FigureĀ 1.
Runx1R188Q/+ mice express similar levels of Runx1R188 and Runx1Q188 in hematopoietic cells. (A) Schematic representation of RUNX1 protein indicating human (hs) and mouse (mm) amino acids and the R188Q mutation. The RUNT homology domain (RHD), nuclear localization signal (NLS), transactivation domain (TAD), and the inhibitory domain (ID) are shown. (B.) Sanger sequencing of region surrounding the edited site in exon 4 from WT and Runx1R188Q/+ tail DNA, and respective amino acid sequences. (C) Quantification of Runx1R188 (blue) and Runx1Q188 (red) transcript isoform levels (relative ratio) from Runx1R188Q/+ BM cells as estimated by Illumina sequencing. (D) Quantification of Runx1 protein levels in lysates from Runx1R188Q/+ BM cells, as estimated by western blot densitometric analysis. (E) Spectra analysis (left) and quantification (right) of Runx1 protein isoform levels from Runx1R188Q/+ BM cells, as estimated by Bead Assisted Mass Spectrometry (BAMS). ns, not significant.

Runx1R188Q/+ mice express similar levels of Runx1R188 and Runx1Q188 in hematopoietic cells. (A) Schematic representation of RUNX1 protein indicating human (hs) and mouse (mm) amino acids and the R188Q mutation. The RUNT homology domain (RHD), nuclear localization signal (NLS), transactivation domain (TAD), and the inhibitory domain (ID) are shown. (B.) Sanger sequencing of region surrounding the edited site in exon 4 from WT and Runx1R188Q/+ tail DNA, and respective amino acid sequences. (C) Quantification of Runx1R188 (blue) and Runx1Q188 (red) transcript isoform levels (relative ratio) from Runx1R188Q/+ BM cells as estimated by Illumina sequencing. (D) Quantification of Runx1 protein levels in lysates from Runx1R188Q/+ BM cells, as estimated by western blot densitometric analysis. (E) Spectra analysis (left) and quantification (right) of Runx1 protein isoform levels from Runx1R188Q/+ BM cells, as estimated by Bead Assisted Mass Spectrometry (BAMS). ns, not significant.

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