PRMT7 (Protein Arginine Methyltransferase 7) is a member of the PRMT enzyme family responsible for post-translational arginine methylation, a key epigenetic modification regulating gene expression, DNA repair, and cellular signaling. Unlike other PRMTs, PRMT7 primarily catalyzes monomethylation of arginine residues and exhibits unique structural features, including a duplicated methyltransferase domain, which may contribute to its substrate specificity. It plays critical roles in diverse biological processes, such as chromatin remodeling, stem cell differentiation, and stress response. Dysregulation of PRMT7 has been linked to developmental disorders, cancer progression, and metabolic diseases.
PRMT7 antibodies are essential tools for studying its expression, localization, and function in cellular and disease contexts. These antibodies are commonly used in techniques like Western blotting, immunofluorescence, and immunoprecipitation to investigate PRMT7's interaction partners and methylation targets. Due to structural similarities among PRMT family members, high-quality PRMT7 antibodies must be rigorously validated for specificity to avoid cross-reactivity. Recent studies employing PRMT7 antibodies have highlighted its role in modulating splicing factors, maintaining genomic stability, and influencing immune responses. Challenges in antibody development include its low cellular abundance and tissue-specific expression patterns. Reliable PRMT7 antibodies continue to advance research into its therapeutic potential and mechanistic contributions to human pathologies.