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| Cat.No | ACP03038 | Target Name | XRCC6 |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 6-222aa | Mol Weight | 28.8kDa |
| Protein Length | Partial | Purity | Greater than 90% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P12956 |
|---|
Uniprot Id
P12956
Target Species
Human
Target Name
XRCC6
Target Full Name
X-ray repair cross-complementing protein 6
Target 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. Required for double-strand break repair and V(D)J recombination. Also has a role in chromosome translocation. 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. 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. Binding to DNA may be mediated by XRCC6. The XRCC5-XRRC6 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-XRRC6 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. 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-XRRC6 dimer together with APEX1 acts as a negative regulator of transcription. In association with NAA15, the XRCC5-XRRC6 dimer binds to the osteocalcin promoter and activates osteocalcin expression. 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.
Target Subcellular Location
Nucleus. Chromosome.
Target Protein Families
Ku70 family
Target Research Area
Epigenetics and Nuclear Signaling
Target Synonyms
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; DNA repair protein XRCC6; G22P1; Ku 70; 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 p70; Thyroid-lupus autoantigen; 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
Target Background
The p70/p80 autoantigen is a nuclear complex consisting of two subunits with molecular masses of approximately 70 and 80 kDa. The complex functions as a single-stranded DNA-dependent ATP-dependent helicase. The complex may be involved in the repair of nonhomologous DNA ends such as that required for double-strand break repair, transposition, and V(D)J recombination. High levels of autoantibodies to p70 and p80 have been found in some patients with systemic lupus erythematosus.
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