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human mdc1 antibody  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc human mdc1 antibody
    Human Mdc1 Antibody, supplied by Cell Signaling Technology 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/product/human+mdc1+antibody/human+mdc1+antibody/pm39684807-375-109-111
    Average 90 stars, based on 1 article reviews
    human mdc1 antibody - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    Control:

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phospho-Ser1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway.
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phosphoSer1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Western Blot:

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phospho-Ser1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway.
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phosphoSer1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Incubation:

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phospho-Ser1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway.
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phosphoSer1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Magnetic Beads:

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phospho-Ser1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway.
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phosphoSer1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Transfection:

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phospho-Ser1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway.
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phosphoSer1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Plasmid Preparation:

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phospho-Ser1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway.
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phosphoSer1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Immunoprecipitation:

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phospho-Ser1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway.
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phosphoSer1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Immunodepletion:

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phospho-Ser1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway.
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phosphoSer1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Binding Assay:

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phospho-Ser1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway.
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phosphoSer1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Recombinant:

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phospho-Ser1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway.
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phosphoSer1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Isolation:

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phospho-Ser1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway.
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phosphoSer1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Activation Assay:

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phospho-Ser1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway.
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phosphoSer1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    SDS Page:

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phospho-Ser1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).

    Article Title: Interaction of DDB1 with NBS1 in a DNA Damage Checkpoint Pathway.
    Article Snippet: Primary antibodies were sourced from established commercial vendors, including HA (Santa Cruz Biotechnology, Dallas, TX, USA), FLAG (Sigma-Aldrich, St. Louis, MO, USA), human NBS1 (Cell Signaling Technology, Danvers, MA, USA), human β-Actin (AbFrontier, Seoul, South Korea), human α-Tubulin (Santa Cruz Biotechnology, Dallas, TX, USA), human ATM (Cell Signaling Technology, Danvers, MA, USA), human ATM phospho-Ser1981 (Cell Signaling Technology, Danvers, MA, USA), human TopBP1 (Bethyl Laboratories, Montgomery, TX, USA), human TopBP1 phosphoSer1138 (Abcam, Cambridge, UK), human Chk1 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk1 phospho-Ser317 (Cell Signaling Technology, Danvers, MA, USA), human Chk2 (Santa Cruz Biotechnology, Dallas, TX, USA), human Chk2 phospho-Thr68 (Cell Signaling Technology, Danvers, MA, USA), and human MDC1 (Cell Signaling Technology, Danvers, MA, USA).



