Human LILRB2/CD85d/ILT4 PE-conjugated Antibody

The immunoglobulin-like transcript (ILT) comprise a family of activating and inhibitory type immunoreceptors whose genes are located in the same locus that encodes killer cell Ig-like receptors (KIR) (1‑3). ILT4, also known as LIR-2 and LILRB2, is a type I transmembrane protein expressed primarily on monocytes and dendritic cells (DC) (4). Human ILT4 is produced as a 598 amino acid (aa) precursor including a 21 aa signal sequence, a 440 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 116 aa cytoplasmic domain. The ECD contains four Ig-like domains, and the cytoplasmic domain contains three immunoreceptor tyrosine-based inhibitory motifs (ITIM) (5). The ECD of human ILT4 shares 76% aa identity with chimpanzee ILT4 and 74%, 81%, 33%, 52%, 77%, 61%, and 64 % aa identity with human ILT1, 2, 3, 5, 6, 7, and 8, respectively. ILT4 binds to classical MHC I proteins as well as the non-classical HLA-G1 and HLA-F molecules (5‑9). It competes with CD8 alpha for MHC I binding but does not compete with KIR2DL1 (7). Ligation of ILT4 induces Tyr phosphorylation within its cytoplasmic ITIMs, a requirement for association with SHP-1 (4, 6). Activation of ILT4 inhibits signaling through Fc gamma RI (4) and Fc epsilon RI (6) and causes DC to become tolerogenic by downregulation of costimulatory molecules (10, 11). ILT4 mediates tolerogenic DC-induced CD4⁺ T cell energy in vitro and in vivo (10‑12).