human replication protein a rpa Search Results


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    Novus Biologicals anti rpa2
    MMS22L foci form during S phase of the cell cycle and colocalize with HR proteins Immunofluorescence images of MMS22L foci formation at etoposide (ETP)‐induced DSBs during S, M, and G1 phases of the cell cycle in HeLa cells. Scale bar: 5 μm. Quantification of a representative experiment from (A) shows number of MMS22L foci per nucleus during indicated cell cycle phases ( n = 2; n nuclei ≥ 60). Immunofluorescence images of CPT‐induced MMS22L, <t>RPA2,</t> BRCA2, and RAD51 foci in U2OS cells. Scale bar: 5 μm. Quantification of a representative experiment ( n = 3) from (C) shows percentage of γH2AX, RPA2, BRCA2, and RAD51 foci colocalizing with MMS22L foci ( n nuclei = 30; nuclei with ≥ 25 MMS22L foci were analyzed). Data information: Boxplots in (B and D) represent distributions per nucleus; boxes indicate the 25–75 percentile and whiskers the 10–90 percentile. Horizontal lines mark the medians. Statistical analysis: Mann–Whitney U ‐test; *** P ≤ 0.0001; ns, not significant.
    Anti Rpa2, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 90/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti rpa2/product/Novus Biologicals
    Average 90 stars, based on 9 article reviews
    Price from $9.99 to $1999.99
    anti rpa2 - by Bioz Stars, 2020-09
    90/100 stars
      Buy from Supplier

    88
    Novus Biologicals rabbit polyclonal rpa70
    MMS22L foci form during S phase of the cell cycle and colocalize with HR proteins Immunofluorescence images of MMS22L foci formation at etoposide (ETP)‐induced DSBs during S, M, and G1 phases of the cell cycle in HeLa cells. Scale bar: 5 μm. Quantification of a representative experiment from (A) shows number of MMS22L foci per nucleus during indicated cell cycle phases ( n = 2; n nuclei ≥ 60). Immunofluorescence images of CPT‐induced MMS22L, <t>RPA2,</t> BRCA2, and RAD51 foci in U2OS cells. Scale bar: 5 μm. Quantification of a representative experiment ( n = 3) from (C) shows percentage of γH2AX, RPA2, BRCA2, and RAD51 foci colocalizing with MMS22L foci ( n nuclei = 30; nuclei with ≥ 25 MMS22L foci were analyzed). Data information: Boxplots in (B and D) represent distributions per nucleus; boxes indicate the 25–75 percentile and whiskers the 10–90 percentile. Horizontal lines mark the medians. Statistical analysis: Mann–Whitney U ‐test; *** P ≤ 0.0001; ns, not significant.
    Rabbit Polyclonal Rpa70, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal rpa70/product/Novus Biologicals
    Average 88 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal rpa70 - by Bioz Stars, 2020-09
    88/100 stars
      Buy from Supplier

    Image Search Results


    MMS22L foci form during S phase of the cell cycle and colocalize with HR proteins Immunofluorescence images of MMS22L foci formation at etoposide (ETP)‐induced DSBs during S, M, and G1 phases of the cell cycle in HeLa cells. Scale bar: 5 μm. Quantification of a representative experiment from (A) shows number of MMS22L foci per nucleus during indicated cell cycle phases ( n = 2; n nuclei ≥ 60). Immunofluorescence images of CPT‐induced MMS22L, RPA2, BRCA2, and RAD51 foci in U2OS cells. Scale bar: 5 μm. Quantification of a representative experiment ( n = 3) from (C) shows percentage of γH2AX, RPA2, BRCA2, and RAD51 foci colocalizing with MMS22L foci ( n nuclei = 30; nuclei with ≥ 25 MMS22L foci were analyzed). Data information: Boxplots in (B and D) represent distributions per nucleus; boxes indicate the 25–75 percentile and whiskers the 10–90 percentile. Horizontal lines mark the medians. Statistical analysis: Mann–Whitney U ‐test; *** P ≤ 0.0001; ns, not significant.

    Journal: The EMBO Journal

    Article Title: The MMS22L–TONSL heterodimer directly promotes RAD51‐dependent recombination upon replication stress

    doi: 10.15252/embj.201593132

    Figure Lengend Snippet: MMS22L foci form during S phase of the cell cycle and colocalize with HR proteins Immunofluorescence images of MMS22L foci formation at etoposide (ETP)‐induced DSBs during S, M, and G1 phases of the cell cycle in HeLa cells. Scale bar: 5 μm. Quantification of a representative experiment from (A) shows number of MMS22L foci per nucleus during indicated cell cycle phases ( n = 2; n nuclei ≥ 60). Immunofluorescence images of CPT‐induced MMS22L, RPA2, BRCA2, and RAD51 foci in U2OS cells. Scale bar: 5 μm. Quantification of a representative experiment ( n = 3) from (C) shows percentage of γH2AX, RPA2, BRCA2, and RAD51 foci colocalizing with MMS22L foci ( n nuclei = 30; nuclei with ≥ 25 MMS22L foci were analyzed). Data information: Boxplots in (B and D) represent distributions per nucleus; boxes indicate the 25–75 percentile and whiskers the 10–90 percentile. Horizontal lines mark the medians. Statistical analysis: Mann–Whitney U ‐test; *** P ≤ 0.0001; ns, not significant.

