Product Datasheet  
Ku70 Monoclonal Antibody  
Catalog Number: 27220  
Technical:tech@swbio.com  
Information:info@swbio.com  
Description  
  • host_species:  
  • Mouse
  • Amount:  
  • 100μgμg
  • Swiss-Prot No.:  
  • Uniprot: P12956

    Gene ID: 2547

  • Form of Antibody:  
  • Purified mouse monoclonal antibody in PBS(pH 7.4) containing with 0.02% sodium azide and 50% glycerol.
  • Storage:  
  • store at -20˚C
  • Immunogen:  
  • Purified recombinant human Ku70 protein fragments expressed in E.coli.
  • reactivity:  
  • Hu Mk
  • appl_detail:  
  • Western blotting: 1:1000

    Immunocytochemistry: 1:200

  • other_names:  
  • 5''-deoxyribose-5-phosphate lyase Ku70; 5''-dRP lyase Ku70; 70 kDa subunit of Ku antigen; ATP dependent DNA helicase 2 subunit 1; ATP dependent DNA helicase II 70 kDa subunit; ATP-dependent DNA helicase 2 subunit 1;
  • Purification:  
  • Affinity purified
  • Specificity:  
  • This antibody detects endogenous levels of Ku70 and does not cross-react with related proteins.
  • Applications:  
  • WB ICC IP
  • 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.




 
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