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Ku70 Antibody
Purified Mouse Monoclonal Antibody (Mab)
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Application 
| WB, ICC, IP |
|---|---|
| Primary Accession | P12956 |
| Reactivity | Human |
| Host | Mouse |
| Clonality | Monoclonal |
| Isotype | IgG1 |
| Calculated MW | 67 KDa |
| Gene ID | 2547 |
|---|---|
| Other Names | 5''-deoxyribose-5-phosphate lyase Ku70;5''-dRP lyase Ku70;70 kDa subunit of Ku antigen; ATP dependent DNA helicase 2 subunit 1;ATP dependent DNA helicase II 70 kDa subunit;ATP-dependent DNA helicase 2 subunit 1;ATP-dependent DNA helicase II 70 kDa subunit;CTC box binding factor 75 kDa subunit;CTC box-binding factor 75 kDa subunit;CTC75;CTCBF;CTCBF; DNA repair protein XRCC6;G22P1;Ku 70;Ku autoantigen 70kDa;Ku autoantigen p70 subunit;Ku autoantigen, 70kDa;Ku p70;Ku70;Ku70 DNA binding component of DNA-dependent proteinkinase complex (thyroid autoantigen 70 kDa;Kup70;Lupus Ku autoantigen protein p70;ML8;Thyroid autoantigen 70kD (Ku antigen);Thyroid autoantigen;Thyroid lupus autoantigen;Thyroid lupus autoantigen;Thyroid lupus autoantigen p70;Thyroid-lupus autoantigen;TLAA;TLAA;X ray repair complementing defective repair in Chinese hamster cells 6;X-ray repair complementing defective repair in Chinese hamster cells 6;X-ray repair cross-complementing protein 6;XRCC 6;XRCC6;XRCC6_HUMAN. |
| Dilution | IP~~1:500 WB~~1:1000 ICC~~1:200 |
| Format | Purified mouse monoclonal antibody in PBS(pH 7.4) containing with 0.09% (W/V) sodium azide and 50% glycerol. |
| Storage | Store at -20 °C.Stable for 12 months from date of receipt |
| Name | XRCC6 |
|---|---|
| Synonyms | G22P1 |
| Function | Single-stranded DNA-dependent ATP-dependent helicase that plays a key role in DNA non-homologous end joining (NHEJ) by recruiting DNA-PK to DNA (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). Required for double-strand break repair and V(D)J recombination (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). Also has a role in chromosome translocation (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). Has a role in chromosome translocation (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). It works in the 3'-5' direction (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). During NHEJ, the XRCC5-XRRC6 dimer performs the recognition step: it recognizes and binds to the broken ends of the DNA and protects them from further resection (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). Binding to DNA may be mediated by XRCC6 (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). The XRCC5-XRRC6 dimer acts as a regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). The XRCC5-XRRC6 dimer is probably involved in stabilizing broken DNA ends and bringing them together (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks (PubMed:20383123). 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined (PubMed:20383123). The XRCC5-XRRC6 dimer together with APEX1 acts as a negative regulator of transcription (PubMed:8621488). In association with NAA15, the XRCC5-XRRC6 dimer binds to the osteocalcin promoter and activates osteocalcin expression (PubMed:12145306). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). |
| Cellular Location | Nucleus. Chromosome |
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Background
Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. Required for osteocalcin gene expression. Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose- 5-phosphate at an abasic site near double-strand breaks. 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription.
References
Chan J.Y.,et al.J. Biol. Chem. 264:3651-3654(1989).
Reeves W.H.,et al.J. Biol. Chem. 264:5047-5052(1989).
Griffith A.J.,et al.Mol. Biol. Rep. 16:91-97(1992).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Halleck A.,et al.Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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