Clone REA302 recognizes the human CD312 antigen, a multi-pass membrane protein also known as EGF-like module-containing mucin-like hormone receptor-like 2 (EMR2) which shares strikingly similar molecular characteristics with CD97. CD312 is a member of the epidermal growth factor-seven transmembrane (EGF-TM7) family of proteins expressed predominantly by cells of the immune system. CD312 fails to interact with CD55, the cellular ligand for CD97, suggesting the possibility of different cellular ligands. CD312 interacts with chondroitin sulphate glycosaminoglycans in an isoform-specific manner. Expression of CD312 is up-regulated during differentiation and maturation of macrophages, and is conversely down-regulated during dendritic cell maturation. In monocytes and macrophages, CD312 can be specifically up-regulated by LPS and interleukin 10 (IL-10) via an IL-10–mediated pathway. In inflamed tissues, CD312 is detected in subpopulations of myeloid cells including macrophages and neutrophils. CD312 plays a role in the migration and adhesion of myeloid cells during cell differentiation, maturation, and activation.

Additional information: Clone REA302 displays negligible binding to Fc receptors.