Fig. 2.

Expression and purification analysis. Escherichia coli BL21(DE3) was transformed with the pET32a-scFv3G1 construct. After induction, cytoplasmic proteins were extracted following sonication. Cytoplasmic fraction was purified by immobilized metal affinity chromatography. Bacterial cytoplasmic extract and purified recombinant scFv3G1 antibody were subjected to 15% SDS-PAGE, stained with Coomassie brilliant blue (a) or transferred to PVDF membrane for Western blot analysis using anti-His-Tag antibody (b). c Western blot analysis of immunoreactivity of scFv3G1. HTNV GP or unrelated HTNV NP was transferred to PVDF membrane, incubated with scFv3G1, and followed by incubation with HRP-conjugated anti-His-Tag antibody. Molecular weight markers are given in kilodaltons indicated on the left