Recombinant human Y2 neuropeptide Y receptor fusion protein expression purification and analysis of bioinformatics.docVIP

 PAGE \* MERGEFORMAT 17 Recombinant human Y2 neuropeptide Y receptor fusion protein expression purification and analysis of bioinformatics Of: Dingke Xiang Dong Ping Zheng Yongchen Yangyong Peng Zhu Xiaoliang Han Jinyun single Zhixin Yu DING Zhen-hua Ding [Abstract] Objective in E. coli expression of human neuropeptide Y Y2 receptor, and of the purification, identification and bioinformatics analysis. Methods are well constructed and confirmation by sequencing the recombinant plasmid pET28a Y2 transformed into E. coli BL21 ( DE3), IPTG induced expression of fusion protein and detected by SDS PAGE and Western blotting, expression products of inclusion bodies by Ni2 + NTA affinity chromatography. and then use the relevant online bioinformatics software Y2 receptor protein. Results IPTG induction of recombinant plasmid containing the pET28a Y2 DE3 bacteria expressing fusion protein of recombinant human Y2. recombinant protein by Ni2 + NTA affinity chromatography purification, got a high purity of the fusion protein. The correlation analysis of online software Y2 obtained by related biological characteristics of the body. concluded that the recombinant plasmid pET28a Y2 successfully expressed in E. coli DE3, affinity chromatography, the fusion protein to obtain higher purity, and biological characteristics of Y2 receptor protein were predicted for further study its biological function and laid the foundation for development of antibodies. [Keywords:] human neuropeptide Y Y2 receptor; fusion protein; inclusion body; purification; Bioinformatics [Abstract] Objective To express human Y2 receptor protein in E. coli, purify and identify it, and conduct bioinformatic analysis of Y2 receptor protein. Methods The recombinant plasmid pET28a Y2 which had been well constructed and sequentially confirmed was transplanted into E.coli BL21 (DE3) and induced by IPTG to express fusion proteins. SDS PAGE and Western blot were used to test and identify the expressed fusi