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    FIGURE 1. Degradation of <t>MDC1</t> is dependent on the ubiquitin-protea- some system. A, MDC1 is a ubiquitylated protein. MCF7 cells were trans- fectedwithaH6-Myc-Ubexpressionvectororacontrolvector.After48h,cells were exposed to PIs for 4 h. Cell lysates were immunoprecipitated with an anti-MDC1 antibody. The MDC1 immunocomplexes were separated on a SDS-5% polyacrylamide gel and transferred to a polyvinylidene difluoride membrane. The membrane was cut vertically and Western-blotted with mixed antibodies including mouse anti-Myc and rabbit anti-MDC1 (lanes 1, 2, and 3) or MDC1 antibody alone (lanes 4 and 5). The left and right membrane halves were lined up by using protein size markers. B, conjugated ubiquitin moieties in MDC1 are dependent on lysine 48 of ubiquitin. MCF7 cells were transfected with a H6-Myc-Ub vector, a vector with a 48R substitution. The ubiquitylation of MDC1 was analyzed as described in A. C, treatment with PIs induces the accumulation of MDC1 protein levels. Exponentially growing MCF7 cells were treated with PIs for 4 h. MDC1 protein expression was iden- tified by immunoblotting using anti-MDC1 antibody (Novus). -Actin is shown as a protein loading control. D, MDC1 protein was identified by immu- nofluorescence staining. MCF7 cells were fixed with 4% formaldehyde and the MDC1 protein was identified by the anti-MDC1 antibody and a Alex- aFluor488-labeled anti-rabbit IgG secondary antibody. The cell nuclei were stained with DAPI (blue).
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    Figure 1 <t>MDC</t> expression by 3LL cells transfected with AdMDC. (a) RT- PCR analysis for human MDC expression in vivo. RNA was extracted from tumors 3 days after intratumoral administration of AdMDC, LacZ or PBS. RT-PCR was performed using specific primers for human MDC and specific primers for -actin. Electrophoresis with 2% agarose gel was performed for the PCR products. Lane 1, marker; lane 2, PBS; lane 3, AdLacZ; lane 4, AdMDC. (b) Western blot analysis of human MDC pro- tein in the cell lysates and in the culture supernatants of 3LL cells trans- fected with AdMDC. Cell lysates (lanes 1, 3, 5) and culture supernatants (lanes 2, 4, 6) were prepared 48 h after transfection with AdMDC or AdLacZ, then electrotransferred on to nitrocellulose membrane and incu- bated with anti-human MDC <t>monoclonal</t> antibody. Lanes 1 and 2, wild- type 3LL cells; lanes 3 and 4, 3LL transfected with AdLacZ; lanes 5 and 6, 3LL transfected with AdMDC.
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    FIGURE 1. Degradation of MDC1 is dependent on the ubiquitin-protea- some system. A, MDC1 is a ubiquitylated protein. MCF7 cells were trans- fectedwithaH6-Myc-Ubexpressionvectororacontrolvector.After48h,cells were exposed to PIs for 4 h. Cell lysates were immunoprecipitated with an anti-MDC1 antibody. The MDC1 immunocomplexes were separated on a SDS-5% polyacrylamide gel and transferred to a polyvinylidene difluoride membrane. The membrane was cut vertically and Western-blotted with mixed antibodies including mouse anti-Myc and rabbit anti-MDC1 (lanes 1, 2, and 3) or MDC1 antibody alone (lanes 4 and 5). The left and right membrane halves were lined up by using protein size markers. B, conjugated ubiquitin moieties in MDC1 are dependent on lysine 48 of ubiquitin. MCF7 cells were transfected with a H6-Myc-Ub vector, a vector with a 48R substitution. The ubiquitylation of MDC1 was analyzed as described in A. C, treatment with PIs induces the accumulation of MDC1 protein levels. Exponentially growing MCF7 cells were treated with PIs for 4 h. MDC1 protein expression was iden- tified by immunoblotting using anti-MDC1 antibody (Novus). -Actin is shown as a protein loading control. D, MDC1 protein was identified by immu- nofluorescence staining. MCF7 cells were fixed with 4% formaldehyde and the MDC1 protein was identified by the anti-MDC1 antibody and a Alex- aFluor488-labeled anti-rabbit IgG secondary antibody. The cell nuclei were stained with DAPI (blue).

    Journal: Journal of Biological Chemistry

    Article Title: Disassembly of MDC1 Foci Is Controlled by Ubiquitin-Proteasome-dependent Degradation

    doi: 10.1074/jbc.m801082200

    Figure Lengend Snippet: FIGURE 1. Degradation of MDC1 is dependent on the ubiquitin-protea- some system. A, MDC1 is a ubiquitylated protein. MCF7 cells were trans- fectedwithaH6-Myc-Ubexpressionvectororacontrolvector.After48h,cells were exposed to PIs for 4 h. Cell lysates were immunoprecipitated with an anti-MDC1 antibody. The MDC1 immunocomplexes were separated on a SDS-5% polyacrylamide gel and transferred to a polyvinylidene difluoride membrane. The membrane was cut vertically and Western-blotted with mixed antibodies including mouse anti-Myc and rabbit anti-MDC1 (lanes 1, 2, and 3) or MDC1 antibody alone (lanes 4 and 5). The left and right membrane halves were lined up by using protein size markers. B, conjugated ubiquitin moieties in MDC1 are dependent on lysine 48 of ubiquitin. MCF7 cells were transfected with a H6-Myc-Ub vector, a vector with a 48R substitution. The ubiquitylation of MDC1 was analyzed as described in A. C, treatment with PIs induces the accumulation of MDC1 protein levels. Exponentially growing MCF7 cells were treated with PIs for 4 h. MDC1 protein expression was iden- tified by immunoblotting using anti-MDC1 antibody (Novus). -Actin is shown as a protein loading control. D, MDC1 protein was identified by immu- nofluorescence staining. MCF7 cells were fixed with 4% formaldehyde and the MDC1 protein was identified by the anti-MDC1 antibody and a Alex- aFluor488-labeled anti-rabbit IgG secondary antibody. The cell nuclei were stained with DAPI (blue).

