Human LILRB2/CD85d/ILT4 Biotinylated 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 down-regulation of
co-stimulatory molecules (10, 11). ILT4 mediates tolerogenic DC-induced CD4⁺ T cell energy in vitro and in vivo (10‑12).