The antibody was purified by affinity chromatography.
Storage & Handling:
The antibody solution should be stored undiluted at 4°C.
Application:
IHC(Frozen)*, IP*, IF * - *This application has been reported in the literature.
Recommended Usage:
Recommended Usage: Each lot of this antibody is quality control tested by Immunofluorescence staining. For immunofluorescence microscopy, suggested working dilution(s): Use a dilution range of 2-4 µg/ml. For immunoprecipitation, this antibody can be used at 2-4 μg /1x107 cell equivalents. It is recommended that the reagent be titrated for optimal performance for each application.
Application References:
1. Fu, X. D., et al. 1990. Nature 343:437.
Description:
Ku, is a heterodimeric DNA end binding complex composed of 70 KD and 80 kD subunits, serves as the DNA binding component of the DNA-dependent protein kinase (DNA-PK). Ku binds to double-stranded DNA breaks (DSBs), activates the catalytic subunit (DNA-PKcs) when DNA is bound, and is essential in DSB repair and V(D)J recombination. Clone 235-1 has been reported to bind the holoprotein (70KD and 80KD heterodimer) and both chains are need for the antigen to be recognized by this antibody. Clone 235-1 has been shown to be useful for Immunoprecipitation and Immunofluorescence staining. This clone is not suitable for Western blotting.
Other Names:
ATP-dependent DNA helicase II 70KD /80 KD subunits, Ku-70/Ku-80, Ku-70/Ku-86, G22P1/ XRCC5
Structure:
Ku is a heterodimeric DNA end binding complex composed of 70 KD and 80 kD subunits, form complex with DNA-PK, and with the DNA ligase IV-XRCC4 complex.
Distribution:
Nucleus and Cytoplasm
Function:
The Ku heterodimer acts as regulatory subunit of the DNA-dependent protein kinase complex by increasing the affinity of the catalytic subunit PRKDC to DNA. Ku functions together with the DNA ligase IV-XRCC4 complex in the repair of DNA double-strand break
Antigen References:
1. Walker, J. R., et al. 2001. Nature 412:607. 2. Mari, P.-O., et al. 2006. Proc. Nat. Acad. Sci. 103:18597. 3. Fu, X. D., et al. 1990. Nature 343:437.
