OTUD6A抗体—艾普蒂

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     Immunohistochemical analysis of paraffin-embedded human infiltrating ductal carcinoma tissue(left) and simple carcinoma of breast cancer tissue(right), showing nuclear localization using PR mouse mAb with DAB staining.    

  
  

OTUD6A (OTU domain-containing protein 6A) is a deubiquitinating enzyme (DUB) belonging to the ovarian tumor (OTU) protease family, which regulates protein stability and signaling by cleaving ubiquitin chains. It is implicated in diverse cellular processes, including protein homeostasis, DNA repair, and immune response regulation. Structurally, OTUD6A contains a conserved OTU domain responsible for its catalytic activity, though it lacks canonical motifs found in other OTU members, suggesting unique substrate specificity. Studies indicate its role in modulating key pathways such as TGF-β and Wnt signaling, often through interactions with signaling intermediates like USP15 or SMAD7.

OTUD6A antibodies are essential tools for detecting and studying this enzyme in research. These antibodies, often raised in rabbits or mice, enable applications like Western blotting, immunofluorescence, and immunoprecipitation to assess OTUD6A expression, localization, and interactions. High-quality antibodies are validated using knockout cell lines or siRNA knockdown to confirm specificity. OTUD6A expression varies across tissues, with elevated levels observed in brain, testis, and certain cancers, linking it to tumor progression and neurodegenerative diseases. Recent research highlights its involvement in maintaining genomic stability by resolving DNA-protein crosslinks and regulating apoptosis. Dysregulation of OTUD6A has been associated with developmental disorders and cancer, making it a potential therapeutic target. Ongoing studies aim to clarify its substrate profiles and disease-specific mechanisms, emphasizing the antibody's utility in both basic and translational research contexts.