Recombinant Human TREM2 His-tag Protein, CF Summary
Product Specifications
His19-Ser174, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
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.
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.
9256-T2
Formulation | Lyophilized from a 0.2 μm filtered solution in HEPES and NaCl. |
Reconstitution | Reconstitute at 500 μg/mL in water. |
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.
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Scientific Data
Recombinant Human TREM-2 (Catalog # 9256-T2) binds fluorescein-conjugatedE.coliBioparticles. The ED50 for this effect is 0.15-0.9 μg/mL using an anti-His Tag Antibody (Catalog # MAB050) coated plate.
Reconstitution Calculator
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).
- Painter, M.M. et al. (2015) Mol. Neurodegener. 10:43.
- Bouchon, A. et al. (2000) J. Immunol. 164:4991.
- Wunderlich, P. et al. (2013) J. Biol. Chem. 288:33027.
- Hamerman, J. A. et al. (2006) J. Immunol. 177:2051.
- Turnbull, I.R. et al. (2006) J. Immunol. 177:3520.
- Takahashi, K. et al. (2005) J. Exp. Med. 201:647.
- Atagi, Y. et al. (2015) J. Biol. Chem. 290:26043.
- Wang, Y. et al. (2016) J. Exp. Med. 213:667.
- Cella, M. et al. (2003) J. Exp. Med. 198:645.
- Park, M. et al. (2015) Diabetes 64:117.
- N'Diaye, E-N. et al. (2009) J. Cell Biol. 184:215.
- Poliani, P.L. et al. (2015) J. Clin. Invest. 125:2161.
- Takegahara, N. et al. (2006) Nat. Cell Biol. 8:615.
- Colonna, M. and Y. Wang (2016) Nat. Rev. Neurosci. 17:201.
- Paloneva, J. et al. (2002) Am. J. Hum. Genet. 71:656.
- Piccio, L. et al. (2008) Brain 131:3081.
- Piccio, L. et al. (2007) Eur. J. Immunol. 37:1290.
Citation for Recombinant Human TREM2 His-tag 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
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Galectin-3 promotes A&beta oligomerization and A&beta toxicity in a mouse model of Alzheimer's disease
Authors: CC Tao, KM Cheng, YL Ma, WL Hsu, YC Chen, JL Fuh, WJ Lee, CC Chao, EHY Lee
Cell Death Differ., 2019-05-24;27(1):192-209.
Species: Human
Sample Types: Hippocampal
Applications: IP
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