Anti-Ku80 (8H1) Mouse antibody

Anti-Ku80 (8H1) Mouse antibody

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Ku80 (8H1) Mouse monoclonal antibody

WB, ICC/IF, IP, ChIP

Human, Monkey

ATP dependent DNA helicase II 80 kDa subunit; ATP dependent DNA helicase II 86 Kd subunit; ATP dependent DNA helicase II; ATP-dependent DNA helicase 2 subunit 2; ATP-dependent DNA helicase II 80 kDa subunit; CTC box binding factor 85 kDa; CTC box-binding antibody

Mouse IgG1

Antigen: Purified recombinant human Ku80 protein fragments expressed in E.coli

Monoclonal

Purified mouse monoclonal antibody in PBS(pH 7.4) containing with 0.02% sodium azide and 50% glycerol.

Store at 4°C short term. Store at -20°C long term. Avoid freeze / thaw cycle.

Swiss-Prot Acc.P13010.Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression. The XRCC5/6 dimer probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription.