USP22抗体;USP22 Antibody—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human brain tissue using P11961(MVD Antibody) at dilution 1/40. (Original magnification: ×200)    

  
  

The ubiquitin-specific protease 22 (USP22) is a deubiquitinating enzyme (DUB) belonging to the ubiquitin-specific protease family, which plays a critical role in regulating protein stability and function by removing ubiquitin chains from target proteins. USP22 is a key component of the human telomerase reverse transcriptase (hTERT)- and Polycomb-repressive deubiquitination (PR-DUB) complex, where it modulates transcriptional regulation, epigenetic modifications, and cellular processes such as cell cycle progression, apoptosis, and stem cell renewal. Notably, USP22 is implicated in cancer biology due to its role in stabilizing oncoproteins (e.g., c-Myc, HIF-1α) and promoting tumor growth, metastasis, and therapy resistance. Its overexpression is associated with poor prognosis in various cancers, making it a potential therapeutic target.

USP22 antibodies are essential tools for studying its expression, localization, and function in both normal and pathological contexts. These antibodies are commonly used in techniques like Western blotting, immunohistochemistry (IHC), immunofluorescence (IF), and co-immunoprecipitation (Co-IP). Validating USP22 antibodies requires specificity testing, often through knockout cell lines or siRNA-mediated knockdown, to ensure minimal cross-reactivity with other USP family members. Researchers also rely on these antibodies to explore USP22's regulatory mechanisms in diseases, including cancer, neurodegenerative disorders, and metabolic syndromes. The development of high-affinity, well-characterized USP22 antibodies continues to advance research into its biological roles and therapeutic potential.