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buffer  (New England Biolabs)
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Buffer, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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phosphatase reaction buffer  (New England Biolabs)
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a eGFP-TOPBP1 domain architecture schematic depicting relative positions of TOPBP1 BRCA1 C-terminal (BRCT) domains 0–8 and its ATR activation domain (AAD). b Western blot analysis of BLM, TOP3A, SLX4, MUS81 and ERCC1 in eGFP-TOPBP1 truncation mutant Co-IPs from HEK293TN cells transiently transfected with WT or C-terminally truncated eGFP-TOPBP1 expression constructs followed by 18 h 100 ng/ml nocodazole synchronisation from Supplementary Fig. . Mock Co-IP from non-transfected HEK293TN cells was conducted as negative control (CTRL). c Western blot analysis of SLX4, MUS81 and ERCC1 in eGFP-TOPBP1 Co-IPs from HEK293TN cells transiently transfected with WT or N-terminally truncated ∆314 (3–8) eGFP-TOPBP1 expression constructs followed by 18 h 100 ng/ml nocodazole synchronisation. Mock Co-IP from non-transfected HEK293TN cells was conducted as negative control (CTRL). For all IP experiments 1% of input was used for analysis by western blot of input lysate. d Domain architecture of SLX4 depicting relative positions of the MUS312/MEI9 interaction-like (MLR), Broad-complex, Tramtrack, and Bric-a-brac (BTB), SAF-A/B, Acinus, and PIAS (SAP) and Conserved C-terminal Domain (CCD) domains and the relative position of the identified pT1260, TOPBP1 BRCT 1 recognition motif. e Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2, BRCT 4-5 and BRCT 7-8 domain containing fragments in the presence of a fluorescein tagged SLX4 pT1260-containing peptide. f Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2 fragment in the presence of fluorescein tagged SLX4 pT1260-containing peptide with or without lambda (λ) <t>phosphatase</t> treatment. g Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2 WT or conserved lysine ‘K’ to glutamic acid ‘E’ mutations in the BRCT1 (K155E) or 2 (K250E) or in BRCT 1 + 2 (K155E + K250E) of the protein fragment, in the presence of fluorescein tagged SLX4 pT1260 containing peptide ( e–g contains data from three independent experiments, error bars display SEM, for all FP experiments raw data was fit with a specific and non-specific component, with the non-specific component subtracted before plotting). h Table showing the dissociation constant of TOPBP1 BRCT 0-1-2 WT or K250E with SLX4 pT1260. i TOPBP1 BRCT 0-1-2 and SLX4 pT260 interaction modelled in AlphaFold 3. j TOPBP1 BRCT 0-1-2 and RAD9 pS387 crystal structure (PDB: 6HM5). Source data are provided as a file.
