Recombinant Human TREM2 Fc Chimera Protein, CF

R&D Systems | Catalog # 1828-T2

R&D Systems
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Key Product Details

  • R&D Systems NS0-derived Recombinant Human TREM2 Fc Chimera Protein (1828-T2)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

NS0

Accession Number

Structure / Form

Disulfide-linked homodimer

Applications

Bioactivity
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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.


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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.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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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

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

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Note: Certificate of Analysis not available for kit components.

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

For research use only

Citations for Recombinant Human TREM2 Fc Chimera Protein, CF

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