U-Blot® Histone H3 (Di Methyl Lys9,Phospho Thr6, ) Rabbit pAb

Background: Histones are basic nuclear proteins that assemble into nucleosomes, the fundamental repeating units of eukaryotic chromatin. Multiple post‑translational modifications can co‑occur on the same histone H3 N‑terminal tail, constituting combinatorial epigenetic codes. H3T6pK9me2 denotes the dual modification of phosphorylated Threonine 6 and dimethyl‑Lysine 9 on histone H3. H3K9me2 is mainly catalyzed by G9a/GLP methyltransferase complex, widely distributed across chromatin and linked to repressive transcriptional states. H3T6 phosphorylation is primarily mediated by PKC‑family kinases and accumulates upon mitotic entry. This combinatorial mark emerges when T6 phosphorylation takes place on pre‑existing H3K9me2‑modified histones during mitosis. In interphase, H3K9me2 contributes to facultative heterochromatin formation and transcriptional silencing. At the onset of M‑phase, phosphorylation at T6 occurs on H3K9me2‑bearing histones, altering the binding interface for chromatin‑reader proteins. This modification participates in mitotic chromatin compaction and chromosome structural reorganization, while preserving H3K9me2 epigenetic information. After mitosis, T6 phosphorylation is erased, allowing re‑establishment of H3K9me2‑dependent repressive chromatin states in daughter cells. Dysregulation of H3T6pK9me2 disturbs mitotic chromatin dynamics and epigenetic inheritance, and is associated with genomic instability.