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Proteintech phosphorylated chk2
Phosphorylated Chk2, supplied by Proteintech, used in various techniques. Bioz Stars score: 95/100, based on 76 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 95 stars, based on 76 article reviews

phosphorylated chk2 - by Bioz Stars, 2026-03

95/100 stars

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Fig. 7. PCM1 promotes CHK1 activation to maintain cell survival upon prolonged replication stress. (A) Depletion of PCM1 did not affect CHK2 activation upon HU treatment. Extracts of control or PCM1-depleted cells were analyzed by western blotting with antibodies against phosphorylated CHK2, CHK2, and tubulin (loading control). (B) Inhibition of CHK2 did not affect U2-OS cell viability upon HU treatment. Quantitative results of relative cell numbers of HU-treated U2-OS cells in the presence of CHK2 inhibitor (CHK2i). (C) Depletion of PCM1 reduced CHK1 activation upon HU treatment. Extracts of control or PCM1-depleted cells were analyzed by western blotting with antibodies against phosphorylated CHK1, CHK1, and tubulin (loading control). (B) Inhibition of CHK1 reduced U2-OS cell viability upon HU treatment. Quantitative results of relative cell numbers of HU-treated U2-OS cells in the presence of CHK1 inhibitor (CHK1i). n.s.: no significance, ***: P < 0.001. Each experiment was repeated at least three times.

Journal: Archives of biochemistry and biophysics

Article Title: Pericentriolar material 1 aggregation maintains cell survival upon prolonged replication stress.

doi: 10.1016/j.abb.2025.110383

Figure Lengend Snippet: Fig. 7. PCM1 promotes CHK1 activation to maintain cell survival upon prolonged replication stress. (A) Depletion of PCM1 did not affect CHK2 activation upon HU treatment. Extracts of control or PCM1-depleted cells were analyzed by western blotting with antibodies against phosphorylated CHK2, CHK2, and tubulin (loading control). (B) Inhibition of CHK2 did not affect U2-OS cell viability upon HU treatment. Quantitative results of relative cell numbers of HU-treated U2-OS cells in the presence of CHK2 inhibitor (CHK2i). (C) Depletion of PCM1 reduced CHK1 activation upon HU treatment. Extracts of control or PCM1-depleted cells were analyzed by western blotting with antibodies against phosphorylated CHK1, CHK1, and tubulin (loading control). (B) Inhibition of CHK1 reduced U2-OS cell viability upon HU treatment. Quantitative results of relative cell numbers of HU-treated U2-OS cells in the presence of CHK1 inhibitor (CHK1i). n.s.: no significance, ***: P < 0.001. Each experiment was repeated at least three times.

Article Snippet: The following antibodies were used for immunofluorescence and Western blot assays: anti-γ-tubulin (Sigma), anti-PCM1, anti-phosphorylated ATR, anti-ATR, anti-CHK1, anti-CHK2, anti-phosphorylated CHK1, anti-phosphorylated CHK2, anti-LC3 A/B (Cell Signaling), antip150glued, anti-GM130 (BD Biosciences), anti-Ku70, anti-α-tubulin, antiATM, anti-β-actin (GeneTex), anti-γ-H2AX, anti-p-ATM (Abcam), antiphosphorylated DNA-PKcs, anti-DNA-PKcs (Santa Cruz Biotech).

Techniques: Activation Assay, Control, Western Blot, Inhibition

A Western blotting of HIF-1α, p-CHK2 Thr68, CHK2, VEGF. For all Western blotting, β-actin was used as a loading control. 1% O 2 was performed in HEK293 cells and HEK293-CHK2-KO cells for indicated times. B Western blotting of HIF-1α, p-CHK2 Thr68 and CHK2. HEK293 cells were stimulated by 1% O 2 , CHK2 inhibitor and combination for 6 h. C , D Flow cytometric analysis of ROS levels and median fluorescence intensity of ROS expression. H1299 cells were stimulated by 1% O 2 with or without NAC for 6 h. ** p < 0.01. E Western blotting of p-ATM S1981, ATM, HIF-1α, p-CHK2 Thr68 and CHK2. HEK293 cells were pretreated with NAC for 4 h and then cultured in 1% O 2 for 6 h. F Western blotting of p-ATM S1981, ATM, HIF-1α, p-CHK2 Thr68 and CHK2. H1299 cells were transfected with the indicated shRNA and exposed to 1% O 2 for indicated times. G Western blotting of p-ATM S1981, ATM, HIF-1α, p-CHK2 Thr68 and CHK2. HEK293 and HEK293-CHK2-KO cells were exposed to 1% O 2 or combination with ATM inhibitor for 6 h. RT-qPCR analysis of PKM2 ( H ), PDK1 ( I ) and BNIP3 ( J ) mRNA in CHK2-deficient or wildtype HEK293 cells treated with or without hypoxia for 6 h. ** p < 0.01, n.s. not significant. K Dual-luciferase reporter gene experiment of PKM2, PDK1 and BNIP3. HEK293-CHK2-KO cells were co-transfected with reporter gene and CHK2 plasmid under normoxia (21% O 2 ) and hypoxia (1% O 2 ) . ** p < 0.01, n.s. not significant.