    Article Snippet: Rabbit anti-human MDC1 antibody (A300–051A) was obtained from Bethyl and was used at 1:1,000 dilution for immunoblotting.

    Techniques: Ubiquitin Proteomics, Immunoprecipitation, Membrane, Western Blot, Transfection, Plasmid Preparation, Expressing, Control, Staining, Labeling

    FIGURE 2. Increased ubiquitylation of MDC1 in response to DSBs. A, ubiq- uitylated MDC1 associates with chromatin before and after exposure to ion- izing radiation (IR). MCF7 cells were transfected with the H6-Myc-Ub and exposed to PIs after 48 h. Four hours after IR treatment, chromatin fractions were prepared as described under “Experimental Procedures.” The chroma- tin-bound proteins were analyzed by immunoprecipitation using the anti- MDC1 antibody. Anti-MDC1 immunoprecipitates were separated by SDS-5% polyacrylamide gel. Immunoblotting was performed as described in Fig. 1. BandC,decreasedMDC1proteinlevelsinresponsetoIR.Exponentiallygrow- ing MCF7 cells were exposed to 8 Gy of IR. After 4 h, the cell lysates were fractionated to separate chromatin. Samples from the whole cell lysate (WCL) or the chromatin fraction (Chro) were analyzed by immunoblotting with anti- MDC1 antibody. The loading control was monitored by being probed with indicated antibodies.

    Journal: Journal of Biological Chemistry

    Article Title: Disassembly of MDC1 Foci Is Controlled by Ubiquitin-Proteasome-dependent Degradation

    doi: 10.1074/jbc.m801082200

    Figure Lengend Snippet: FIGURE 2. Increased ubiquitylation of MDC1 in response to DSBs. A, ubiq- uitylated MDC1 associates with chromatin before and after exposure to ion- izing radiation (IR). MCF7 cells were transfected with the H6-Myc-Ub and exposed to PIs after 48 h. Four hours after IR treatment, chromatin fractions were prepared as described under “Experimental Procedures.” The chroma- tin-bound proteins were analyzed by immunoprecipitation using the anti- MDC1 antibody. Anti-MDC1 immunoprecipitates were separated by SDS-5% polyacrylamide gel. Immunoblotting was performed as described in Fig. 1. BandC,decreasedMDC1proteinlevelsinresponsetoIR.Exponentiallygrow- ing MCF7 cells were exposed to 8 Gy of IR. After 4 h, the cell lysates were fractionated to separate chromatin. Samples from the whole cell lysate (WCL) or the chromatin fraction (Chro) were analyzed by immunoblotting with anti- MDC1 antibody. The loading control was monitored by being probed with indicated antibodies.

    Article Snippet: Rabbit anti-human MDC1 antibody (A300–051A) was obtained from Bethyl and was used at 1:1,000 dilution for immunoblotting.

