Anti-OTUD3 / OTU domain-containing protein 3

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. OTUD3 antibody detects OTU domain-containing protein 3, a deubiquitinating enzyme that regulates protein stability, signaling, and cellular stress responses. Encoded by the OTUD3 gene on chromosome 1p36.13, this protein belongs to the OTU (ovarian tumor) family of cysteine proteases that cleave ubiquitin from substrate proteins, reversing ubiquitination and modulating protein degradation. OTUD3 functions as a negative regulator of the ubiquitin-proteasome system and contributes to homeostatic control of multiple signaling pathways, including p53 and AKT.Structurally, OTUD3 contains an OTU catalytic domain responsible for hydrolyzing lysine-linked ubiquitin chains, particularly K63 and K48 linkages, which regulate protein turnover and signal transduction. It stabilizes tumor suppressor p53 by removing ubiquitin moieties added by MDM2 and promotes the degradation of AKT to restrain oncogenic signaling. Through these opposing actions, OTUD3 maintains a balance between proliferation and apoptosis in response to cellular stress.The OTUD3 antibody is used in cancer biology, proteostasis, and signal transduction research to study ubiquitin signaling, protein turnover, and stress regulation. Western blot analysis identifies a 45 kilodalton band corresponding to OTUD3, while immunofluorescence shows cytoplasmic and nuclear localization depending on cellular state. This antibody supports the investigation of deubiquitination mechanisms and ubiquitin-mediated signaling networks.Alterations in OTUD3 expression are associated with tumorigenesis, neurodegeneration, and inflammatory diseases. Overexpression of OTUD3 stabilizes p53 and enhances apoptosis, while loss of expression correlates with increased AKT activity and cancer progression. The OTUD3 antibody provides a validated tool for examining these regulatory mechanisms. NSJ Bioreagents supplies this antibody validated for its applications, ensuring consistent detection for ubiquitin signaling research.