Journal: Oncogene

Article Title: ROS-ATM-CHK2 axis stabilizes HIF-1α and promotes tumor angiogenesis in hypoxic microenvironment

doi: 10.1038/s41388-025-03336-w

Figure Lengend Snippet: A Western blotting of HIF-1α, p-CHK2 Thr68, CHK2, VEGF. For all Western blotting, β-actin was used as a loading control. 1% O 2 was performed in HEK293 cells and HEK293-CHK2-KO cells for indicated times. B Western blotting of HIF-1α, p-CHK2 Thr68 and CHK2. HEK293 cells were stimulated by 1% O 2 , CHK2 inhibitor and combination for 6 h. C , D Flow cytometric analysis of ROS levels and median fluorescence intensity of ROS expression. H1299 cells were stimulated by 1% O 2 with or without NAC for 6 h. ** p < 0.01. E Western blotting of p-ATM S1981, ATM, HIF-1α, p-CHK2 Thr68 and CHK2. HEK293 cells were pretreated with NAC for 4 h and then cultured in 1% O 2 for 6 h. F Western blotting of p-ATM S1981, ATM, HIF-1α, p-CHK2 Thr68 and CHK2. H1299 cells were transfected with the indicated shRNA and exposed to 1% O 2 for indicated times. G Western blotting of p-ATM S1981, ATM, HIF-1α, p-CHK2 Thr68 and CHK2. HEK293 and HEK293-CHK2-KO cells were exposed to 1% O 2 or combination with ATM inhibitor for 6 h. RT-qPCR analysis of PKM2 ( H ), PDK1 ( I ) and BNIP3 ( J ) mRNA in CHK2-deficient or wildtype HEK293 cells treated with or without hypoxia for 6 h. ** p < 0.01, n.s. not significant. K Dual-luciferase reporter gene experiment of PKM2, PDK1 and BNIP3. HEK293-CHK2-KO cells were co-transfected with reporter gene and CHK2 plasmid under normoxia (21% O 2 ) and hypoxia (1% O 2 ) . ** p < 0.01, n.s. not significant.

Article Snippet: Antibodies targeting phosphorylated CHK2 (Thr68, #2661), ATM (#2873), p-ATM (Ser1981, #13050), VEGF-A (#50661), ubiquitin (#3933S), β-actin (#3700), human influenza hemagglutinin (HA)-tag (#2367) and His-tag (#2365) were sourced from Cell Signaling Technology, Inc. (Danvers, MA, USA).

Techniques: Western Blot, Control, Fluorescence, Expressing, Cell Culture, Transfection, shRNA, Quantitative RT-PCR, Luciferase, Plasmid Preparation

A Western blotting of exogenous HA-HIF-1α and Flag-tagged CHK2. HA-tagged HIF-1α (3 μg) and Flag-tagged CHK2 (1 μg, 3 μg) was transiently transfected into H1299 cells and then exposed to 1% O 2 . B Western blotting of exogenous HA-HIF-1α and CHK2. HA-tagged HIF-1α was transiently transfected into HEK293 and HEK293-CHK2-KO cells under hypoxic microenvironment. MG132 and CQ was then added to above cells respectively or together as indicated. C Endogenous HIF-1α ubiquitination in HEK293 and HEK293-CHK2-KO cells under hypoxia (1% O 2 ) for 6 h. Exogenous HA-HIF-1α ubiquitination under normoxia ( D ) and hypoxia ( E ) in HEK293-CHK2-KO cells transiently transfected with indicated plasmids. F Western blotting of exogenous double mutant HIF-1α protein at both hydroxylation sites P402A/P564A (HA-HIF-1α-DM). HEK293 cells were transfected with an increasing amount of Flag-CHK2 expression plasmid and exposed to hypoxia. G Western blotting of exogenous triple mutant HIF-1α protein at P402A/P564A/N803A (HA-HIF-1α-TM). HEK293 cells were transfected with an increasing amount of Flag-CHK2 expression plasmid and exposed to hypoxia.

