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Figure 1.

$(A) SDS–PAGE analysis of INTS3FL protein eluted from glutathione resin digested with PreScission protease. M, marker; 1–7, fractions collected. (B) Chromatographic profile of the recombinant INTS3FL protein eluted from a Sephacryl S-300 HR column. Peaks are indicated. (C) SDS–PAGE analysis of the gel filtration-eluted INTS3FL fractions. P1, peak 1; P2, peak 2. (D) Western blot analysis of the purified proteins (shown in C) using an anti-INTS3 antibody. (E) Silver staining of INTS3FL fractions from the sucrose gradient centrifugation. Thirty microliter for each fractions (1–28) was loaded per lane. The positions of standards are indicated at the top. (F) CD spectrum of INTS3FL protein.$

Purification of full-length INTS3 protein.

(A) SDS–PAGE analysis of INTS3^FL protein eluted from glutathione resin digested with PreScission protease. M, marker; 1–7, fractions collected. (B) Chromatographic profile of the recombinant INTS3^FL protein eluted from a Sephacryl S-300 HR column. Peaks are indicated. (C) SDS–PAGE analysis of the gel filtration-eluted INTS3^FL fractions. P1, peak 1; P2, peak 2. (D) Western blot analysis of the purified proteins (shown in C) using an anti-INTS3 antibody. (E) Silver staining of INTS3^FL fractions from the sucrose gradient centrifugation. Thirty microliter for each fractions (1–28) was loaded per lane. The positions of standards are indicated at the top. (F) CD spectrum of INTS3^FL protein.

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