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. Author manuscript; available in PMC: 2023 Jun 22.
Published in final edited form as: Bioconjug Chem. 2019 Dec 16;31(1):104–112. doi: 10.1021/acs.bioconjchem.9b00781

Figure 1.

Figure 1.

(A) SDS-PAGE of purified affibody-enzyme fusion proteins: (left to right) ladder, N23BP-CodA, WT-CodA, and free CodA. The molecular weights of the ladder proteins are (top to bottom): 200, 150, 100, 75, 50, and 37 kDa. (B) SDS-PAGE of affibody-enzyme fusion proteins photocrosslinked with the soluble extracellular fragment (ECF) of EGFR. Only the combination of N23BP-CodA and UV leads to the formation of a new band (red arrow). The affibody bands and the free EGFR ECF bands are shown in green and blue arrows, respectively. Left to right: Ladder, (+) N23BP-CodA (+) EGFR (−) UV, (+) N23BP-CodA (+) EGFR (+) UV, (−) affibody (+) EGFR (+) UV, (+) WT-CodA (+) EGFR (−) UV, and (+) WT-CodA (+) EGFR (+) UV. Ladder molecular weights are same as for (A).