tom1 ha Search Results


tom1 ha  (Proteintech)
90
Proteintech tom1 ha
MST analysis of the binding interactions between Dbf4 H‐BRCT and Cy5‐labeled phospho (filled circles) and non‐phospho‐peptides (empty circles) from Cbf1, and Cy5‐labeled phospho (filled circles) peptides from <t>Tom1.</t> No measurements were made using Cy5‐labeled non‐phospho‐peptides from Tom1. K D represents the equilibrium dissociation constant. The K D for interactions with the non‐phospho‐peptides could not be determined (n.d.). ΔFnorm [0/00] represents the change in fluorescence during thermophoresis normalized to the initial fluorescence. Data are represented as the mean ± SEM from at least three independent measurements.
Tom1 Ha, supplied by Proteintech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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tom1 ha - by Bioz Stars, 2026-02
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MST analysis of the binding interactions between Dbf4 H‐BRCT and Cy5‐labeled phospho (filled circles) and non‐phospho‐peptides (empty circles) from Cbf1, and Cy5‐labeled phospho (filled circles) peptides from Tom1. No measurements were made using Cy5‐labeled non‐phospho‐peptides from Tom1. K D represents the equilibrium dissociation constant. The K D for interactions with the non‐phospho‐peptides could not be determined (n.d.). ΔFnorm [0/00] represents the change in fluorescence during thermophoresis normalized to the initial fluorescence. Data are represented as the mean ± SEM from at least three independent measurements.

Journal: The EMBO Journal

Article Title: The Sir4 H‐ BRCT domain interacts with phospho‐proteins to sequester and repress yeast heterochromatin

doi: 10.15252/embj.2019101744

Figure Lengend Snippet: MST analysis of the binding interactions between Dbf4 H‐BRCT and Cy5‐labeled phospho (filled circles) and non‐phospho‐peptides (empty circles) from Cbf1, and Cy5‐labeled phospho (filled circles) peptides from Tom1. No measurements were made using Cy5‐labeled non‐phospho‐peptides from Tom1. K D represents the equilibrium dissociation constant. The K D for interactions with the non‐phospho‐peptides could not be determined (n.d.). ΔFnorm [0/00] represents the change in fluorescence during thermophoresis normalized to the initial fluorescence. Data are represented as the mean ± SEM from at least three independent measurements.

Article Snippet: Interacting factors were immunoprecipitated from whole cell extracts using Myc‐Trap magnetic beads (ChromoTek), and the co‐precipitation of Tom1‐HA was monitored with an anti‐HA antibody (Fig D).

Techniques: Binding Assay, Labeling, Fluorescence

Binding motifs of phospho‐peptides

Journal: The EMBO Journal

Article Title: The Sir4 H‐ BRCT domain interacts with phospho‐proteins to sequester and repress yeast heterochromatin

doi: 10.15252/embj.2019101744

Figure Lengend Snippet: Binding motifs of phospho‐peptides

Article Snippet: Interacting factors were immunoprecipitated from whole cell extracts using Myc‐Trap magnetic beads (ChromoTek), and the co‐precipitation of Tom1‐HA was monitored with an anti‐HA antibody (Fig D).

Techniques: Binding Assay