SLAMF2/CD48 Protein, Human (HEK293, His)

The SLAMF2/CD48 Protein, a glycosylphosphatidylinositol (GPI)-anchored cell surface glycoprotein, plays a pivotal role in immune cell regulation and activation by interacting through its N-terminal immunoglobulin domain with cell surface receptors, such as 2B4/CD244 or CD2. In T-cell signaling transduction, SLAMF2 associates with CD2, facilitating the efficient recruitment of the Src family protein kinase LCK and LAT to the TCR/CD3 complex, thereby promoting LCK phosphorylation and subsequent activation. Furthermore, SLAMF2 induces the phosphorylation of the cytoplasmic immunoreceptor tyrosine switch motifs (ITSMs) of CD244, initiating a cascade of signaling events that culminate in the formation of the immunological synapse and the directed release of cytolytic granules containing perforin and granzymes by T-lymphocytes and NK-cells. Notably, SLAMF2 interacts directly with CD2, CD244, and LCK, highlighting its intricate involvement in immune cell function and signaling pathways.