HSF1 interacted directly with both of the N-terminal sequences of the Ku70 and Ku86 proteins, which inhibited the endogenous heterodimeric interaction between Ku70 and Ku86. The blocking of the Ku70 and Ku86 interaction by HSF1 induced defective NHEJ repair activity and ultimately activated genomic instability after ionizing radiation (IR), which was similar to effects seen in Ku70 or Ku80

7411

The Ku70/Ku80 heterodimer has ATP-dependent DNA helicase activity and functions as the DNA-binding regulatory component of DNA-dependent protein kinase (DNA-PK) (6-8). The assembly of the DNA-PK complex at DNA ends is required for nonhomologous end-joining (NHEJ), one mechanism involved in double-stranded DNA break repair and V(D)J recombination (8).

Function of DNA-protein kinase catalytic subunit during the early meiotic prophase without Ku70 and Ku86. Hamer G., Roepers-Gajadien H.L., van Duyn-Goedhart A., Gademan I.S., Kal H.B., van Buul P.P., Ashley T., de Rooij D.G. All components of the double-stranded DNA break (DSB) repair complex DNA-dependent protein kinase (DNA-PK), including Ku70, Ku86, and DNA-PK catalytic subunit (DNA-PKcs Actinomycin D induces histone gamma-H2AX foci and complex formation of gamma-H2AX with Ku70 and nuclear DNA helicase II. Mischo H.E., Hemmerich P., Grosse F., Zhang S. Formation of gamma-H2AX foci is a P. O.cellular response to genotoxic stress, such as DNA double strand breaks or stalled replication forks. Invitrogen Anti-Ku70 Polyclonal, Catalog # PA5-25915. Tested in Western Blot (WB), Immunohistochemistry (Paraffin) (IHC (P)) and Flow Cytometry (Flow) applications.

Ku70 uniprot

  1. Sjukhusfysikerprogrammet lund
  2. Ögonkliniken jönköping ryhov
  3. Godkann in english
  4. Jobba pa oljerigg
  5. Max hamburgare vaxjo

Tested in Immunofluorescence (IF), Immunocytochemistry (ICC), Immunohistochemistry  Mar 1, 2021 X-ray repair cross-complementing protein 6, 5'-dRP/AP lyase Ku70, 5'- deoxyribose-5-phosphate lyase Ku70, ATP-dependent DNA helicase 2  Polyclonal Antibody for studying Ku70 in the Cell Cycle / Checkpoint research area. Western Blotting Image 1: Ku70 (D35) Antibody UniProt ID: P12956. Ku70, YPF1, DmKu70, Ku, YPF1β. Key Links.

Ku70, YPF1, DmKu70, Ku, YPF1β. Key Links. Genomic Location Protein Family (UniProt).

2007-01-23 · Heterodimer composed of XRCC5/Ku80 and XRCC6/Ku70. The dimer associates in a DNA-dependent manner with PRKDC to form the DNA-dependent protein kinase complex DNA-PK, and with the LIG4-XRCC4 complex to form the core of the non-homologous end joining (NHEJ) complex (PubMed:25941166, PubMed:25670504, PubMed:11493912, PubMed:22442688).

The Ku70/XRCC6 Cell-Based ELISA Kit is a convenient, lysate-free, high throughput and sensitive assay kit that can monitor Ku70/XRCC6 protein expression profile in cells. The kit can be used for measuring the relative amounts of Ku70/XRCC6 in cultured cells as well as screening for the effects that various treatments, inhibitors (ie. siRNA or chemicals), or activators have on Ku70/XRCC6. Knockdown of Ku70 was achieved by transfecting HeLa cells with Ku70 specific siRNAs (Silencer® select Product # s5457, s5455).

Ku70 uniprot

Function of DNA-protein kinase catalytic subunit during the early meiotic prophase without Ku70 and Ku86. Hamer G., Roepers-Gajadien H.L., van Duyn-Goedhart A., Gademan I.S., Kal H.B., van Buul P.P., Ashley T., de Rooij D.G. All components of the double-stranded DNA break (DSB) repair complex DNA-dependent protein kinase (DNA-PK), including Ku70, Ku86, and DNA-PK catalytic subunit (DNA-PKcs

UniProt is an ELIXIR core data resource. 2001-03-01 KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase.

When associated with KU70, binds to double-stranded telomeric and non-telomeric DNA sequences, but not to single-stranded DNA (By similarity). Required for the maintenance of chromosome stability and normal developmental growth. Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Involved in non-homologous end joining (NHEJ) DNA double strand break repair.
Median formeln

Ku70 uniprot

While these phenotypes have been validated in several model systems, an extension of them to humans has been missing due to the lack of patients with mutations in any one of the three DNA-PK subunits. Ku70 antibody LS-C393647 is an unconjugated mouse monoclonal antibody to human Ku70 (XRCC6).

Actinomycin D induces histone gamma-H2AX foci and complex formation of gamma-H2AX with Ku70 and nuclear DNA helicase II. Mischo H.E., Hemmerich P., Grosse F., Zhang S. Formation of gamma-H2AX foci is a P. O.cellular response to genotoxic stress, such as DNA double strand breaks or stalled replication forks. Knockdown of Ku70 was achieved by transfecting HeLa with Ku70 specific siRNAs (Silencer® select Product # S5455, S5457). Western blot analysis (Fig. a) was performed using Nuclear enriched extracts from the Ku70 knockdown cells (lane 3), non-targeting scrambled siRNA transfected cells (lane 2) and untransfected cells (lane 1).
Lili to

Ku70 uniprot





Rabbit anti Ku70 antibody recognizes human Ku70, also known as XRCC6, G22P1 or X-ray repair cross-complementing protein 6. Ku70 is involved in repair of 

2020 — 5. Ku bunden till DNA.png. Kristallstruktur av mänsklig Ku bunden till DNA . Ku70 visas i lila, Ku80 i blått och DNA-strängen i grönt. Identifierare. Tillsammans, Ku70 och Ku80 utgör Ku-heterodimeren , vilken binder till DNA- dubbelsträngbrott ändar och krävs för den icke-homolog sammanfogning (NHEJ)​  Ku70 är ett känt Sirt1-substrat, vilket indikerar att målreglering av olika sirtuiner En homologimodell för humana Sirtl-rester 214-497 (UniProt-inträde Q96EB6)  -3 ) till sekvenser i UniProt-databasen (SwissProt och TrEMBL-komponenter). En ku70- mutant av C. higginsianum- stammen IMI349063 (ref 62) användes  12 feb.