Recombinant Human TREM-2 Protein (C-6His)

Name: Recombinant Human TREM-2 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0624NP
Availability: InStock

BL-0624NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality recombinant proteins, Other recombinant proteins, Others immune checkpoint proteins

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Product Overview

Description	Recombinant Human Triggering Receptor Expressed On Myeloid Cells 2 is produced by our Mammalian expression system and the target gene encoding His19-Ser174 is expressed with a 6His tag at the C-terminus.
Accession	Q9NZC2
Synonym	Triggering receptor expressed on myeloid cells 2; TREM-2; Triggering receptor expressed on monocytes 2; TREM2
Gene Background	Triggering Receptor Expressed on Myeloid cells 2 (TREM2)is a 35 kDa type I transmembrane member of the TREM family and Ig superfamily. 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. 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. A positively charged lysine within the transmembrane segment allows association with the signal adapter protein, DAP12 and inhibition of macrophage activation. TREM2 is expressed on macrophages, immature myeloid dendritic cells, osteoclasts, microglia, and adipocytes.It promotes the differentiation and function of osteoclasts, the production of inflammatory cytokines by adipocytes, insulin resistance, and the phagocytic clearance of bacteria.
Molecular Mass	18.3 KDa
Apmol Mass	22-40 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.; [Isoform 3]: Secreted.
Database References	HGNC: 17761 OMIM: 221770 KEGG: hsa:54209 STRING: 9606.ENSP00000362205 UniGene: PMID: 29587871 Data indicate a novel role for PS1 in regulating TREM2 intracellular trafficking and pathophysiological function. PMID: 29611543 Homozygous TREM2 R47C carrier presenting with an FTD rather than an Alzheimer's disease phenotype. PMID: 29748150 Our results suggest that deficiency of microglial TREM2 leads to heightened tau pathology coupled with widespread increases in activated neuronal stress kinases PMID: 29037207 In the current study, we evaluated the rs75932628 polymorphism in the Chinese Han population. However, we did not detect any rs75932628-T in our cohort, indicating that the single nucleotide polymorphism of TREM2 may not be a genetic marker to assess the risk of LOAD in the Chinese Han population. PMID: 29256968 TREM-2 promotes acquired cholesteatoma-induced bone destruction by modulating TLR4 signaling pathway and osteoclasts activation PMID: 27934908 ADAM17 is the main sheddase for the generation of human triggering receptor expressed in myeloid cells (hTREM2) ectodomain and cleaves TREM2 after Histidine 157. Findings reveal a link between shedding of TREM2 and its regulation during inflammatory conditions or chronic neurodegenerative disease in which activity or expression of sheddases might be altered. PMID: 28923481 In rheumatoid arthritis (RA), the expression of TREM-2 was reduced at first and then up-regulated after stimulation by TNF-alpha. TREM-2 also inhibited the activation of TNF-alpha induced of inflammation in RA-fibroblast-like synovial cells (FLSs) by the p38 pathway. PMID: 28869414 TREM2 is shed by proteases of the ADAM (a disintegrin and metalloproteinase domain containing protein) family C-terminal to histidine 157, a position where an AD-associated coding variant has been discovered (p.H157Y) in the Han Chinese population. PMID: 28855300 Selective partial inhibition of cleavage of triggering receptor expressed on myeloid cells 2 TREM2 at H157-Ser158 bond might provide a potential therapeutic strategy for carriers of the Alzheimer's disease-associated H157Y variant and possibly for individuals with wild-type TREM2. PMID: 28855301 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 This study demonstrated that Lower DNA methylation at TREM2 intron 1 caused higher TREM2 mRNA expression in the leukocytes of Alzheimer's disease subjects versus controls and may be a biomarker for Alzheimer's disease. PMID: 28412600 investigated consequences of TREM2 loss of function on microglia transcriptome; microglia lacking TREM2 migrate less towards apoptotic neurons, and outgrowth of microglial processes towards sites of damage in the somatosensory cortex is slowed; the apparent lack of chemotactic stimulation upon depletion of TREM2 is consistent with stable expression profile of genes characterizing the homoeostatic signature of microglia PMID: 28483841 This study shown that Peripheral TREM2 mRNA levels are higher in AD and are associated with AD-related cognitive deficits and hippocampal atrophy. PMID: 28453482 The data of this study provided evidence that the A192T variant in TREM2 could contribute risk for Alzheimer's disease. PMID: 28376694 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 Recent studies have advanced our understanding of TREM2 biology and microglial activities in aging and neurodegenerative brains, providing new insights into TREM2 functions in amyloid plaque maintenance, microglial envelopment of plaque, microglia viability, and the identification of novel TREM2 ligands. PMID: 28442216 In this meta-analysis, genetic datasets demonstrate that TREM2 is a potent risk factor for Parkinson's Disease. PMID: 26365049 High amount of TREM2 mRNA expression in leukocytes is specific to SCZ but not MDD and that changes in TREM2 mRNA expression may be a trait biomarker for SCZ. PMID: 27130565 Its genetic variation contributes to pathogenesis of Alzheimer disease. PMID: 28789839 results indicate that TREM-2 might act as a negative immuno-regulatory molecule...and partially predicts prognosis in lung cancer