Cloning and fusion expression of POZ domain of human Zbtb7A in Escherichia coli
Human Zbtb7A is a critical molecular switch in the cellular response to oncogenic transformation. However, the POZ domain, located at the N-terminal of human Zbtb7A, acts an important protein-protein interaction motif. For the sake of obtaining the protein of POZ domain of human Zbtb7A, its cDNA was obtained by RT-PCR from K562 cell lines and cloned into pMD 18-T Simple vector. After the target fragment was confirmed by DNA sequencing, it was inserted into the E. coli expression vector pGEX4T1 and the yield recombinant plasmid was transformed to the E. coli BL21 (DE3). Induced with IPTG and detected with 15％ SDS-PAGE, a band corresponding to a protein of 40KD was obtained. The protein fused with GST was distributed mainly in the insoluble fraction. The recombinant protein of POZ domain may be applied for further study for the function of Zbtb7A.
Zbtb7A POZ domain pGEX4T1 E. coli BL21 (DE3)
Hui Wang Qingling Wang Guangfeng Zhao Yahong Huang Yayi Hou
Immunology and Reproductive Biology Lab, Medical School and State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing, PR China, 210093
国际会议
The 5th International Forum on Post-genome Technologies(5IFPT)(第五届国际后基因组生命科学技术学术论坛)
苏州
英文
2007-09-10（万方平台首次上网日期，不代表论文的发表时间）