SETDB1 (SET domain bifurcated 1), also known as ESET or KMT1E, is a histone methyltransferase that catalyzes the addition of methyl groups to lysine 9 of histone H3 (H3K9), primarily generating H3K9me3 marks. This enzyme plays a critical role in epigenetic regulation, heterochromatin formation, gene silencing, and maintaining genomic stability. SETDB1 functions as part of multi-protein complexes, interacting with cofactors like ATF7IP (hAM), to mediate transcriptional repression of retrotransposons, endogenous retroviruses, and specific gene promoters. Its activity is essential for embryonic development, X-chromosome inactivation, and neuronal differentiation. Dysregulation of SETDB1 has been implicated in cancers, neurodegenerative disorders, and autoimmune diseases, making it a focus of therapeutic research.
SETDB1 antibodies are essential tools for studying its expression, localization, and molecular interactions. These antibodies are widely used in techniques such as chromatin immunoprecipitation (ChIP-seq), western blotting (WB), immunohistochemistry (IHC), and immunofluorescence (IF). Validated antibodies specifically recognize SETDB1’s unique domains, including its Tudor domain or methyltransferase region. Researchers employ them to investigate SETDB1’s role in gene silencing, viral restriction, and chromatin remodeling. Commercial SETDB1 antibodies are typically raised in rabbits or mice, with validation via knockout cell lines or siRNA knockdown to confirm specificity. Proper antibody selection is crucial for distinguishing SETDB1 from related H3K9 methyltransferases like SUV39H1 or G9a.