XRCC4 antibody
Quick Overview for XRCC4 antibody (ABIN967264)
Target
See all XRCC4 AntibodiesReactivity
Host
Clonality
Conjugate
Application
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Immunogen
- Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-residues of human XRCC4(X-ray repair cross-complementing protein 4)
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Restrictions
- For Research Use only
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Storage
- 4 °C
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: "Ku recruits the XRCC4-ligase IV complex to DNA ends." in: Molecular and cellular biology, Vol. 20, Issue 9, pp. 2996-3003, (2000) (PubMed).
: "The XRCC4 gene product is a target for and interacts with the DNA-dependent protein kinase." in: The Journal of biological chemistry, Vol. 273, Issue 3, pp. 1794-801, (1998) (PubMed).
: "Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells." in: Nature, Vol. 388, Issue 6641, pp. 492-5, (1997) (PubMed).
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- XRCC4 (X-Ray Repair Complementing Defective Repair in Chinese Hamster Cells 4 (XRCC4))
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Alternative Name
- XRCC4
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Background
- XRCC4 (X-ray repair cross-complementing protein 4) is involved in DNA nonhomologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. XRCC4 binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends. XRCC4 is a homodimer and homotetramer in solution. The homodimer associates with LIG4, and the LIG4-XRCC4 complex associates in a DNA-dependent manner with the DNA-PK complex formed by the Ku p70/p86 dimer (G22P1/G22P2) and PRKDC. XRCC4 seems to interact directly with PRKDC but not with the Ku p70/86 dimer. It interacts with XLF/Cernunnos. Interacts with APTX and APLF. Sumoylation at Lys-210 is required for nuclear localization and recombination efficiency. It has no effect on ubiquitination.
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Pathways
- DNA Damage Repair, Production of Molecular Mediator of Immune Response
Target
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