Recombinant Mouse TREM-2b Protein (C-Fc)

Name: Recombinant Mouse TREM-2b Protein (C-Fc)
Brand: Beta LifeScience
SKU: BL-2755NP
Availability: InStock

BL-2755NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Triggering Receptor Expressed On Myeloid Cells 2b is produced by our Mammalian expression system and the target gene encoding Leu19-Pro168 is expressed with a human IgG1 Fc tag at the C-terminus.
Accession	Q99NH8
Synonym	Triggering Receptor Expressed on Myeloid Cells 2b; Triggering receptor expressed on myeloid cells 2; TREM-2; Triggering receptor expressed on monocytes 2; Trem2; Trem2a; Trem2b; Trem2c; TREM-2b
Gene Background	Triggering receptor expressed on myeloid cells-2 (TREM-2) is a cell surface receptor primarily expressed on macrophages, osteoclasts, microglia and dendritic cells. TREM-2 is one member of the TREM family, inhibiting the releasing of inflammatory mediators, so it is an important in vivo anti-inflammatory receptor. TREM-2 consists of 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. A soluble form of TREM-2 (TREM-2b) created by alternate splicing diverges at aa 161. TREM-2 transduces intracellular signals through the adaptor DAP12. After binding of TREM-2 with ligand, the TREM-2/DAP12 (dead-cell-activated-receptor-associated protein)-mediated signal transduction pathway causes a series of intracellular protein tyrosine phosphorylation reactions and enzymatic reactions, which then activate the myeloid cells and participate T cell responses.
Molecular Mass	43.7 KDa
Apmol Mass	55-70 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Forms a receptor signaling complex with TYROBP which mediates signaling and cell activation following ligand binding. 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. 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. 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. Binds phospholipids (preferably anionic lipids) such as phosphatidylserine, phosphatidylethanolamine, phosphatidylglycerol and sphingomyelin. Regulates microglial proliferation by acting as an upstream regulator of the Wnt/beta-catenin signaling cascade. Required for microglial phagocytosis of apoptotic neurons. Also required for microglial activation and phagocytosis of myelin debris after neuronal injury and of neuronal synapses during synapse elimination in the developing brain. Regulates microglial chemotaxis and process outgrowth, and also the microglial response to oxidative stress and lipopolysaccharide. 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. During oxidative stress, it promotes anti-apoptotic NF-kappa-B signaling and ERK signaling. Plays a role in microglial MTOR activation and metabolism. Regulates age-related changes in microglial numbers. Triggers activation of the immune responses in macrophages and dendritic cells. Mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages. In dendritic cells, it mediates up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival. Involved in the positive regulation of osteoclast differentiation.
Subcellular Location	[Isoform 1]: Cell membrane; Single-pass type I membrane protein.; [Isoform 2]: Secreted.
Database References	KEGG: mmu:83433 STRING: 10090.ENSMUSP00000024791 UniGene: PMID: 29407460 Our data establish a critical link between oAbeta1-42, a major pathological component of Alzheimer's disease and TREM2 PMID: 29587871 These data suggest that the Alzheimer's disease-associated TREM2 R47H variant increases risk for Alzheimer's disease by conferring a loss of TREM2 function and enhancing neuritic dystrophy around plaques. PMID: 29859094 Data indicate a novel role for PS1 in regulating TREM2 intracellular trafficking and pathophysiological function. PMID: 29611543 whereas complete TREM2 deficiency protected against tau-mediated microglial activation and atrophy, TREM2 haploinsufficiency elevated expression of proinflammatory markers and exacerbated atrophy at a late stage of disease. The differential effects of partial and complete loss of TREM2 on microglial function and tau pathology PMID: 30232263 TREM2 plays a crucial role in altering the proinflammatory M1 microglia to M2 phenotype and has beneficial effects in the immune pathogenesis of Parkinson's disease. PMID: 29621548 Overexpression of TREM2 downregulated the levels of IL-1beta, ameliorated T396 expression, inhibited the activity of GSK-3beta, and improved sickness behavior. Increased Arg1 expression and a high level of synaptophysin were also observed in the transgenic mice following TREM2 overexpression. PMID: 29689568 These studies of the role of TREM2 in neuroinflammation and neurodegeneration suggest that impairing microglial TREM2 signaling reduces pure tauopathy. PMID: 29073081 This article suggests a potential explanation of why TREM2-deficient microglia are unable to respond to neurotoxic plaques in the Alzheimer's disease brain and highlight a further need to understand microglial biology. PMID: 28978423 TREM2 protects against cerebral ischemia/reperfusion injury through the aspect of post-ischemic inflammatory response and neuronal apoptosis. PMID: 28592261 Results suggest that TREM2 plays a critical role in inflammation and neuronal cell survival and in neurogenesis. Study showed that TREM2 is a soluble protein transported by macrophages through ventricle walls and choroid plexus, and then enters the brain parenchyma via radial glial cells. TREM2 protein is essential for neuroplasticity and myelination. A lack of TREM2 protein may accelerate aging. PMID: 27662313 TREM2 deficiency influences both acute and chronic responses to traumatic brain injury, with altered macrophage response early on and improved functional outcome at later time points. PMID: 26976047 A central role of TREM2 is in the regulation of microglia response to acute neurotoxic insults. PMID: 28189343 Loss of TREM2 reduces the ability of microglia to engulf amyloid beta-peptide. PMID: 27402340 TREM2 and TREML2 play opposite roles in microglia activation. PMID: 27143430 Our study suggests that Vps35/retromer is responsible for recycling of Trem2 in the regulation of microglial function such as proinflammatory responses, whereas R47H mutation impairs Trem2 trafficking, which might