Recombinant Cynomolgus Monkey TREM2 Fc Chimera Protein, CF Summary
| Details of Functionality |
Measured by its ability to bind fluorescein-conjugated E. coli Bioparticles. The ED50 for this effect is 20.0-120 ng/mL. |
| Source |
Human embryonic kidney cell, HEK293-derived cynomolgus monkey TREM2 protein Cynomolgus Monkey TREM2 (His19-Ser174) Accession # XP_005553122.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | | N-terminus | | C-terminus | |
|
| Accession # |
|
| N-terminal Sequence |
His19 |
| Structure / Form |
Disulfide-linked homodimer |
| Protein/Peptide Type |
Recombinant Proteins |
| Purity |
>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. |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
44 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. |
| SDS-PAGE |
55-65 kDa, under reducing conditions |
Packaging, Storage & Formulations
| 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.
|
| Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
| Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Cynomolgus Monkey TREM2 Fc Chimera Protein, CF
Background
Triggering Receptor Expressed on Myeloid cells-2 (TREM2) is
a type I transmembrane member of the TREM subfamily within the much larger Ig
superfamily. In humans, there are 7 TREM and TREM-like receptors which play
important roles in the regulation of both innate and adaptive immune response (1).
Mature cynomologus TREM2 consists of an extracellular domain (ECD) with one
V-type Ig-like domain, a transmembrane domain with a conserved positively-charged
lysine residue, and a short cytoplasmic tail (1). The ECD of Cynomologus TREM2
shares 97% amino acid identity with human TREM2. TREM2 is expressed on
macrophages, immature myeloid dendritic cells, osteoclasts, microglia, and adipocytes
(2-6). It promotes the differentiation and function of osteoclasts, the
production of inflammatory cytokines by adipocytes, insulin resistance, and the
phagocytic clearance of bacteria (6-8). TREM2 associates with the signaling
adapter protein DAP12, both preferentially expressed in microglia, to modulate
cytokine production (2). Additionally in the CNS, TREM2 binds to ApoE, ApoA1,
and ApoB and mediates the clearance of apoptotic neurons, amyloid plaques, and
cell debris following demyelination (3-5, 9). TREM2 also interacts with and
modifies the signaling of Plexin A1 on dendritic cells and osteoclasts (10).
Mutations in TREM2 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 (11, 12). Soluble TREM2 is elevated in cerebrospinal
fluid of patients with active multiple sclerosis (MS), and TREM2 blockade
exacerbates disease symptoms in the experimental EAE model of MS (13, 14).
- Klesney-Tait,
J. et al. (2006) Nat Immunol 7:1266.
- 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.
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