摘要
Based on the protein comparison between zebrafish Gli2 and fruit fly C_i and the analysis of hydrophilicity/hydrophobicity of Gli2 protein by computer programmer, the recombination N-terminal partial protein of Gli2 protein was designed.After the DNA fragment encoding the N-terminal part was cloned out by PCR, it was ligated with an expression vector containing His-tag and transformed into BL-21, a bacterial expression strain, to express this protein.After the expression condition was optimized, the protein can be expressed at high level after having been induced for 3 hours when the inducer—IPTG was at 0.6 mmol/L.The protein is soluble in solution, a bacterial protein extraction solution.After the protein solution was diluted in B-per solution, the recombination protein can bind to the Ni-NTA column and be purified highly.
Based on the protein comparison between zebrafish Gli2 and fruit fly C_i and the analysis of hydrophilicity/hydrophobicity of Gli2 protein by computer programmer, the recombination N-terminal partial protein of Gli2 protein was designed.After the DNA fragment encoding the N-terminal part was cloned out by PCR, it was ligated with an expression vector containing His-tag and transformed into BL-21, a bacterial expression strain, to express this protein.After the expression condition was optimized, the protein can be expressed at high level after having been induced for 3 hours when the inducer—IPTG was at 0.6 mmol/L.The protein is soluble in solution, a bacterial protein extraction solution.After the protein solution was diluted in B-per solution, the recombination protein can bind to the Ni-NTA column and be purified highly.
出处
《海洋科学集刊》
CAS
2006年第1期140-148,共9页
Studia Marina Sinica
基金
国家自然科学基金项目(30210403202)资助。
