Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2019 Oct 2;9:14159. doi: 10.1038/s41598-019-50335-5

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Characterization of binding, depletion and competition properties of the new kinobeads mix. (a) Distribution of depletion factors for all identified kinases from an experiment using a lysate mix consisting of K562, HEK293 and human placenta shows that majority of kinases are only weakly depleted. (depletion factor F = 1 + [B]/K_dB, with [B] indicating the bead ligand concentration and K_dB being the respective dissociation constant). (b) Scatterplot displaying residual binding of all identified kinases on the beads when 50 µM free compound mix was present versus the depletion factor for kinases. Target proteins should ideally be in the left corner. Kinases in the right corner (red circle), which are neither depleted nor competed, bound unspecifically to the matrix. (c) Same plot as in b but for all non-kinase proteins. Square indicates non-kinase proteins with less than 25% residual binding at 50 µM free compound mix. (d) Compounds used for the lipid kinobeads. (e) Heatmap displaying residual binding for all kinases captured with the lipid kinobeads (n = 2, see also Supplementary Table 4).