Recombinant Human TREM2 Fc Chimera Protein, CF

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1828-T2-050
R&D Systems Recombinant Proteins and Enzymes
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Recombinant Human TREM2 Fc Chimera Protein, CF Summary

Product Specifications

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.
Activity
Measured by its ability to bind fluorescein-conjugated E. coli Bioparticles. The ED50 for this effect is 0.04-0.16 μg/mL.
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
Accession #
N-terminal Sequence
Analysis
His19
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
44 kDa (monomer)
SDS-PAGE
60-65 kDa, reducing conditions

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1828-T2

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.

1828-T2

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

Citation for Recombinant Human 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.

1 Citation: Showing 1 - 1

  1. TREM2 Is a Receptor for ?-Amyloid that Mediates Microglial Function
    Authors: Y Zhao, X Wu, X Li, LL Jiang, X Gui, Y Liu, Y Sun, B Zhu, JC Piña-Cresp, M Zhang, N Zhang, X Chen, G Bu, Z An, TY Huang, H Xu
    Neuron, 2018;97(5):1023-1031.e7.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay

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Recombinant Human TREM2 Fc Chimera Protein, CF
By Anonymous on 10/06/2021
Application: Binding assay/Protein-protein interaction