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KU70 (-/-) and DNA-PKcs (-/-/-)chicken DT40 cells are reportedly highly sensitive to the DNA topoisomerase II inhibitor etoposide. Here we report that KU70 and DNA-PKcs unexpectedly function together during the induction of apoptosis after exposure to high levels of etoposide. In the presence of 100 microM etoposide, apoptosis was induced within 1 h in wild type DT40 cells but not in KU70 (-/-) and DNA-PKcs (-/-/-) cells. Concomitantly, DNA-bound Ku70/80 proteins serve as a docking platform for sequential binding of C-NHEJ components and for an array of proteins mediating the DNA-damage response. Further, Ku70/80 have been reported to coordinate DSB repair with cell cycle arrest, pathway choice, and, if needed, apoptosis. Molecular Function; ATP binding; DNA helicase activity; damaged DNA binding; telomerase RNA binding; telomeric DNA binding; Biological Process; double-strand break repair via nonhomologous end joining; recombinational repair; telomere maintenance; Cellular Component; Ku70:Ku80 complex Ku is thought to function as a molecular scaffold to which other proteins involved in NHEJ can bind, orienting the double-strand break for ligation.

In addition, the DNA-PK inhibitors NU7026 and wortmannin, as well as the caspase inhibitor Z-VAD-FMK, inhibited etoposide-induced apoptosis in wild type cells. Ku70/80 also interacts with the telomeric factor Trf1 and plays an important role in telomere maintenance (Bailey et al., 1999; Hsu et al., 1999, 2000; Gasser, 2000). Conformational changes in Ku70/80 could affect this interaction and impinge upon whether Ku70/80 binds Trf1 and acts at telomeres, or alternatively participates in NHEJ. Invitrogen Anti-Ku70/Ku80 Monoclonal (162), Catalog # MA1-21818.

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Supplied as 500 µL purified antibody (0.2 mg/mL). of the Ku70/80 heterodimer in vitro. We further deﬁned the function of the Ku70 and Ku80 C-terminal domains in DNA end binding and DNA-PKCS interaction. 2.

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In fact, the role of Ku70/80 proteins is highly complex and integrates different aspects of DNA repair. 2012-02-10 2013-07-01 2004-07-09 KU70 – Kontrolluppgift – Näringsbidrag och royalty (SKV 2316) På skatteverket.se använder vi kakor (cookies) för att webbplatsen ska fungera på ett bra sätt för dig. Genom att surfa vidare godkänner du att vi använder kakor.

KuP70/P80 Human Recombinant produced in SF9 insect cells is a glycosylated, polypeptide chain having a molecular mass of 70,638 Dalton for the p70 subunit and 83,528 Dalton for the p80 subunit. Ku (P70/P80) is expressed with a -6xHis tag and purified by proprietary chromatographic techniques. Request PDF | KARP-1 works as a heterodimer with Ku70, but the function of KARP-1 cannot perfectly replace that of Ku80 in DSB repair | Ku, the heterodimer of Ku70 and Ku80, plays an essential Recombinant Human Ku70 & Ku80 Heterodimer Protein (Met1-Ile732 & Met1-Asp609) CT018-H07B with a fusion His Tag, is expressed in Baculovirus-Insect Cells.
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2492-2496. Research output: Contribution to journal › Article 2019-05-17 2004-04-02 Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection.

Five of these, K539 Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Ku70 + Ku80 antibody (ab53126) ab53126 at 1/50 dilution staining Ku70 + Ku80 in human breast carcinoma by Immunohistochemistry, Paraffin embedded tissue in the absence and … 2013-02-06 The Ku70 protein is involved in numerous cell functions, the nonhomologous end joining (NHEJ) DNA repair pathway being the best known.
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The Ku70/80 heterodimer rapidly responds to DSBs, stimulating recruitment of downstream NHEJ factors to protect, process, and ligate broken DNA ends. Work in our lab has shown that a D192A/D195R mutation in helix five of the Ku70 von Willebrand A (vWA) domain leads to an NHEJ defect.

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The Ku70 and Ku80 proteins consist of three structural domains. The N-terminal domain is an alpha/beta domain. This domain only makes a small contribution to the dimer interface. Ku70/80 is an heterodimeric factor that plays a critical role in the repair of double strand breaks by non-homologous end joining (NHEJ). In this process, Ku is though to facilitate the ligation of broken DNA ends by promoting the recruitment of nuclease, ligases and polymerases necessary for the repair .

The double-stranded breaks in DNA that arise from such cross-links can be repaired in an error-free manner or through an error-prone repair pathway. Pace et al The Ku70/80 complex recognizes DNA breaks and serves as an essential hub for recruitment of NHEJ components. Here, we describe intramolecular interactions of the Ku70 C‐terminal domain, known as the SAP domain. Ku70 was immunoprecipitated using 0.5mg Hela whole cell extract, 5µg of Rabbit polyclonal to Ku70 and 50µl of protein G magnetic beads (+). No antibody was added to the control (-). The antibody was incubated under agitation with Protein G beads for 10min, Hela whole cell extract lysate diluted in RIPA buffer was added to each sample and incubated for a further 10min under agitation.