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. 2017 Aug 4;24(8):e00153-17. doi: 10.1128/CVI.00153-17

FIG 1.

FIG 1

(A) SDS-PAGE profile of the expressed rmu3ABC protein. Lane M, prestained protein ladder (Thermo Scientific, USA); lane 1, uninduced E. coli cell extract; lane 2, soluble protein fraction; lane 3, insoluble protein fraction. (B) SDS-PAGE profile of the expressed r2C protein. Lane M, prestained protein ladder; lane 1, soluble protein fraction; lane 2, insoluble protein fraction; lane 3, uninduced E. coli cell extract. (C) SDS-PAGE profile of the purified rmu3ABC protein determined using nickel affinity chromatography. Lane M, prestained protein ladder; lane 1, the proteins after washes with IB washing buffer; lane 2, unbound protein; lanes 3 and 4, the eluted purified protein. (D) SDS-PAGE profile showing the r2C protein affinity purified using Ni-NTA resin. Lane M, prestained protein ladder; lanes 1 and 2, the eluted purified 2C protein. (E) Western blots showing the reactivity of rmu3ABC and r2C proteins with sera from FMDV-infected animals. Lane M, prestained protein ladder; lane 1, affinity-purified rmu3ABC protein; lane 2, affinity-purified r2C protein.