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Specifications
- Conjugation:Unconjugated
- Protein/Peptide Type:Recombinant
- Source:NS0 cells
- Species:Human
- Size:50 µg
- Storage Conditions:Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 ░C as supplied. 1 month, 2 to 8 ░C under sterile conditions after reconstitution. 3 months, -20 to -70 ░C under sterile conditions after reconstitution.
- Endotoxin Content:<1.0 EU per 1 ╡g of the protein by the LAL method.
- Gene ID:54209
- Reconstitution Instructions:Reconstitute at 300 μg/mL in PBS
- Protein Synonyms:Trem2b|triggering receptor expressed on myeloid cells 2|TREM2|TREM-2triggering receptor expressed on myeloid cells 2a|Trem2a|Triggering receptor expressed on monocytes 2|Trem2c
- Accession No.:NP_061838
- Protein/Peptide Name:TREM-2
- Purity:>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie« Blue Staining.
- Molecular Weight:60-65 kDa, reducing conditions
- Endotoxin Level:<1.0 EU per 1 μg of the protein by the LAL method
- Formulation:Lyophilized from a 0.2 μm filtered solution in PBS
- Cat. No.:102870-308
- Supplier no.:1828-T2-050
Specifications
About this item
The Recombinant Human TREM-2 Fc Chimera Protein from R&D Systems is derived from NS0. The Recombinant Human TREM-2 Fc Chimera Protein has been validated for the following applications: Bioactivity.
- N-terminal sequence: His19
- Structure or form: Disulfide-linked homodimer
TREM-2 (Triggering Receptor Expressed on Myeloid cells-2) is a 35 kDa type I transmembrane member of the TREM family and Ig superfamily. Mature human TREM-2 consists of a 156 amino acid (aa) extracellular domain (ECD) with one V-type Ig-like domain, a 21 aa transmembrane (TM) domain, and a 35 aa cytoplasmic tail. Within the ECD, human TREM-2 shares 73% and 74% aa sequence identity with mouse and rat TREM-2, respectively.
Soluble forms of the TREM-2 ECD are generated by alternative splicing or proteolytic cleavage, and the cytoplasmic domain can be liberated by gamma-Secretase mediated intramembrane cleavage. A positively charged lysine within the transmembrane segment allows association with the signal adapter protein, DAP12 and inhibition of macrophage activation. TREM-2 is expressed on macrophages, immature myeloid dendritic cells, osteoclasts, microglia, and adipocytes. It promotes the differentiation and function of osteoclasts, the production of inflammatory cytokines by adipocytes, insulin resistance, and the phagocytic clearance of bacteria.
In the CNS, TREM-2 binds to ApoE, ApoA1, and ApoB and mediates the clearance of apoptotic neurons, amyloid plaques, and cell debris following demyelination. TREM-2 also interacts with and modifies signaling through Plexin A1 on dendritic cells and osteoclasts. Mutations in TREM-2 or DAP12 are associated with the development of Alzheimer's disease and Nasu-Hakola disease (NHD/PLOSL) which is characterized by presenile dementia and bone cysts. Soluble TREM-2 is elevated in cerebrospinal fluid of patients with active multiple sclerosis (MS), and TREM-2 blockade exacerbates disease symptoms in the experimental EAE model of MS.