TREM‑2 in Mouse Splenocytes. |
TREM‑2 was detected in immersion fixed mouse splenocytes using Mouse Anti-TREM‑2 Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF1729) at 10 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Streptavidin (yellow; Catalog # NL999) and counterstained with DAPI (blue). View our protocol for Fluorescent ICC Staining of Non-adherent Cells.
TREM-2 (Triggering Receptor Expressed by Myeloid cells) is an Ig superfamily cell surface receptor that activates a number of myeloid cell types (1). It is a member of a small gene family located on human chromosome 6p21 and mouse chromosome 17 in a region linked to the MHC (2). A single human TREM-2 gene has been described, however, two closely related orthologs were reported in mouse (3). The proteins differ by only three amino acids and were designated TREM‑2a and TREM‑2b. TREM-2 is type I transmembrane protein consisting of a single extracellular immunoglobulin (V-like) domain, a transmembrane domain with a positively charged lysine residue, and a short cytoplasmic tail (1). It associates with the signal adapter protein, DAP12, for signaling and function. DAP12 has a cytoplasmic ITAM that is phosphorylated upon ligand binding leading to the subsequent activation of cytoplasmic tyrosine kinases. TREM‑2 is expressed by immature monocyte‑derived dendritic cells (DC), and expression is down-regulated upon activation of DC by microbial products and co‑stimulatory signals (4). Ligation of TREM‑2 on immature DC with anti-TREM‑2 antibodies results in partial DC activation and the up-regulation of CCR7 and some co-stimulatory molecules. A role for TREM‑2 in the functioning of osteoclasts and microglia is suggested by the discovery that homozygous loss-of-function mutations in either TREM‑2 or DAP12 result in Nasu-Hakola disease characterized by a combination of presenile demetia and bone cysts (5). In vitro studies indicate that the differentiation of myeloid precursors into osteoclasts is dramatically impaired in TREM‑2 deficient individuals (6).
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