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     The image is immunohistochemistry of paraffin-embedded Human lung cancer tissue using P09299(UBASH3A Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P09299(UBASH3A Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

The UBASH3A (Ubiquitin-associated and SH3 domain-containing protein A) antibody targets a protein encoded by the *UBASH3A* gene, located on human chromosome 21q22.3. UBASH3A, also known as STS-2 or TULA-2. is a member of the T-cell ubiquitin ligand family and functions as a regulator of immune signaling. It contains an N-terminal ubiquitin-binding domain and a C-terminal SH3 domain, enabling interactions with signaling molecules involved in T-cell receptor (TCR) pathways. UBASH3A modulates TCR signaling by dephosphorylating key tyrosine residues or promoting ubiquitin-mediated degradation of signaling components, thereby acting as a negative regulator of T-cell activation.

UBASH3A antibodies are essential tools in studying its expression, localization, and function in immune cells. They are widely used in techniques like Western blotting, immunohistochemistry, and flow cytometry to investigate UBASH3A's role in autoimmune diseases, such as type 1 diabetes, rheumatoid arthritis, and systemic lupus erythematosus, where dysregulated T-cell activity is implicated. Genetic variations in *UBASH3A* are linked to altered autoimmune disease susceptibility, highlighting its clinical relevance.

Research utilizing UBASH3A antibodies has also explored its tumor-suppressive potential in certain cancers, given its role in apoptosis and cell cycle regulation. These studies underscore UBASH3A's dual role in immune homeostasis and oncogenesis, making it a compelling target for therapeutic development.