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BioMed Research International
Volume 2013, Article ID 836429, 9 pages
Research Article

High Expression and Purification of Amino-Terminal Fragment of Human Amyloid Precursor Protein in Pichia pastoris and Partial Analysis of Its Properties

School of Life Science, Southwest University, Chongqing 400715, China

Received 29 April 2013; Revised 5 July 2013; Accepted 4 September 2013

Academic Editor: Chiu-Chung Young

Copyright © 2013 Wei Li et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The cleaved amino-terminal fragment of human amyloid precursor protein (N-APP) binds death receptor 6 (DR6) and triggers a caspase-dependent self-destruction process, which was suggested to contribute to Alzheimer’s disease. To investigate the N-APP-DR6-induced degeneration pathway at the molecular level, obtaining abundant and purified N-APP is fundamental and critical. The recombinant N-APP has been produced in mammalian expression system. However, the cost and yield disadvantages of mammalian expression system make it less ideal for protein mass production. Here, we successfully expressed and purified recombinant N-terminal 18-285 amino acid residues of human amyloid precursor protein from the methylotrophic yeast Pichia pastoris with a high yield of 50 mg/L. Flow cytometry indicated the purified N-APP-induced obvious apoptosis of human neuroblastoma SHEP cells.