Development of an indirect ELISA for detection of anti-

摘要

Expression and purification of the Mhp366-N protein. SDS-PAGE (a) and Western blotting (b) showing Mhp366-N in recombinant bacteria. Soluble (Lane 2, Fig. 1 a and b) and insoluble forms (Lane 3, Fig. 1 a and b) of Mhp366-N protein were expressed using IPTG induction (Lane 1, Fig. 1 a). No Mhp366-N was detected in E. coli BL21(DE3) containing the pET-28a(+) empty vector (Lane 1, Fig. 1 b). c Mhp366-N protein was purified by Ni affinity chromatography. Lane 1: loading material; Lane 2: flow through; Lane 3–5: affinity purification with a linear imidazole gradient, 0.1 M (Lane 3), 0.2 M (Lane 4), and 0.5 M (Lane 5); Lane 6–9: isolation of target protein