Phosphatase Reaction Buffer, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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a eGFP-TOPBP1 domain architecture schematic depicting relative positions of TOPBP1 BRCA1 C-terminal (BRCT) domains 0–8 and its ATR activation domain (AAD). b Western blot analysis of BLM, TOP3A, SLX4, MUS81 and ERCC1 in eGFP-TOPBP1 truncation mutant Co-IPs from HEK293TN cells transiently transfected with WT or C-terminally truncated eGFP-TOPBP1 expression constructs followed by 18 h 100 ng/ml nocodazole synchronisation from Supplementary Fig. . Mock Co-IP from non-transfected HEK293TN cells was conducted as negative control (CTRL). c Western blot analysis of SLX4, MUS81 and ERCC1 in eGFP-TOPBP1 Co-IPs from HEK293TN cells transiently transfected with WT or N-terminally truncated ∆314 (3–8) eGFP-TOPBP1 expression constructs followed by 18 h 100 ng/ml nocodazole synchronisation. Mock Co-IP from non-transfected HEK293TN cells was conducted as negative control (CTRL). For all IP experiments 1% of input was used for analysis by western blot of input lysate. d Domain architecture of SLX4 depicting relative positions of the MUS312/MEI9 interaction-like (MLR), Broad-complex, Tramtrack, and Bric-a-brac (BTB), SAF-A/B, Acinus, and PIAS (SAP) and Conserved C-terminal Domain (CCD) domains and the relative position of the identified pT1260, TOPBP1 BRCT 1 recognition motif. e Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2, BRCT 4-5 and BRCT 7-8 domain containing fragments in the presence of a fluorescein tagged SLX4 pT1260-containing peptide. f Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2 fragment in the presence of fluorescein tagged SLX4 pT1260-containing peptide with or without lambda (λ) <t>phosphatase</t> treatment. g Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2 WT or conserved lysine ‘K’ to glutamic acid ‘E’ mutations in the BRCT1 (K155E) or 2 (K250E) or in BRCT 1 + 2 (K155E + K250E) of the protein fragment, in the presence of fluorescein tagged SLX4 pT1260 containing peptide ( e–g contains data from three independent experiments, error bars display SEM, for all FP experiments raw data was fit with a specific and non-specific component, with the non-specific component subtracted before plotting). h Table showing the dissociation constant of TOPBP1 BRCT 0-1-2 WT or K250E with SLX4 pT1260. i TOPBP1 BRCT 0-1-2 and SLX4 pT260 interaction modelled in AlphaFold 3. j TOPBP1 BRCT 0-1-2 and RAD9 pS387 crystal structure (PDB: 6HM5). Source data are provided as a file.
Antarctic Phosphatase Reaction Buffer, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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10x antarctic phosphatase buffer  (New England Biolabs)
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a eGFP-TOPBP1 domain architecture schematic depicting relative positions of TOPBP1 BRCA1 C-terminal (BRCT) domains 0–8 and its ATR activation domain (AAD). b Western blot analysis of BLM, TOP3A, SLX4, MUS81 and ERCC1 in eGFP-TOPBP1 truncation mutant Co-IPs from HEK293TN cells transiently transfected with WT or C-terminally truncated eGFP-TOPBP1 expression constructs followed by 18 h 100 ng/ml nocodazole synchronisation from Supplementary Fig. . Mock Co-IP from non-transfected HEK293TN cells was conducted as negative control (CTRL). c Western blot analysis of SLX4, MUS81 and ERCC1 in eGFP-TOPBP1 Co-IPs from HEK293TN cells transiently transfected with WT or N-terminally truncated ∆314 (3–8) eGFP-TOPBP1 expression constructs followed by 18 h 100 ng/ml nocodazole synchronisation. Mock Co-IP from non-transfected HEK293TN cells was conducted as negative control (CTRL). For all IP experiments 1% of input was used for analysis by western blot of input lysate. d Domain architecture of SLX4 depicting relative positions of the MUS312/MEI9 interaction-like (MLR), Broad-complex, Tramtrack, and Bric-a-brac (BTB), SAF-A/B, Acinus, and PIAS (SAP) and Conserved C-terminal Domain (CCD) domains and the relative position of the identified pT1260, TOPBP1 BRCT 1 recognition motif. e Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2, BRCT 4-5 and BRCT 7-8 domain containing fragments in the presence of a fluorescein tagged SLX4 pT1260-containing peptide. f Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2 fragment in the presence of fluorescein tagged SLX4 pT1260-containing peptide with or without lambda (λ) <t>phosphatase</t> treatment. g Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2 WT or conserved lysine ‘K’ to glutamic acid ‘E’ mutations in the BRCT1 (K155E) or 2 (K250E) or in BRCT 1 + 2 (K155E + K250E) of the protein fragment, in the presence of fluorescein tagged SLX4 pT1260 containing peptide ( e–g contains data from three independent experiments, error bars display SEM, for all FP experiments raw data was fit with a specific and non-specific component, with the non-specific component subtracted before plotting). h Table showing the dissociation constant of TOPBP1 BRCT 0-1-2 WT or K250E with SLX4 pT1260. i TOPBP1 BRCT 0-1-2 and SLX4 pT260 interaction modelled in AlphaFold 3. j TOPBP1 BRCT 0-1-2 and RAD9 pS387 crystal structure (PDB: 6HM5). Source data are provided as a file.