    Techniques: Transfection, Immunoprecipitation, Western Blot, Control

    FIGURE3.MDC1regulatesconjugatedubiquitinfociinresponsetoDNAdamage.AandB,knockdownofRNF8 by siRNA. Exponentially growing MCF7 cells were transfected with two rounds of RNF8 (siRNF8) or control siRNA (sicon),separatedbya24-hourinterval.Experimentswereperformed72hafterfirstsiRNAtransfection.RNF8knock- down was confirmed by Western blot and immunostaining. RNF8 knockdown by immunofluorescence staining analogous to A. C, residual FK2 foci in cells with RNF8 knockdown. MCF7 cells transfected with siRNA twice were irradiatedwith8Gy,andimmunostainingwasperformed4hafterIR.Brieflythecellsweredetergent-extractedwith 0.5% Triton X-100 CSK buffer and fixed with 4% formaldehyde. The fixed cells were then permeabilized using 0.1% Triton X-100, which was followed by blocking and incubation with FK2 and anti-RNF8 antibodies. Foci were visual- ized by AlexaFluor594-labeled anti-mouse IgG secondary antibody (red) or AlexaFluor488-labeled anti-rabbit anti- body (green). Cell nuclei were stained with DAPI. D, MDC1 foci co-localize with conjugated ubiquitin in both untreated and IR-treated cells. Exponentially growing MCF7 cells were mock-treated or irradiated with 8 Gy and fixedattheindicatedtimepoints.ThefixedcellswithandwithoutIRtreatmentwereco-stainedwithanti-MDC1and anti-ubiquitin (FK2) antibodies. This was followed by incubation with the secondary antibodies. Co-localization is indicated by a yellow signal. E–G, MDC1 knockdown resulted in inhibition of conjugated ubiquitin foci. Exponen- tiallygrowingMCF7cellsweretransfectedwithtworoundsofMDC1orcontrolsiRNAasdescribedinAandB.MDC1 knockdown was monitored by Western blot (E) and immunostaining (F).

    Journal: Journal of Biological Chemistry

    Article Title: Disassembly of MDC1 Foci Is Controlled by Ubiquitin-Proteasome-dependent Degradation

    doi: 10.1074/jbc.m801082200

    Figure Lengend Snippet: FIGURE3.MDC1regulatesconjugatedubiquitinfociinresponsetoDNAdamage.AandB,knockdownofRNF8 by siRNA. Exponentially growing MCF7 cells were transfected with two rounds of RNF8 (siRNF8) or control siRNA (sicon),separatedbya24-hourinterval.Experimentswereperformed72hafterfirstsiRNAtransfection.RNF8knock- down was confirmed by Western blot and immunostaining. RNF8 knockdown by immunofluorescence staining analogous to A. C, residual FK2 foci in cells with RNF8 knockdown. MCF7 cells transfected with siRNA twice were irradiatedwith8Gy,andimmunostainingwasperformed4hafterIR.Brieflythecellsweredetergent-extractedwith 0.5% Triton X-100 CSK buffer and fixed with 4% formaldehyde. The fixed cells were then permeabilized using 0.1% Triton X-100, which was followed by blocking and incubation with FK2 and anti-RNF8 antibodies. Foci were visual- ized by AlexaFluor594-labeled anti-mouse IgG secondary antibody (red) or AlexaFluor488-labeled anti-rabbit anti- body (green). Cell nuclei were stained with DAPI. D, MDC1 foci co-localize with conjugated ubiquitin in both untreated and IR-treated cells. Exponentially growing MCF7 cells were mock-treated or irradiated with 8 Gy and fixedattheindicatedtimepoints.ThefixedcellswithandwithoutIRtreatmentwereco-stainedwithanti-MDC1and anti-ubiquitin (FK2) antibodies. This was followed by incubation with the secondary antibodies. Co-localization is indicated by a yellow signal. E–G, MDC1 knockdown resulted in inhibition of conjugated ubiquitin foci. Exponen- tiallygrowingMCF7cellsweretransfectedwithtworoundsofMDC1orcontrolsiRNAasdescribedinAandB.MDC1 knockdown was monitored by Western blot (E) and immunostaining (F).

    Article Snippet: Rabbit anti-human MDC1 antibody (A300–051A) was obtained from Bethyl and was used at 1:1,000 dilution for immunoblotting.