Journal: Oncogene

Article Title: ROS-ATM-CHK2 axis stabilizes HIF-1α and promotes tumor angiogenesis in hypoxic microenvironment

doi: 10.1038/s41388-025-03336-w

Figure Lengend Snippet: A Western blotting of exogenous HA-HIF-1α and Flag-tagged CHK2. HA-tagged HIF-1α (3 μg) and Flag-tagged CHK2 (1 μg, 3 μg) was transiently transfected into H1299 cells and then exposed to 1% O 2 . B Western blotting of exogenous HA-HIF-1α and CHK2. HA-tagged HIF-1α was transiently transfected into HEK293 and HEK293-CHK2-KO cells under hypoxic microenvironment. MG132 and CQ was then added to above cells respectively or together as indicated. C Endogenous HIF-1α ubiquitination in HEK293 and HEK293-CHK2-KO cells under hypoxia (1% O 2 ) for 6 h. Exogenous HA-HIF-1α ubiquitination under normoxia ( D ) and hypoxia ( E ) in HEK293-CHK2-KO cells transiently transfected with indicated plasmids. F Western blotting of exogenous double mutant HIF-1α protein at both hydroxylation sites P402A/P564A (HA-HIF-1α-DM). HEK293 cells were transfected with an increasing amount of Flag-CHK2 expression plasmid and exposed to hypoxia. G Western blotting of exogenous triple mutant HIF-1α protein at P402A/P564A/N803A (HA-HIF-1α-TM). HEK293 cells were transfected with an increasing amount of Flag-CHK2 expression plasmid and exposed to hypoxia.

Techniques: Western Blot, Transfection, Ubiquitin Proteomics, Mutagenesis, Expressing, Plasmid Preparation

A Colocalization of CHK2 and HIF-1α shown by representative confocal microscopic images of NSCLC tissues and H1299 cells. For H1299 cells, experiments were conducted under normoxia (21% O 2 ) and hypoxia (1% O 2 ), respectively. B , C . Co-IP of endogenous CHK2 with HIF-1α in H1299 cells under normoxia (21% O 2 ) and hypoxia (1% O 2 ). IgG, immunoglobulin G. D Co-IP of endogenous CHK2 with HIF-1α in H1299 cells pretreated with NAC for 4 h and then cultured in 1% O 2 for 6 h. E GST-pull-down assay of His-HIF-1α fusion proteins with bacterially expressed GST-CHK2 fragments. Coomassie Brilliant Blue (CBB) staining shows expression of GST and GST-CHK2 fragments. F GST-pull-down assay of His-CHK2 fusion proteins with bacterially expressed GST-HIF-1α fragments. CBB staining shows expression of GST and GST-HIF-1α fragments. G , H Co-IP of exogenous HA-HIF-1α with Flag-CHK2 under normoxia (21% O 2 ) and hypoxia (1% O 2 ) in HEK293-CHK2-KO cells transiently transfected with indicated plasmids.

Journal: Oncogene

Article Title: ROS-ATM-CHK2 axis stabilizes HIF-1α and promotes tumor angiogenesis in hypoxic microenvironment

doi: 10.1038/s41388-025-03336-w

Figure Lengend Snippet: A Colocalization of CHK2 and HIF-1α shown by representative confocal microscopic images of NSCLC tissues and H1299 cells. For H1299 cells, experiments were conducted under normoxia (21% O 2 ) and hypoxia (1% O 2 ), respectively. B , C . Co-IP of endogenous CHK2 with HIF-1α in H1299 cells under normoxia (21% O 2 ) and hypoxia (1% O 2 ). IgG, immunoglobulin G. D Co-IP of endogenous CHK2 with HIF-1α in H1299 cells pretreated with NAC for 4 h and then cultured in 1% O 2 for 6 h. E GST-pull-down assay of His-HIF-1α fusion proteins with bacterially expressed GST-CHK2 fragments. Coomassie Brilliant Blue (CBB) staining shows expression of GST and GST-CHK2 fragments. F GST-pull-down assay of His-CHK2 fusion proteins with bacterially expressed GST-HIF-1α fragments. CBB staining shows expression of GST and GST-HIF-1α fragments. G , H Co-IP of exogenous HA-HIF-1α with Flag-CHK2 under normoxia (21% O 2 ) and hypoxia (1% O 2 ) in HEK293-CHK2-KO cells transiently transfected with indicated plasmids.

