Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to bind fluorescein-conjugated S. aureus Bioparticles. Daws, M.R. et al. (2003) J. Immunol. 171:594. The ED 50 for this effect is 20-120 ng/mL using a His tag antibody coated plate.
Source
Mouse myeloma cell line, NS0-derived Leu19-Ser171, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
AnalysisLeu19
Predicted Molecular Mass
18 kDa
9228-T2 |
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Formulation Lyophilized from a 0.2 μm filtered solution in HEPES and NaCl. | ||
Reconstitution Reconstitute at 500 μg/mL in water. | ||
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | ||
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Data Images
Bioactivity
| Recombinant Mouse TREM-2 (Catalog # 9228-T2) bindsfluorescein-conjugated |
Background: TREM-2
TREM-2 (Triggering Receptor Expressed on Myeloid cells-2) is a 35 kDa type I transmembrane member of the TREM family and Ig superfamily (1). Mature mouse TREM-2 consists of a 153 amino acid (aa) extracellular domain (ECD) with one Ig-like domain, a 21 aa transmembrane segment, and a 35 aa cytoplasmic domain (2). Within the ECD, mouse TREM-2 shares 73% and 90% aa sequence identity with human 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 (3). A positively charged lysine within the transmembrane segment allows association with the signal adapter protein, DAP12 and inhibition of macrophage activation (4, 5). TREM-2 is expressed on macrophages, immature myeloid dendritic cells, osteoclasts, microglia, and adipocytes (5-9). It promotes the differentiation and function of osteoclasts, the production of inflammatory cytokines by adipocytes, insulin resistance, and the phagocytic clearance of bacteria (9-11). 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 (6-8, 12). TREM-2 also interacts with and modifies signaling through Plexin A1 on dendritic cells and osteoclasts (13). 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 (14, 15). 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 (16, 17).
References:
Painter, M.M. et al. (2015) Mol. Neurodegener. 10:43.
Daws, M.R. et al. (2001) Eur. J. Immunol. 31:783.
Wunderlich, P. et al. (2013) J. Biol. Chem. 288:33027.
Hamerman, J. A. et al. (2006) J. Immunol. 177:2051.
Turnbull, I.R. et al. (2006) J. Immunol. 177:3520.
Takahashi, K. et al. (2005) J. Exp. Med. 201:647.
Atagi, Y. et al. (2015) J. Biol. Chem. 290:26043.
Wang, Y. et al. (2016) J. Exp. Med. 213:667.
Cella, M. et al. (2003) J. Exp. Med. 198:645.
Park, M. et al. (2015) Diabetes 64:117.
N'Diaye, E-N. et al. (2009) J. Cell Biol. 184:215.
Poliani, P.L. et al. (2015) J. Clin. Invest. 125:2161.
Takegahara, N. et al. (2006) Nat. Cell Biol. 8:615.
Colonna, M. and Y. Wang (2016) Nat. Rev. Neurosci. 17:201.
Paloneva, J. et al. (2002) Am. J. Hum. Genet. 71:656.
Piccio, L. et al. (2008) Brain 131:3081.
Piccio, L. et al. (2007) Eur. J. Immunol. 37:1290.
Long Name:
Triggering Receptor Expressed on Myeloid Cells 2
Entrez Gene IDs:
54209 (Human)
Alternate Names:
TREM2; TREM-2; Trem2a; Trem2b; Trem2c; TREM-2triggering receptor expressed on myeloid cells 2a; Triggering receptor expressed on monocytes 2; triggering receptor expressed on myeloid cells 2
