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a Alignment analysis in exon 9 of human and murine WT <t>CALR</t> revealed 87.9% identity and 97.0% similarity in the amino acid sequences. b Analysis of the alignment between the common amino acid sequence of human CALR mutants and the counterpart murine CALR mutant. The amino acid sequences of the C-terminal portions of the human CALR del52 mutant and murine CALR del19 mutant are shown. The analysis revealed an identity of only 59.6% but a similarity of 72.3%. Negatively charged amino acids are indicated in blue letters, and positively charged amino acids are indicated in red letters. Alignment analyses were performed using EMBOSS NEEDLE, an online software program ( http://emboss.bioinformatics.nl/cgi-bin/emboss/needle )
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a Alignment analysis in exon 9 of human and murine WT <t>CALR</t> revealed 87.9% identity and 97.0% similarity in the amino acid sequences. b Analysis of the alignment between the common amino acid sequence of human CALR mutants and the counterpart murine CALR mutant. The amino acid sequences of the C-terminal portions of the human CALR del52 mutant and murine CALR del19 mutant are shown. The analysis revealed an identity of only 59.6% but a similarity of 72.3%. Negatively charged amino acids are indicated in blue letters, and positively charged amino acids are indicated in red letters. Alignment analyses were performed using EMBOSS NEEDLE, an online software program ( http://emboss.bioinformatics.nl/cgi-bin/emboss/needle )
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a Alignment analysis in exon 9 of human and murine WT CALR revealed 87.9% identity and 97.0% similarity in the amino acid sequences. b Analysis of the alignment between the common amino acid sequence of human CALR mutants and the counterpart murine CALR mutant. The amino acid sequences of the C-terminal portions of the human CALR del52 mutant and murine CALR del19 mutant are shown. The analysis revealed an identity of only 59.6% but a similarity of 72.3%. Negatively charged amino acids are indicated in blue letters, and positively charged amino acids are indicated in red letters. Alignment analyses were performed using EMBOSS NEEDLE, an online software program ( http://emboss.bioinformatics.nl/cgi-bin/emboss/needle )

Journal: Blood Cancer Journal

Article Title: Mice with Calr mutations homologous to human CALR mutations only exhibit mild thrombocytosis

doi: 10.1038/s41408-019-0202-z

Figure Lengend Snippet: a Alignment analysis in exon 9 of human and murine WT CALR revealed 87.9% identity and 97.0% similarity in the amino acid sequences. b Analysis of the alignment between the common amino acid sequence of human CALR mutants and the counterpart murine CALR mutant. The amino acid sequences of the C-terminal portions of the human CALR del52 mutant and murine CALR del19 mutant are shown. The analysis revealed an identity of only 59.6% but a similarity of 72.3%. Negatively charged amino acids are indicated in blue letters, and positively charged amino acids are indicated in red letters. Alignment analyses were performed using EMBOSS NEEDLE, an online software program ( http://emboss.bioinformatics.nl/cgi-bin/emboss/needle )

Article Snippet: Murine Calr WT cDNA (MGC clone 2655918) was purchased from DNAFORM and cloned into the pMCs-IG vector.

Techniques: Sequencing, Mutagenesis, Software

a STAT5 transcription activity measured using a luciferase assay. 293T cells were transiently transfected with STAT5-LUC and the CALR WT, CALR del52 mutant, Calr WT, or Calr del19 mutant in the presence of the human thrombopoietin receptor ( MPL ) or murine Mpl . The y -axis indicates the fold induction of luciferase activity compared with WT CALR. * P < 0.05, ** P < 0.01; NS, not significant vs. WT CALR. The average values for relative luciferase activity generated in three independent experiment are shown. Data are presented as means ± SEM. A two-tailed Student’s t test was used. b Binding of human or murine CALR mutant (FLAG-tagged) to human or murine MPL (Myc-tagged) examined by immunoprecipitation and western blot analysis. Binding between the murine CALR del19 mutant and murine MPL was weakest in comparison with the other three combinations

Journal: Blood Cancer Journal

Article Title: Mice with Calr mutations homologous to human CALR mutations only exhibit mild thrombocytosis

doi: 10.1038/s41408-019-0202-z

Figure Lengend Snippet: a STAT5 transcription activity measured using a luciferase assay. 293T cells were transiently transfected with STAT5-LUC and the CALR WT, CALR del52 mutant, Calr WT, or Calr del19 mutant in the presence of the human thrombopoietin receptor ( MPL ) or murine Mpl . The y -axis indicates the fold induction of luciferase activity compared with WT CALR. * P < 0.05, ** P < 0.01; NS, not significant vs. WT CALR. The average values for relative luciferase activity generated in three independent experiment are shown. Data are presented as means ± SEM. A two-tailed Student’s t test was used. b Binding of human or murine CALR mutant (FLAG-tagged) to human or murine MPL (Myc-tagged) examined by immunoprecipitation and western blot analysis. Binding between the murine CALR del19 mutant and murine MPL was weakest in comparison with the other three combinations

Article Snippet: Murine Calr WT cDNA (MGC clone 2655918) was purchased from DNAFORM and cloned into the pMCs-IG vector.

Techniques: Activity Assay, Luciferase, Transfection, Mutagenesis, Generated, Two Tailed Test, Binding Assay, Immunoprecipitation, Western Blot, Comparison