Recombinant Mouse TREM2 Fc Chimera Protein, CF Summary
Product Specifications
| Mouse TREM-2 (Leu19-Pro168) Accession # Q99NH8 |
IEGRMD | Human IgG1 (Pro100-Lys330) |
| N-terminus | C-terminus | |
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.
1729-T2
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
| 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.
|
Reconstitution Calculator
Background: TREM2
TREM-2 (Triggering Receptor Expressed on Myeloid cells-2) is a type I transmembrane member of the TREM family and Ig superfamily (1, 2). Mouse TREM-2 cDNA encodes 227 amino acids (aa) that include an 18 aa signal sequence, a 153 aa extracellular domain (ECD) with one V-type Ig-like domain, a 21 aa transmembrane (TM) domain, and a 35 aa cytoplasmic tail (1). A soluble, 249 aa form of TREM-2 (TREM-2b) created by alternate splicing diverges at aa 161 (1-3). Within aa 19-161, mouse TREM-2b shares 73%, 88%, 73% and 71% aa sequence identity with the human, rat, bovine and equine TREM-2 ECD, respectively. In both TREM-1 and TREM-2, a positively charged lysine within the TM domain allows association and signaling through the signal adapter protein, DAP12 (1, 2). While TREM-1 induces macrophage activation, TREM-2 coupled with the linker protein LAT2 is inhibitory (5-7). TREM-2 is detected on newly differentiated and alternatively activated tissue macrophages, immature myeloid dendritic cells and osteoclasts, but not on circulating or tissue-resident myeloid cells (2, 6, 7). It is active in several settings that involve membrane fusion, including phagocytosis of microbes by macrophages and apoptotic neurons by microglia, and formation of osteoclasts and multinucleated giant cells from macrophages (2, 4, 8-11). TREM-2 is also interacts with and modifies signaling through dendritic cell and osteoclast Plexin A1, a semaphorin receptor (12). Mutations in human TREM-2 or DAP12 can result in Nasu-Hakola disease (NHD), also called PLOSL (polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy; 2, 11, 13). NHD patients show presenile dementia and bone cysts, presumably due to persistence of apoptotic neurons and faulty osteoclast development (2, 11, 13). Soluble TREM-2 antagonizes full-length TREM-2 and is elevated in cerebrospinal fluid of patients with active multiple sclerosis, and blockade of full-length TREM-2 exacerbates the mouse multiple sclerosis model, EAE (2, 4, 14).
- Daws, M. et al. (2001) Eur. J. Immunol. 31:783.
- Ford, J.W. and D.W. McVicar (2009) Curr. Opin. Immunol. 21:38.
- Swiss-Prot Accession Q99NH8
- Piccio, L. et al. (2008) Brain 131:3081.
- Hamerman, J. A. et al. (2006) J. Immunol. 177:2051.
- Whittaker, G.C. et al. (2010) J. Biol. Chem. 285:2976.
- Turnbull, I.R. et al. (2006) J. Immunol. 177:3520.
- N’Diaye, E-N. et al. (2009) J. Cell Biol. 184:215.
- Helming, L. et al. (2008) Sci. Signal. 1:ra11.
- Takahashi, K. et al. (2005) J. Exp. Med. 201:647.
- Cella, M. et al. (2003) J. Exp. Med. 198:645.
- Takegahara, N. et al. (2006) Nat. Cell Biol. 8:615.
- Paloneva, J. et al. (2002) Am. J. Hum. Genet. 71:656.
- Piccio, L. et al. (2007) Eur. J. Immunol. 37:1290.
Citations for Recombinant Mouse 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.