10x Antarctic Phosphatase Buffer, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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reaction buffer  (New England Biolabs)
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a eGFP-TOPBP1 domain architecture schematic depicting relative positions of TOPBP1 BRCA1 C-terminal (BRCT) domains 0–8 and its ATR activation domain (AAD). b Western blot analysis of BLM, TOP3A, SLX4, MUS81 and ERCC1 in eGFP-TOPBP1 truncation mutant Co-IPs from HEK293TN cells transiently transfected with WT or C-terminally truncated eGFP-TOPBP1 expression constructs followed by 18 h 100 ng/ml nocodazole synchronisation from Supplementary Fig. . Mock Co-IP from non-transfected HEK293TN cells was conducted as negative control (CTRL). c Western blot analysis of SLX4, MUS81 and ERCC1 in eGFP-TOPBP1 Co-IPs from HEK293TN cells transiently transfected with WT or N-terminally truncated ∆314 (3–8) eGFP-TOPBP1 expression constructs followed by 18 h 100 ng/ml nocodazole synchronisation. Mock Co-IP from non-transfected HEK293TN cells was conducted as negative control (CTRL). For all IP experiments 1% of input was used for analysis by western blot of input lysate. d Domain architecture of SLX4 depicting relative positions of the MUS312/MEI9 interaction-like (MLR), Broad-complex, Tramtrack, and Bric-a-brac (BTB), SAF-A/B, Acinus, and PIAS (SAP) and Conserved C-terminal Domain (CCD) domains and the relative position of the identified pT1260, TOPBP1 BRCT 1 recognition motif. e Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2, BRCT 4-5 and BRCT 7-8 domain containing fragments in the presence of a fluorescein tagged SLX4 pT1260-containing peptide. f Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2 fragment in the presence of fluorescein tagged SLX4 pT1260-containing peptide with or without lambda (λ) <t>phosphatase</t> treatment. g Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2 WT or conserved lysine ‘K’ to glutamic acid ‘E’ mutations in the BRCT1 (K155E) or 2 (K250E) or in BRCT 1 + 2 (K155E + K250E) of the protein fragment, in the presence of fluorescein tagged SLX4 pT1260 containing peptide ( e–g contains data from three independent experiments, error bars display SEM, for all FP experiments raw data was fit with a specific and non-specific component, with the non-specific component subtracted before plotting). h Table showing the dissociation constant of TOPBP1 BRCT 0-1-2 WT or K250E with SLX4 pT1260. i TOPBP1 BRCT 0-1-2 and SLX4 pT260 interaction modelled in AlphaFold 3. j TOPBP1 BRCT 0-1-2 and RAD9 pS387 crystal structure (PDB: 6HM5). Source data are provided as a file.
