SLAMF2/CD48 Protein, Rat (HEK293, hFc)

SLAMF2, also known as CD48, is a glycosylphosphatidylinositol (GPI)-anchored cell surface glycoprotein that plays a crucial role in immune cell regulation. Through its N-terminal immunoglobulin domain, SLAMF2 interacts with cell surface receptors, such as 2B4/CD244 or CD2, to modulate immune cell function and activation. In T-cell signaling transduction, SLAMF2 forms complexes with CD2, facilitating the recruitment of the Src family protein kinase LCK and LAT to the TCR/CD3 complex. This interaction leads to the phosphorylation and subsequent activation of LCK. Additionally, SLAMF2 induces the phosphorylation of the cytoplasmic immunoreceptor tyrosine switch motifs (ITSMs) of CD244, initiating signaling events that culminate in the formation of the immunological synapse and the targeted release of cytolytic granules containing perforin and granzymes by T-lymphocytes and NK-cells. SLAMF2 establishes direct interactions with CD2, CD244, and LCK, contributing to its regulatory role in immune responses.