chk2 rabbit polyclonal antibody Search Results


anti p thr68 chk2  (OriGene)
90
OriGene anti p thr68 chk2
HDACi impairs checkpoint signalling upon replicative stress. a HCT116 cells were stimulated with 1 mM hydroxyurea (HU) and 2 µM MS-275 for 24 h. Western blot analyses of whole-cell lysates were performed to detect ATM and ATR as well as their phosphorylated forms (pATM S1981; pATR T1989). β-Actin served as loading control. Numbers indicate densitometric analysis of signals relative to HU-treated samples and normalised to β-Actin ( n = 3). b Densitometric evaluation of ATM phosphorylation at S1981 and ATM levels (after 24 h) following protein detection via immunoblot. Data were normalised to the loading controls. The respective amounts (phosphorylated) proteins are compared to those of HU-treated cells. Results represent the mean ± SD ( n = 3; one-way ANOVA; **** P < 0.0001). c Cells were treated with 1 mM HU and 2 µM MS-275 for 6-24 h. Whole-cell extracts were blotted to two membranes to detect phosphorylated and total levels of ATM, CHK1 (pCHK1 S317) and <t>CHK2</t> (pCHK2 T68) by immunoblot. HSP70 and mSIN3A are loading controls. Numbers indicate densitometric analysis of signal relative to HU-treated cells and normalised to the respective loading control ( n = 3). d Densitometric analysis of phosphorylated (S317) and total CHK1 levels after 24 h detected via western blot. Data were normalised to the respective loading controls. Results display relative amounts of pCHK1/CHK1 compared to HU-treated cells as mean ± SD ( n = 3). Statistical analysis was performed using one-way ANOVA (**** P < 0.0001). e Cells were either pre-incubated with 2 µM MS-275 or were left untreated for 24 h and subsequently exposed to 10 J/m 2 UVC. Plates were harvested 0, 1, 2 and 3 h after irradiation. Indicated proteins were detected via western blot. HSP70 and β-Actin served as loading controls
Anti P Thr68 Chk2, supplied by OriGene, 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/result/anti p thr68 chk2/product/OriGene
Average 90 stars, based on 1 article reviews
anti p thr68 chk2 - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier
polyclonal chk-2 antibodies  (Pocono Rabbit Farm)
90
Pocono Rabbit Farm polyclonal chk-2 antibodies
HDACi impairs checkpoint signalling upon replicative stress. a HCT116 cells were stimulated with 1 mM hydroxyurea (HU) and 2 µM MS-275 for 24 h. Western blot analyses of whole-cell lysates were performed to detect ATM and ATR as well as their phosphorylated forms (pATM S1981; pATR T1989). β-Actin served as loading control. Numbers indicate densitometric analysis of signals relative to HU-treated samples and normalised to β-Actin ( n = 3). b Densitometric evaluation of ATM phosphorylation at S1981 and ATM levels (after 24 h) following protein detection via immunoblot. Data were normalised to the loading controls. The respective amounts (phosphorylated) proteins are compared to those of HU-treated cells. Results represent the mean ± SD ( n = 3; one-way ANOVA; **** P < 0.0001). c Cells were treated with 1 mM HU and 2 µM MS-275 for 6-24 h. Whole-cell extracts were blotted to two membranes to detect phosphorylated and total levels of ATM, CHK1 (pCHK1 S317) and <t>CHK2</t> (pCHK2 T68) by immunoblot. HSP70 and mSIN3A are loading controls. Numbers indicate densitometric analysis of signal relative to HU-treated cells and normalised to the respective loading control ( n = 3). d Densitometric analysis of phosphorylated (S317) and total CHK1 levels after 24 h detected via western blot. Data were normalised to the respective loading controls. Results display relative amounts of pCHK1/CHK1 compared to HU-treated cells as mean ± SD ( n = 3). Statistical analysis was performed using one-way ANOVA (**** P < 0.0001). e Cells were either pre-incubated with 2 µM MS-275 or were left untreated for 24 h and subsequently exposed to 10 J/m 2 UVC. Plates were harvested 0, 1, 2 and 3 h after irradiation. Indicated proteins were detected via western blot. HSP70 and β-Actin served as loading controls
Polyclonal Chk 2 Antibodies, supplied by Pocono Rabbit Farm, 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/result/polyclonal chk-2 antibodies/product/Pocono Rabbit Farm
Average 90 stars, based on 1 article reviews
polyclonal chk-2 antibodies - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier
anti-chk2 rabbit polyclonal antibody  (Protein Sciences Inc)
90
Protein Sciences Inc anti-chk2 rabbit polyclonal antibody
HDACi impairs checkpoint signalling upon replicative stress. a HCT116 cells were stimulated with 1 mM hydroxyurea (HU) and 2 µM MS-275 for 24 h. Western blot analyses of whole-cell lysates were performed to detect ATM and ATR as well as their phosphorylated forms (pATM S1981; pATR T1989). β-Actin served as loading control. Numbers indicate densitometric analysis of signals relative to HU-treated samples and normalised to β-Actin ( n = 3). b Densitometric evaluation of ATM phosphorylation at S1981 and ATM levels (after 24 h) following protein detection via immunoblot. Data were normalised to the loading controls. The respective amounts (phosphorylated) proteins are compared to those of HU-treated cells. Results represent the mean ± SD ( n = 3; one-way ANOVA; **** P < 0.0001). c Cells were treated with 1 mM HU and 2 µM MS-275 for 6-24 h. Whole-cell extracts were blotted to two membranes to detect phosphorylated and total levels of ATM, CHK1 (pCHK1 S317) and <t>CHK2</t> (pCHK2 T68) by immunoblot. HSP70 and mSIN3A are loading controls. Numbers indicate densitometric analysis of signal relative to HU-treated cells and normalised to the respective loading control ( n = 3). d Densitometric analysis of phosphorylated (S317) and total CHK1 levels after 24 h detected via western blot. Data were normalised to the respective loading controls. Results display relative amounts of pCHK1/CHK1 compared to HU-treated cells as mean ± SD ( n = 3). Statistical analysis was performed using one-way ANOVA (**** P < 0.0001). e Cells were either pre-incubated with 2 µM MS-275 or were left untreated for 24 h and subsequently exposed to 10 J/m 2 UVC. Plates were harvested 0, 1, 2 and 3 h after irradiation. Indicated proteins were detected via western blot. HSP70 and β-Actin served as loading controls
Anti Chk2 Rabbit Polyclonal Antibody, supplied by Protein Sciences Inc, 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/result/anti-chk2 rabbit polyclonal antibody/product/Protein Sciences Inc
Average 90 stars, based on 1 article reviews
anti-chk2 rabbit polyclonal antibody - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier

