Histone H3 (tri methyl K27) Recombinant Rabbit mAb (S-4098)

Histone H3 lysine 27 trimethylation (abbreviated as H3K27me3) is a classic transcription-repressive epigenetic mark, catalyzed by the core catalytic subunits EZH1 or EZH2 of Polycomb Repressive Complex 2 (PRC2). This modification serves as the central executor of PRC2-mediated gene silencing. Its primary function is to recruit and stabilize effector proteins, such as the PRC1 complex, collectively promoting the formation of compact, higher-order chromatin structures to stably and long-term suppress the expression of specific genes at the epigenetic level. H3K27me3 plays a crucial role in development, extensively participating in key biological processes including cell fate determination, maintenance of stem cell pluripotency, somatic cell reprogramming, and X-chromosome inactivation. By precisely establishing and maintaining a "gene expression blueprint," it ensures the correct identity of cells. However, when this powerful silencing function becomes dysregulated, it can lead to severe consequences. For instance, gain-of-function mutations or aberrant expression of genes encoding PRC2 components (such as EZH2) result in disrupted H3K27me3 levels, a phenomenon widely observed in various malignancies including lymphoma, prostate cancer, sarcoma, and glioma, making it a key driver of tumorigenesis. Notably, its function is often antagonistic to the activating mark H3K4me3, and together they can form "bivalent chromatin domains," which co-mark key developmental regulator genes in embryonic stem cells that are poised for activation upon differentiation. Therefore, H3K27me3 is not only a central molecule in developmental biology and disease research but has also become an important target for the development of current epigenetic drugs, such as EZH2 inhibitors.