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. 2021 Mar 25;21:321. doi: 10.1186/s12885-021-08056-4

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© The Author(s) 2021

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 1 — Prokaryotic expression of recombinant proteins. (a) The sequences of the anti-p21Ras scFv, RGD4C-scFv, RGD4C-linker-scFv, and RGD4C-EGFP were separately ligated into the pET28a (+) vector to construct recombinant expression plasmids. (b) The insertion sequences were detected by polymerase chain reaction (PCR) analysis in E. coli BL21 (DE3). (*): unoptimized coding sequence. (c) SDS-PAGE analysis showed that the molecular weight of the anti-p21Ras scFv was 34 kDa, that of RGD4C-scFv was 35 kDa, that of RGD4C-linker-scFv was 36 kDa, and that of RGD4C-EGFP was 34 kDa. Codon optimization did not change the molecular weights of the expression products