Soluble Expression and Characterization of Biologically Active Bacillus anthracis Protective Antigen in Escherichia coli

Figure 5

SDS-PAGE analysis of purified protein from soluble and denatured fractions of all the seven clones. 5 μL of each fraction was mixed with 5 μL 2x SDS sample lysis buffer and was loaded onto the gel and electrophoresed. M, protein molecular weight marker; lanes 1, 3, 4, 6, 8, 10, and 12, purified soluble PA protein from pQE30-M15, pQE30-XL-1 blue, pPROEXHTa-DH5α, pPROEXHTa-BL21-DE3, pPROEXHTa-DE3-pLysS, pET32c-BL21-DE3, and pET32c-DE3-pLysS, respectively; lanes 2, 5, 7, 9, 11, and 13, purified denatured PA protein from pQE30-M15, pQE30-XL-1 blue, pPROEXHTa-DH5α, pPROEXHTa-BL21-DE3, pPROEXHTa-DE3-pLysS, pET32c-BL21-DE3, and pET32c-DE3-pLysS, respectively.