The structure of ULBP1 consists of the alpha-1 and alpha-2 domains, which are connected to the cell membrane via the GPI anchor . This protein plays a crucial role in the immune system by binding and activating the KLRK1/NKG2D receptor on natural killer (NK) cells and some T-cells . This interaction mediates NK cell cytotoxicity, which is essential for the immune response against infected or transformed cells .
The recombinant form of ULBP1 is produced in Sf9 Baculovirus cells . This method allows for the production of a single, glycosylated polypeptide chain that retains the functional properties of the native protein . The recombinant ULBP1 produced in Sf9 cells is used in various research applications, including studies on immune response and viral evasion mechanisms .
ULBP1 is widely used in research to study its role in the immune system and its interactions with viral proteins. It is also used to investigate the mechanisms of NK cell activation and the pathways involved in immune responses . Additionally, recombinant ULBP1 is valuable for developing therapeutic strategies targeting immune evasion by viruses and enhancing NK cell-mediated cytotoxicity .