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phosphatase buffer  (New England Biolabs)
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a eGFP-TOPBP1 domain architecture schematic depicting relative positions of TOPBP1 BRCA1 C-terminal (BRCT) domains 0–8 and its ATR activation domain (AAD). b Western blot analysis of BLM, TOP3A, SLX4, MUS81 and ERCC1 in eGFP-TOPBP1 truncation mutant Co-IPs from HEK293TN cells transiently transfected with WT or C-terminally truncated eGFP-TOPBP1 expression constructs followed by 18 h 100 ng/ml nocodazole synchronisation from Supplementary Fig. . Mock Co-IP from non-transfected HEK293TN cells was conducted as negative control (CTRL). c Western blot analysis of SLX4, MUS81 and ERCC1 in eGFP-TOPBP1 Co-IPs from HEK293TN cells transiently transfected with WT or N-terminally truncated ∆314 (3–8) eGFP-TOPBP1 expression constructs followed by 18 h 100 ng/ml nocodazole synchronisation. Mock Co-IP from non-transfected HEK293TN cells was conducted as negative control (CTRL). For all IP experiments 1% of input was used for analysis by western blot of input lysate. d Domain architecture of SLX4 depicting relative positions of the MUS312/MEI9 interaction-like (MLR), Broad-complex, Tramtrack, and Bric-a-brac (BTB), SAF-A/B, Acinus, and PIAS (SAP) and Conserved C-terminal Domain (CCD) domains and the relative position of the identified pT1260, TOPBP1 BRCT 1 recognition motif. e Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2, BRCT 4-5 and BRCT 7-8 domain containing fragments in the presence of a fluorescein tagged SLX4 pT1260-containing peptide. f Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2 fragment in the presence of fluorescein tagged SLX4 pT1260-containing peptide with or without lambda (λ) <t>phosphatase</t> treatment. g Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2 WT or conserved lysine ‘K’ to glutamic acid ‘E’ mutations in the BRCT1 (K155E) or 2 (K250E) or in BRCT 1 + 2 (K155E + K250E) of the protein fragment, in the presence of fluorescein tagged SLX4 pT1260 containing peptide ( e–g contains data from three independent experiments, error bars display SEM, for all FP experiments raw data was fit with a specific and non-specific component, with the non-specific component subtracted before plotting). h Table showing the dissociation constant of TOPBP1 BRCT 0-1-2 WT or K250E with SLX4 pT1260. i TOPBP1 BRCT 0-1-2 and SLX4 pT260 interaction modelled in AlphaFold 3. j TOPBP1 BRCT 0-1-2 and RAD9 pS387 crystal structure (PDB: 6HM5). Source data are provided as a file.
Phosphatase Buffer, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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a eGFP-TOPBP1 domain architecture schematic depicting relative positions of TOPBP1 BRCA1 C-terminal (BRCT) domains 0–8 and its ATR activation domain (AAD). b Western blot analysis of BLM, TOP3A, SLX4, MUS81 and ERCC1 in eGFP-TOPBP1 truncation mutant Co-IPs from HEK293TN cells transiently transfected with WT or C-terminally truncated eGFP-TOPBP1 expression constructs followed by 18 h 100 ng/ml nocodazole synchronisation from Supplementary Fig. . Mock Co-IP from non-transfected HEK293TN cells was conducted as negative control (CTRL). c Western blot analysis of SLX4, MUS81 and ERCC1 in eGFP-TOPBP1 Co-IPs from HEK293TN cells transiently transfected with WT or N-terminally truncated ∆314 (3–8) eGFP-TOPBP1 expression constructs followed by 18 h 100 ng/ml nocodazole synchronisation. Mock Co-IP from non-transfected HEK293TN cells was conducted as negative control (CTRL). For all IP experiments 1% of input was used for analysis by western blot of input lysate. d Domain architecture of SLX4 depicting relative positions of the MUS312/MEI9 interaction-like (MLR), Broad-complex, Tramtrack, and Bric-a-brac (BTB), SAF-A/B, Acinus, and PIAS (SAP) and Conserved C-terminal Domain (CCD) domains and the relative position of the identified pT1260, TOPBP1 BRCT 1 recognition motif. e Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2, BRCT 4-5 and BRCT 7-8 domain containing fragments in the presence of a fluorescein tagged SLX4 pT1260-containing peptide. f Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2 fragment in the presence of fluorescein tagged SLX4 pT1260-containing peptide with or without lambda (λ) phosphatase treatment. g Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2 WT or conserved lysine ‘K’ to glutamic acid ‘E’ mutations in the BRCT1 (K155E) or 2 (K250E) or in BRCT 1 + 2 (K155E + K250E) of the protein fragment, in the presence of fluorescein tagged SLX4 pT1260 containing peptide ( e–g contains data from three independent experiments, error bars display SEM, for all FP experiments raw data was fit with a specific and non-specific component, with the non-specific component subtracted before plotting). h Table showing the dissociation constant of TOPBP1 BRCT 0-1-2 WT or K250E with SLX4 pT1260. i TOPBP1 BRCT 0-1-2 and SLX4 pT260 interaction modelled in AlphaFold 3. j TOPBP1 BRCT 0-1-2 and RAD9 pS387 crystal structure (PDB: 6HM5). Source data are provided as a file.

