Production, Purification, and Biological Activity Analysis of Recombinant Human Persephin Expressed in Insect Cells

Title: Production, Purification, and Biological Activity Analysis of Recombinant Human Persephin Expressed in Insect Cells

Volume: 8 Issue: 2

Author(s): Zhe-Yu Chen, Xing-Dong Zheng, Li Cao, Chang-Lin Lu, Xiang-Fu Wu and Cheng He

Affiliation:

Keywords: human persephin, human persephin psp, trichoplusia ni, neurturin NTN

Abstract: Recombinant human Persephin (PSP) has been expressed at high levels in recombinant baculavirus infected Trichoplusia ni (Tn-5B1-4) cells. The expressed protein was purified by nickel affinity chromatography. Pure, recombinant human PSP promoted the survival of embryonic motor neurons in vitro but failed to protect adult rat spinal cord motor neurons after sciatic nerve transection in vivo. Because recombinant bioactive human PSP can be obtained in large quantities, and purified to near homogeneity, they are suitable for further biological activity investigation.

Cite this article as:

Chen Zhe-Yu, Zheng Xing-Dong, Cao Li, Lu Chang-Lin, Wu Xiang-Fu and He Cheng, Production, Purification, and Biological Activity Analysis of Recombinant Human Persephin Expressed in Insect Cells, Protein & Peptide Letters 2001; 8 (2) . https://dx.doi.org/10.2174/0929866013409553