The SETD2 (SET Domain Containing 2) antibody is a crucial tool for studying the epigenetic regulator SETD2. a histone methyltransferase responsible for catalyzing trimethylation of histone H3 at lysine 36 (H3K36me3). This post-translational modification is associated with active transcription, DNA repair, and chromatin stability. SETD2 is the sole enzyme generating H3K36me3 in humans, linking it to diverse cellular processes, including mRNA splicing, replication fork dynamics, and tumor suppression.
Mutations or dysregulation of SETD2 are implicated in cancers, particularly clear cell renal cell carcinoma (ccRCC), pediatric high-grade gliomas, and leukemia. Loss-of-function mutations correlate with poor prognosis, underscoring its role as a tumor suppressor. Researchers use SETD2 antibodies in techniques like Western blotting, immunofluorescence, and ChIP-seq to investigate its expression patterns, subcellular localization, and interaction with chromatin.
Validating antibody specificity is critical due to potential cross-reactivity with other methyltransferases or epitope similarities. Commercial SETD2 antibodies often target distinct regions (e.g., N-terminal, catalytic SET domain, or C-terminal regions), enabling studies of domain-specific functions or truncation variants. Proper controls, including knockout cell lines or siRNA-mediated knockdown, are essential to confirm antibody reliability. These tools continue to advance our understanding of SETD2's role in epigenetics, disease mechanisms, and potential therapeutic targeting.