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Beschreibung

"Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the 'beads on a string' structure. Histone proteins are highly post-translationally modified however Histone H3 is the most extensively modified of the five histones. Histone H3 sequence variants and variable modification states are thought to play a role in the dynamic and long term regulation of genes. Trimethylation of histone H3 on Lys9 (H3K9me3) is one of the most highly studied epigenetic marks. H3K9me3 functions in the repression of euchromatic genes, and in epigenetic control of heterochromatin assembly, most likely by acting as a recognition motif for the binding of chromatin-associated proteins, such as Swi6 or HP1alpha. The enzymes responsible for H3K9 trimethylation are SUV39H1 and SUV39H2., All ChIPAb+ antibodies are individually validated for chromatin precipitation, every lot, every time. Each ChIPAb+ antibody set includes control primers (tested every lot by qPCR) to biologically validate your IP results in a locus-specific context. The qPCR protocol and primer sequences are provided, allowing researchers to validate ChIP protocols when using our antibody in their chromatin context. Each set also includes a negative control antibody to ensure specificity of the ChIP reaction. The ChIPAb+ Trimethyl-Histone H3 (Lys9) set includes the Trimethyl-Histone H3 (Lys9) antibody, a Normal mouse IgG, and control primers which amplify a 117 bp region of ChIP Primers, ZNF554. The Trimethyl-Histone H3 (Lys9) and negative controls are supplied in a scalable ""per ChIP"" reaction size and can be used to functionally validate the precipitation of Trimethyl-Histone H3 (Lys9) -associated chromatin."