    Techniques: Transfection, Control, Western Blot, Immunostaining, Knockdown, Immunofluorescence, Staining, Blocking Assay, Incubation, Labeling, Ubiquitin Proteomics, Irradiation, Inhibition

    FIGURE 4. Kinetics of MDC1 and -H2AX focus formation without and with PI treatment. A, representative MDC1 foci in cells with and without PI treatment at 4 h after irradiation with 8 Gy. B, dynamics of MDC1 focus formation after irradiation of MCF7 cells with 8 Gy. The percentage of cells with more than five nuclear foci was calculated. In each experiment, 200–300 nuclei were counted per data point. Error bars indicate S.E. from three independent experiments. C, representative -H2AX foci in cells with and without PI treatment 4 h after irradiation with 8 Gy. D, dynamics of -H2AX focus formation after irradiation of MCF7 cells with 8 Gy. -H2AX foci kinetics was determined as in B.

    Journal: Journal of Biological Chemistry

    Article Title: Disassembly of MDC1 Foci Is Controlled by Ubiquitin-Proteasome-dependent Degradation

    doi: 10.1074/jbc.m801082200

    Figure Lengend Snippet: FIGURE 4. Kinetics of MDC1 and -H2AX focus formation without and with PI treatment. A, representative MDC1 foci in cells with and without PI treatment at 4 h after irradiation with 8 Gy. B, dynamics of MDC1 focus formation after irradiation of MCF7 cells with 8 Gy. The percentage of cells with more than five nuclear foci was calculated. In each experiment, 200–300 nuclei were counted per data point. Error bars indicate S.E. from three independent experiments. C, representative -H2AX foci in cells with and without PI treatment 4 h after irradiation with 8 Gy. D, dynamics of -H2AX focus formation after irradiation of MCF7 cells with 8 Gy. -H2AX foci kinetics was determined as in B.

    Article Snippet: Rabbit anti-human MDC1 antibody (A300–051A) was obtained from Bethyl and was used at 1:1,000 dilution for immunoblotting.

    Techniques: Irradiation

    FIGURE5.DetectionoftheenhancedMDC1proteinaccumulationatchro- mosomalDSBsitesinthepresenceofPIsasdeterminedbyChIP.A,induc- tion of site-directed DSBs, as reflected by subsequent homology-mediated repair, was measured by dual-color flow cytometric detection of GFP-positive cells. Representative flow cytometric analyses of H1299/DR-GFP cells treated with and without infection of the adenoviral I-SceI expression construct (Ad- SceI-NG) are shown. Left panel show cells without DSB induction, with few GFP-positive cells detected. The right panel shows cells 24 h after infection with Ad-Sce-ING. B, expression of HA-tagged I-SceI endonuclease was moni- tored by Western blot using anti-HA antibody. H1299/DR-GFP cells were infected with and without Ad-SceI-NG, and whole cell lysate was prepared at theindicatedtimepoints.C,schematicrepresentationofthepositionofprim- ers used for real-time PCR quantification of ChIPs respective to the DSB cre- ated by I-SceI endonuclease in vivo. Real-time PCR on ChIP samples were car- ried out at 94–378 nucleotides from the break (52). D, ChIP of MDC1 protein on DSB after Ad-SceI-NG. -Fold enrichment represents the enrichment of MDC1 proteins compared with an IgG control and normalized to a PCR inter- nal control for a chromosomal locus distinct from the DSB site (52). Data points represent an average of four independent repeated experiments. E, ChIP analysis of MDC1 in the presence and absence of PIs (upper panel). Samples were prepared in parallel to monitor the amount of pulled-down MDC1 proteins using immunoprecipitation. The anti-MDC1 immunoprecipi- tate was probed with anti-MDC1 antibody (bottom panel). Shown is one rep- resentative result from three independent repeated experiments.

