OTUB1抗体—艾普蒂

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     Western blot analysis using MYL3 (1) and MYL2 (2) mouse mAb against rat fetal heart tissues lysate.    

  
  

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     Immunohistochemical analysis of paraffin-embedded human heart tissues using MYL3 mouse mAb.    

  
  

OTUB1 (OTU deubiquitinase, ubiquitin aldehyde binding 1) is a deubiquitinating enzyme (DUB) belonging to the ovarian tumor (OTU) domain protease family. It plays a critical role in regulating cellular processes such as DNA damage repair, immune response, and apoptosis by removing ubiquitin chains from substrate proteins. Unlike many DUBs, OTUB1 primarily inhibits ubiquitination through a non-catalytic mechanism by binding to E2 ubiquitin-conjugating enzymes, thereby blocking their interaction with E3 ligases. This unique activity positions OTUB1 as a key modulator of ubiquitin-dependent signaling pathways, including the p53 and NF-κB pathways.

Antibodies targeting OTUB1 are essential tools for studying its expression, localization, and functional interactions. They are widely used in techniques like Western blotting, immunoprecipitation, immunofluorescence, and immunohistochemistry to investigate OTUB1's role in diseases such as cancer, neurodegenerative disorders, and autoimmune conditions. For example, elevated OTUB1 levels have been linked to tumor progression and chemoresistance in certain cancers, while its dysregulation is implicated in immune system abnormalities. Researchers often validate OTUB1 antibodies using knockout cell lines or recombinant protein controls to ensure specificity, given the structural similarities among OTU family members. These antibodies enable insights into OTUB1’s dual enzymatic and scaffolding functions, aiding therapeutic discovery for diseases tied to ubiquitination defects.