Recombinant Human USP52 Protein (Baculovirus)，His & GST

USP52, a member of the ubiquitin-specific protease family, plays a crucial role in regulating protein degradation and cellular homeostasis by deubiquitinating target proteins. The dysregulation of deubiquitinases like USP52 has been implicated in various diseases, including cancer, neurodegenerative disorders, and immune dysfunctions. Research has shown that USP52 can influence critical cellular processes such as signal transduction, cell cycle progression, and apoptosis, making it a potential therapeutic target. Additionally, studies indicate that USP52 interacts with key signaling pathways, including the PI3K/Akt and NF-κB pathways, further emphasizing its importance in modulating cellular responses to stress and inflammation. Given its pivotal role in these physiological and pathological processes, understanding the mechanisms underlying USP52 function and regulation is essential for developing novel strategies for therapeutic intervention. Ongoing investigations into the structural and functional characterization of USP52, coupled with advancements in proteomic and genomic technologies, aim to delineate its specific substrates and regulatory mechanisms. This research not only contributes to the fundamental knowledge of ubiquitin-mediated signaling but also holds promise for identifying biomarkers and therapeutic targets in cancer and other diseases associated with aberrant ubiquitination.