Anti-Ku80

0.5mg/ml if reconstituted with 0.2ml sterile DI water. XRCC5 (X-ray Repair, Complementing Defective, In Chinese Hamster, 5), also known as Ku80 or Ku86, is a protein that in humans, is encoded by the XRCC5 gene. The XRCC5 gene encodes the 80-kD subunit of the Ku autoantigen, a heterodimer which contributes to genomic integrity through its ability to bind DNA double-strand breaks and facilitate repair by the nonhomologous end joining (NHEJ) pathway. The XRCC5 gene is mapped to 2q35. Human colon cancer cells heterozygous for Ku86 are haploinsufficient with an increase in polyploid cells, a reduction in cell proliferation, elevated p53 levels, and a slight hypersensitivity to ionizing radiation. Functional inactivation of the second Ku86 allele results in cells with a drastically reduced doubling time. The Ku86 locus is essential in human somatic tissue culture cells by experiments demonstration. A rare microsatellite polymorphism in XRCC5 is associated with cancer in patients of varying radiosensitivity. 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 (PubMed:12145306, PubMed:20383123, PubMed:7957065, PubMed:8621488). 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 (PubMed:20383123). 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 (PubMed:8621488). [The UniProt Consortium]