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. 2022 Jun 17;30(4):380–388. doi: 10.4062/biomolther.2022.063

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Copyright © 2022, The Korean Society of Applied Pharmacology

This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. 1 — Physical interaction between Snail and the Baculoviral inhibitor of apoptosis protein (IAP) repeat-containing protein 3 (BIRC3). (A) Positive interactions were observed by monitoring cell growth over 3 days at 30°C on a medium lacking leucine. The values of β-galactosidase activity (unit) calculated by adding O-nitrophenyl β-D-galactopyranoside (ONPG) are indicated below the corresponding lanes. (B) Co-immunoprecipitation (Co-IP) of Snail with BIRC3. Immunoprecipitation was carried out using an anti-Flag antibody with lysates from transfected breast carcinoma cells. After immunoprecipitation, precipitated proteins were immunoblotted with anti-Snail and anti-BIRC3 antibodies: lane 1, pcDNA3.1 (vector only) and pcDNA3.1/Flag-BIRC3 transfectant; lane 2, pcDNA3.1-Snail and pcDNA3.1/Flag-BIRC3 transfectant. (C) Co-IP of endogenous BIRC3 and Snail shows the interaction between the two proteins in HEK 293T cells. β-actin was used as a loading control.