACS analysis (top). The specified proteins were examined by immunoblotting (bottom). h U2OS cells stably expressing GFP, GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3 for 48 h. Cells were then exposed to 15 J/m 2 UVC and repaired for 4 h. The TIF and WCL were harvested and analyzed with the indicated antibodies. i Working model of how SART3 regulates HR repair. In ( a – e ), and ( g ) error bars represent mean ± SEM ( N = 3 independent experiments), and p values were calculated using one-way ANOVA analysis with Tukey test ( a , b ) or unpaired two-tailed Student’s t test ( c – e , g ). Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: SART3 promotes homologous recombination repair by stimulating DNA-RNA hybrids removal and DNA end resection

    doi: 10.1038/s41467-025-57599-8

    Figure Lengend Snippet: a , b U2OS cells stably expressing GFP, GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3 and treated with CPT for 24 h followed by CCK8 assay (a), or Olaparib for 48 h followed by colony formation assay (b). c U2OS-DR-GFP stably expressing Flag, Flag-SART3, or Flag-SART3-YA1 were transfected with siSART3, then infected with I-SceI lentivirus. The percentage of GFP-positive cells was quantitated by FACS (left). The specified proteins were examined by immunoblotting (right). d U2OS cells stably expressing GFP, GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3, treated with ETO (RPA32, BRCA1 and BARD1) or CPT (DDX1) and further recovery for 2 h. Immunostainings was performed. The percentages of cells with more than 10 or 20 foci were quantified (bottom). Representative images are shown (top). Scale bars for overall and magnified images are respectively 50 and 10 µm. e U2OS-ER-AsiSI cells stably expressing GFP, GFP-SART3 or GFP-SART3-YA1 were transfected with the indicated siRNAs and treated with 4-OHT, followed by qPCR to measure DNA end resection (top). Immunoblotting verifies the knockdown of SART3 and CtIP (bottom). f HEK293T cells transfected with the indicated constructs were treated with CPT (5 µM, 2 h). Chromatin fractions were isolated for immunoprecipitation with anti-GFP beads, followed by immunoblotting with indicated antibodies. Asterisks indicate none-specific bands. CF-IP stands for Chromatin Fractions-IP. g U2OS-GFP-MMEJ cells stably expressing Flag, Flag-SART3, Flag-SART3-R836W, or Flag-SART3-YA1 were transfected with the indicated siRNAs followed by infection with I-SceI lentivirus. The percentage of GFP-positive cells was quantified by FACS analysis (top). The specified proteins were examined by immunoblotting (bottom). h U2OS cells stably expressing GFP, GFP-SART3, or GFP-SART3-YA1 were transfected with siSART3 for 48 h. Cells were then exposed to 15 J/m 2 UVC and repaired for 4 h. The TIF and WCL were harvested and analyzed with the indicated antibodies. i Working model of how SART3 regulates HR repair. In ( a – e ), and ( g ) error bars represent mean ± SEM ( N = 3 independent experiments), and p values were calculated using one-way ANOVA analysis with Tukey test ( a , b ) or unpaired two-tailed Student’s t test ( c – e , g ). Source data are provided as a Source Data file.

    Article Snippet: The antibodies applied to this study include the following: Flag (F1804, Sigma); γH2AX (ab2893, Abcam); H3 (ab1791, Abcam); RPA32 (ab2175, Abcam); SART3 (ab36137, Abcam); V5 (ab15828, Abcam); PARP1 (sc-8007, Santa Cruz); GFP (sc-8334, Santa Cruz); DDX1 (sc-271438, Santa Cruz); BRCA1 (sc-6954, Santa Cruz); γH2AX (05-636, Millipore); RNF8 (09-813, Millipore); RNA168 (ABE367, Millipore); Top1cc (MABE1084, Millipore); pRPA32-S33 (A300-246A, Bethyl); BARD1 (A300-263A, Bethyl); USP15 (67557-1-Ig, Proteintech); DDX21 (10528-1-AP, Proteintech); DDX1 (CL594-67991, Proteintech); GST (10000-0-AP, Proteintech); Tubulin (AbM59005-37B-PU, Beijing protein innovation); PAR (ALX-210-890A-0100, Enzo life science); CtIP (61141, Active motif); Myc (HT101-02, TransGen Biotech); GFP (AE012, Abclonal); HA (902302, BioLegend); S9.6 (ENH001, Kerafast); MRE11 (NB100-142, Novus); 53BP1 (4937S, Cell Signaling Technology); BrdU (347580, BD-BDIS).

