UHRF1 (Ubiquitin-like with PHD and RING Finger domains 1), also known as ICBP90 or NP95. is a multifunctional epigenetic regulator critical for maintaining DNA methylation and histone modification patterns during DNA replication. It plays a pivotal role in connecting DNA methylation with histone marks, ensuring the inheritance of epigenetic information across cell divisions. Structurally, UHRF1 contains a ubiquitin-like domain, tandem Tudor domain (TTP), plant homeodomain (PHD), SET- and RING-associated (SRA) domain, and a RING finger domain, enabling interactions with DNA, histones, and chromatin-modifying enzymes. Its SRA domain recognizes hemi-methylated DNA, while the RING domain exhibits E3 ubiquitin ligase activity, targeting histone H3 for ubiquitination to recruit DNA methyltransferase DNMT1.
UHRF1 antibodies are essential tools for studying its expression, localization, and function in epigenetic regulation, cell cycle progression, and genome stability. These antibodies are widely used in techniques like Western blotting, immunohistochemistry, and immunoprecipitation. Dysregulation of UHRF1 is linked to cancer, as its overexpression is observed in various malignancies, correlating with poor prognosis, uncontrolled proliferation, and silencing of tumor suppressor genes via hypermethylation. Research on UHRF1 antibodies also supports drug discovery efforts, particularly in developing inhibitors targeting its oncogenic activity. Validating antibody specificity is crucial, as cross-reactivity with homologous proteins (e.g., UHRF2) or splice variants may lead to experimental artifacts. High-quality UHRF1 antibodies enable insights into its role in diseases and potential therapeutic applications.