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     Western blot analysis of SAE2 / UBA2 expression in A549 cell lysate.    

  
  

The SAE2/UBA2 antibody targets a critical component of the SUMOylation machinery, a post-translational modification system analogous to ubiquitination. SAE2 (SUMO-activating enzyme subunit 2), also known as UBA2. forms a heterodimer with SAE1 to constitute the E1-activating enzyme responsible for initiating SUMO (Small Ubiquitin-like Modifier) conjugation. This enzyme activates SUMO proteins via ATP-dependent adenylation, enabling their transfer to E2-conjugating enzymes and subsequent attachment to substrate proteins. SUMOylation regulates diverse cellular processes, including transcription, DNA repair, nuclear transport, and stress responses.

SAE2/UBA2 antibodies are widely used in research to study SUMOylation dynamics in diseases such as cancer, neurodegenerative disorders, and viral infections, where aberrant SUMO modification is implicated. They enable detection of SAE2/UBA2 expression levels, localization (primarily nuclear), and interactions via techniques like Western blot, immunofluorescence, and immunoprecipitation. Additionally, these antibodies aid in exploring therapeutic strategies targeting the SUMO pathway, as inhibitors of SAE2/UBA2 are investigated for anticancer and antiviral applications. Their specificity and reliability make them essential tools for dissecting SUMO-mediated regulatory mechanisms in cellular homeostasis and pathology.