Recombinant Mouse TREM2 His-tag Protein, CF


Recombinant Mouse TREM-2 (Catalog # 9228-T2) bindsfluorescein-conjugated S. aureus Bioparticles. The ED50 for this effect is20-120 ng/mL using an anti-His tag antibody (Catalog # MAB050) coated plate.

Product Details

Reactivity MuSpecies Glossary
Applications Bioactivity

Order Details

Recombinant Mouse TREM2 His-tag Protein, CF Summary

Details of Functionality
Measured by its ability to bind fluorescein-conjugated S. aureus Bioparticles. Daws, M.R. et al. (2003) J. Immunol. 171:594. The ED50 for this effect is 20-120 ng/mL using a His tag antibody coated plate.
Mouse myeloma cell line, NS0-derived mouse TREM2 protein
Leu19-Ser171, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Proteins
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.


  • Bioactivity
Theoretical MW
18 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
25 - 75 kDa, under reducing conditions.
Read Publication using
9228-T2 in the following applications:

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in HEPES and NaCl.
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in water.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse TREM2 His-tag Protein, CF

  • PLOSL2
  • 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


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).
  1. Painter, M.M. et al. (2015) Mol. Neurodegener. 10:43.
  2. Daws, M.R. et al. (2001) Eur. J. Immunol. 31:783.
  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.

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Publications for TREM2 (9228-T2)(1)

We have publications tested in 1 confirmed species: Mouse.

We have publications tested in 1 application: ELISA Standard.

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