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. 2008 Sep 17;82(23):11682–11694. doi: 10.1128/JVI.01562-08

FIG. 1.

FIG. 1.

TRIM5-21R expression and purification. (A) Western blot (upper, anti-FLAG) and Coomassie blue-stained SDS-PAGE gel (lower) showing the stepwise purification of recombinant TRIM5-21R proteins. Lane 1, soluble lysate from control SF-21 cells; lane 2, lysate from SF-21 cells infected with baculovirus expressing TRIM5-21R; lane 3, StrepTactin affinity-purified TRIM5-21R; lanes 4 and 5, monomeric (M, early eluting peak) and dimeric (D, late eluting peak) TRIM5-21R proteins purified by anion-exchange chromatography; lanes 6 and 7, monomeric (M, late eluting peak) and dimeric (D, early eluting peak) TRIM5-21R proteins purified by gel filtration chromatography. (B) Anion-exchange (upper) and gel filtration (lower) chromatographs showing the elution profiles of monomeric (M) and dimeric (D) TRIM5-21R proteins. Inset (upper panel) shows a Coomassie blue-stained SDS-PAGE analysis of the designated fractions. Elution positions of control molecular mass standards are shown below the gel filtration chromatograph for reference, and estimated molecular masses are given above the peaks of monomeric and dimeric TRIM5-21R.