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. 2015 Dec 1;34(6):404–417. doi: 10.1089/mab.2015.0036

FIG. 4.

FIG. 4.

(A) 12% SDS-PAGE analysis of humanized scFv expression from periplasmic extract. Lanes 1 and 2, periplasmic expression of h2H10scFv-C and h5E11scFv-C, respectively; lanes 3 and 4, periplasmic expression of h2H10scFv and h5E11scFv, respectively. (B) Effects of condition optimization on hscFv-C expression. Lanes 1 and 2, periplasmic expression of h2H10scFv-C and h5E11scFv-C, respectively; lanes 3–5, periplasmic expression of h2H10scFv-C from E. coli cultured with 0.4M sucrose, 1% Triton X-100, and 2% glycine, respectively; lanes 6–8, periplasmic expression of h5E11scFv-C from E. coli cultured with 0.4 M sucrose, 2% glycine, and 1% Triton X-100, respectively; lanes 9 and 10, purified h2H10scFv-C and h5E11scFv-C, respectively; lane M, protein molecular weight marker. Band for scFv is indicated by arrow, with expected molecular mass of 29 kDa.