9
Citations: Showing 1 - 9
Filter your results:
Filter by:
-
Trem2 deficiency attenuates breast cancer tumor growth in lean, but not obese or weight loss, mice and is associated with alterations of clonal T cell populations
Authors: Pierro, EW;Cottam, MA;An, H;Lehmann, BD;Pietenpol, JA;Wellen, KE;Makowski, L;Rathmell, JC;Fingleton, B;Hasty, AH;
bioRxiv : the preprint server for biology
Species: Mouse
Sample Types: Recombinant Protein
Applications: ELISA Control -
Target delivery of a PD-1-TREM2 scFv by CAR-T cells enhances anti-tumor efficacy in colorectal cancer
Authors: Chen, J;Zhu, T;Jiang, G;Zeng, Q;Li, Z;Huang, X;
Molecular cancer
Species: Mouse
Sample Types: Tissue Homogenates
Applications: ELISA Capture -
BRI2-mediated regulation of TREM2 processing in microglia and its potential implications for Alzheimer's disease and related dementias
Authors: Yin, T;D'Adamio, L;
bioRxiv : the preprint server for biology
Species: N/A
Sample Types: Antibody
Applications: ELISA Standard -
MS4A4A modifies the risk of Alzheimer disease by regulating lipid metabolism and immune response in a unique microglia state
Authors: SF You, L Brase, F Filipello, AK Iyer, J Del-Aguila, J He, R D'Oliveira, J Budde, J Norton, J Gentsch, NM Dräger, SM Sattler, M Kampmann, L Piccio, JC Morris, RJ Perrin, E McDade, Dominantly, SM Paul, AG Cashikar, BA Benitez, O Harari, CM Karch
medRxiv : the preprint server for health sciences, 2023-02-08;0(0):.
Species: Mouse
Sample Types: Cell Culture Supernates
Applications: Reference Standard -
Oxidized phosphatidylcholines found in multiple sclerosis lesions mediate neurodegeneration and are neutralized by microglia
Authors: Y Dong, C D'Mello, W Pinsky, BM Lozinski, DK Kaushik, S Ghorbani, D Moezzi, D Brown, FC Melo, S Zandee, T Vo, A Prat, SN Whitehead, VW Yong
Nature Neuroscience, 2021-02-18;0(0):.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Triggering receptor expressed on myeloid cells 2 (TREM2) deficiency attenuates phagocytic activities of microglia and exacerbates ischemic damage in experimental stroke.
Authors: Kawabori M, Kacimi R, Kauppinen T, Calosing C, Kim J, Hsieh C, Nakamura M, Yenari M
J Neurosci, 2015-02-25;35(8):3384-96.
Species: Mouse
Sample Types: Whole Tissue
Applications: Bioassay -
Differential modulation of TREM2 protein during postnatal brain development in mice.
Authors: Chertoff M, Shrivastava K, Gonzalez B, Acarin L, Gimenez-Llort L
PLoS ONE, 2013-08-19;8(8):e72083.
Applications: Neutralization -
A role for TREM2 ligands in the phagocytosis of apoptotic neuronal cells by microglia.
Authors: Hsieh CL, Koike M, Spusta SC, Niemi EC, Yenari M, Nakamura MC, Seaman WE
J. Neurochem., 2009-03-19;109(4):1144-56.
Species: Mouse
Sample Types: Whole Cells
Applications: Flow Cytometry, ICC -
Cutting edge: inhibition of TLR and FcR responses in macrophages by triggering receptor expressed on myeloid cells (TREM)-2 and DAP12.
Authors: Hamerman JA, Jarjoura JR, Humphrey MB, Nakamura MC, Seaman WE, Lanier LL
J. Immunol., 2006-08-15;177(4):2051-5.
Species: Mouse
Sample Types: Whole Cells
Applications: Flow Cytometry
FAQs
No product specific FAQs exist for this product, however you may
View all Proteins and Enzyme FAQsReviews for Recombinant Mouse TREM2 Fc Chimera Protein, CF
There are currently no reviews for this product. Be the first to review Recombinant Mouse TREM2 Fc Chimera Protein, CF and earn rewards!
Have you used Recombinant Mouse TREM2 Fc Chimera Protein, CF?
Submit a review and receive an Amazon gift card.
$25/€18/£15/$25CAN/¥75 Yuan/¥2500 Yen for a review with an image
$10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen for a review without an image