Techniques: Co-Immunoprecipitation Assay, Cell Culture, Pull Down Assay, Staining, Expressing, Transfection

A Mass spectrogram of phosphorylation sites of HIF-1α protein T645. B Sequence alignment surrounding the T645 residue of HIF-1α homologs in various species. C Western blotting of HA-HIF-1α, p-CHK2 and CHK2. CHK2 inhibitor was added to HEK2923 cells transiently transfected with plasmids as indicated under hypoxia (1% O 2 ). D Western blotting of HA-HIF-1α and CHK2. shCHK2, HA-HIF-1α and HA-HIF-1α Thr645A plasmids was transiently transfected into HEK293 cells as indicated under hypoxia (1% O 2 ). E Representative images of HUVEC tube formation assay after 24 h incubation in the indicated conditioned media from H1299 cells. F Mean tube length in E was quantified. ** p < 0.01, n.s. not significant. G Exogenous HA-HIF-1α ubiquitination was detected by Co-IP. Flag-CHK2, HA-HIF-1α and HA-HIF-1α Thr645A plasmids were transiently transfected into HEK293 cells as indicated under hypoxia (1% O 2 ). H Co-IP of endogenous HIF-1α with USP7 in HEK293 cells and HEK293-CHK2-KO cells under normoxia (21% O 2 ) and hypoxia (1% O 2 ). I Co-IP of endogenous HIF-1α with USP7. Flag-CHK2 plasmids was transiently transfected into HEK293 cells as indicated under normoxia (21% O 2 ) and hypoxia (1% O 2 ). J Ubiquitination of Flag-HIF-1α WT and Flag-HIF-1α T645A. Flag-HIF-1α and Flag-HIF-1α Thr645A plasmids were transiently transfected into HEK293 cells as indicated under hypoxia (1% O 2 ).

Journal: Oncogene

Article Title: ROS-ATM-CHK2 axis stabilizes HIF-1α and promotes tumor angiogenesis in hypoxic microenvironment

doi: 10.1038/s41388-025-03336-w

Figure Lengend Snippet: A Mass spectrogram of phosphorylation sites of HIF-1α protein T645. B Sequence alignment surrounding the T645 residue of HIF-1α homologs in various species. C Western blotting of HA-HIF-1α, p-CHK2 and CHK2. CHK2 inhibitor was added to HEK2923 cells transiently transfected with plasmids as indicated under hypoxia (1% O 2 ). D Western blotting of HA-HIF-1α and CHK2. shCHK2, HA-HIF-1α and HA-HIF-1α Thr645A plasmids was transiently transfected into HEK293 cells as indicated under hypoxia (1% O 2 ). E Representative images of HUVEC tube formation assay after 24 h incubation in the indicated conditioned media from H1299 cells. F Mean tube length in E was quantified. ** p < 0.01, n.s. not significant. G Exogenous HA-HIF-1α ubiquitination was detected by Co-IP. Flag-CHK2, HA-HIF-1α and HA-HIF-1α Thr645A plasmids were transiently transfected into HEK293 cells as indicated under hypoxia (1% O 2 ). H Co-IP of endogenous HIF-1α with USP7 in HEK293 cells and HEK293-CHK2-KO cells under normoxia (21% O 2 ) and hypoxia (1% O 2 ). I Co-IP of endogenous HIF-1α with USP7. Flag-CHK2 plasmids was transiently transfected into HEK293 cells as indicated under normoxia (21% O 2 ) and hypoxia (1% O 2 ). J Ubiquitination of Flag-HIF-1α WT and Flag-HIF-1α T645A. Flag-HIF-1α and Flag-HIF-1α Thr645A plasmids were transiently transfected into HEK293 cells as indicated under hypoxia (1% O 2 ).

