|Other Names||Protein artemis, 31--, DNA cross-link repair 1C protein, Protein A-SCID, SNM1 homolog C, hSNM1C, SNM1-like protein, DCLRE1C, ARTEMIS, ASCID, SCIDA, SNM1C|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||ARTEMIS, ASCID, SCIDA, SNM1C|
|Function||Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ.|
|Tissue Location||Ubiquitously expressed, with highest levels in the kidney, lung, pancreas and placenta (at the mRNA level) Expression is not increased in thymus or bone marrow, sites of V(D)J recombination.|
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DCLRE1C is a nuclear protein that is involved in V(D)J recombination and DNA repair. The protein has single-strand-specific 5'-3' exonuclease activity; it also exhibits endonuclease activity on 5' and 3' overhangs and hairpins when complexed with protein kinase, DNA-activated, catalytic polypeptide.
Beucher, A., et al. EMBO J. 28(21):3413-3427(2009)Rivera-Munoz, P., et al. Blood 114(17):3601-3609(2009)Wang, H., et al. J. Biol. Chem. 284(27):18236-18243(2009)
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