The KLRK1 antibody targets NKG2D, a receptor that plays a critical role in immunosurveillance. Upon binding to various cellular stress-inducible ligands (e.g., MICA, MICB, RAET1E, RAET1G, RAET1L/ULBP6, ULBP1, ULBP2, ULBP3, and ULBP4) expressed on the surface of tumor and virus-infected cells, NKG2D functions as both an activating and costimulatory receptor. This binding initiates stimulatory and costimulatory innate immune responses in activated natural killer (NK) cells, leading to cytotoxic activity and the elimination of ligand-expressing tumor cells via perforin-mediated mechanisms. Furthermore, NKG2D acts as a costimulatory receptor for the T-cell receptor (TCR) in CD8+ T-cell-mediated adaptive immune responses, thereby amplifying T-cell activation. Signaling through NKG2D involves calcium influx and subsequent TNF-α expression. NKG2D is also implicated in NK cell-mediated bone marrow graft rejection and may regulate NK cell differentiation and survival. Ligand binding affinity varies; with ULBP2 exhibiting the highest affinity, followed by ULBP1 and then ULBP3.