Hauptseite > Workflowsammlungen > Publikationsgebühren > High-efficient production and biophysical characterisation of nicastrin, and ist interaction with APPC100 > print

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100 1 _ |a Yu, Kun
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245 _ _ |a High-efficient production and biophysical characterisation of nicastrin, and ist interaction with APPC100
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520 _ _ |a Nicastrin, the largest member among the four components of the γ-secretase complex, has been identified to be the substrate recognizer for the proteolytic activity of the complex. Here we report that full-length human nicastrin (hNCT) can be obtained by heterologous expression in E. coli. Milligram quantities of the target protein are purified in a two-step purification protocol using affinity chromatography followed by SEC. The FOS-choline 14 purified tetrameric hNCT exhibits a proper folding with 31% α-helix and 23% β-sheet content. Thermal stability studies reveal stable secondary and tertiary structure of the detergent purified hNCT. A physical interaction between nicastrin and the γ-secretase substrate APPC100 confirmed the functionality of hNCT as a substrate recognizer.
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