JOSD1抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human cervical cancer tissue using P10297(JOSD1 Antibody) at dilution 1/70. (Original magnification: ×200)    

  
  

The JOSD1 antibody targets the Josephin domain-containing protein 1 (JOSD1), a member of the Josephin family of deubiquitinating enzymes (DUBs). JOSD1 is characterized by a conserved Josephin domain, which confers catalytic activity for cleaving ubiquitin chains, though its specific enzymatic mechanism remains less studied compared to other DUBs. Functionally, JOSD1 is implicated in protein quality control, endoplasmic reticulum-associated degradation (ERAD), and cellular stress responses. It interacts with key components of the ubiquitin-proteasome system, modulating substrate ubiquitination and degradation. Research suggests JOSD1 plays roles in cancer progression, neurodegenerative disorders, and immune regulation, with altered expression observed in hepatocellular carcinoma, glioblastoma, and other malignancies.

JOSD1 antibodies are essential tools for investigating its expression, localization, and molecular interactions. They enable detection via Western blotting, immunohistochemistry, and immunofluorescence, aiding studies on JOSD1's involvement in disease pathways. For example, elevated JOSD1 levels correlate with poor prognosis in liver cancer, while its downregulation links to neurodegenerative conditions like spinocerebellar ataxia. These antibodies also facilitate exploration of JOSD1's regulatory mechanisms, including post-translational modifications and binding partners. As interest grows in targeting DUBs for therapeutic intervention, JOSD1 antibodies contribute to validating its potential as a biomarker or drug target in precision medicine approaches.