Recombinant Human TREM2 Fc Chimera Avi-tag Protein, CF

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When Biotinylated Recombinant Human TREM-2 Fc Chimera Avi-tag Protein (Catalog # AVI1828) is immobilized onto Streptavidin coated plate (CP004), it binds fluorescein-conjugated E. coli Bioparticles with an ED50 of ...read more
2 μg/lane of Biotinylated Recombinant Human TREM2 Fc Chimera Avitag Protein (Catalog # AVI1828) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

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 ED50 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
IEGRMDHuman IgG1
(Pro100-Lys330)
Avi-tag
N-terminusC-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
  • Bioactivity
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

  • PLOSL2
  • TREM2
  • TREM-2
  • Trem2a
  • Trem2b
  • Trem2c
  • TREM-2triggering receptor expressed on myeloid cells 2a
  • Triggering receptor expressed on monocytes 2
  • triggering receptor expressed on myeloid cells 2

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.
  1. Klesney-Tait, J. et al. (2006) Nat Immunol. 7:1266.
  2. Turnbull, I.R. et al. (2006) J. Immunol. 177:3520.
  3. Takahashi, K. et al. (2005) J. Exp. Med. 201:647.
  4. Atagi, Y. et al. (2015) J. Biol. Chem. 290:26043.
  5. Wang, Y. et al. (2016) J. Exp. Med. 213:667.
  6. Cella, M. et al. (2003) J. Exp. Med. 198:645.
  7. Park, M. et al. (2015) Diabetes 64:117.
  8. N'Diaye, E-N. et al. (2009) J. Cell Biol. 184:215.
  9. Poliani, P.L. et al. (2015) J. Clin. Invest. 125:2161.
  10. Takegahara, N. et al. (2006) Nat. Cell Biol. 8:615.
  11. Colonna, M. and Y. Wang (2016) Nat. Rev. Neurosci. 17:201.
  12. Paloneva, J. et al. (2002) Am. J. Hum. Genet. 71:656.
  13. Piccio, L. et al. (2008) Brain 131:3081.
  14. Piccio, L. et al. (2007) Eur. J. Immunol. 37:1290.

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