Human TREM2 Antibody Summary
His19-Ser174
Accession # Q9NZC2
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
Detection of TREM2 in Human Lung. TREM2 was detected in immersion fixed paraffin-embedded sections of human lung using Rabbit Anti-Human TREM2 Monoclonal Antibody (Catalog # MAB11618) at 3 µg/ml for 1 hour at room temperature followed by incubation with the Anti-Rabbit IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC003). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using VisUCyte Antigen Retrieval Reagent-Basic (Catalog # VCTS021). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to the cytoplasm. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents.
Detection of TREM2 in Human Brain Cortex. TREM2 was detected in immersion fixed paraffin-embedded sections of human brain cortex using Rabbit Anti-Human TREM2 Monoclonal Antibody (Catalog # MAB11618) at 3 µg/ml for 1 hour at room temperature followed by incubation with the Anti-Rabbit IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC003). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using VisUCyte Antigen Retrieval Reagent-Basic (Catalog # VCTS021). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to the cytoplasm of microglia. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: TREM2
TREM2 (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 TREM2 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 TREM2 shares 73% and 74% aa sequence identity with mouse and rat TREM2, respectively. Soluble forms of the TREM2 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). TREM2 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, TREM2 binds to ApoE, ApoA1, and ApoB and mediates the clearance of apoptotic neurons, amyloid plaques, and cell debris following demyelination (6-8, 12). TREM2 also interacts with and modifies signaling through Plexin A1 on dendritic cells and osteoclasts (13). 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 (14, 15). 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 (16, 17).
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- 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.
- Akahashi, 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.
- Akegahara, 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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