itc buffer (NanoTemper Technologies)
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itc buffer
Itc Buffer, supplied by NanoTemper Technologies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/itc+buffer/itc+buffer/pmc06130945-557-14-33
Average 90 stars, based on 1 article reviews
Itc Buffer, supplied by NanoTemper Technologies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/itc+buffer/itc+buffer/pmc06130945-557-14-33
Average 90 stars, based on 1 article reviews
itc buffer - by Bioz Stars,
2026-10
90/100 stars
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1) Product Images from "Characterization of the binding mode of JNK-interacting protein 1 (JIP1) to kinesin-light chain 1 (KLC1)"
Article Title: Characterization of the binding mode of JNK-interacting protein 1 (JIP1) to kinesin-light chain 1 (KLC1)
Journal: The Journal of Biological Chemistry
doi: 10.1074/jbc.RA118.003916
Figure Legend Snippet: Thermodynamic parameters of the ITC experiments between various KLC1-TPR fragments and mutants and JIP1-C10 peptides
Techniques Used:
![Mechanism of JIP1-Cter binding to KLC1-TPR domain. A, isothermal titration calorimetry measurements of the reference KLC1-TPR-[A1-B6] fragment with the JIP1-C10-wt peptide. This reference measurement was performed at 25 °C in a buffer containing 25 mm Hepes, pH 7.0, and 150 mm NaCl. B, superposition of ITC curves of the reference KLC1-TPR-[A1-B6] fragment with the JIP1-C10-wt peptide at 25 °C in a buffer containing variable ionic strength (150, 250, or 500 mm NaCl). C, superposition of ITC curves showing the interaction between the reference KLC1-TPR-[A1-B6] fragment and JIP1-C10-E706A/D707A double mutant (blue), JIP1-C10-I708A/L710A double mutant (green), and JIP1-C10-Y709A mutant (red). For comparison, the reference measurement between the KLC1-TPR-[A1-B6] fragment and the JIP1-C10-wt peptide is reported (black). Sequence alignment of the different JIP1-C10 peptides used for this experiment is shown below. The solid lines drawn through the data points match the best fit to the data.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_0945/pmc06130945/pmc06130945__zbc0371892930001.jpg "... 7.0, and 150 mm NaCl. B, superposition of ITC curves of the reference KLC1-TPR-[A1-B6] fragment with the ...")
Figure Legend Snippet: Mechanism of JIP1-Cter binding to KLC1-TPR domain. A, isothermal titration calorimetry measurements of the reference KLC1-TPR-[A1-B6] fragment with the JIP1-C10-wt peptide. This reference measurement was performed at 25 °C in a buffer containing 25 mm Hepes, pH 7.0, and 150 mm NaCl. B, superposition of ITC curves of the reference KLC1-TPR-[A1-B6] fragment with the JIP1-C10-wt peptide at 25 °C in a buffer containing variable ionic strength (150, 250, or 500 mm NaCl). C, superposition of ITC curves showing the interaction between the reference KLC1-TPR-[A1-B6] fragment and JIP1-C10-E706A/D707A double mutant (blue), JIP1-C10-I708A/L710A double mutant (green), and JIP1-C10-Y709A mutant (red). For comparison, the reference measurement between the KLC1-TPR-[A1-B6] fragment and the JIP1-C10-wt peptide is reported (black). Sequence alignment of the different JIP1-C10 peptides used for this experiment is shown below. The solid lines drawn through the data points match the best fit to the data.
Techniques Used: Binding Assay, Isothermal Titration Calorimetry, Mutagenesis, Comparison, Sequencing
![Binding experiments between SH2D6 peptides and the reference KLC1-TPR-[A1-B6] fragment. A, sequence alignment of the different SH2D6 and JIP1-C10 peptides used for these binding experiments. B, superposition of ITC curves showing the interaction between the reference KLC1-TPR-[A1-B6] fragment and JIP1-C10 WT (reference measurement; black), SH2D6-[172–181] peptide (blue) and SH2D6-[170–181] peptide (green), as well as the interaction between an equivalent KLC2-TPR-[A1-B6]-wt fragment and SH2D6-[170–181] peptide (red). The solid lines drawn through the data points match the best fit to the data. C, superposition of MST curves showing the interaction between the labeled KLC1-TPR-[A1-B6] fragment and JIP1-C10 WT (reference measurement; green) and the SH2D6-[172–181] (red) peptides. The curves represent an average of three independent measurements with the S.D. shown by error bars.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_0945/pmc06130945/pmc06130945__zbc0371892930002.jpg "... used for these binding experiments. B, superposition of ITC curves showing the interaction between the reference KLC1-TPR-[A1-B6] ...")
