The antibody was purified by affinity chromatography and conjugated with PE under optimal conditions. The solution is free of unconjugated PE and unconjugated antibody.
Trem-like transcript 2 protein (TLT2), also known as TREML2, is a 33 kD (unglycosylated) type I transmembrane protein with a single IgV domain contains two potential N-glycosylation sites, a serine/threonine-rich region with numerous predicted O-linked glycosylation sites, a single membrane-spanning region, and a short cytoplasmic tail. TLT2 is expressed on B lineage cells, macrophages, neutrophils in bone marrow and periphery, and the expression level can be upregulated in response to inflammation. As a receptor, TLT2 likely plays a role in innate immunity. Recent studies have demonstrated that ligation of TLT2 inhibits the oxidative burst in neutrophils upon fMLP stimulation, indicating that TLT2 may function as an inhibitory receptor that attenuates activation of neutrophils, and possibly macrophages. Recently TLT-2 protein has been found on CD8+ T cells and is induced on activated CD4+ T cells.