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H3K27me2 Catalog Number H3108 Lyophilized Store At -20°C Or -80°C
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, reaching 70%, while H3K27me1 and H3K27me3 only occupy 7 and 4% of the total H3, respectively .
H3K27me3 is mainly enriched within the promoters of silenced genes; conversely, H3K27me1 and H3K27ac accumulate on transcriptionally active genes. PHF20L1 is a histone methylation reader protein, which recognizes H3K27me2 and collaborates with PRC2 and the NuRD complex in regulating H3K27 modifications to suppress a series of tumor suppressors, ultimately promoting the Warburg effect and breast tumorigenesis.
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H3K27me2 Catalog Number H3108 Lyophilized Store At -20°C Or -80°C
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, reaching 70%, while H3K27me1 and H3K27me3 only occupy 7 and 4% of the total H3, respectively .
H3K27me3 is mainly enriched within the promoters of silenced genes; conversely, H3K27me1 and H3K27ac accumulate on transcriptionally active genes. PHF20L1 is a histone methylation reader protein, which recognizes H3K27me2 and collaborates with PRC2 and the NuRD complex in regulating H3K27 modifications to suppress a series of tumor suppressors, ultimately promoting the Warburg effect and breast tumorigenesis.