2. Signaling Pathways
  3. Cell Cycle/DNA Damage
  4. Deubiquitinase
  5. USP4 Isoform

USP4

Ubiquitin Specific Peptidase 4 (USP4) is a deubiquitinating enzyme that plays a critical role in regulating protein stability and signaling pathways by removing ubiquitin chains from target substrates[1]. USP4 has been implicated in various cellular processes, including DNA damage response, cell cycle regulation, and apoptosis, highlighting its importance in maintaining genomic integrity[2]. It is known to interact with key regulators such as p53 and SMAD proteins, modulating their activity and half-life through deubiquitination[3]. In the context of cancer, USP4 acts as both a tumor suppressor and an oncogene depending on the cellular environment and substrate specificity, underscoring its dual functional nature[4]. Recent studies have demonstrated that USP4 regulates TGF-β signaling by stabilizing SMAD4, thereby influencing epithelial-mesenchymal transition (EMT) and metastasis[5]. Furthermore, USP4 has been linked to neurodegenerative diseases due to its involvement in the degradation of misfolded proteins via the ubiquitin-proteasome system[6]. Its distinct substrate selectivity and catalytic mechanism differentiate it from other members of the USP family, particularly USP7 and USP10, which share structural similarities but exhibit divergent biological roles[7]. Research tools such as USP4-specific inhibitors and knockout models are emerging, enabling more precise investigation into its physiological and pathological functions[8].

USP4 Related Products (1):

Cat. No. Product Name Effect Purity
  • HY-180171
    USP11-IN-1
    		Inhibitor
    USP11-IN-1 (Compound 26) is a selective ubiquitin-specific protease 11 (USP11) inhibitor with an IC50 of 10.9 μM. USP11-IN-1 shows IC50 values of 18.1 and >500 μM for USP4 (SI = 1.7 fold) and USP15 (SI > 100 fold). USP11-IN-1 can be used for the research of USP11-related malignant tumors.