What is x h3

Antibody Type:. Published Applications The following applications have been published using this antibody. Immunogen This H3. Sodium azide is highly toxic. Background Histones H3. Storage Some products may be shipped at room temperature. Guarantee This product is guaranteed for 12 months from date of receipt. Epigenetic News Sign up for our monthly newsletter highlighting recent publications in the field of epigenetics. Curated 1 Publication Manual assertion based on experiment in i Ref.

ModBase i Search The information is filed in different subsections. Length: Mass Da : 16, It is useful for tracking sequence updates. The algorithm is described in the ISO standard. Full view. These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary citable accession number'.

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Do not show this banner again. Recommended name: Histone H3. Alternative name s : Histone H3. Homo sapiens Human. This is known as the 'taxonomic identifier' or 'taxid'.

It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first. Human Gene Nomenclature Database More HGNC i. Open Targets More Here, we show that DUX4 induces the expression of the histone variants H3. X and H3. We have used a myoblast cell line with doxycycline-inducible DUX4 to show that these histone variants are incorporated throughout the body of DUX4-induced genes.

X had a C score of 0. Y had a C score of 1. In both cases, the second-best model had a considerably lower C score. In this case, histones were chemically modified beforehand by treatment with propionic anhydride Merck to convert free amino groups of lysine residues to propionic amides. The resulting data were analyzed via the Mascot Software Matrix Science using a home-made database that contains the diverse H3 sequences.

Fragment spectra were also interpreted manually. Y or H3. The following double-stranded siRNAs, which had differences of at least three nucleotides from other targets, were used. Cells were seeded in E plates 1 d after the second siRNA transfection. Cell growth was monitored over the next 4 d. To eliminate side effects caused by the lack of nutrients or the accumulation of waste products, growth medium was exchanged every day. RNA amplification, labeling, and hybridization to Human Gene 1.

Genes that had a log2 expression value of at least 4 in at least one of the treatment conditions were kept for downstream analyses. Differential expression estimation was based on a moderated t statistic limma package with subsequent calculation of the local false discovery rate lfdr; locfdr package.

Genes were classified as responders by an lfdr cutoff of 0. S1 shows H3. Y alignments, evolutionary origin, and expression level determination. S2 shows analysis of H3. X- and H3. S3 shows evaluation of human H3. X sequences and inducible endogenous H3. S4 shows purification and mass spectrometrical identification of endogenous H3. Y protein. S5 shows H3. Table S1 shows a GO list with shared up-regulated genes after H3. Y knockdown. Table S2 shows a GO list with shared down-regulated genes after H3.

This work was supported by the Deutsche Forschungsgemeinschaft part of the Sonderforschungsbereich Chromatin Transregio 5 to S. Hake, H. Leonhardt, L. Schermelleh, and E. Hake and H. A Amino acid sequence alignment of human histone variants H3. Identical amino acids are highlighted in dark gray, similar amino acids are highlighted in light gray, and changes are set apart on a white background. The black bar indicates the peptide sequence used for antibody generation.

Black stars mark known PTM sites in H3. The gray star indicates an H3. Amino acid numbers are indicated on top. Y and to a lesser extent H3. Primer pair H3. Y nucleotide sequences, whereas another primer pair is H3. X specific H3. X, light gray. Controls generated without reverse transcription were used to assess amplification threshold. Error bars represent SEM of two independent biological experiments.

C Expression of H3. Y mRNA in normal and malignant human tissues. Commercially available total RNA from human tissues was analyzed for H3.

X expression in qPCR experiments and compared with results obtained with controls generated without reverse transcription. The number of samples that were positive for H3. Subcellular localization of HA-H3. Y histone proteins. X, and -H3. Y proteins. Overlay is shown on the right merge. All HA-H3 variants are incorporated into chromosomes.

Structure and stability of H3. Y-containing nucleosomes. A In silico homology model of H3. X purple, left and H3. Y light blue, right protein structures in overlay with the crystal structure of H3. B Crystal structure of nucleosome with H3. Y light blue, right , respectively. Y shows incorporation of novel H3 variants into nucleosomes.

Bioanalyzer evaluation of purified DNA after IP of MNase-treated chromatin unbound and bound material shows digestion of chromatin to mononucleosomes and their successful precipitation left; see also Fig. S2 A for DNA size and quality. Notice that endogenous H3 is coimmunoprecipitated with all H3 variants analyzed. D FRAP experiments to evaluate nucleosomal stability of novel H3 variants using spinning disk confocal microscopy. Y constructs. A small nuclear area was photobleached box and the recovery of the fluorescent signal was monitored over 1 min and up to 8 h see Fig.

Mean curves of 10—20 individual cells are shown. All GFP-H3 variants show almost no recovery within the first 60 s after bleaching, which indicates that all expressed fusion protein was stably incorporated into nucleosomes. Detection of endogenous H3.

A A monoclonal antibody against H3. Y aa 9—20, see also black line in Fig. Immunoblots of acid-extracted histones from HeLa cells stably transfected with empty vector, or vectors containing HA-H3. Y were used 1 and 2. Y, but not in lanes containing general HA-H3 variants, which demonstrates the specificity of the antibody toward the novel variants in immunoblotting. Note that all bands run slower, as expected, because of the HA tag. X runs even slower than all other HA-H3 variants because of its extended C-terminal tail.

X served as positive control, and histones from mouse NIH3T3 cells served as a negative control. A faint signal in the lane containing U2OS histones can be seen.

B, bottom The identical membrane was stained with Ponceau S solution before antibody incubation to control for protein loading. Dotted lines indicate that intervening lanes have been spliced out. Confocal midsections are shown. The boxed inlet shows enlargement of one chromosome. Depicted are cells expressing low left and high right levels of H3. The number of cells expressing H3.

Y is increased by nutritional and proliferative stress. Error bars represent SEM of three independent biological experiments. B qPCR analysis of H3. From the same plates described in Fig. A clear increase in H3. C Immunoblot analysis of H3. Y proteins isolated from U2OS cells grown under different conditions. A clear increase in a kD signal can be seen in U2OS cells grown under different stress conditions.

Recombinant H3. Staining of the same membrane with Ponceau S solution before antibody incubation was performed to ensure similar loading bottom. One representative blot from three independent biological experiments is shown. Purification and identification of endogenous H3. Y variant protein. Acid-extracted histones from starved and overgrown U2OS cells Fig. The two anti-H3. C List of H3-, H3. Amino acids highlighted in bold are specific for H3.

Y; a bold and underlined amino acid is found only in H3. Influence of H3. Y expression on global gene regulation and cell growth. A Specificity determination of siRNAs against novel variants. B qPCR analysis to verify efficient H3. Y RNAi knockdown before global transcriptome analysis. Y nucleotide sequences, whereas two other primer pairs are H3.

X- light gray or H3. Y-specific white. Controls generated without reverse transcriptase were used to assess amplification threshold.

C Venn diagrams of genes deregulated after H3. Y yellow RNAi in SO-treated U2OS cells, as identified by microarray analyses of two independent experiments when compared with luciferase control knockdown. Digits indicate numbers of genes significantly up- left or down-regulated right in comparison to luciferase control knockdown. D Simplified GO analysis of overlapping genes after H3. Y siRNA. Arrows mark changes of growth medium. The boxed section from A is shown. One out of three representative stainings is shown.