    Journal: Journal of Biological Chemistry

    Article Title: Disassembly of MDC1 Foci Is Controlled by Ubiquitin-Proteasome-dependent Degradation

    doi: 10.1074/jbc.m801082200

    Figure Lengend Snippet: FIGURE5.DetectionoftheenhancedMDC1proteinaccumulationatchro- mosomalDSBsitesinthepresenceofPIsasdeterminedbyChIP.A,induc- tion of site-directed DSBs, as reflected by subsequent homology-mediated repair, was measured by dual-color flow cytometric detection of GFP-positive cells. Representative flow cytometric analyses of H1299/DR-GFP cells treated with and without infection of the adenoviral I-SceI expression construct (Ad- SceI-NG) are shown. Left panel show cells without DSB induction, with few GFP-positive cells detected. The right panel shows cells 24 h after infection with Ad-Sce-ING. B, expression of HA-tagged I-SceI endonuclease was moni- tored by Western blot using anti-HA antibody. H1299/DR-GFP cells were infected with and without Ad-SceI-NG, and whole cell lysate was prepared at theindicatedtimepoints.C,schematicrepresentationofthepositionofprim- ers used for real-time PCR quantification of ChIPs respective to the DSB cre- ated by I-SceI endonuclease in vivo. Real-time PCR on ChIP samples were car- ried out at 94–378 nucleotides from the break (52). D, ChIP of MDC1 protein on DSB after Ad-SceI-NG. -Fold enrichment represents the enrichment of MDC1 proteins compared with an IgG control and normalized to a PCR inter- nal control for a chromosomal locus distinct from the DSB site (52). Data points represent an average of four independent repeated experiments. E, ChIP analysis of MDC1 in the presence and absence of PIs (upper panel). Samples were prepared in parallel to monitor the amount of pulled-down MDC1 proteins using immunoprecipitation. The anti-MDC1 immunoprecipi- tate was probed with anti-MDC1 antibody (bottom panel). Shown is one rep- resentative result from three independent repeated experiments.

    Article Snippet: Rabbit anti-human MDC1 antibody (A300–051A) was obtained from Bethyl and was used at 1:1,000 dilution for immunoblotting.

    Techniques: Infection, Expressing, Construct, Western Blot, Real-time Polymerase Chain Reaction, In Vivo, Control, Immunoprecipitation

    FIGURE 6. Kinetics of BRCA1 focus formation with and without PI treat- ment. A, illustration of MDC1 foci and BRCA1 foci at the 4-hour time point. Cells lose MDC1 foci as BRCA1 foci are being formed (upper row). After treat- ment, MDC1 foci persist while BRCA1 foci fail to form (lower row). B, Western blot developed using an anti-BRCA1 antibody (Oncogene, Ab-1) on whole cellextractsfromMCF7cellswithorwithoutPItreatmentfor4–6h.C,dynam- ics of BRCA1 focus formation after irradiation of MCF7 cells with 8 Gy. The percentage of cells with more than five nuclear foci was calculated. In each experiment, 200–300 nuclei were counted per data point. Error bars indicate S.E. from three independent repeated experiments with and without PI treatment.

    Journal: Journal of Biological Chemistry

    Article Title: Disassembly of MDC1 Foci Is Controlled by Ubiquitin-Proteasome-dependent Degradation

    doi: 10.1074/jbc.m801082200

    Figure Lengend Snippet: FIGURE 6. Kinetics of BRCA1 focus formation with and without PI treat- ment. A, illustration of MDC1 foci and BRCA1 foci at the 4-hour time point. Cells lose MDC1 foci as BRCA1 foci are being formed (upper row). After treat- ment, MDC1 foci persist while BRCA1 foci fail to form (lower row). B, Western blot developed using an anti-BRCA1 antibody (Oncogene, Ab-1) on whole cellextractsfromMCF7cellswithorwithoutPItreatmentfor4–6h.C,dynam- ics of BRCA1 focus formation after irradiation of MCF7 cells with 8 Gy. The percentage of cells with more than five nuclear foci was calculated. In each experiment, 200–300 nuclei were counted per data point. Error bars indicate S.E. from three independent repeated experiments with and without PI treatment.

