Description
CD2-like receptor activating cytotoxic cells (CRACC), also known as CS1, novel Ly9, SLAMF7, and CD319, is a type I transmembrane glycoprotein in the SLAM subgroup of the CD2 family (1). Mature human CRACC consists of an extracellular domain (ECD) with one Ig-like V-set domain and one Ig-like C2-set domain, a transmembrane segment, and a cytoplasmic domain with one immunoreceptor tyrosine-based switch motif (ITSM) (2, 3). Within the ECD, human CRACC shares 54% and 52% amino acid sequence identity with mouse and rat CRACC, respectively. There are seven known isoforms of CRACC which are distinguished by deletions and/or substitutions in both their ECD and cytoplasmic domains. CRACC is expressed on the surface of NK cells, CD8+ T cells, activated B cells, and mature dendritic cells (4, 5). Its homophilic interaction induces NK, CTL, and B cell activation (4-7). In human NK cells, activated CRACC transmits signals following association with the adaptor protein EAT-2 (8).Our Avi-tag Biotinylated Recombinant Human CRACC/SLAMF7 features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity