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Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists. 2008-11-1 · KU70/80, DNA-PKcs, and Artemis are essential for the rapid induction of apoptosis after massive DSB formation. Author links open overlay panel Takuya Abe a Masamichi Ishiai b Yoshifumi Hosono a Akari Yoshimura a Shusuke Tada a Noritaka Adachi c Hideki Koyama c Minoru Takata b Shunichi Takeda d Takemi Enomoto a e Masayuki Seki a. The yeast homologue of Ku70/80, yKu70/80, fails to bind IP 6, indicating that the function of IP 6 in non‐homologous end‐joining, like that of DNA‐PK cs, is unique to the mammalian end‐joining process. 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 … Our previous studies indicated that the Werner syndrome protein (WRN) interacts with Ku, a heterodimeric factor of 70- and 80-kDa subunits implicated in the repair of double strand DNA breaks. Moreover, we demonstrated that Ku70/80 strongly stimulates and alters WRN exonuclease activity.

Surprisingly, specific inhibitors of the Ku70/80 heterodimer are currently not available. The Ku70/80 heterodimer is the regulatory subunit of the DNA-dependent protein kinase (DNA-PK) and its DNA-binding activity mediates DNA double-strand breaks repair. Although Ku80 was recently The Ku70/80 heterodimer (Ku), the catalytic subunit of the DNA-dependent protein kinase (DNA-PKcs), DNA ligase IV (LigIV), XRCC4 and XLF form a long-range synaptic complex, in which the DNA ends The Ku70/80 crystal structure (Fig. 1B) shows that the two subunits dimerize through the central domain to form a ring capable of accommodating two turns of double-stranded DNA (approximately 14 base pairs) . This ring, consisting of intertwined strands of both Ku70 and Ku80, is lined with positively charged residues positioned to interact with Heterodimers of the 70 and 80 kDa Ku autoantigens (Ku70 and Ku80) activate the DNA‐dependent protein kinase (DNA‐PK). Mutations in any of the three subunits of this protein kinase (Ku70, Ku80 and DNA‐PKcs) lead to sensitivity to ionizing radiation (IR) and to DNA double‐strand breaks, and V(D)J recombination product formation defects.

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It is also required for V (D)J recombination, which utilizes the NHEJ pathway to promote antigen diversity in the mammalian immune system. The Ku70/80 heterodimer protein plays a pivotal role in the NHEJ process. It possesses a ring-shaped structure with high affinity for DSBs and serves as the first responder and central scaffold around which the rest of the repair complex is assembled. KU70 (-/-) and DNA-PKcs (-/-/-)chicken DT40 cells are reportedly highly sensitive to the DNA topoisomerase II inhibitor etoposide.

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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 … Our previous studies indicated that the Werner syndrome protein (WRN) interacts with Ku, a heterodimeric factor of 70- and 80-kDa subunits implicated in the repair of double strand DNA breaks. Moreover, we demonstrated that Ku70/80 strongly stimulates and alters WRN exonuclease activity. A Ku70/Ku80 complex binds initially to two DNA ends at the DSB site, and then recruits a DNA‐dependent protein kinase (DNA‐PKcs), which has not been identified in plants. DNA‐PKcs phosphorylates and activates many proteins, including nuclease and itself.

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Moreover, we demonstrated that Ku70/80 strongly stimulates and alters WRN exonuclease activity. A Ku70/Ku80 complex binds initially to two DNA ends at the DSB site, and then recruits a DNA‐dependent protein kinase (DNA‐PKcs), which has not been identified in plants.

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Sv. Urologi nr 1 2017 - Svensk Urologisk Förening

Our previous studies indicated that the Werner syndrome protein (WRN) interacts with Ku, a heterodimeric factor of 70- and 80-kDa subunits implicated in the repair of double strand DNA breaks. Moreover, we demonstrated that Ku70/80 strongly stimulates and alters WRN exonuclease activity. The yeast homologue of Ku70/80, yKu70/80, fails to bind IP 6, indicating that the function of IP 6 in non‐homologous end‐joining, like that of DNA‐PK cs, is unique to the mammalian end‐joining process.

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Molecular biology 4-11-18 - StuDocu

Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists. Rabbit polyclonal Ku70 + Ku80 antibody. Validated in WB, IHC and tested in Human. Cited in 4 publication(s). Immunogen corresponding to synthetic peptide.