Expression of recombinant terminal C peptide of mouse Periostin in E.coli and identification of the biological activity of the expressed product
Abstract：AIM: To express the recombinant mouse periostin in Escherichia coli and identify the biological activity of the expressed product. METHODS: The DNA fragment encoding the terminal C of periostin was inserted into expression vector pRSET-B, in which the foreign gene is controlled by T7 promoters. The recombinant plasmid pRS-B-Periostin was transformed into E.coli BL21(DE3) and induced at IPTG to express the encoded protein The expressed product was purified and refolded. Its adhesion and spreading activity were assayed in vitro. RESULTS: After induction with IPTG for 5h, a new anticipated 36000Mr protein band appeared on SDS-PAGE gel. The expressed product existed in a form of inclusion body. After being purified and refolded, recombinant periostin with purity more than 95% was obtained, which could promote the adhesion and spreading of osteoblast. CONCLUSION: The recombinant mouse periostin has been successfully expressed in engineered E. coli BL21(DE3) with good biological activity.
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Publication Date：2001-01-01
Online Publishing Date：2025-08-15(First online date of this platform, not the publication date of the document)
Pages：3( 186-188 )