ULBP3 Background Information The immune system contains genetically encoded subsystems, which monitor the extracellular environment in order to eliminate pathogens and resolve abnormal or transformed tissues. Cytomegalovirus UL16 binding proteins, known as ULBPs, are GPI-linked glycoproteins that belong to the extended MHC class I family and are distantly related to MHC class I polypeptide-related sequence B, known as MICB (1–3). ULBP and MICB proteins are ligands for the activating receptor NKG2D/DAP10, which causes lymphocyte activation resulting in the secretion of cytokines, such as interferon-gamma, and tumor cell lysis (2–4). The interaction of ULBP or MICB with NKG2D/DAP10 can be blocked by the soluble form of UL16 (3,4). ULBPs stimulate cytokine and chemokine production from NK cells, CD8 alpha/beta T cells, and gamma/delta T cells (4,5). Soluble forms of ULBPs induce protein tyrosine phosphorylation and activation of the Janus kinase 2, STAT5, extracellular signal-regulated kinase, mitogen-activated protein kinase and phosphatidylinositol 3-kinase (PI 3-kinase)/Akt signal transduction pathways (2).
ULBP3 (2F9): sc-53132. Indirect FCM analysis of C1R mock (black line histogram) and C1R-ULBP3 transfectants (solid histogram) stained with ULBP3 (2F9) followed by PE-conjugated goat anti-mouse IgG. Kindly provided by Nobuyoshi Hanaoka and Veronika Groh at Fred Hutchinson Cancer Research Center.
