Abstract
Human osteoprotegrin (OPG) and its truncated mutant OPG-280 and lengthened mutant OPG-Fc were constructed and successfully expressed in Trichoplusia ni cells and Bombyx mori larvae. Native SDSPAGE and Western blot analysis revealed that OPG-Fc is present as a homodimer in Tn cells or B. mori larvae compared with OPG and OPG-280. Furthermore, the hypocalcemic effect assay showed that truncation of the C-terminal 100 residues OPG does not abolish the biological activity and Fc can be helpful in forming the OPG homodimer with improved biological activity.
Keywords: opg, mutant, trichoplusia ni cell, bombyx mori larvae
Protein & Peptide Letters
Title: Production of Recombinant Human Osteoprotegrin from Trichoplusia Ni Cells and Bombyx Mori Larvae
Volume: 11 Issue: 4
Author(s): Zhen Liu, Guan-zhen Yang and Xiang-Fu Wu
Affiliation:
Keywords: opg, mutant, trichoplusia ni cell, bombyx mori larvae
Abstract: Human osteoprotegrin (OPG) and its truncated mutant OPG-280 and lengthened mutant OPG-Fc were constructed and successfully expressed in Trichoplusia ni cells and Bombyx mori larvae. Native SDSPAGE and Western blot analysis revealed that OPG-Fc is present as a homodimer in Tn cells or B. mori larvae compared with OPG and OPG-280. Furthermore, the hypocalcemic effect assay showed that truncation of the C-terminal 100 residues OPG does not abolish the biological activity and Fc can be helpful in forming the OPG homodimer with improved biological activity.
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Cite this article as:
Liu Zhen, Yang Guan-zhen and Wu Xiang-Fu, Production of Recombinant Human Osteoprotegrin from Trichoplusia Ni Cells and Bombyx Mori Larvae, Protein & Peptide Letters 2004; 11 (4) . https://dx.doi.org/10.2174/0929866043406904
DOI https://dx.doi.org/10.2174/0929866043406904 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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