Image Search Results


HDACi impairs checkpoint signalling upon replicative stress. a HCT116 cells were stimulated with 1 mM hydroxyurea (HU) and 2 µM MS-275 for 24 h. Western blot analyses of whole-cell lysates were performed to detect ATM and ATR as well as their phosphorylated forms (pATM S1981; pATR T1989). β-Actin served as loading control. Numbers indicate densitometric analysis of signals relative to HU-treated samples and normalised to β-Actin ( n = 3). b Densitometric evaluation of ATM phosphorylation at S1981 and ATM levels (after 24 h) following protein detection via immunoblot. Data were normalised to the loading controls. The respective amounts (phosphorylated) proteins are compared to those of HU-treated cells. Results represent the mean ± SD ( n = 3; one-way ANOVA; **** P < 0.0001). c Cells were treated with 1 mM HU and 2 µM MS-275 for 6-24 h. Whole-cell extracts were blotted to two membranes to detect phosphorylated and total levels of ATM, CHK1 (pCHK1 S317) and CHK2 (pCHK2 T68) by immunoblot. HSP70 and mSIN3A are loading controls. Numbers indicate densitometric analysis of signal relative to HU-treated cells and normalised to the respective loading control ( n = 3). d Densitometric analysis of phosphorylated (S317) and total CHK1 levels after 24 h detected via western blot. Data were normalised to the respective loading controls. Results display relative amounts of pCHK1/CHK1 compared to HU-treated cells as mean ± SD ( n = 3). Statistical analysis was performed using one-way ANOVA (**** P < 0.0001). e Cells were either pre-incubated with 2 µM MS-275 or were left untreated for 24 h and subsequently exposed to 10 J/m 2 UVC. Plates were harvested 0, 1, 2 and 3 h after irradiation. Indicated proteins were detected via western blot. HSP70 and β-Actin served as loading controls

