Trem-1 Fc

Triggering receptor expressed on myeloid cells-1 (TREM-1) is a type 1 transmembrane glycoprotein belonging to the immunoglobulin superfamily of cell surface receptors that is constitutively expressed on the surface of monocytes, neutrophils and macrophages. The first identified member of the TREM family of receptors, TREM-1 is a proponent of amplified inflammatory responses triggered by bacterial and fungal infection, and functions in association with the signal transduction adaptor molecule DAP12. TREM-1 activation induces the sustained secretion of proinflammatory chemokines (IL-8 and MCP-1) and cytokines (TNF-α, IL-1β, and IL-6), the respiratory burst and degranulation of neutrophils, the upregulation of adhesion molecules involved in leukocyte extravasation, and tissue degradation. Involvement and increased expression of TREM-1, or soluble TREM-1, in infectious, as well as some non-infectious, inflammatory conditions may highlight the protein’s potential as a possible diagnostic marker in cases of severe inflammation, such as myocardial dysfunction related to severe sepsis and spontaneous preterm labor. TREM-1 involvement in inflammatory response has also been noted as a predictor of both progression and aggression in certain cancers. Recombinant Human TREM-1 Fc is a glycosylated, disulfide-linked homodimer of 826 amino acid residues whose monomer consists of the 180-amino-acid length extracellular portion of TREM-1 fused to the 231-amino-acid length Fc portion of human IgG1 by two glycines. The calculated molecular weight of Recombinant Human TREM-1 Fc dimer is 92.6 kDa; however, due to glycosylation, the monomer and dimer migrate at apparent molecular weights of approximately 60-65 kDa and 110-116 kDa by SDS-PAGE analysis under reducing conditions.