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Human X-Ray Repair Cross Complementing 6 (XRCC6) ELISA Kit

Due to the possibility of mismatching between antigens from other origin and antibodies used in our kits (e.g., antibody targets conformational epitope rather than linear epitope), some native or recombinant proteins from other manufacturers may not be recognized by our products.

Principle of the Assay

The microtiter plate provided in this kit has been pre-coated with an antibody specific to XRCC6. Standards or samples are then added to the appropriate microtiter plate wells with a biotin-conjugated antibody preparation specific to XRCC6. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After the TMB substrate solution is added, only those wells that contain XRCC6, biotin-conjugated antibody, and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution, and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of XRCC6 in the samples is then determined by comparing the O.D. of the samples to the standard curve.


For Use with serum, plasma, and cell culture supernatants. For Research Use Only. Not for use in diagnostic procedures.

Target Information

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:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912, PubMed:20493174, PubMed:2466842, PubMed:9742108). Required for double-strand break repair and V(D)J recombination (PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912, PubMed:20493174, PubMed:2466842, PubMed:9742108). Also has a role in chromosome translocation (PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912, PubMed:20493174, PubMed:2466842, PubMed:9742108). Has a role in chromosome translocation (PubMed:7957065, PubMed:20493174, PubMed:2466842, PubMed:9742108, PubMed:8621488, PubMed:12145306, PubMed:11493912). The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner (PubMed:7957065, PubMed:8621488, PubMed:20493174, PubMed:2466842, PubMed:9742108, PubMed:12145306, PubMed:11493912). It works in the 3'-5' direction (PubMed:20493174, PubMed:2466842, PubMed:9742108, PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912). 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:7957065, PubMed:8621488, PubMed:20493174, PubMed:2466842, PubMed:9742108, PubMed:12145306, PubMed:11493912). Binding to DNA may be mediated by XRCC6 (PubMed:20493174, PubMed:2466842, PubMed:9742108, PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912). 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 (PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912, PubMed:20493174, PubMed:2466842, PubMed:9742108). The XRCC5-XRRC6 dimer is probably involved in stabilizing broken DNA ends and bringing them together (PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912, PubMed:20493174, PubMed:2466842, PubMed:9742108). The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step (PubMed:7957065, PubMed:8621488, PubMed:12145306, PubMed:11493912, PubMed:20493174, PubMed:2466842, 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).

GENE ID 2547
SWISS PROT P12956
SYNONYMS Ku70; CTC75; CTCBF; G22P1; ML8; TLAA; Lupus Ku Autoantigen Protein P70; ATP-Dependent DNA Helicase 2 Subunit 1; CTC box-binding factor 75 kDa; Thyroid-lupus autoantigen


Materials Supplied

Kit Components 96 Wells Quantity/Size
Pre-coated, ready-to-use 96-well strip plate 1 plate
Plate sealer for 96 wells 2
Standard
2 tubes
Diluent buffer 1 bottle
Detection Reagent A 1 bottle
Detection Reagent B 1 bottle
TMB Substrate 1 tube
Stop Solution 1 tube
Wash Buffer (30 ℅ concentrate) 1 tube
Product data sheet 1 copy

Storage

Storage The TMB Substrate, Wash Buffer (30X concentrate), and the Stop Solution should be stored at 4°C upon receipt, while the other items should be stored at -20°C.

Performance Characteristics

REPEATABILITY

Intra-assay Precision (Precision within an assay): 3 samples with low, middle, and high-level XRCC6 were tested 20 times on one plate, respectively.
Inter-assay Precision (Precision between assays): 3 samples with low, middle, and high-level XRCC6 were tested on 3 different plates, with 8 replicates in each plate.
CV(%) = SD/meanX100

Intra-Assay: CV<10%
Inter-Assay: CV<12%

SENSITIVITY The minimum detectable dose was 0.112ng/mL.
ASSAY RANGE 0.312-20ng/mL
SPECIFICITY This assay has high sensitivity and excellent specificity for the detection of XRCC6.
No significant cross-reactivity or interference between XRCC6 and analogs was observed.
Note:
Limited by current skills and knowledge, it is impossible to perform all possible cross-reactivity detection tests between XRCC6 and all analogs, therefore, cross reactivity may still exist.