Anti-Ku70 + Ku80, clone KU729

1 mg/ml in sterile PBS, BSA free, sodium azide free. This antibody recognizes a dimer of two proteins of 70kDa (Ku70) and ~80kDa (Ku80), identified as two subunits of Ku. Antbody KU729 recognizes a conformational epitope of the Ku70 + Ku80 dimer, which is destroyed during Western blotting. The Ku70 + Ku80 dimer is important for function of a 460kDa DNA-dependent protein kinase. Ku protein plays a role in cell signaling, proliferation, DNA repair, replication, transcriptional activation, and apoptosis. Protein function: 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. Required for osteocalcin gene expression. 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. 5'-dRP lyase activity 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. [The UniProt Consortium]