X-Ray Repair Complementing Defective Repair in Chinese Hamster Cells 6 (XRCC6) antibody

Details for Product No. ABIN649971
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Antigen
Synonyms CTC75, CTCBF, G22P1, KU70, ML8, TLAA, 70kDa, G22p1, Ku70, Kup70
Reactivity
Human
(170), (59), (34), (13), (13), (13), (8), (6), (1)
Host
Rabbit
(118), (50), (7)
Clonality
Monoclonal
Conjugate
Un-conjugated
(5), (5), (5), (4), (4), (4), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Western Blotting (WB), Immunohistochemistry (IHC), Immunofluorescence (IF)
(158), (80), (76), (47), (36), (35), (27), (19), (10), (3), (2), (2), (1), (1)
Pubmed 5 references available
Quantity 100 µL
Options
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Catalog No. ABIN649971
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Specificity A synthetic peptide corresponding to residues in human Ku70 was used as an immunogen.
Alternative Name Ku70
Background ATP-dependent DNA helicase 2 subunit 1 (Ku70) is a single stranded DNA-dependent helicase originally recognized by the sera of patients with autoimmune diseases (1, 2). It plays a key role in multiple nuclear processes such as DNA repair, chromosome maintenance, transcription regulation, and V(D)J recombination (3). Ku70 forms a heterodimer with Ku80 and contributes to genomic integrity through its ability to bind DNA double-strand breaks and facilitate repair by the non-homologous end-joining (NHEJ) pathway (4). The dimer associates in a DNA-dependent manner with PRKDC to form the DNA-dependent protein kinase complex, DNA-PK (1). Together, the Ku70/Ku80 heterodimer and DNA-PKcs are required for V(D)J recombination and DNA double-strand break repair and may also play a role in transcription regulation (5). In addition, the dimer associates with NARG1 to bind to the osteocalcin promoter and activate osteocalcin expression (1).
Molecular Weight 70 kDA
Gene ID 1152
UniProt P12956
Research Area Signaling, Phospho-specific antibodies, Protein Modifications, Transcription Factors, Chromatin, Metabolism, Cell Structure
Application Notes The suggested dilution is: WB: = 1:2000-10000 ,IHC: = 1:100-250
Comment

Background: ATP-dependent DNA helicase 2 subunit 1 (Ku70) is a single stranded DNA-dependent helicase originally recognized by the sera of patients with autoimmune diseases (1, 2). It plays a key role in multiple nuclear processes such as DNA repair, chromosome maintenance, transcription regulation, and V(D)J recombination (3). Ku70 forms a heterodimer with Ku80 and contributes to genomic integrity through its ability to bind DNA double-strand breaks and facilitate repair by the non-homologous end-joining (NHEJ) pathway (4). The dimer associates in a DNA-dependent manner with PRKDC to form the DNA-dependent protein kinase complex, DNA-PK (1). Together, the Ku70/Ku80 heterodimer and DNA-PKcs are required for V(D)J recombination and DNA double-strand break repair and may also play a role in transcription regulation (5). In addition, the dimer associates with NARG1 to bind to the osteocalcin promoter and activate osteocalcin expression (1).

Restrictions For Research Use only
Format Liquid
Buffer 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Storage Comment Ku70 Antibody can be stored at -20°C for up to 12 months from time of receipt.
Expiry Date 12 months
Background publications Yaneva, Wen, Ayala et al.: "cDNA-derived amino acid sequence of the 86-kDa subunit of the Ku antigen." in: The Journal of biological chemistry, Vol. 264, Issue 23, pp. 13407-11, 1989 (PubMed).

Chan, Ye, Veillette et al.: "DNA-dependent protein kinase phosphorylation sites in Ku 70/80 heterodimer." in: Biochemistry, Vol. 38, Issue 6, pp. 1819-28, 1999 (PubMed).

Walker, Corpina, Goldberg: "Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair." in: Nature, Vol. 412, Issue 6847, pp. 607-14, 2001 (PubMed).

Koike: "Dimerization, translocation and localization of Ku70 and Ku80 proteins." in: Journal of radiation research, Vol. 43, Issue 3, pp. 223-36, 2003 (PubMed).

"The Universal Protein Resource (UniProt) 2009." in: Nucleic acids research, Vol. 37, Issue Database issue, pp. D169-74, 2008 (PubMed).

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