Techniques: Phospho-proteomics, Sequencing, Residue, Western Blot, Transfection, HUVEC Tube Formation Assay, Incubation, Ubiquitin Proteomics, Co-Immunoprecipitation Assay

A Ten mice (n = 5/group) were injected with H1299 cells. DMSO or the CHK2 inhibitor (1 mg/kg) was administered intraperitoneally on alternate days for 20 days. B Representative CD31 and Ki-67 staining of harvested xenografts of mice treated by DMSO or CHK2 inhibitor. Scale bar = 50 μm. C Quantification of IHC. ** p < 0.01. D Western blotting of HA-tagged protein in HIF-1α-WT and HIF-1α-T645A stable transduced H1299 cells. E , F Flow cytometry and statistical analysis showing cell apoptosis exposed to hypoxia of the H1299 cells with indicated transfection. ** p < 0.01. G H1299 cells stably expressing HIF-1α WT or HIF-1α T645A were injected subcutaneously into the rear flanks of athymic nude mice ( n = 6). H IHC of harvested tumors in G with antibodies specific for CD31 and Ki-67 to assess angiogenesis and proliferation respectively. I Measurement of tumor volume of mice in ( G ). ** p < 0.01. J Representative CHK2 and CD31 staining in NSCLC tissues, n = 50. K Scattering plot depicting the correlation between CHK2 and CD31 score.

Journal: Oncogene

Article Title: ROS-ATM-CHK2 axis stabilizes HIF-1α and promotes tumor angiogenesis in hypoxic microenvironment

doi: 10.1038/s41388-025-03336-w

Figure Lengend Snippet: A Ten mice (n = 5/group) were injected with H1299 cells. DMSO or the CHK2 inhibitor (1 mg/kg) was administered intraperitoneally on alternate days for 20 days. B Representative CD31 and Ki-67 staining of harvested xenografts of mice treated by DMSO or CHK2 inhibitor. Scale bar = 50 μm. C Quantification of IHC. ** p < 0.01. D Western blotting of HA-tagged protein in HIF-1α-WT and HIF-1α-T645A stable transduced H1299 cells. E , F Flow cytometry and statistical analysis showing cell apoptosis exposed to hypoxia of the H1299 cells with indicated transfection. ** p < 0.01. G H1299 cells stably expressing HIF-1α WT or HIF-1α T645A were injected subcutaneously into the rear flanks of athymic nude mice ( n = 6). H IHC of harvested tumors in G with antibodies specific for CD31 and Ki-67 to assess angiogenesis and proliferation respectively. I Measurement of tumor volume of mice in ( G ). ** p < 0.01. J Representative CHK2 and CD31 staining in NSCLC tissues, n = 50. K Scattering plot depicting the correlation between CHK2 and CD31 score.

Techniques: Injection, Staining, Paraffin-embedded Immunohistochemistry, Western Blot, Flow Cytometry, Transfection, Stable Transfection, Expressing

Model showing CHK2 interaction with the HIF-1α inhibitory domain and phosphorylate HIF-1α at Thr645 site, enhancing HIF-1α binding to its deubiquitinating enzyme USP7, prohibiting HIF-1α ubiquitination and thus triggering angiogenesis by upregulating VEGF.

Journal: Oncogene

Article Title: ROS-ATM-CHK2 axis stabilizes HIF-1α and promotes tumor angiogenesis in hypoxic microenvironment

doi: 10.1038/s41388-025-03336-w

Figure Lengend Snippet: Model showing CHK2 interaction with the HIF-1α inhibitory domain and phosphorylate HIF-1α at Thr645 site, enhancing HIF-1α binding to its deubiquitinating enzyme USP7, prohibiting HIF-1α ubiquitination and thus triggering angiogenesis by upregulating VEGF.

