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. 2021 Aug 20;11(8):1506. doi: 10.3390/diagnostics11081506

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© 2021 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Characterization of the RBD protein. The RBD protein was expressed in HEK 293 cell cultures and purified on a HisTrap™ Nickel column; two fractions were obtained. (A) Native SEC analysis evinced that Fraction 1 (RBD F1; black line) was mainly composed of a ~100 kDa protein and Fraction 2 (RBD F2; blue line) by a ~30 kDa protein, which may correspond to the trimer and monomer of the RBD protein, respectively. (B) Fraction 2 also exhibits the main band at ~30 kDa when analyzed in denaturing SDS-PAGE using two reducing agents (BME and DTT). Fraction 2 was used for the rest of the work.