Journal: Nature Communications

Article Title: The CIP2A-TOPBP1 axis facilitates mitotic DNA repair via MiDAS and MMEJ

doi: 10.1038/s41467-025-65594-2

Figure Lengend Snippet: a eGFP-TOPBP1 domain architecture schematic depicting relative positions of TOPBP1 BRCA1 C-terminal (BRCT) domains 0–8 and its ATR activation domain (AAD). b Western blot analysis of BLM, TOP3A, SLX4, MUS81 and ERCC1 in eGFP-TOPBP1 truncation mutant Co-IPs from HEK293TN cells transiently transfected with WT or C-terminally truncated eGFP-TOPBP1 expression constructs followed by 18 h 100 ng/ml nocodazole synchronisation from Supplementary Fig. . Mock Co-IP from non-transfected HEK293TN cells was conducted as negative control (CTRL). c Western blot analysis of SLX4, MUS81 and ERCC1 in eGFP-TOPBP1 Co-IPs from HEK293TN cells transiently transfected with WT or N-terminally truncated ∆314 (3–8) eGFP-TOPBP1 expression constructs followed by 18 h 100 ng/ml nocodazole synchronisation. Mock Co-IP from non-transfected HEK293TN cells was conducted as negative control (CTRL). For all IP experiments 1% of input was used for analysis by western blot of input lysate. d Domain architecture of SLX4 depicting relative positions of the MUS312/MEI9 interaction-like (MLR), Broad-complex, Tramtrack, and Bric-a-brac (BTB), SAF-A/B, Acinus, and PIAS (SAP) and Conserved C-terminal Domain (CCD) domains and the relative position of the identified pT1260, TOPBP1 BRCT 1 recognition motif. e Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2, BRCT 4-5 and BRCT 7-8 domain containing fragments in the presence of a fluorescein tagged SLX4 pT1260-containing peptide. f Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2 fragment in the presence of fluorescein tagged SLX4 pT1260-containing peptide with or without lambda (λ) phosphatase treatment. g Fluorescence polarisation analysis of recombinant TOPBP1 BRCT0-1-2 WT or conserved lysine ‘K’ to glutamic acid ‘E’ mutations in the BRCT1 (K155E) or 2 (K250E) or in BRCT 1 + 2 (K155E + K250E) of the protein fragment, in the presence of fluorescein tagged SLX4 pT1260 containing peptide ( e–g contains data from three independent experiments, error bars display SEM, for all FP experiments raw data was fit with a specific and non-specific component, with the non-specific component subtracted before plotting). h Table showing the dissociation constant of TOPBP1 BRCT 0-1-2 WT or K250E with SLX4 pT1260. i TOPBP1 BRCT 0-1-2 and SLX4 pT260 interaction modelled in AlphaFold 3. j TOPBP1 BRCT 0-1-2 and RAD9 pS387 crystal structure (PDB: 6HM5). Source data are provided as a file.

Article Snippet: The divided membrane was then separated into two 50 ml centrifuge tubes containing 10 ml phosphatase reaction buffer (NEB, 1x rCutSmart buffer B6004SVIAL) supplemented with 1 mM MgCl 2.

Techniques: Activation Assay, Western Blot, Mutagenesis, Transfection, Expressing, Construct, Co-Immunoprecipitation Assay, Negative Control, Fluorescence, Recombinant