Techniques: Binding Assay, Ubiquitin Proteomics

A In vitro kinase assays were performed with different concentrations of His-tagged human APE1 (His-hAPE1) as indicated, Flag-tagged WT human ATM (Flag-hATM) and His-tagged kinase-deficient human Chk2 (His-hChk2), with DMSO or ATM inhibitor KU55933 (1 mM). ATM kinase activity was indicated by Chk2 phosphorylation (P-hChk2) via immunoblotting using anti-Chk2 T68 phosphorylation specific antibodies. B Kinase assays were performed with different concentrations of His-hAPE1 as indicated, WT or KD (kinase-dead) Flag-hATM and His-hChk2. ATM kinase activity was indicated by P-hChk2. C Kinase assays were performed with Control (PBS), GST, WT or ΔNT34 GST- Xenopus APE1, Flag-hATM and His-hChk2, with the addition of DMSO or KU55933 (1 mM). ATM kinase activity was indicated by P-hChk2. D Kinase assays were performed with Control (PBS), GST, GST- Xenopus APE1 WT or ΔNT34, Flag-tagged WT or kinase-dead (KD) ATM and His-hChk2. ATM kinase activity was indicated by P-hChk2. E Quantification and statistical analysis of the ratio of P-hChk2 vs. hChk2 from Panel C . Data are presented as mean values ± SD. ** p (GST vs GST-APE1-WT) = 0.0001; ** p (GST-APE1-WT vs GST-APE1-ΔNT34) = 0.0016; two-tailed, unpaired t-test, n = 3. F Kinase assays were performed with different concentrations of His-tagged APE1 NT34 (His-APE1-NT34) and DMSO/KU55933 as indicated. Chk2 phosphorylation was examined via immunoblotting analysis. The data presented in Panel A – D and F are representative of three biological replicates. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Distinct regulation of ATM signaling by DNA single-strand breaks and APE1

doi: 10.1038/s41467-024-50836-6

Figure Lengend Snippet: A In vitro kinase assays were performed with different concentrations of His-tagged human APE1 (His-hAPE1) as indicated, Flag-tagged WT human ATM (Flag-hATM) and His-tagged kinase-deficient human Chk2 (His-hChk2), with DMSO or ATM inhibitor KU55933 (1 mM). ATM kinase activity was indicated by Chk2 phosphorylation (P-hChk2) via immunoblotting using anti-Chk2 T68 phosphorylation specific antibodies. B Kinase assays were performed with different concentrations of His-hAPE1 as indicated, WT or KD (kinase-dead) Flag-hATM and His-hChk2. ATM kinase activity was indicated by P-hChk2. C Kinase assays were performed with Control (PBS), GST, WT or ΔNT34 GST- Xenopus APE1, Flag-hATM and His-hChk2, with the addition of DMSO or KU55933 (1 mM). ATM kinase activity was indicated by P-hChk2. D Kinase assays were performed with Control (PBS), GST, GST- Xenopus APE1 WT or ΔNT34, Flag-tagged WT or kinase-dead (KD) ATM and His-hChk2. ATM kinase activity was indicated by P-hChk2. E Quantification and statistical analysis of the ratio of P-hChk2 vs. hChk2 from Panel C . Data are presented as mean values ± SD. ** p (GST vs GST-APE1-WT) = 0.0001; ** p (GST-APE1-WT vs GST-APE1-ΔNT34) = 0.0016; two-tailed, unpaired t-test, n = 3. F Kinase assays were performed with different concentrations of His-tagged APE1 NT34 (His-APE1-NT34) and DMSO/KU55933 as indicated. Chk2 phosphorylation was examined via immunoblotting analysis. The data presented in Panel A – D and F are representative of three biological replicates. Source data are provided as a Source Data file.

Article Snippet: Antibodies against ATM phosphorylation at Ser1981 (Rockland Immunochemicals, Cat#200-301-500), Chk1 (Santa Cruz Biotechnology, Cat#sc-8408), Chk1 phosphorylation at Ser345 (Cell Signaling Technology, Cat#2348), Chk2 (Santa Cruz Biotechnology, Cat#sc-9064), Chk2 phosphorylation at Thr68 (Santa Cruz Biotechnology, Cat#sc-16297-R), Flag (Thermo Fisher, Cat#MA1-91878), GST (Santa Cruz Biotechnology, Cat#sc-138), H2AX (Cell Signaling Technology, Cat#7631 S), H2AX phosphorylation at Ser139 (Cell Signaling Technology, Cat#2577 S), H3 (Abcam, Cat#ab1791), His (Santa Cruz Biotechnology, Cat#sc-8036), Myc (Santa Cruz Biotechnology, Cat#sc-40), RPA32 phosphorylation at Ser33 (Bethyl Laboratories, Cat#A300-246A), and PCNA (Santa Cruz Biotechnology, Cat#sc-56) were purchased from commercially available vendors.

Techniques: In Vitro, Activity Assay, Western Blot, Control, Two Tailed Test

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