Recombinant Human TREM2 Fc Chimera Avi-tag Protein, CF Summary
| Additional Information |
Biotinylated |
| Details of Functionality |
When Biotinylated Recombinant Human TREM-2 Fc Chimera Avi-tag is immobilized onto Streptavidin coated plate
(Catalog #
CP004), it binds fluorescein-conjugated E. coli Bioparticles with an ED 50 of 0.100-0.600 µg/mL. |
| Source |
Chinese Hamster Ovary cell line, CHO-derived human TREM2 protein Human TREM-2 (His19-Ser174) Accession # Q9NZC2.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag | | N-terminus | | | C-terminus | |
|
| Accession # |
|
| N-terminal Sequence |
His19 |
| Structure / Form |
Disulfide-linked homodimer Biotinylated via Avi-tag |
| Protein/Peptide Type |
Recombinant Proteins |
| Purity |
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
| Endotoxin Note |
<1.0 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
46 kDa (monomer). 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 |
60-70 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 |
>90%, 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 Human TREM2 Fc Chimera Avi-tag 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 humanTREM2 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 human TREM2 shares
73% amino acid sequence identity with mouse 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). Our
Avi-tag Biotinylated TREM2 features biotinylation at a single site contained
within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when
bound to streptavidin-coated surface due to the precise control of
biotinylation and the rest of the protein is unchanged so there is no
interference in the protein's bioactivity.
- 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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