Anti-XRCC3 Monoclonal Antibody (Clone: 10F1/6)

The x-ray repair cross-complementing (XRCC) proteins are responsible for efficiently repairing and maintaining genetic stability following DNA base damage. These genes share sequence similarity with the yeast DNA repair protein Rad51. XRCC1 is a protein that facilitates the DNA base excision repair pathway by interacting with DNA ligase III and DNA polymerase to repair DNA single-strand breaks. XRCC2 and XRCC3 are both involved in maintaining chromosome stability during cell division. XRCC2 is required for efficient repair of DNA double-strand breaks by homologous recombination between sister chromatids, and XRCC3 interacts directly with Rad51 to cooperate with Rad51 during recombinational repair. XRCC4 is an accessory factor of DNA Ligase IV that preferentially binds DNA with nicks or broken ends. XRCC4 binds to DNA Ligase IV and enhances its joining activity, and it is also involved in V(D)J recombination. Any defect in one of the known components of the DNA repair/V(D)J recombination machinery (Ku-70, Ku-80, DNA-PKCS, XRCC4 and DNA Ligase IV) leads to abortion of the V(D)J rearrangement process and early block in both T and B cell maturation. Protein function: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the RAD21 paralog protein complex CX3 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, CX3 acts downstream of RAD51 recruitment, the complex binds predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junctions of replication forks. Involved in HJ resolution and thus in processing HR intermediates late in the DNA repair process, the function may be linked to the CX3 complex and seems to involve GEN1 during mitotic cell cycle progression. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and RAD51C. [The UniProt Consortium]