DCLRE1C antibody (DNA Cross-Link Repair 1C)

Details for Product anti-DCLRE1C Antibody No. ABIN965976, Supplier: Log in to see
Antigen
  • artemis
  • A-SCID
  • DCLREC1C
  • RS-SCID
  • SCIDA
  • SNM1C
  • hSNM1C
  • Snm1l
  • nuclease
  • 9930121L06Rik
  • AI661365
  • Art
  • DNA cross-link repair 1C
  • DNA cross-link repair 1C, PSO2 homolog (S. cerevisiae)
  • DCLRE1C
  • Dclre1c
Alternatives
anti-Human DCLRE1C antibody for Enzyme Immunoassay
Reactivity
Human
88
37
22
5
4
4
4
3
3
2
1
1
1
1
1
Host
Rabbit
78
10
1
Clonality
Polyclonal
Conjugate
This DCLRE1C antibody is un-conjugated
2
2
2
2
2
2
Application
Immunohistochemistry (IHC)
78
44
38
22
14
3
1
1
1
Options
Supplier
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Supplier Product No.
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Immunogen Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-residues of human DCLRE1C (DNA cross-link repair 1C protein)
Alternative Name DCLRE1C (DCLRE1C Antibody Abstract)
Background DCLRE1C (DNA cross-link repair 1C protein) is 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.
Synonyms: ARTEMIS, ASCID, SCIDA, SNM1C
Pathways DNA Damage Repair
Restrictions For Research Use only
Product cited in: Pannicke, Ma, Hopfner, Niewolik, Lieber, Schwarz: "Functional and biochemical dissection of the structure-specific nuclease ARTEMIS." in: The EMBO journal, Vol. 23, Issue 9, pp. 1987-97, 2004 (PubMed).

Poinsignon, de Chasseval, Soubeyrand, Moshous, Fischer, Haché, de Villartay: "Phosphorylation of Artemis following irradiation-induced DNA damage." in: European journal of immunology, Vol. 34, Issue 11, pp. 3146-55, 2004 (PubMed).

Poinsignon, Moshous, Callebaut, de Chasseval, Villey, de Villartay: "The metallo-beta-lactamase/beta-CASP domain of Artemis constitutes the catalytic core for V(D)J recombination." in: The Journal of experimental medicine, Vol. 199, Issue 3, pp. 315-21, 2004 (PubMed).

Ma, Lu, Tippin, Goodman, Shimazaki, Koiwai, Hsieh, Schwarz, Lieber: "A biochemically defined system for mammalian nonhomologous DNA end joining." in: Molecular cell, Vol. 16, Issue 5, pp. 701-13, 2004 (PubMed).

Ma, Pannicke, Schwarz, Lieber: "Hairpin opening and overhang processing by an Artemis/DNA-dependent protein kinase complex in nonhomologous end joining and V(D)J recombination." in: Cell, Vol. 108, Issue 6, pp. 781-94, 2002 (PubMed).

Callebaut, Moshous, Mornon, de Villartay: "Metallo-beta-lactamase fold within nucleic acids processing enzymes: the beta-CASP family." in: Nucleic acids research, Vol. 30, Issue 16, pp. 3592-601, 2002 (PubMed).

Moshous, Callebaut, de Chasseval, Corneo, Cavazzana-Calvo, Le Deist, Tezcan, Sanal, Bertrand, Philippe, Fischer, de Villartay: "Artemis, a novel DNA double-strand break repair/V(D)J recombination protein, is mutated in human severe combined immune deficiency." in: Cell, Vol. 105, Issue 2, pp. 177-86, 2001 (PubMed).

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