Links to databases
Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3 (PubMed:22307388). The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery (PubMed:22307388).
Recommended sample types are EDTA plasma and serum. A range of additional sample types are compatible with the technology (PEA), including citrate plasma, heparin plasma, cerebrospinal fluid, (CSF), tissue and cell lysates, fine needle biopsis, microdialysis fluid, cell culture media, dried blood spots, synovial fluid, saliva, plaque extract and microvesicles. Please note that protein expression levels are expected to vary in different sample types. Certain assays are differentially affected by interfering substances such as hemolysate. Download any of our Data Validation documents or contact firstname.lastname@example.org for more information.
Analytical Measuring Range
Please note: the technical data reported below refers to the measured value in the in vitro validation assays. The calibrator curve below shows the performance of the assay with the estimated sensitivity and dynamic range parameters indicated. These curves are generated during the assay validation process using recombinant antigens. Please note that when analyzing biological samples the data generated will be given in the form of relative quantification (NPX values) and cannot be converted to absolute protein concentrations. For more info about NPX measurements, please visit our FAQ page (https://www.olink.com/question/what-is-npx).
Calibrator curve for validation data (generated in multiplex)
- Within run precision Coefficient of Variation (CV)
- Between run precision Coefficient of Variation (CV)
Precision (repeatability) is calculated from linearized NPX values over LOD.
Biomarker Validation Data
Additional validation data, as well as a more detailed description of how the Olink panels are quality controlled can be found in our Data Validation documents. To download or to learn more go to the Data Validation page.