Phospho-Histone H2B (Thr129) antibody is a specialized tool used to study histone modifications linked to chromatin dynamics and cellular stress responses. Histone H2B, a core component of nucleosomes, undergoes post-translational modifications such as phosphorylation, which regulate DNA accessibility and genome stability. Phosphorylation at threonine 129 (T129) in H2B is associated with DNA damage response pathways, particularly in lower eukaryotes like yeast, where it is triggered by genotoxic stress (e.g., UV radiation, chemicals) and mediated by checkpoint kinases such as Rad3/Mec1. This modification facilitates chromatin remodeling, promoting repair mechanisms or apoptosis.
In mammals, H2B-T129 phosphorylation is less characterized but has been implicated in mitosis and meiotic processes. Studies suggest roles in chromosome condensation, segregation, and transcriptional regulation. The antibody detects this specific phosphorylation event, enabling researchers to investigate its spatial and temporal dynamics via techniques like Western blotting, immunofluorescence, or immunohistochemistry. It is particularly valuable in cancer research, neurodegeneration studies, and toxicology to assess DNA damage, cell cycle arrest, or aberrant chromatin signaling.
Validation of antibody specificity is critical, as cross-reactivity with other phospho-epitopes or histone variants may occur. Overall, Phospho-Histone H2B (T129) antibody serves as a key reagent for exploring epigenetic regulation and stress adaptation mechanisms.