The Histone H3 symmetric dimethylarginine at residue 17 (H3R17me2s) antibody is a critical tool for studying post-translational modifications (PTMs) associated with epigenetic regulation. Histone H3 is a core component of nucleosomes, and arginine methylation at specific residues, such as R17. plays a role in modulating chromatin structure and gene expression. Symmetric dimethylation of H3R17 is catalyzed by protein arginine methyltransferases (PRMTs), particularly PRMT5. which transfers methyl groups to arginine residues in a symmetrical configuration. This modification is linked to transcriptional regulation, DNA repair, and cellular differentiation.
H3R17me2s is implicated in both gene activation and repression, depending on the genomic context and interacting proteins. It has been associated with maintaining heterochromatin stability and recruiting effector proteins that mediate downstream signaling. Dysregulation of H3R17 methylation is observed in cancers, developmental disorders, and other diseases, making this modification a potential therapeutic target.
The H3R17me2s antibody enables researchers to detect and quantify this PTM using techniques like chromatin immunoprecipitation (ChIP), immunofluorescence, and Western blotting. Specificity validation is crucial, often involving knockout cells or peptide competition assays to ensure the antibody does not cross-react with similar epitopes (e.g., asymmetric dimethylarginine or other methylated histone residues). Its application advances studies in epigenetics, cancer biology, and stem cell research, providing insights into how arginine methylation fine-tunes cellular processes.