Journal: Nature Communications

Article Title: HDAC1 and HDAC2 integrate checkpoint kinase phosphorylation and cell fate through the phosphatase-2A subunit PR130

doi: 10.1038/s41467-018-03096-0

Figure Lengend Snippet: HDACi impairs checkpoint signalling upon replicative stress. a HCT116 cells were stimulated with 1 mM hydroxyurea (HU) and 2 µM MS-275 for 24 h. Western blot analyses of whole-cell lysates were performed to detect ATM and ATR as well as their phosphorylated forms (pATM S1981; pATR T1989). β-Actin served as loading control. Numbers indicate densitometric analysis of signals relative to HU-treated samples and normalised to β-Actin ( n = 3). b Densitometric evaluation of ATM phosphorylation at S1981 and ATM levels (after 24 h) following protein detection via immunoblot. Data were normalised to the loading controls. The respective amounts (phosphorylated) proteins are compared to those of HU-treated cells. Results represent the mean ± SD ( n = 3; one-way ANOVA; **** P < 0.0001). c Cells were treated with 1 mM HU and 2 µM MS-275 for 6-24 h. Whole-cell extracts were blotted to two membranes to detect phosphorylated and total levels of ATM, CHK1 (pCHK1 S317) and CHK2 (pCHK2 T68) by immunoblot. HSP70 and mSIN3A are loading controls. Numbers indicate densitometric analysis of signal relative to HU-treated cells and normalised to the respective loading control ( n = 3). d Densitometric analysis of phosphorylated (S317) and total CHK1 levels after 24 h detected via western blot. Data were normalised to the respective loading controls. Results display relative amounts of pCHK1/CHK1 compared to HU-treated cells as mean ± SD ( n = 3). Statistical analysis was performed using one-way ANOVA (**** P < 0.0001). e Cells were either pre-incubated with 2 µM MS-275 or were left untreated for 24 h and subsequently exposed to 10 J/m 2 UVC. Plates were harvested 0, 1, 2 and 3 h after irradiation. Indicated proteins were detected via western blot. HSP70 and β-Actin served as loading controls

Article Snippet: The following antibodies were used during this study: anti-p-Ser1981-ATM (ab81292; 1 : 750), anti-ATM (ab32420; 1 : 1000), anti-p-Thr68-CHK2 (ab32148; 1 : 1000), anti-HDAC1 (ab46985, 1 : 1000), anti-HDAC3 (ab16047; 1 : 1000) from Abcam; anti-p-Thr68-CHK2 (AP01556PU-N; 1 : 500) from Acris Antibodies; anti-Cyclin B1 (ARP30161; 1 : 2000) from Aviva, anti-BrdU (347580; 1 : 1500), anti-cleaved-PARP1 (552596; 1 : 5000) from BD Pharmingen; anti-p-Ser317-CHK1 (A300-163A; 1 : 1000), anti-WIP1 (A300-664A; 1 : 5000) from Bethyl Laboratories; anti-Vinculin (BZL-03106; 1 : 5000) from Biozol; anti-acetyl-Lysine (9681; 1 : 1000), anti-ATR (2790; 1 : 1000), anti-p-Tyr15-cdc2(CDK1) (4539; 1 : 1000), anti-p-Ser317-CHK1 (2344; 1 : 1000), anti-p-Ser296-CHK1 (2349; 1 : 1000), anti-CHK1 (2360; 1 : 1000), anti-p-Thr68-CHK2 (2661; 1 : 500), anti-CHK2 (2662; 1 : 1000), anti-p-Ser139-H2AX (9718; 1 : 1000), anti-p-Ser15-p53 (9284; 1 : 5000), anti-PP2Ac (2259; 1 : 1000) from Cell Signalling Technology; anti-p-Thr1989-ATR (GTX128145; 1 : 1000), anti-PPP2R3B (GTX47038; 1 : 750) from GeneTex; anti-acetyl-Histone3 (06-599; 1 : 2000), anti-ATM (PC116; 0.8 µg), anti-pS421/S423-HDAC2 (07-1575; 1 : 1000), anti-RPA (NA19L; 1 : 1000) from Millipore; anti-ATM (NB100-309; 1 : 1000), anti-PPP2R3A (NBP1-87233; 1 : 2000) from Novus Biologicals; anti-BrdU (OBT0030; 1 : 1000) from Oxford Biotechnologies; anti-p-Ser1981-ATM (#200-301-400; 1 : 1000) from Rockland Immunochemicals; anti-beta-Actin (sc-47778; 1 : 5000), anti-B56β (sc-515676; 1 : 1000), anti-CHK1 (sc-8408; 1 : 2000), anti-CHK2 (sc-9064; 1 : 1000), anti-GAPDH (sc-32233; 1 : 2000), anti-HA (sc-7392; 1 : 1000), anti-HDAC2 (sc-7899; 1 : 2000), anti-HSP70 (sc-24; 1 : 2000), anti-mSIN3A (sc-994; 1 : 20,000), anti-p21 (sc-6246; 1 : 2000), anti-p53 (sc-81168; 1 : 50,000), anti-PP2A-Aα/β (sc-13600; 1 : 1000), anti-PPP2R3A (sc-6115), anti-WEE1 (sc-5285; 1 : 750) from Santa Cruz Biotechnology; anti-Tubulin (T5168; 1 : 50,000), anti-Actin (A2066; 1 : 10,000) from Sigma-Aldrich; anti-acetyl-Histone3 (06–599; 1 : 1000) from Upstate.

