Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2020 Mar 19;43(6):1819–1830. doi: 10.3892/or.2020.7554

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright: © Gao et al.

This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

PMC Copyright notice

Figure 5. — Validation of proteomic results. (A) Acetylation and (B) succinylation of whole proteins in breast cancer tissues (T) and adjacent normal tissues (N) examined via western blotting. GAPDH was used as a loading control. (C) Acetylation and succinylation of proteins ~40 kDa (used for indicating NPM1) in breast cancer tissues (T) and adjacent normal tissues (N) examined via western blotting. GAPDH was used as a loading control. (D) MCF-7 cells overexpressing NPM1 (MCF-7-NPM1) and PCDNA3.0 (MCF-7-PCDNA3.0, used as control) were collected for the protein extraction. Expression level of NPM1 and its acetylation and succinylation were detected via western blotting. GAPDH was used as a loading control. (E) BT549 cells overexpressing NPM1 (BT549-NPM1), PCI2 (BT549-PCI2, used as control) and the variants of NPM1 (NPM1-K27R, lysine mutated into arginine) were collected for protein extraction. Expression level of NPM1 and its acetylation and succinylation were detected via western blotting. GAPDH was used as a loading control. (F) Viability of BT549 cells overexpressing NPM1 (NPM1), PCI2 (PCI2, used as control) and the variants of NPM1 (K27R, lysine mutated into arginine) was detected via MTT methods. *P<0.05. (G) Expression of H2A.X in breast cancer tissues (T) and adjacent normal tissues (N) were detected via western blotting. GAPDH was used as a loading control. The H2A.X and the succinylation bands from N4 to T6 shows non-adjacent bands from the same gel, therefore they used the same GAPDH result. NPM1, nucleophosmin; H2A.X, histone H2A.X.