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. 2010 Nov 5;77(2):395–399. doi: 10.1128/AEM.01714-10

FIG. 1.

FIG. 1.

Cloning, overexpression, and purification of HetR from E. coli. (A) Overexpression of HetR protein in E. coli BL21(DE3)/pLysS/pET29ahetR. Various lanes of a 12% SDS-PAGE electrophoretogram stained with CBB depict an SDS-7 protein molecular mass marker (Sigma Chemical Co., United Kingdom) (lane M) and time-dependent induction of the 31-kDa recombinant HetR-His6 protein by 1 mM IPTG up to 4 h (lanes 2 to 6). (B) Western blotting and immunodetection of IPTG-induced recombinant HetR-His6 protein by anti-His antibody at the time points shown in panel A. (C) CBB-stained SDS-polyacrylamide gel showing the purified recombinant HetR protein. (D) Western blot and immunodetection of HetR protein after 30 min IPTG induction in cell extracts of E. coli BL21(pET29ahetR), using the anti-AnHetR antibody.