patients PMID: 27102437 sTREM2 is increased in dominantly inherited Alzheimer's disease after amyloid deposition and neuronal injury PMID: 27974666 Authors find, using a cell-free coat protein complex II (COPII) vesicle budding reaction, that mutant TREM2 is exported efficiently from the ER. Mutant TREM2 becomes sensitive to cleavage by endoglycosidase D under conditions that inhibit recycling to the ER, indicating that it normally reaches a post-ER compartment. PMID: 28768830 Mutations in TREM2 gene are known to cause Nasu-Hakola disease. PMID: 28214109 TREM2 upregulation in the frontal cortex in AD is a late event and may not play a role early in the development of AD pathogenesis and the onset of clinical dementia. PMID: 28365005 Our results suggest that TREM2 expression is increased in Alzheimer's disease and support previous findings that suggest that p.R47H variant affects TREM2 function by altering binding properties of the receptor rather than expression. PMID: 27887626 Data show that protein-altering changes are in PLCG2, ABI3, and TREM2 genes highly expressed in microglia and highlight an immune-related protein-protein interaction network in Alzheimer's disease. PMID: 28714976 Study found that rare variation in TREM2, including two variants within the extracellular Ig-like domain, may be associated with risk for Alzheimer's disease; suggests that impaired overall and cell surface expression of TREM2 may contribute to risk for Alzheimer's disease. PMID: 27589997 Increased DNA methylation near TREM2 is seen in the superior temporal gyrus of patients with Alzheimer's disease PMID: 27522519 results indicated thatTREM2 p.H157Y was associated with an increased risk of Alzheimer's Disease PMID: 27501831 Our work identifies the TREM2-APOE pathway as a major regulator of microglial functional phenotype in neurodegenerative diseases and serves as a novel target that could aid in the restoration of homeostatic microglia. PMID: 28930663 Found increased Alzheimer's disease risk associated with several TREM2 variants, and show that these variants decreased or markedly increased binding to TREM2 ligands. Results suggest that TREM2 signaling helps protect against Alzheimer's disease but can cause harm in excess, supporting the idea that proper TREM2 function is important to counteract disease progression. PMID: 27520774 SNPs involved in pathways related to virus cellular entry and vesicular trafficking were overrepresented, suggesting that cerebrospinal fluid soluble TREM2 levels could be an informative phenotype for Alzheimer disease PMID: 26754641 Its mutation plays a role in pathogenesis of Alzheimer's disease. PMID: 27084067 Rare coding variants of TREM2 may play an important role in AD in Han Chinese. PMID: 27067662 These data demonstrate that cerebrospinal fluid soluble TREM2 levels are increased in the early symptomatic phase of Alzheimer's disease, probably reflecting a corresponding change of the microglia activation status in response to neuronal degeneration. PMID: 26941262 link three genetic risk factors for Alzheimer's disease and reveal a possible mechanism by which mutant TREM2 increases risk of AD PMID: 27477018 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 TREM2 deficiency may disrupt the formation of a neuroprotective microglia barrier that regulates amyloid compaction and insulation PMID: 27196974 flow cytometry analyses indicated significantly lower surface expression of T66M TREM2 variant than wild type or other TREM2 variants PMID: 28490631 silencing TREM-2 downregulated the expression levels of Bcl2 and PCNA, and upregulated the expression levels of Bax and caspase-3 in renal cell carcinoma cells. Depletion of TREM-2 inactivated PI3K/Akt pathway through increasing the expression of PTEN. TREM-2 acts as an oncogene in the development of renal cell carcinoma and can be considered as a novel therapeutic factor in the treatment of renal cell carcinoma. PMID: 27779645 TREM2 expression is significantly upregulated in human masticatory mucosa during wound healing PMID: 28005267 this study shows that activation of TREM-2 may restrain h-MSC immune activation and promote differentiation for tissue repair PMID: 26079507 The TREM family members are also considered to involve in Alzheimer's disease (AD) and cerebrospinal fluid (CSF) soluble form of TREM2 (sTREM2) levels has also been associated with respond to progression of disease. PMID: 27769848 Study provides evidence that TREM2 mRNA is upregulated in the human hippocampus affected by Alzheimer's disease (AD). Findings also suggest that 5hmC may play a role in regulating TREM2 mRNA expression in AD hippocampus. PMID: 27051467 The study suggests that TREM2 may work as an oncogene and a new effective therapeutic target for glioma treatment. PMID: 26506595 CSF concentrations of soluble TREM2 are higher in Alzheimer's disease than in controls PMID: 26754172 Variant p.R47H of TREM2 was not associated with Parkinson's disease PMID: 26651418 Our results corroborate and extend previous findings, concluding that the variant rs75932628-T (p.R47H) in TREM2 is not a risk factor for leucoaraiosis or Parkinson's disease in the Han Chinese population. PMID: 26758262 the minor T allele at TREM2 (p.R47H, rs75932628) showed nominally significant association with AD risk (OR 5 5.73, 95% CI 5 1.80-18.25, P 5 .0232), whereas no significant association for risk of frontotemporal lobar degeneration (FTLD), amyotrophic lateral sclerosis (ALS), and Parkinson's disease. PMID: 25936935

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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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