    Article Snippet: Rabbit anti-human MDC1 antibody (A300–051A) was obtained from Bethyl and was used at 1:1,000 dilution for immunoblotting.

    Techniques: Western Blot, Irradiation

    FIGURE 7. Importance of MDC1 ubiquitylation and RNF8 for BRCA1 foci recruitment. A, BRCA1 focus formation at the 4 h after IR in control siRNA, RNF8 siRNA, or MDC1 siRNA-transfected cells. The proportion of cells with IR-induced BRCA1 foci is shown. Bars represent the mean with S.E. based on 3–4 independent experiments. B, effect of persisting MDC1 foci on recruitment of BRCA1 in the presence of PIs is independent of RNF8. Exponentially growing MCF7 cells were transfected twice with either control (sicon) or RNF8 siRNA (siRNF8) as described in Fig. 3. Cells were then treated with DMSO or PIs for 1–2 h and exposed to 8 Gy IR. Focus formation was analyzed 4 h after IR as in Fig. 3. One representative result from three independent experiments is shown. C and D, stability of BRCA1 protein expression in siRNA-transfected cells. Lysate protein was resolved by SDS-PAGE and visualized using an anti-BRCA1 antibody (Oncogene, Ab-1) 72 h after the first siRNA transfection.

    Journal: Journal of Biological Chemistry

    Article Title: Disassembly of MDC1 Foci Is Controlled by Ubiquitin-Proteasome-dependent Degradation

    doi: 10.1074/jbc.m801082200

    Figure Lengend Snippet: FIGURE 7. Importance of MDC1 ubiquitylation and RNF8 for BRCA1 foci recruitment. A, BRCA1 focus formation at the 4 h after IR in control siRNA, RNF8 siRNA, or MDC1 siRNA-transfected cells. The proportion of cells with IR-induced BRCA1 foci is shown. Bars represent the mean with S.E. based on 3–4 independent experiments. B, effect of persisting MDC1 foci on recruitment of BRCA1 in the presence of PIs is independent of RNF8. Exponentially growing MCF7 cells were transfected twice with either control (sicon) or RNF8 siRNA (siRNF8) as described in Fig. 3. Cells were then treated with DMSO or PIs for 1–2 h and exposed to 8 Gy IR. Focus formation was analyzed 4 h after IR as in Fig. 3. One representative result from three independent experiments is shown. C and D, stability of BRCA1 protein expression in siRNA-transfected cells. Lysate protein was resolved by SDS-PAGE and visualized using an anti-BRCA1 antibody (Oncogene, Ab-1) 72 h after the first siRNA transfection.

    Article Snippet: Rabbit anti-human MDC1 antibody (A300–051A) was obtained from Bethyl and was used at 1:1,000 dilution for immunoblotting.

    Techniques: Control, Transfection, Expressing, SDS Page

    Figure 1 MDC expression by 3LL cells transfected with AdMDC. (a) RT- PCR analysis for human MDC expression in vivo. RNA was extracted from tumors 3 days after intratumoral administration of AdMDC, LacZ or PBS. RT-PCR was performed using specific primers for human MDC and specific primers for -actin. Electrophoresis with 2% agarose gel was performed for the PCR products. Lane 1, marker; lane 2, PBS; lane 3, AdLacZ; lane 4, AdMDC. (b) Western blot analysis of human MDC pro- tein in the cell lysates and in the culture supernatants of 3LL cells trans- fected with AdMDC. Cell lysates (lanes 1, 3, 5) and culture supernatants (lanes 2, 4, 6) were prepared 48 h after transfection with AdMDC or AdLacZ, then electrotransferred on to nitrocellulose membrane and incu- bated with anti-human MDC monoclonal antibody. Lanes 1 and 2, wild- type 3LL cells; lanes 3 and 4, 3LL transfected with AdLacZ; lanes 5 and 6, 3LL transfected with AdMDC.