Techniques: Western Blot, Incubation, Irradiation

Checkpoint kinases ensure cell survival upon replicative stress. a HCT116 cells were pretreated with 3 µM KU-60019 for 1 h followed by stimulation with 1 mM hydroxyurea (HU) for 24–48 h. Cell death was detected using PI staining and flow cytometry. Results are displayed as mean ± SD ( n 24 h = 3, n 48 h = 4; one-way ANOVA, *** P < 0.001; **** P < 0.0001). b Western blot analysis of HCT116 cells treated with KU-60019 and HU for 24 h as described in a . ɣH2AX was detected with specific antibodies. HSP90 served as loading control. c siRNA transfection was performed as described in the Methods section. Twenty-four hours after transfection, HCT116 cells were incubated with 1 mM HU for 24–48 h. Cell death analysis was performed as described in a . Data are presented as mean ± SD ( n = 4; one-way ANOVA, * P < 0.05; **** P < 0.0001). d Transfection with indicated siRNAs and treatment were performed as described in c . ATM, ATR, pCHK1 (S317) and mSIN3A (loading control) were analysed by immunoblotting. e HCT116 cells were treated with 1 mM HU for 24–48 h after 1 h pre-incubation with 1–3 µM VE-821. SubG1 fractions were measured as described in a . Results represent mean ± SD ( n = 2; one-way ANOVA, * P < 0.05, ** P < 0.01). f HCT116 cells were treated with VE-821 and/or HU for 24 h as described in e . Western blot analysis was performed to detect pATM (S1981), pCHK1 (S317), CHK1 and ɣH2AX. β-Actin served as loading control. g Cells were pre-incubated with 300 nM LY2603618 or MK-8776 for 1 h followed by HU treatment (1 mM) for 24-48 h. Cell death was analysed as described in a . Results are displayed as mean ± SD ( n 24 h = 4, n 48 h = 3; one-way ANOVA, **** P < 0.0001). h Western blot analysis of HCT116 treated for 24 h as described in g . ɣH2AX, pCHK1 (S296) and CHK1 levels were detected with specific antibodies. β-Actin served as loading control. i HCT116 cells and their comparative CHK2 −/− cell line were treated with 1 mM HU for the indicated time periods. Indicated proteins were detected via western blot

Journal: Nature Communications

Article Title: HDAC1 and HDAC2 integrate checkpoint kinase phosphorylation and cell fate through the phosphatase-2A subunit PR130

doi: 10.1038/s41467-018-03096-0

Figure Lengend Snippet: Checkpoint kinases ensure cell survival upon replicative stress. a HCT116 cells were pretreated with 3 µM KU-60019 for 1 h followed by stimulation with 1 mM hydroxyurea (HU) for 24–48 h. Cell death was detected using PI staining and flow cytometry. Results are displayed as mean ± SD ( n 24 h = 3, n 48 h = 4; one-way ANOVA, *** P < 0.001; **** P < 0.0001). b Western blot analysis of HCT116 cells treated with KU-60019 and HU for 24 h as described in a . ɣH2AX was detected with specific antibodies. HSP90 served as loading control. c siRNA transfection was performed as described in the Methods section. Twenty-four hours after transfection, HCT116 cells were incubated with 1 mM HU for 24–48 h. Cell death analysis was performed as described in a . Data are presented as mean ± SD ( n = 4; one-way ANOVA, * P < 0.05; **** P < 0.0001). d Transfection with indicated siRNAs and treatment were performed as described in c . ATM, ATR, pCHK1 (S317) and mSIN3A (loading control) were analysed by immunoblotting. e HCT116 cells were treated with 1 mM HU for 24–48 h after 1 h pre-incubation with 1–3 µM VE-821. SubG1 fractions were measured as described in a . Results represent mean ± SD ( n = 2; one-way ANOVA, * P < 0.05, ** P < 0.01). f HCT116 cells were treated with VE-821 and/or HU for 24 h as described in e . Western blot analysis was performed to detect pATM (S1981), pCHK1 (S317), CHK1 and ɣH2AX. β-Actin served as loading control. g Cells were pre-incubated with 300 nM LY2603618 or MK-8776 for 1 h followed by HU treatment (1 mM) for 24-48 h. Cell death was analysed as described in a . Results are displayed as mean ± SD ( n 24 h = 4, n 48 h = 3; one-way ANOVA, **** P < 0.0001). h Western blot analysis of HCT116 treated for 24 h as described in g . ɣH2AX, pCHK1 (S296) and CHK1 levels were detected with specific antibodies. β-Actin served as loading control. i HCT116 cells and their comparative CHK2 −/− cell line were treated with 1 mM HU for the indicated time periods. Indicated proteins were detected via western blot

