CD162. also known as P-selectin glycoprotein ligand-1 (PSGL-1), is a cell surface glycoprotein predominantly expressed on leukocytes. It plays a critical role in mediating cell adhesion interactions, particularly during inflammatory responses by binding to P-selectin on activated endothelial cells and platelets. This interaction facilitates leukocyte rolling, activation, and migration to sites of inflammation or injury. CD162 antibodies are monoclonal or polyclonal reagents designed to target specific epitopes of the PSGL-1 protein. They are widely used in research to study leukocyte trafficking, immune cell activation, and inflammatory diseases (e.g., atherosclerosis, autoimmune disorders). Clinically, CD162 antibodies have applications in flow cytometry for immunophenotyping hematopoietic cells, aiding in the diagnosis of certain leukemias or lymphomas where aberrant PSGL-1 expression is observed. Some therapeutic antibodies targeting CD162 are under investigation for modulating inflammatory responses or blocking pathogenic cell interactions. Structurally, CD162 antibodies often recognize sulfated tyrosine residues or glycosylation-dependent epitopes critical for its ligand-binding function. Variations in antibody clones (e.g., KPL-1. AK4) may exhibit differences in binding specificity, blocking efficiency, or cross-reactivity across species, influencing their experimental or therapeutic utility.