    Techniques: Stable Transfection, Expressing, Transfection, CCK-8 Assay, Colony Assay, Infection, Western Blot, Knockdown, Construct, Isolation, Immunoprecipitation, Two Tailed Test

    a RNF25 +/+ and RNF25 -/- H1299 cells were transfected with indicated siRNAs for 48 h before conducting the DNA fiber fork degradation assay. 150 fibers were analyzed per condition with means shown using bars. This figure is a representative experiment from two biological replicates. Statistics: two-tailed Mann-Whitney test. b Schematic depicting the role of RNF25 in basal replication and following replication stress. Under basal conditions, RNF25 promotes fork movement. Under replication stress conditions, RNF25 protects reversed forks by recruiting REV7. REV1 and REV3L also function in the same fork protection pathway. However, in RNF25 deficient cells, fork degradation is mediated by nucleases MRE11 and CtIP.

    Journal: bioRxiv

    Article Title: The RING Finger E3 Ligase RNF25 Protects DNA Replication Forks Independently of its Canonical Roles in Ubiquitin Signaling

    doi: 10.1101/2025.01.09.632184

    Figure Lengend Snippet: a RNF25 +/+ and RNF25 -/- H1299 cells were transfected with indicated siRNAs for 48 h before conducting the DNA fiber fork degradation assay. 150 fibers were analyzed per condition with means shown using bars. This figure is a representative experiment from two biological replicates. Statistics: two-tailed Mann-Whitney test. b Schematic depicting the role of RNF25 in basal replication and following replication stress. Under basal conditions, RNF25 promotes fork movement. Under replication stress conditions, RNF25 protects reversed forks by recruiting REV7. REV1 and REV3L also function in the same fork protection pathway. However, in RNF25 deficient cells, fork degradation is mediated by nucleases MRE11 and CtIP.

    Article Snippet: Antibodies used: TRIM11 (ab111694), pIRF3 S386 (ab76493), MUS81 (ab14387), and MRE11 (ab214) from Abcam; RNF25 (A303-844A), pRPA S33 (A300-246A), pRPA S4/S8 (A300-245A), ZRANB3 (A303-033A), HLTF (A300-230A), Pol η (A301-231A), RAD18 (A301-340A), and HA (A190-138A) from Bethyl Laboratories; Vinculin (V4505) and γH2AX (05-636) from Sigma Millipore; RPA 34 (NA19L) from Calbiochem; pATM S1981 (sc-47739), β-actin (sc-47778), GAPDH (sc-32233), TNKS1/2 (sc-365897), PARP1 (sc-8007), UBE2D2 (sc-100617), REV1 (sc-393022), FANCD2 (sc-28194), and PCNA (sc-56) from Santa Cruz Biotech; CDC2 pTyr15 (CST 9111), PIAS1 (CST 3550), Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (CST 9106), pSTING Ser366 (CST 19781), STING (CST 13647), pSTAT1 Tyr701 (CST 9167) and STAT1 (CST 9175) from Cell Signaling Technology; REV7 (12683-1-AP), EXO1 (16253-1-AP), and PRIMPOL (29824-1-AP) from Proteintech; CtIP (61141) from Active Motif.

    Techniques: Transfection, Degradation Assay, Two Tailed Test, MANN-WHITNEY