Article Snippet: The following antibodies were used during this study: anti-p-Ser1981-ATM (ab81292; 1 : 750), anti-ATM (ab32420; 1 : 1000), anti-p-Thr68-CHK2 (ab32148; 1 : 1000), anti-HDAC1 (ab46985, 1 : 1000), anti-HDAC3 (ab16047; 1 : 1000) from Abcam; anti-p-Thr68-CHK2 (AP01556PU-N; 1 : 500) from Acris Antibodies; anti-Cyclin B1 (ARP30161; 1 : 2000) from Aviva, anti-BrdU (347580; 1 : 1500), anti-cleaved-PARP1 (552596; 1 : 5000) from BD Pharmingen; anti-p-Ser317-CHK1 (A300-163A; 1 : 1000), anti-WIP1 (A300-664A; 1 : 5000) from Bethyl Laboratories; anti-Vinculin (BZL-03106; 1 : 5000) from Biozol; anti-acetyl-Lysine (9681; 1 : 1000), anti-ATR (2790; 1 : 1000), anti-p-Tyr15-cdc2(CDK1) (4539; 1 : 1000), anti-p-Ser317-CHK1 (2344; 1 : 1000), anti-p-Ser296-CHK1 (2349; 1 : 1000), anti-CHK1 (2360; 1 : 1000), anti-p-Thr68-CHK2 (2661; 1 : 500), anti-CHK2 (2662; 1 : 1000), anti-p-Ser139-H2AX (9718; 1 : 1000), anti-p-Ser15-p53 (9284; 1 : 5000), anti-PP2Ac (2259; 1 : 1000) from Cell Signalling Technology; anti-p-Thr1989-ATR (GTX128145; 1 : 1000), anti-PPP2R3B (GTX47038; 1 : 750) from GeneTex; anti-acetyl-Histone3 (06-599; 1 : 2000), anti-ATM (PC116; 0.8 µg), anti-pS421/S423-HDAC2 (07-1575; 1 : 1000), anti-RPA (NA19L; 1 : 1000) from Millipore; anti-ATM (NB100-309; 1 : 1000), anti-PPP2R3A (NBP1-87233; 1 : 2000) from Novus Biologicals; anti-BrdU (OBT0030; 1 : 1000) from Oxford Biotechnologies; anti-p-Ser1981-ATM (#200-301-400; 1 : 1000) from Rockland Immunochemicals; anti-beta-Actin (sc-47778; 1 : 5000), anti-B56β (sc-515676; 1 : 1000), anti-CHK1 (sc-8408; 1 : 2000), anti-CHK2 (sc-9064; 1 : 1000), anti-GAPDH (sc-32233; 1 : 2000), anti-HA (sc-7392; 1 : 1000), anti-HDAC2 (sc-7899; 1 : 2000), anti-HSP70 (sc-24; 1 : 2000), anti-mSIN3A (sc-994; 1 : 20,000), anti-p21 (sc-6246; 1 : 2000), anti-p53 (sc-81168; 1 : 50,000), anti-PP2A-Aα/β (sc-13600; 1 : 1000), anti-PPP2R3A (sc-6115), anti-WEE1 (sc-5285; 1 : 750) from Santa Cruz Biotechnology; anti-Tubulin (T5168; 1 : 50,000), anti-Actin (A2066; 1 : 10,000) from Sigma-Aldrich; anti-acetyl-Histone3 (06–599; 1 : 1000) from Upstate.

Techniques: Staining, Flow Cytometry, Western Blot, Transfection, Incubation