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. 2017 Jul 27;16(4):3917–3921. doi: 10.3892/mmr.2017.7102

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Copyright: © Tomiyama 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.

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Figure 2. — Asparagine at position 417 of human vimentin is critical for V9 mAb recognition of vimentin. (A and B) Whole cell extracts from MIA PaCa-2 (human pancreatic cancer cell line) and mouse NIH3T3 and L fibroblast cell lines were analyzed for vimentin expression by Western blotting with the indicated antibodies. β-actin was used as a loading control. (C) Amino acid sequence alignment of the C-terminal region of vimentin (residues 392–466) from different species. The red box shows the only amino acid difference between the sequence of mouse vimentin and that of human, hamster, rat, and pig. Multiple sequence alignment was performed using Clustal Omega software. (D) Western blot analysis of bacterially expressed GST-tagged wild-type and mutant (N417T) human full-length vimentin with the indicated antibodies.