    Article Snippet: The following commercial antibodies were used: anti‐RAD51 (H‐92, Santa Cruz Biotech, 1:2,000), anti‐PCNA (PC10, Santa Cruz Biotech, 1:5,000), anti‐RPA2 (9H8, Imgenex, 1:2,000), anti‐RPA2 pS33 (A300–246A, Bethyl Laboratories, 1:1,000), anti‐RPA2 pS4/8 (A300–245A, Bethyl Laboratories, 1:1,000), anti‐MCM4 (clone B01P, Abnova, 1:1,000), anti‐α‐tubulin (DM1A, Sigma‐Aldrich, 1:10,000), anti‐HA.11 (16B12, Covance, 1:2,000), anti‐ASF1A (C6E10, Cell Signaling, 1:5,000), anti‐GAPDH (MAB374, Millipore, 1:5,000), and peroxidase‐conjugated anti‐mouse or anti‐rabbit antibodies (Pierce, 1:5,000).

    Techniques: Immunofluorescence, Cycling Probe Technology, MANN-WHITNEY

    MMS22L–TONSL regulates RAD51 recruitment at stalled replication forks A iPOND assay schematic (top) and immunoblots (bottom) show effects of CPT and HU treatments on the RPA2 phosphorylation status in HeLa cells. Note that 30‐min treatment with 1 μM CPT stalls forks without inducing fork breakage, as the phosphorylation status of RPA2 using specific antibodies indicates the presence of pS33 associated with ssDNA rather than pS4/8 associated with DSBs (induced at later time point; 90 min). Asterisks indicate cross‐reactive bands. B Schematic representation (top) of TONSL, TONSL LRR*: E1089K and D1104N mutations within the LRR domain identified in ovarian cancer patient (COSMIC sample OCC06PT (Forbes et al )) and TONSL ΔLRR: C‐terminal TONSL truncation deleting the LRR domain; LRR, leucine‐rich repeats. Streptavidin pulldown (bottom) of indicated stably integrated HSS‐tagged‐TONSL variants overexpressed in HeLa cells. Input and coprecipitated proteins were detected by immunoblotting. ASF1A, known to interact with the N‐terminal region of TONSL (Duro et al ; O'Donnell et al ), was included as a control. C, D The presence of the indicated proteins at replication forks was analyzed by the iPOND‐CPT‐release assay in cells expressing either HSS‐tagged wild‐type TONSL, or TONSL LRR* or TONSL ΔLRR mutants and depleted for endogenous TONSL by siRNA targeting 3′UTR. The experiments were quantified and shown as average; n = 2 except for LRR* n = 1; error bars, SEM. TONSL and its interaction with MMS22L are required for normal levels of RAD51 at stalled replication forks.

    Journal: The EMBO Journal

    Article Title: The MMS22L–TONSL heterodimer directly promotes RAD51‐dependent recombination upon replication stress

    doi: 10.15252/embj.201593132

    Figure Lengend Snippet: MMS22L–TONSL regulates RAD51 recruitment at stalled replication forks A iPOND assay schematic (top) and immunoblots (bottom) show effects of CPT and HU treatments on the RPA2 phosphorylation status in HeLa cells. Note that 30‐min treatment with 1 μM CPT stalls forks without inducing fork breakage, as the phosphorylation status of RPA2 using specific antibodies indicates the presence of pS33 associated with ssDNA rather than pS4/8 associated with DSBs (induced at later time point; 90 min). Asterisks indicate cross‐reactive bands. B Schematic representation (top) of TONSL, TONSL LRR*: E1089K and D1104N mutations within the LRR domain identified in ovarian cancer patient (COSMIC sample OCC06PT (Forbes et al )) and TONSL ΔLRR: C‐terminal TONSL truncation deleting the LRR domain; LRR, leucine‐rich repeats. Streptavidin pulldown (bottom) of indicated stably integrated HSS‐tagged‐TONSL variants overexpressed in HeLa cells. Input and coprecipitated proteins were detected by immunoblotting. ASF1A, known to interact with the N‐terminal region of TONSL (Duro et al ; O'Donnell et al ), was included as a control. C, D The presence of the indicated proteins at replication forks was analyzed by the iPOND‐CPT‐release assay in cells expressing either HSS‐tagged wild‐type TONSL, or TONSL LRR* or TONSL ΔLRR mutants and depleted for endogenous TONSL by siRNA targeting 3′UTR. The experiments were quantified and shown as average; n = 2 except for LRR* n = 1; error bars, SEM. TONSL and its interaction with MMS22L are required for normal levels of RAD51 at stalled replication forks.

    Article Snippet: The following commercial antibodies were used: anti‐RAD51 (H‐92, Santa Cruz Biotech, 1:2,000), anti‐PCNA (PC10, Santa Cruz Biotech, 1:5,000), anti‐RPA2 (9H8, Imgenex, 1:2,000), anti‐RPA2 pS33 (A300–246A, Bethyl Laboratories, 1:1,000), anti‐RPA2 pS4/8 (A300–245A, Bethyl Laboratories, 1:1,000), anti‐MCM4 (clone B01P, Abnova, 1:1,000), anti‐α‐tubulin (DM1A, Sigma‐Aldrich, 1:10,000), anti‐HA.11 (16B12, Covance, 1:2,000), anti‐ASF1A (C6E10, Cell Signaling, 1:5,000), anti‐GAPDH (MAB374, Millipore, 1:5,000), and peroxidase‐conjugated anti‐mouse or anti‐rabbit antibodies (Pierce, 1:5,000).

    Techniques: Western Blot, Cycling Probe Technology, Stable Transfection, Release Assay, Expressing