+ +

•  

   

     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P00650(SELPLG Antibody) at dilution 1/50. (Original magnification: ×200)    

  
  

•  

   

     The image is immunohistochemistry of paraffin-embedded Human brain  tissue using P00650(SELPLG Antibody) at dilution 1/50. (Original magnification: ×200)    

  
  

SELPLG (Selectin P Ligand), also known as CD162. is a cell surface glycoprotein primarily expressed on leukocytes. It serves as a ligand for P-selectin, a cell adhesion molecule involved in mediating leukocyte rolling and recruitment during inflammatory responses. SELPLG plays a critical role in immune cell trafficking, including neutrophil and lymphocyte homing to sites of inflammation or injury. Its interaction with P-selectin is essential for the initial tethering of circulating leukocytes to activated endothelial cells, a key step in the leukocyte adhesion cascade.

Antibodies targeting SELPLG are widely used in research to study leukocyte-endothelial interactions, inflammatory diseases (e.g., atherosclerosis, rheumatoid arthritis), and immune dysregulation. Monoclonal anti-SELPLG antibodies can block ligand-receptor binding, enabling functional studies of leukocyte migration in vitro and in vivo. They are also employed in flow cytometry for immunophenotyping and quantifying SELPLG expression on immune cells. In clinical contexts, SELPLG antibodies have potential therapeutic applications, particularly in conditions driven by excessive leukocyte infiltration, though clinical development remains exploratory. Commercial SELPLG antibodies are typically validated for specificity through knockout controls or blocking assays, given the protein's post-translational modifications and structural complexity.