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- W2388097315 abstract "Objective To express the C-terminal fragment of human mannan-binding lectin(MBL)associated serine proteases-1 and 2(MASP1,2)in E.coli.Methods The target sequence in pGEM-MASP1 and pGEM-MASP2 plasmid containing human MASP1 and MASP2 cDNA were amplified by PCR,and then inserted into prokaryotic expression vector pET17b.After identification by restriction mapping and sequencing,the recombinant expression vectors were transformed into E.coli BL21(DE3)cells.The expressed products were purified by Ni2+-NTA Immobilized Metal Affinity Chromatography(IMAC)and identified by SDS-PAGE and Western blot assay;the binding-activity of the protein to HRP-His antibody were analyzed by an indirect enzyme-linked immunosorbent assay(ELISA).Results The DNA fragment of about 1 300 bp,encoding the C-terminal region of human MASP1 and MASP2,was amplified from pGEM-MASP1 and pGEM-MASP2 plasmid and the recombinant expression vectors,pGEX4T-MASP1-C and pGEX4T-MASP2-C,were constructed,whose restriction maps and sequence were consistent with those expected.The component of Mr 40 000 in the purified recombinant products was found by SDS-PAGE and could be recognized by anti-His antibody in Western blot assay.The purified recombinant products could react with anti-His antibody in the indirect ELISA.Conclusion The recombinant human MASP1-C(rhMASP1-C)and rhMASP2-C proteins and their expressing strains were successfully obtained,which provides the basis for further research of MASPs molecules." @default.
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- W2388097315 date "2007-01-01" @default.
- W2388097315 modified "2023-09-23" @default.
- W2388097315 title "Prokaryotic expression of the C terminal fragment of mannan-binding lectin-associated serine protease-1 and-2" @default.
- W2388097315 hasPublicationYear "2007" @default.
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