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| Expression,purification and identification of mIL-17RAaa32-322 |
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Abstract ［Abstract］Objective: To clone the extracellular region of mouse interleukin17 receptor (mIL17RAaa32-322) and mouse IgG2AFc (mIgG2AFc), construct the recombinant prokaryotic expression vector of mIL17RA aa32-322mIgG2AFc, and then to express, purify and identify the fusion protein.Methods: The prokaryotic expression vector pET32a (+)mIL17RAaa32-322mIgG2AFc was constructed by using recombinant DNA technology and expressed in E. coli Rosetta. Then mIL17RAaa32-322mIgG2AFc fusion protein was purified by nickelchelating chromatography and identified by SDSPAGE electrophoresis and Western blot assay. Results: The prokaryotic expression vector pET32a(+)mIL17RAaa32-322mIgG2AFc was successfully constructed, which can express fusion protein of high purity. The mIL17RAaa32-322mIgG2AFc was confirmed by Western blot. Conclusion: Recombinant prokaryotic expression vector pET32a(+)mIL17RAaa32-322mIgG2AFc was successfully constructed and mIL17RAaa32-322mIgG2AFc fusion protein was purified for the research and application of foundation in the treatment of autoimmune disease.
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2012, Vol. 22 
