Mouse TREM2 Protein 3462

$315.00 – $1,050.00

Summary

Expression: HEK293
Functional: Yes (ELISA)
Amino Acid Range: Leu19-Ser171

SKU: 3462parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	Q99NH8
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE
background	TREM-2 (Triggering Receptor Expressed on Myeloid cells-2) is a 35 kDa type I transmembrane member of the TREM family and Ig superfamily. Mature human TREM-2 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. TREM-2 forms a receptor signaling complex with TYROBP which mediates signaling and cell activation following ligand binding (PubMed:10799849). Acts as a receptor for amyloid-beta protein 42, a cleavage product of the amyloid-beta precursor protein APP, and mediates its uptake and degradation by microglia.
molecular weight	The protein has a predicted MW of 17.9 kDa. Due to glycosylation, the protein migrates to 35-45 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per ug by the LAL method.

Mouse TREM2 Protein 3462

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
TREM-2 (Triggering Receptor Expressed on Myeloid cells-2) is a 35 kDa type I transmembrane member of the TREM family and Ig superfamily. Mature human TREM-2Â 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. TREM-2 forms a receptor signaling complex with TYROBP which mediates signaling and cell activation following ligand binding (PubMed:10799849). Acts as a receptor for amyloid-beta protein 42, a cleavage product of the amyloid-beta precursor protein APP, and mediates its uptake and degradation by microglia.
Protein names Triggering receptor expressed on myeloid cells 2 (TREM-2) (Triggering receptor expressed on monocytes 2)
Gene names Trem2,Trem2 Trem2a Trem2b Trem2c
Mass 10090Da
Function Forms a receptor signaling complex with TYROBP which mediates signaling and cell activation following ligand binding (PubMed:11241283). Acts as a receptor for amyloid-beta protein 42, a cleavage product of the amyloid-beta precursor protein APP, and mediates its uptake and degradation by microglia (PubMed:27477018, PubMed:29518356). Binding to amyloid-beta 42 mediates microglial activation, proliferation, migration, apoptosis and expression of pro-inflammatory cytokines, such as IL6R and CCL3, and the anti-inflammatory cytokine ARG1 (PubMed:27477018, PubMed:29518356). Acts as a receptor for lipoprotein particles such as LDL, VLDL, and HDL and for apolipoproteins such as APOA1, APOA2, APOB, APOE, APOE2, APOE3, APOE4, and CLU and enhances their uptake in microglia (PubMed:27477018). Binds phospholipids (preferably anionic lipids) such as phosphatidylserine, phosphatidylethanolamine, phosphatidylglycerol and sphingomyelin (By similarity). Regulates microglial proliferation by acting as an upstream regulator of the Wnt/beta-catenin signaling cascade (PubMed:28077724). Required for microglial phagocytosis of apoptotic neurons (PubMed:24990881). Also required for microglial activation and phagocytosis of myelin debris after neuronal injury and of neuronal synapses during synapse elimination in the developing brain (PubMed:15728241, PubMed:25631124, PubMed:28592261, PubMed:29752066). Regulates microglial chemotaxis and process outgrowth, and also the microglial response to oxidative stress and lipopolysaccharide (PubMed:28483841, PubMed:29663649, PubMed:29859094, PubMed:30232263). It suppresses PI3K and NF-kappa-B signaling in response to lipopolysaccharide; thus promoting phagocytosis, suppressing pro-inflammatory cytokine and nitric oxide production, inhibiting apoptosis and increasing expression of IL10 and TGFB (PubMed:29663649). During oxidative stress, it promotes anti-apoptotic NF-kappa-B signaling and ERK signaling (PubMed:28592261). Plays a role in microglial MTOR activation and metabolism (PubMed:28802038). Regulates age-related changes in microglial numbers (PubMed:25631124, PubMed:29752066, PubMed:30548312). Triggers activation of the immune responses in macrophages and dendritic cells (By similarity). Mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages (PubMed:18957693). In dendritic cells, it mediates up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival (By similarity). Involved in the positive regulation of osteoclast differentiation (PubMed:16418779).
Subellular location [Isoform 1]: Cell membrane ; Single-pass type I membrane protein .; [Isoform 2]: Secreted .
Tissues Expressed in the brain, specifically in microglia (at protein level) (PubMed:15728241, PubMed:27477018, PubMed:28077724, PubMed:28559417, PubMed:28592261, PubMed:28802038, PubMed:28855301, PubMed:29752066, PubMed:29794134). Expressed in macrophages (at protein level) (PubMed:11241283, PubMed:28559417, PubMed:28802038). Expressed at higher levels in the CNS, heart and lung than in lymph nodes or in other non-lymphoid tissues such as kidney, liver and testis (PubMed:12472885). In the CNS not all microglia express TREM2 (PubMed:12472885). Brain regions with an incomplete blood-brain barrier had the lowest percentages of TREM2 expressing microglia, whereas the lateral entorhinal and cingulate cortex had the highest percentages (PubMed:12472885).
Structure Monomer (By similarity). After ectodomain shedding, the extracellular domain oligomerizes, which is enhanced and stabilized by binding of phosphatidylserine (By similarity). Interacts with TYROBP/DAP12 (PubMed:11241283, PubMed:29518356). Interaction with TYROBP is required for stabilization of the TREM2 C-terminal fragment (TREM2-CTF) which is produced by proteolytic processing (By similarity).
Post-translational modification Undergoes ectodomain shedding through proteolytic cleavage by ADAM10 and ADAM17 to produce a transmembrane segment, the TREM2 C-terminal fragment (TREM2-CTF), which is subsequently cleaved by gamma-secretase.
Target Relevance information above includes information from UniProt accession: Q99NH8
The UniProt Consortium

Immobilized Mouse TREM2, His Tag at 1µg/ml (100µl/Well) on the plate. Dose response curve for Anti-TREM2 Antibody, hFc Tag with the EC50 of 2.5ng/ml determined by ELISA.

Mouse TREM2 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

1. What is the concentration of the Mouse TREM2 protein provided?
- The Mouse TREM2 protein provided has a concentration of 0.5 mg/ml.

2. How should the Mouse TREM2 protein be stored?
- The Mouse TREM2 protein should be stored at -20°C upon arrival. For long-term storage, it is recommended to aliquot and store at -80°C to prevent multiple freeze-thaw cycles.

3. Is the Mouse TREM2 protein suitable for functional studies or bioassays?
- Yes, the Mouse TREM2 protein is suitable for functional studies and bioassays. It can be used in applications such as ELISA, Western blotting, and cell signaling studies.

4. Can the Mouse TREM2 protein be used for in vivo experiments?
- This Mouse TREM2 protein is recommended for in vitro research applications. For in vivo experiments, please consult with our technical support team for further guidance on suitability.

5. Is the Mouse TREM2 protein compatible with multiple assay formats?
- Yes, the Mouse TREM2 protein is compatible with various assay formats, including ELISA, immunoblotting, immunofluorescence, and protein-protein interaction studies.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.