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. 2024 Sep 14;25(18):9919. doi: 10.3390/ijms25189919

Figure 2.

Figure 2

Purified sACE2-Fc proteins. The Coomassie blue-stained SDS-PAGE gel image is presented for the purified sACE2-Fc proteins. The sACE2-Fc proteins are attached to Fc for expression and purification (see Section 3 Methods). The minor bands in the 200 kDa region are likely the dimer of sACE2-Fc fusion that remains in the sample due to incomplete reduction of the disulfide bond-linked original sACE2-Fc dimer. All bands in the SDS-PAGE gel contain Fc because the samples were purified by the protein A affinity chromatography, and the sizes of the bands indicate that they are sACE2-Fc fusion proteins. The SDS-PAGE gel is shown here to verify the purity of the samples. The spike protein binding activity of the samples was verified in the molecular and cellular assays (see the Section 2.4 and Section 2.5). Lane 1 represents the wild-type protein, and lanes 2–10 are for the mutant sACE2-Fc proteins (M1–M9) in Table 1. Positions for the molecular weight markers are indicated.