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- W2358972816 abstract "To clone MUC1/Y full length cDNA and express and purify its extra|cellular fragment protein from E.coli for further functional and tumor therapeutic research purposes.MUC1/Y cDNA was amplified by RT|PCR from HeLa cells and cloned into pGEM|T for sequence analysis.MUC1/Y extra|celluar fragment (MUC1/Yex) was then amplified by PCR and cloned into pGEX|2T fusion expression vector. E.coli DH5α was transformed with the new constructed expression vector pGEX|Yex and induced by IPTG.The fusion protein GST|Yex was purified by affinity column and identified by thrombin digestion,GST activity and N|terminal protein sequencing.Polyclonal antibody was prepared by immunizing rabbits.The results showed that the open reading frame(ORF) of MUC1/Y cDNA from HeLa cells consisted of 759 bp with a 9 bp deletion in its signal peptide|coding region and a G to A transition at the site of 331 bp which caused a V to M amino acid mutation (GenBank access number AF125525).The expressed fusion protein GST|Tex was about 40 kD which was 25%-30% of total host proteins.70%-80% of the GST|Yex proteins existed as soluble ones and after one|step affinity purification the purity of GST|Yex was over 90% with 0^21 U/μg GST activity.MUC1/Yex protein can be cleaved from GST|Yex and N|terminal protein sequencing confirmed that is was consistent with the sequence published.The titer of polyserum generated was 1∶250 000 by ELISA.In conclusion,MUC1/Y full length cDNA was cloned.MUC1/Yex protein and its polyclonal antibody were obtained for further research purposes." @default.
- W2358972816 created "2016-06-24" @default.
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- W2358972816 date "2001-01-01" @default.
- W2358972816 modified "2023-09-25" @default.
- W2358972816 title "Molecular Cloning of MUC1/Y and Soluble Expression of Its Extra-cellular Fragment in E.coli" @default.
- W2358972816 hasPublicationYear "2001" @default.
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