TPST2抗体

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     The image is immunohistochemistry of paraffin-embedded Human esophagus cancer tissue using P12321(TPST2 Antibody) at dilution 1/35. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human breast cancer tissue using P12321(TPST2 Antibody) at dilution 1/35. (Original magnification: ×200)    

  
  

The tyrosine sulfotransferase 2 (TPST2) enzyme, encoded by the TPST2 gene in humans, catalyzes the post-translational sulfation of tyrosine residues in secretory and membrane proteins. This modification enhances protein-protein interactions critical for various biological processes, including immune response, hormone signaling, and hemostasis. TPST2 primarily sulfates substrates like chemokine receptors (e.g., CCR5) and adhesion molecules (e.g., PSGL-1), influencing leukocyte trafficking, inflammation, and pathogen entry. Dysregulation of TPST2 activity has been implicated in diseases such as cancer, autoimmune disorders, and viral infections (e.g., HIV).

TPST2 antibodies are immunological tools designed to detect, quantify, or inhibit TPST2 in research and diagnostic contexts. These antibodies enable studies on TPST2 expression patterns, subcellular localization, and functional roles in disease mechanisms. Monoclonal TPST2 antibodies, in particular, are used in techniques like Western blotting, immunohistochemistry, and flow cytometry to assess protein levels in tissues or cell lines. Some therapeutic applications are being explored, including targeting TPST2 to modulate sulfation-dependent pathways in inflammatory or oncogenic processes. However, TPST2's broad substrate specificity and overlapping functions with TPST1 pose challenges in dissecting its unique contributions. Current research continues to clarify TPST2's regulatory mechanisms and its potential as a biomarker or therapeutic target.