Product Datasheet  
X-ray repair cross-complementing protein 6 Polyclonal Antibody  
Catalog Number: 42275  
Technical:tech@swbio.com  
Information:info@swbio.com  
Description  
  • host_species：  
  • Rabbit
  • Amount：  
  • 100μgμg
  • Swiss-Prot No.：  
  • Swiss-Prot#: P12956
  • Form of Antibody：  
  • Preservative: 0.03% Proclin 300 Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
  • Storage：  
  • Store at -20˚C
  • Immunogen：  
  • Recombinant human X-ray repair cross-complementing protein 6 ptotein
  • reactivity：  
  • Hu
  • appl_detail：  
  • Western blotting: 1:500 - 1:1000
    Immunohistochemistry: 1:20 - 1:200
  • other_names：  
  • 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
  • Purification：  
  • Caprylic Acid Ammonium Sulfate Precipitation purified
  • Specificity：  
  • The antibody detects endogenous level of total X-ray repair cross-complementing protein 6 polyclonal antibody.
  • Applications：  
  • WB IHC
  • 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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