5-deoxyribose-5-phosphate lyase Ku70, 70 kDa subunit of Ku antigen, ATP-dependent DNA helicase 2 subunit 1, ATP-dependent DNA helicase II 70 kDa subunit , CTC box-binding factor 75 kDa subunit
Recombinant human X-ray repair cross-complementing protein 6 ptotein (2-609AA)
ELISA;Not yet tested in other applications.
Background / 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 5deoxyribose-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.
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze.
Caprylic Acid Ammonium Sulfate Precipitation purified
Epigenetics and Nuclear Signaling
LiteratureCloning and characterization of a cDNA that encodes a 70-kDa novel human thyroid autoantigen.Chan J.Y., Lerman M.I., Prabhakar B.S., Isozaki O., Santisteban P., Kuppers R.C., Oates E.L., Notkins A.L., Kohn L.D.J. Biol. Chem. 264:3651-365