    Journal: Gene therapy

    Article Title: Macrophage-derived chemokine gene transfer results in tumor regression in murine lung carcinoma model through efficient induction of antitumor immunity.

    doi: 10.1038/sj.gt.3301688

    Figure Lengend Snippet: Figure 1 MDC expression by 3LL cells transfected with AdMDC. (a) RT- PCR analysis for human MDC expression in vivo. RNA was extracted from tumors 3 days after intratumoral administration of AdMDC, LacZ or PBS. RT-PCR was performed using specific primers for human MDC and specific primers for -actin. Electrophoresis with 2% agarose gel was performed for the PCR products. Lane 1, marker; lane 2, PBS; lane 3, AdLacZ; lane 4, AdMDC. (b) Western blot analysis of human MDC pro- tein in the cell lysates and in the culture supernatants of 3LL cells trans- fected with AdMDC. Cell lysates (lanes 1, 3, 5) and culture supernatants (lanes 2, 4, 6) were prepared 48 h after transfection with AdMDC or AdLacZ, then electrotransferred on to nitrocellulose membrane and incu- bated with anti-human MDC monoclonal antibody. Lanes 1 and 2, wild- type 3LL cells; lanes 3 and 4, 3LL transfected with AdLacZ; lanes 5 and 6, 3LL transfected with AdMDC.

    Article Snippet: 801Membranes were incubated with anti-human MDC monoclonal antibody (R&D Systems, Minneapolis, MN, USA) and subsequently with anti-mouse secondary antibody.

    Techniques: Expressing, Transfection, Reverse Transcription Polymerase Chain Reaction, In Vivo, Electrophoresis, Agarose Gel Electrophoresis, Marker, Western Blot, Membrane

    Figure 4 Effector cells involved in the antitumor response of MDC gene transfer. (a) Induction of tumor-specific CTL in tumor-bearing mice after treatment with AdMDC. Splenic lymphocytes were isolated from tumor- bearing mice 12 days after adenovirus administration and were cocultured at a concentration of 1 × 107 cells/ml with 1 × 106 cells/ml inactivated 3LL tumor cells for 7 days to induce CTL effector cells. The cytotoxicity was determined by a standard 4-h 51Cr-release assay by utilizing 3LL cells as target cells. The syngeneic EL4 lymphoma cells were used as control target cells. Each point represents the mean of triplicates. The experiment was repeated once with similar results. (b) In vivo depletion analysis with anti-CD4, anti-CD8 or anti-NK monoclonal antibodies was performed as described in Materials and methods.

    Journal: Gene therapy

    Article Title: Macrophage-derived chemokine gene transfer results in tumor regression in murine lung carcinoma model through efficient induction of antitumor immunity.

    doi: 10.1038/sj.gt.3301688

    Figure Lengend Snippet: Figure 4 Effector cells involved in the antitumor response of MDC gene transfer. (a) Induction of tumor-specific CTL in tumor-bearing mice after treatment with AdMDC. Splenic lymphocytes were isolated from tumor- bearing mice 12 days after adenovirus administration and were cocultured at a concentration of 1 × 107 cells/ml with 1 × 106 cells/ml inactivated 3LL tumor cells for 7 days to induce CTL effector cells. The cytotoxicity was determined by a standard 4-h 51Cr-release assay by utilizing 3LL cells as target cells. The syngeneic EL4 lymphoma cells were used as control target cells. Each point represents the mean of triplicates. The experiment was repeated once with similar results. (b) In vivo depletion analysis with anti-CD4, anti-CD8 or anti-NK monoclonal antibodies was performed as described in Materials and methods.

    Article Snippet: 801Membranes were incubated with anti-human MDC monoclonal antibody (R&D Systems, Minneapolis, MN, USA) and subsequently with anti-mouse secondary antibody.

    Techniques: Isolation, Concentration Assay, Release Assay, Control, In Vivo, Bioprocessing