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. 2014 Sep 19;46(9):e114. doi: 10.1038/emm.2014.57

Figure 1.

Figure 1

Expression and deglycosylation of the recombinant NT-proBNP-Fc fusion protein. (a) The recombinant NT-proBNP-Fc was expressed in HEK293F cells and purified by protein A column chromatography. The purified protein, bovine fetuin (O-glycosylated protein control), and an scFv-Fc protein (non O-glycosylated protein control) were treated with glycosidase and subjected to SDS-polyacrylamide gel electrophoresis and Coomassie staining along with the nontreated protein. (b) The untreated or treated recombinant NT-proBNP-Fc fusion proteins separated on the gel were transferred to a nitrocellulose membrane and probed with the NPBR9 antibody or the NPBC20 antibody, followed by an anti-human Fc antibody conjugated with horseradish peroxidase (HRP). The membrane was also probed with anti-rabbit Fc antibody conjugated with HRP to visualize the recombinant NT-proBNP-Fc fusion protein. NT-proBNP, N-terminal fragment of prohormone brain natriuretic peptide; scFv, single-chain variable fragment.