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H3K27me3 Catalog Number H3109 Lyophilized Store At -20C Or -80C Chemically synthesized histone H3 protein, corresponding to residues within 1-135 of human histone H3, trimethylation at K27. H3K27me3 is often seen to interact with H3K4me3 in bivalent domains . These domains are usually found in embryonic stem cells and are pivotal for proper cell differentiation. H3K27me3 and H3K4me3 determine whether a cell will remain unspecified or will eventually differentiate. The Grb10

Types of histone modification Chromatin architecture, nucleosomal positioning, and ultimately access to DNA for gene transcription, is largely controlled by histone proteins. Each nucleosome is made of two identical subunits, each of which contains four histones: H2A, H2B, H3, and H4. Meanwhile, the H1 protein acts as the linker histone to stabilize internucleosomal DNA and does not form part of the nucleosome itself. Histone proteins undergo post-translational modification

H3K27me2 Catalog Number H3108 Lyophilized Store At -20C Or -80C Chemically synthesized histone H3 protein, corresponding to residues within 1-135 of human histone H3, dimethylationat K27. H3K27me2 is broadly distributed within the core histone H3 and is believed to play a protective role by inhibiting non-cell-type specific enhancers. Ultimately, this leads to the inactivation of transcription. In mouse embryonic stem cells, H3K27me2 is the dominant modification form,

H3-K27me1 Catalog Number H3107 Lyophilized Store At -20C Or -80C Chemically synthesized histone H3 protein, corresponding to residues within 1-135 of human histone H3, monomethylation at K27. H3K27me1 is linked to promotion of transcription and is seen to accumulate in transcribed genes. Histone-histone interactions play a role in this process. Regulation occurs via Setd2-dependent H3K36me3 deposition. H3K27me1 shows an inverse distribution to H3K27me3 that defines the