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Recombinant Human TREM2 Fc Chimera Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 1828-T2

R&D Systems, part of Bio-Techne
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1828-T2-050

Key Product Details

Source

NS0

Accession #

Structure / Form

Disulfide-linked homodimer

Conjugate

Unconjugated

Applications

Bioactivity

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human TREM2 protein
Human TREM-2
(His19 - Ser174)
Accession # NP_061838.1
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus

Purity

>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

His19

Predicted Molecular Mass

44 kDa (monomer)

SDS-PAGE

60-65 kDa, reducing conditions

Activity

Measured by its ability to bind fluorescein-conjugated E. coli Bioparticles.
The ED50 for this effect is 0.04-0.16 μg/mL.

Reviewed Applications

Read 1 review rated 4 using 1828-T2 in the following applications:

Formulation, Preparation and Storage

1828-T2
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution
Reconstitute at 300 μg/mL in PBS.

Reconstitution Buffer Available:
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Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage 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.

Background: TREM2

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 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 (2). 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 (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

  1. Painter, M.M. et al. (2015) Mol. Neurodegener. 10:43.
  2. Bouchon, A. et al. (2000) J. Immunol. 164:4991.
  3. Wunderlich, P. et al. (2013) J. Biol. Chem. 288:33027.
  4. Hamerman, J. A. et al. (2006) J. Immunol. 177:2051.
  5. Turnbull, I.R. et al. (2006) J. Immunol. 177:3520.
  6. Takahashi, K. et al. (2005) J. Exp. Med. 201:647.
  7. Atagi, Y. et al. (2015) J. Biol. Chem. 290:26043.
  8. Wang, Y. et al. (2016) J. Exp. Med. 213:667.
  9. Cella, M. et al. (2003) J. Exp. Med. 198:645.
  10. Park, M. et al. (2015) Diabetes 64:117.
  11. N'Diaye, E-N. et al. (2009) J. Cell Biol. 184:215.
  12. Poliani, P.L. et al. (2015) J. Clin. Invest. 125:2161.
  13. Takegahara, N. et al. (2006) Nat. Cell Biol. 8:615.
  14. Colonna, M. and Y. Wang (2016) Nat. Rev. Neurosci. 17:201.
  15. Paloneva, J. et al. (2002) Am. J. Hum. Genet. 71:656.
  16. Piccio, L. et al. (2008) Brain 131:3081.
  17. Piccio, L. et al. (2007) Eur. J. Immunol. 37:1290.

Long Name

Triggering Receptor Expressed on Myeloid Cells 2

Alternate Names

PLOSL2, TREM-2

Entrez Gene IDs

54209 (Human); 102133279 (Cynomolgus Monkey)

Gene Symbol

TREM2

Additional TREM2 Products

Product Documents for Recombinant Human TREM2 Fc Chimera Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human TREM2 Fc Chimera Protein, CF

For research use only

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