Recombinant Human CD2F-10/SLAMF9 Fc Chimera Protein, CF

The CD2 family of receptors is a subset of the immunoglobulin superfamily of glycoproteins. The CD2F-10 protein, also known as SF2001 and CD85-H1, was identified as a CD2 subfamily member using genome sequence data. Based on its structural organization, CD2F-10 belongs to the SLAM (Signaling Lymphocyte Activation Molecule) subfamily of CD2 receptors and is designated SLAMF9. SLAM proteins function as co-receptors for lymphocyte activation and/or adhesion (1). Mature human CD2F-10 is a type I transmembrane glycoprotein that consists of a 218 amino acid (aa) extracellular domain (ECD) with one Ig-like C2-set domain, a 21 aa transmembrane segment, and a 32 aa cytoplasmic domain (2-4). Unlike other SLAM proteins, the cytoplasmic domain of CD2F-10 does not contain consensus immunoreceptor tyrosine-based switch motifs (ITSMs) that mediate interactions with the signal transduction proteins SAP or EAT-2 (1). Within aa 19-210, human CD2F-10 shares 57% and 59% aa sequence identity with mouse and rat CD2F-10, respectively. Alternative splicing of human CD2F-10 generates an isoform that lacks the Ig-like C2-set domain. CD2F-10 is expressed in hematopoietic tissues and cell lines (3). R&D in house data indicate that CD2F-10 inhibits the secretion of IL-2 from activated human T cells.