The ubiquitin-specific protease 39 (USP39) is a deubiquitinating enzyme involved in pre-mRNA splicing and cell cycle regulation. As a component of the spliceosome, USP39 plays a critical role in spliceosome assembly and catalytic activation, contributing to mRNA maturation and genomic stability. Studies have linked USP39 to the regulation of key cell cycle checkpoints, particularly through interactions with proteins like Aurora B and cyclin-dependent kinases. Dysregulation of USP39 has been implicated in various cancers, including hepatocellular carcinoma, breast cancer, and colorectal cancer, where its overexpression often correlates with tumor progression, metastasis, and poor prognosis.
USP39 antibodies are essential tools for investigating its biological functions and clinical relevance. These antibodies are widely used in techniques such as Western blotting, immunofluorescence, and immunoprecipitation to detect USP39 expression levels, subcellular localization, and protein-protein interactions. Specificity and validation are crucial, as USP39 shares structural homology with other spliceosomal components. Researchers utilize these antibodies to explore USP39's role in splicing defects, DNA damage response, and therapeutic resistance. Commercially available USP39 antibodies are typically raised against epitopes in its conserved N-terminal or C-terminal regions. Ongoing studies aim to clarify USP39's dual roles in maintaining cellular homeostasis and promoting oncogenesis, highlighting its potential as a diagnostic marker or therapeutic target in precision oncology.