摘要
将人单核细胞趋化蛋白-1(MCP-1)的cDNA插入融合蛋白表达载体pGEX-4T-1中,构建成质粒pGEX/MCP转化大肠杆菌JM109,经IPTG诱导后合成GST-MCP-1融合蛋白。用12%SDS-PAGE检测在30kD左右有新生蛋白条带出现,表达量约占菌体总蛋白的31.7%。趋化实验证明,该产物具备明确的单核细胞趋化活性。
A gene fragment encoding human monocyte chemotactic protein-1 (MCP-1 ) was inserted into the fusion protein expression vector pGEX-AT-1 to construct a plasmid pGEX-MCP.The expression rate of the GST-MCP-1 fusion protein in E. Colt JM109 was about 31. 7% of the total bacterial products detected by 12% SDS-PAGE. The results of the chemotaxis assay indicated that the GST-MCP-1 fusion protein should possess obvious monocyte chemotactic activity.
出处
《细胞与分子免疫学杂志》
CAS
CSCD
1996年第3期24-26,共3页
Chinese Journal of Cellular and Molecular Immunology