LILRA2, also known as ILT1, CD85h, and LIR7, is an approximately 70 kDa variably glycosylated transmembrane protein that regulates immune cell activation (1). Mature human LILRA2 consists of a 426 amino acid (aa) extracellular domain (ECD) with 4 Ig-like domains, a 21 aa transmembrane segment, and a 13 aa cytoplasmic tail (2). Alternative splicing generates isoforms with short deletions between the fourth Ig-like domain and the transmembrane region, and an isoform that is truncated C-terminal to the fourth Ig-like domain (3, 4). LILRA2 is expressed on monocytes, neutrophils, basophils, and eosinophils (5-7). It contains a positively charged  arginine residue in its transmembrane segment, enabling association with the signaling protein Fc epsilon RI gamma (5). Cross-linking of LILRA2 on monocytes induces the production of multiple cytokines as well as the upregulation of Fc gamma receptors (6, 7). Cross-linking also restricts monocyte differentiation into immature dendritic cells, phagocytic activity, and antigen presentation to T cells (6, 7). R&D Systems in-house testing indicates that LILRA2 binds to Angiopoietin-like 7, consistent with the demonstrated functional interactions between other members of these protein families (8).