Figure Legend Snippet: Binding experiments between SH2D6 peptides and the reference KLC1-TPR-[A1-B6] fragment. A, sequence alignment of the different SH2D6 and JIP1-C10 peptides used for these binding experiments. B, superposition of ITC curves showing the interaction between the reference KLC1-TPR-[A1-B6] fragment and JIP1-C10 WT (reference measurement; black), SH2D6-[172–181] peptide (blue) and SH2D6-[170–181] peptide (green), as well as the interaction between an equivalent KLC2-TPR-[A1-B6]-wt fragment and SH2D6-[170–181] peptide (red). The solid lines drawn through the data points match the best fit to the data. C, superposition of MST curves showing the interaction between the labeled KLC1-TPR-[A1-B6] fragment and JIP1-C10 WT (reference measurement; green) and the SH2D6-[172–181] (red) peptides. The curves represent an average of three independent measurements with the S.D. shown by error bars.
Techniques Used: Binding Assay, Sequencing, Labeling
![Minimal region of KLC1-TPR for JIP1-C10 binding. Superposition of ITC curves shows the interaction between the JIP1-C10-wt peptide and N-terminal truncated fragments (A) and C-terminal truncated fragments (B) of KLC1-TPR domain. For comparison, the reference measurement between the JIP1-C10-wt peptide and the complete KLC1-TPR-[A1-B6] fragment is reported (black). C, color-based representation of the 3D template structure of the KLC1-TPR domain (PDB code 3NF1) according to the -fold decrease in binding affinity (Kd) measured in ITC. The solid lines drawn through the data points match the best fit to the data.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_0945/pmc06130945/pmc06130945__zbc0371892930004.jpg "... region of KLC1-TPR for JIP1-C10 binding. Superposition of ITC curves shows the interaction between the JIP1-C10-wt peptide ...")
Figure Legend Snippet: Minimal region of KLC1-TPR for JIP1-C10 binding. Superposition of ITC curves shows the interaction between the JIP1-C10-wt peptide and N-terminal truncated fragments (A) and C-terminal truncated fragments (B) of KLC1-TPR domain. For comparison, the reference measurement between the JIP1-C10-wt peptide and the complete KLC1-TPR-[A1-B6] fragment is reported (black). C, color-based representation of the 3D template structure of the KLC1-TPR domain (PDB code 3NF1) according to the -fold decrease in binding affinity (Kd) measured in ITC. The solid lines drawn through the data points match the best fit to the data.
Techniques Used: Binding Assay, Comparison
![Identification of critical residues of KLC1-TPR for JIP1-C10 binding. A, KLC1-TPR residues examined by ITC for their binding to JIP1-C10-wt peptide are indicated by white spheres and labeled on the 3D template structure of the KLC1-TPR domain. The critical Asn343 position is indicated with a red star (15). KLC1-TPR is shown in a cartoon and colored according to the -fold decrease in binding affinity (Kd) measured in ITC, as shown in Fig. 4C. B and C, superposition of ITC curves showing the interaction of the JIP1-C10-wt peptide with the asparagine mutants (B) and the arginine/lysine mutants (C) of the reference KLC1-TPR-[A1-B6] fragment. For comparison, the reference measurement between the JIP1-C10-wt peptide and the complete KLC1-TPR-[A1-B6] fragment is reported (black). The solid lines drawn through the data points match the best fit to the data. D, surface representation of the 3D structure of KLC1-TPR template (PDB code 3NF1; same orientation as in A) colored in white with critical residues indicated in red and residues in close proximity indicated in pink.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_0945/pmc06130945/pmc06130945__zbc0371892930005.jpg "... for JIP1-C10 binding. A, KLC1-TPR residues examined by ITC for their binding to JIP1-C10-wt peptide are indicated ...")
Figure Legend Snippet: Identification of critical residues of KLC1-TPR for JIP1-C10 binding. A, KLC1-TPR residues examined by ITC for their binding to JIP1-C10-wt peptide are indicated by white spheres and labeled on the 3D template structure of the KLC1-TPR domain. The critical Asn343 position is indicated with a red star (15). KLC1-TPR is shown in a cartoon and colored according to the -fold decrease in binding affinity (Kd) measured in ITC, as shown in Fig. 4C. B and C, superposition of ITC curves showing the interaction of the JIP1-C10-wt peptide with the asparagine mutants (B) and the arginine/lysine mutants (C) of the reference KLC1-TPR-[A1-B6] fragment. For comparison, the reference measurement between the JIP1-C10-wt peptide and the complete KLC1-TPR-[A1-B6] fragment is reported (black). The solid lines drawn through the data points match the best fit to the data. D, surface representation of the 3D structure of KLC1-TPR template (PDB code 3NF1; same orientation as in A) colored in white with critical residues indicated in red and residues in close proximity indicated in pink.
Techniques Used: Binding Assay, Labeling, Comparison
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