Product Datasheet  
Ku70 Antibody  
Catalog Number: 33426  
Technical:tech@swbio.com  
Information:info@swbio.com  
Description  
  • host_species：  
  • Rabbit
  • Amount：  
  • 100μgμg
  • Swiss-Prot No.：  
  • Swiss-Prot: P12956
    NCBI Gene ID: 2547
  • Form of Antibody：  
  • Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
  • Storage：  
  • Store at -20˚C
  • Immunogen：  
  • Synthesized peptide derived from human Ku70.
  • reactivity：  
  • Hu
  • appl_detail：  
  • Western blotting: 1:500~1:3000
    Immunohistochemistry: 1:50~1:100
    Immunofluorescence: 1:100~1:500
  • other_names：  
  • 70 kDa subunit of Ku antigen; ATP-dependent DNA helicase II; 70 kDa subunit; CTC box binding factor 75 kDa subunit; CTC75
  • Purification：  
  • The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
  • Specificity：  
  • The antibody detects endogenous levels of total Ku70 protein.
  • Applications：  
  • WB IHC IF
  • Background：  
  • 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.

    Nicholas S. Y. Ting, Nucleic Acids Res., Apr 2005; 33: 2090 - 2098.
    Yansong Gu, PNAS, Jul 1997; 94: 8076.
    Suparna Mazumder, Mol. Cell. Biol., May 2007; 27: 3511 - 3520.
    Roopashree Narasimhaiah, Cereb Cortex, Jun 2005; 15: 696 - 707.



 
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