Recombinant Mouse TREM2 Fc Chimera Protein, CF

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Recombinant Mouse TREM2 Fc Chimera Protein, CF Summary

Product Specifications

>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
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 0.3-1.5 µg/mL.
Mouse myeloma cell line, NS0-derived mouse TREM-2 protein
Mouse TREM-2
Accession # Q99NH8
N-terminus C-terminus
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
43 kDa (monomer)
60-70 kDa, reducing conditions

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
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.
  • 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.
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Background: TREM2

TREM-2 (Triggering Receptor Expressed on Myeloid cells-2) is a type I transmembrane member of the TREM family and Ig superfamily (1, 2). Mouse TREM-2 cDNA encodes 227 amino acids (aa) that include an 18 aa signal sequence, a 153 aa extracellular domain (ECD) with one V-type Ig-like domain, a 21 aa transmembrane (TM) domain, and a 35 aa cytoplasmic tail (1). A soluble, 249 aa form of TREM-2 (TREM-2b) created by alternate splicing diverges at aa 161 (1-3). Within aa 19-161, mouse TREM-2b shares 73%, 88%, 73% and 71% aa sequence identity with the human, rat, bovine and equine TREM-2 ECD, respectively. In both TREM-1 and TREM-2, a positively charged lysine within the TM domain allows association and signaling through the signal adapter protein, DAP12 (1, 2). While TREM-1 induces macrophage activation, TREM-2 coupled with the linker protein LAT2 is inhibitory (5-7). TREM-2 is detected on newly differentiated and alternatively activated tissue macrophages, immature myeloid dendritic cells and osteoclasts, but not on circulating or tissue-resident myeloid cells (2, 6, 7). It is active in several settings that involve membrane fusion, including phagocytosis of microbes by macrophages and apoptotic neurons by microglia, and formation of osteoclasts and multinucleated giant cells from macrophages (2, 4, 8-11). TREM-2 is also interacts with and modifies signaling through dendritic cell and osteoclast Plexin A1, a semaphorin receptor (12). Mutations in human TREM-2 or DAP12 can result in Nasu-Hakola disease (NHD), also called PLOSL (polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy; 2, 11, 13). NHD patients show presenile dementia and bone cysts, presumably due to persistence of apoptotic neurons and faulty osteoclast development (2, 11, 13). Soluble TREM-2 antagonizes full-length TREM-2 and is elevated in cerebrospinal fluid of patients with active multiple sclerosis, and blockade of full-length TREM-2 exacerbates the mouse multiple sclerosis model, EAE (2, 4, 14).

  1. Daws, M. et al. (2001) Eur. J. Immunol. 31:783.
  2. Ford, J.W. and D.W. McVicar (2009) Curr. Opin. Immunol. 21:38.
  3. Swiss-Prot Accession Q99NH8
  4. Piccio, L. et al. (2008) Brain 131:3081.
  5. Hamerman, J. A. et al. (2006) J. Immunol. 177:2051.
  6. Whittaker, G.C. et al. (2010) J. Biol. Chem. 285:2976.
  7. Turnbull, I.R. et al. (2006) J. Immunol. 177:3520.
  8. N’Diaye, E-N. et al. (2009) J. Cell Biol. 184:215.
  9. Helming, L. et al. (2008) Sci. Signal. 1:ra11.
  10. Takahashi, K. et al. (2005) J. Exp. Med. 201:647.
  11. Cella, M. et al. (2003) J. Exp. Med. 198:645.
  12. Takegahara, N. et al. (2006) Nat. Cell Biol. 8:615.
  13. Paloneva, J. et al. (2002) Am. J. Hum. Genet. 71:656.
  14. Piccio, L. et al. (2007) Eur. J. Immunol. 37:1290.
Long Name
Triggering Receptor Expressed on Myeloid Cells 2
Entrez Gene IDs
54209 (Human); 102133279 (Cynomolgus Monkey)
Alternate Names
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

Citations for Recombinant Mouse TREM2 Fc Chimera Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

5 Citations: Showing 1 - 5
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  1. Oxidized phosphatidylcholines found in multiple sclerosis lesions mediate neurodegeneration and are neutralized by microglia
    Authors: Y Dong, C D'Mello, W Pinsky, BM Lozinski, DK Kaushik, S Ghorbani, D Moezzi, D Brown, FC Melo, S Zandee, T Vo, A Prat, SN Whitehead, VW Yong
    Nature Neuroscience, 2021;0(0):.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Triggering receptor expressed on myeloid cells 2 (TREM2) deficiency attenuates phagocytic activities of microglia and exacerbates ischemic damage in experimental stroke.
    Authors: Kawabori M, Kacimi R, Kauppinen T, Calosing C, Kim J, Hsieh C, Nakamura M, Yenari M
    J Neurosci, 2015;35(8):3384-96.
    Species: Mouse
    Sample Types: Whole Tissue
    Applications: Bioassay
  3. Differential modulation of TREM2 protein during postnatal brain development in mice.
    Authors: Chertoff M, Shrivastava K, Gonzalez B, Acarin L, Gimenez-Llort L
    PLoS ONE, 2013;8(8):e72083.
    Species: N/A
    Sample Types: Antibody
    Applications: Neutralization
  4. A role for TREM2 ligands in the phagocytosis of apoptotic neuronal cells by microglia.
    Authors: Hsieh CL, Koike M, Spusta SC, Niemi EC, Yenari M, Nakamura MC, Seaman WE
    J. Neurochem., 2009;109(4):1144-56.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Flow Cytometry
  5. Cutting edge: inhibition of TLR and FcR responses in macrophages by triggering receptor expressed on myeloid cells (TREM)-2 and DAP12.
    Authors: Hamerman JA, Jarjoura JR, Humphrey MB, Nakamura MC, Seaman WE, Lanier LL
    J. Immunol., 2006;177(4):2051-5.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Flow Cytometry


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