contribute to Alzheimer disease. PMID: 27717139 sTREM2 plays a crucial role in regulating microglial cell survival and inflammatory responses. PMID: 28209725 Microglia in Alzheimer's disease (AD) patients carrying TREM2 risk variants and TREM2-deficient mice with AD-like pathology have abundant autophagic vesicles, as do TREM2-deficient macrophages under growth-factor limitation or endoplasmic reticulum (ER) stress. Study concludes that TREM2 enables microglial responses during AD by sustaining cellular energetic and biosynthetic metabolism. PMID: 28802038 This study demonstrate a critical role of TREM2-mediated Wnt/beta-catenin pathway in microglial viability and suggest that modulating this pathway therapeutically may help to combat the impaired microglial survival. PMID: 28077724 Triggering receptor expressed on myeloid cells 2 (TREM2) is an immunoglobulin-like receptor of the TREM family and is expressed on activated macrophages, immature dendritic cells, osteoclasts, and microglia. PMID: 28398927 TREM2 deficiency may disrupt the formation of a neuroprotective microglia barrier that regulates amyloid compaction and insulation PMID: 27196974 TREM2 deficiency has opposing effects on Alzheimer's disease-related pathologies at early and late stages of disease progression. PMID: 28100745 TREM2 protects from Alzheimer's disease by enabling microglia to surround and alter Abeta plaque structure, thereby limiting neuritic damage. PMID: 27091843 Recent studies have revealed that activated microglia in the spinal dorsal horn exacerbate neuropathic pain, which has suggested that suppression of microglial activity should be considered as a therapeutic target. However, only a few molecules have been identified as regulators of microglial activity. In this study, we focused on a receptor complex of TREM2 and DAP12, both of which are expressed by microglia and have bee PMID: 27798193 The authors demonstrate that a TREM2 loss-of-function mutation causes brain-wide metabolic alterations pointing toward a possible function of microglia in regulating brain glucose metabolism. PMID: 28559417 flow cytometry analyses indicated significantly lower surface expression of T66M TREM2 variant than wild type or other TREM2 variants PMID: 28490631 Study found that TREM2 was upregulated in the brain of P301S mice, an animal model of tau pathology, during disease progression and showed that TREM2 overexpression rescued spatial cognitive impairments and ameliorated neuropathologies including neuronal and synaptic loss as well as tau hyperphosphorylation. PMID: 26802771 This study showed that TREM-2 deficiency restricts the inflammatory response, thereby decreasing organ damage and mortality. PMID: 27253382 TREM2 attenuates tau kinase activity through restriction of neuroinflammation, and thus protects against tau pathology. PMID: 26364736 TREM2 is involved in prion-induced microglial activation but does not noticeably modulate the pathogenesis of experimental prion infections. PMID: 25816748 These findings provide a novel interpretation of Brucella intracellular growth through inhibition of NO production produced by TREM-2-mediated activated macrophages. PMID: 25563793 TREM-1/TREM-3 macrophage expression improved host defense against Klebsiella-derived pneumosepsis, whereas TREM-2 did not have a role. PMID: 25860078 These findings place TREM2 as a key regulator of microglia activation in vivo in response to tissue damage PMID: 25631124 TREM-2 has a protective effect on inflammatory response of endotoxin-induced acute lung injury in mice. PMID: 24916365 results support a role of DAP12 in stabilizing TREM2-CTF, thereby protecting against excessive pro-inflammatory responses. PMID: 25957402 Corpus callosum microglia normally expand with age, but aged Trem2(-/-) mice had fewer microglia with an abnormal morphology which failed to amplify transcripts indicative of activation, phagocytosis, and lipid catabolism in response to myelin damage. PMID: 25893602 Data (including data from studies using knockout mice) suggest that TREM2 is expressed on alveolar macrophages and lung mucosa and plays role innate immunity during pneumococcal pneumonia; knockout of TREM2 increases phagocytosis and survival. PMID: 24945405 viral replication increases lung macrophage levels of intracellular and cell surface TREM-2, and this action prevents macrophage apoptosis PMID: 25897174 TREM2 knockdown reduced microglial activation, decreased phagocytosis of injured neurons and worsened stroke damage. PMID: 25716838 Upon infection with Escherichia coli, the otherwise beneficial effect of an exaggerated early immune response in TREM-2(-/-) animals was counteracted by a 50% reduction in bacterial phagocytosis. PMID: 25477281 important role for TREM2 in inflammatory macrophages and neuroinflammation PMID: 25732305 TREM2 detects damage-associated lipid patterns associated with neurodegeneration, sustaining the microglial response to beta-amyloid accumulation. PMID: 25728668 TREM2 promotes adipogenesis and diet-induced obesity by upregulating adipogenic regulators in conjunction with inhibiting the Wnt10b/beta-catenin signaling pathway. PMID: 25114293 It may play a protective role against aging-related neuroinflammation and cognitive impairment. PMID: 24368090 These data suggest that TREM2 is important for the microglial response to Amyloid-beta deposition PMID: 24893973 Results suggest that an epigenetic mechanism involving an aluminum-triggered, NF-kB-sensitive, miRNA-34a-mediated down-regulation of triggering receptor expressed in myeloid cells 2 (TREM2) expression may impair phagocytic responses. PMID: 23778113 TREM-2-mediated bacterial killing is dependent on the activation of PI3K/Akt signaling. PMID: 24383713 TREM2 protein is expressed only in microglia/macrophages and is developmentally downregulated in a region-dependent manner. PMID: 23977213 TREM2 governs Kupffer cell activation and explains belr1 genetic resistance to malaria liver stage infection. PMID: 24218563 Trem-2 plays an important role in the host defense response to sepsis by enhancing bacterial clearance. PMID: 23721075

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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