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- W2369699306 abstract "Objective:To obtain purified heavey chain molecule of soluble HLA-G1 protein produced by prokaryotic expression system,and to provide a firm basis on construction of soluble HLA-G1 protein.Methods:Through point mutation of primer,sHLA- G1-hc cDNA sequences without encoding signal peptide were amplified by RT-PCR followed by sequencing. After restrictive enzyme digestion,the subclonal fragments were inserted into expression vectors to construct the recombinant expression vectors pET22b(+)/sHLA-G1-hc,which were then expressed as G1-hc-6×his fusion proteins induced by IPTG.The fusion proteins was expressed mostly in the form of inclusion bodies.After inclusion bodies dissolving in 8 mol/L urea,then flowing through Ni 2+ affinity chromatography and finally dialysis,the purification effects of this fusion proteins were identified by SDS-PAGE and westernblot.Results:The G1-hc gene was homologous with the published gene sequences of sHLA-G1. The target proteins (MW 33 kD ) expressed by E.coli took account of 20% total cell proteins, the purified recombinant proteins with purity up to 95%.Conclusion:The prokaryotic expression vector for heavey chain molecule of sHLA-G1 have been established successfully, providing firm basis on clarification the function of sHLA-G1." @default.
- W2369699306 created "2016-06-24" @default.
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- W2369699306 date "2005-01-01" @default.
- W2369699306 modified "2023-09-25" @default.
- W2369699306 title "Expression and its purif ication of a heavy chain molecule of soluble HLA2G in E. coli" @default.
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