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- W2393038909 abstract "OBJECTIVE:To express and purify the tumor fibroblast activation protein(FAP)fragment enriched T cell epitopes.METHODS:Amino acid sequence of FAP was analysed by SYFPEITHI software combined with PAProC software,and then target fragment AA264-AA449(NP_032012.1)with abundant T cell epitopes and lack of cleavage sites of protease were selected.The corresponding target gene for the polypeptide was mRNA798-1418(GenBank:BC019190.1).Gene fragment mRNA798-1418was amplified from pCDNA3.1-FAP by PCR and cloned into pET-28a(+)vector,the recombinant protein His6-FAP264-449was expressed in BL21engineering bacteria and then purified by His tag.RESULTS:The prokaryotic expression plasmid of FAP with abundant T cell epitopes was successfully constructed,and the results identified by double digestion with BamH1/Xho1corresponded exactly well as expected.The fusion protein His6-FAP264-449was expressed and mainly existed in the form of inclusion body.Then the fusion protein was purified,its purity reached 95%through the gray-scale analysis.CONCLUSION:The FAP fragment enriched T cell epitopes was expressed and purified successfully,that provided a basis for tumor immunotherapy targeting FAP." @default.
- W2393038909 created "2016-06-24" @default.
- W2393038909 creator A5090670258 @default.
- W2393038909 date "2014-01-01" @default.
- W2393038909 modified "2023-09-26" @default.
- W2393038909 title "Cloning expression and purification of the polypeptide with abundant T cell epitopes from tumor fibroblast activation protein" @default.
- W2393038909 hasPublicationYear "2014" @default.
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