OTULINL抗体

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     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane: Human placenta tissue lysate, Primary antibody: P09675(OTULINL Antibody) at dilution 1/400, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 15 seconds    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human tonsil tissue using P09675(OTULINL Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

OTULIN (OTU deubiquitinase with linear linkage specificity) is a deubiquitinating enzyme that specifically hydrolyzes linear (Met1-linked) ubiquitin chains, crucial regulators of NF-κB signaling and inflammatory responses. It binds to the LUBAC (linear ubiquitin chain assembly complex) to maintain homeostasis by counteracting LUBAC-mediated ubiquitination. Dysregulation of OTULIN is linked to autoinflammatory diseases, immune disorders, and cancer. For instance, biallelic OTULIN mutations cause OTULIN-related autoinflammatory syndrome (ORAS), characterized by systemic inflammation. OTULIN also modulates cell death pathways and is implicated in microbial infection responses.

OTULIN antibodies are essential tools for studying its expression, localization, and interactions. They enable detection via Western blotting, immunofluorescence, or immunohistochemistry, aiding research on its role in immune regulation and disease. Monoclonal and polyclonal antibodies are used to explore OTULIN's involvement in NF-κB signaling, apoptosis, and inflammasome activation. Recent studies also highlight its potential as a therapeutic target, particularly in cancers with dysregulated ubiquitination pathways. Validated antibodies ensure specificity for linear ubiquitin chain-related studies, distinguishing OTULIN from other deubiquitinases. Research using these antibodies enhances understanding of ubiquitin-dependent signaling and supports drug development for inflammation-related pathologies.