Fig. 1: Antibody characterization by peptide and nucleosome ELISA. | Nature Communications

Fig. 1: Antibody characterization by peptide and nucleosome ELISA.

From: Release of Histone H3K4-reading transcription factors from chromosomes in mitosis is independent of adjacent H3 phosphorylation

Fig. 1: Antibody characterization by peptide and nucleosome ELISA.The alternative text for this image may have been generated using AI.

A H3T3ph antibody B8634 binding to various H3 peptides (for no peptide n = 5; for unmodified n = 7; for T3ph and T3phK4me3 n = 8; for T3phK4me1 and T3phK4me2 n = 3; for K4me3 n = 4). B H3K4me3 antibody C42D8 binding to various H3 peptides (for no peptide, unmodified and T3phK4me2 n = 4; for K4me1 n = 5; for K4me2, K4me3, and T3phK4me3 n = 6; for T3phK4me2 n = 3). C H3T3ph antibody B8634 binding to peptide and nucleosomal substrates (n = 3). D. H3K4me3 antibody C42D8 binding to peptide and nucleosomal substrates (n = 3). E H3T3ph antibody B8634 binding to nucleosomes in the presence of sheared chromatin (n = 3). Data were normalized to the mean signal of the antibodies binding the expected target peptide or nucleosome (i.e. H3T3ph or H3K4me3). Bars represent mean ± SD; n refers to the number of independent ELISA experiments. Statistical analysis was carried out with non-normalized data using a mixed effects model with Dunnett’s adjustment for multiple comparisons (A, B), or by a repeated measures one-way ANOVA with Šídák’s adjustment for multiple comparisons (C–E), ***p < 0.0001, **p < 0.001, *p < 0.01 when compared to binding to the expected modification (H3T3ph or H3K4me3). Source data including exact p values are provided as a Source Data file.

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