Recombinant Human c-MER Protein

Name: Recombinant Human c-MER Protein
Brand: Beta LifeScience
SKU: BL-0474SG
Availability: InStock

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Tag	GST
Host Species	Human
Accession	NM_006343
Synonym	MER, MERTK, MGC133349
Background	c-MER is a tyrosine kinase and a member of the MER/AXL/TYRO3 receptor kinase family (1). The c-MER gene encodes a transmembrane protein with two fibronectin type-III domains, two Ig-like C2-type domains, and one tyrosine kinase domain. Functional knockout of c-MER in mice shows the mice to have macrophages deficient in the clearance of apoptotic thymocytes thereby demonstrating the critical role for c-MER in the engulfment and efficient clearance of apoptotic cells. Defects in c-MER have been associated with retinitis pigmentosa, a phenotype that can be reversed by replacement of the c-MER gene product (2).
Description	Recombinant human c-MER (528-end) was produced by baculovirus in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods.
Source	Sf9 insect cells
AA Sequence	528a.a.-end
Molecular Weight	~82 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Active
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human c-MER Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis). Ligand binding at the cell surface induces autophosphorylation of MERTK on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with GRB2 or PLCG2 and induces phosphorylation of MAPK1, MAPK2, FAK/PTK2 or RAC1. MERTK signaling plays a role in various processes such as macrophage clearance of apoptotic cells, platelet aggregation, cytoskeleton reorganization and engulfment. Functions in the retinal pigment epithelium (RPE) as a regulator of rod outer segments fragments phagocytosis. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3.
Subcellular Location	Membrane; Single-pass type I membrane protein.
Protein Families	Protein kinase superfamily, Tyr protein kinase family, AXL/UFO subfamily
Database References	HGNC: 7027 OMIM: 604705 KEGG: hsa:10461 STRING: 9606.ENSP00000295408 UniGene: PMID: 29437494 We observed that the frequency for the wild-type haplotype was higher in the control group, compared to that in the group of patients with COPD, in the subgroup analysis of current smokers, although the difference was not statistically significant PMID: 29359540 Study describes a novel cellular pathway involved in diabetic efferocytosis, wherein diabetes-induced decrease in miR-126 expression results in upregulation of ADAM9 expression that in-turn leads proteolytic cleavage of MerTK and formation of inactive soluble Mer. Decrease in MerTK phosphorylation leads to reduced downstream cytoskeletal signaling required for engulfment and thus decreases efferocytosis. PMID: 27827458 Phosphatidylserine mediated hyperactivation of Mertk.MERTK promotes epithelial cell efferocytosis in a tyrosine kinase-dependent manner.MERTK role in AKT-dependent drug resistance. PMID: 28184013 STK 11 testing can confirm those at risk of Peutz-Jeghers syndrome, who require lifelong surveillance, and possibly release those with a simple dermatosis, such as Laugier-Hunziker syndrome, from invasive and thus potentially harmful surveillance. PMID: 26768676 The broad-spectrum activity mediated by UNC2025 in leukemia patient samples and xenograft models, alone or in combination with cytotoxic chemotherapy, supports continued development of MERTK inhibitors for treatment of leukemia PMID: 27649555 The expression of MerTK and AxlTK varied according to the deposition of immunoglobulin and complements on glomeruli. Both MerTK and AxlTK expressions were increased on glomeruli and varied according to pathological classifications. PMID: 28127639 Study identified the Gas6/TAM receptor pathway with Tyro3 and Mer as novel targets in colorectal cancer. PMID: 27486820 MERTK is frequently overexpressed in head and neck squamous cell carcinoma and plays an important role in tumor cell motility. PMID: 27081701 these data suggest that endogenous GAS6 and Mer receptor signaling contribute to the establishment of prostate cancer stem cells in the bone marrow microenvironment PMID: 27028863 Sequence analysis revealed that the proband was a compound heterozygote with two independent mutations in MERTK, a novel nonsense mutation (c.2179C > T) and a previously reported missense variant (c.2530C > T). The proband's affected brother also had both mutations PMID: 28462455 this study shows that viral infection sensitizes fetal membranes by MERTK Inhibition PMID: 28916522 Knockdown of MERTK by shRNA in prostate cancer cells induced a decreased ratio of P-Erk1/2 to P-p38, increased expression of p27, NR2F1, SOX2, and NANOG, induced higher levels of histone H3K9me3 and H3K27me3, and induced a G1/G0 arrest, all of which are associated with dormancy. PMID: 27753136 MERTK G > A variant affects liver disease, nutrient oxidation and glucose metabolism in NAFLD. PMID: 28334911 Monocyte-induced MerTK cleavage on proreparative MHCII(LO) cardiac macrophages is a novel contributor to myocardial ischemic reperfusion injury. PMID: 28851810 Patients with macroalbuminuria diabetes had higher circulating levels of sMer and more urinary soluble Tyro3 and sMer than normoalbuminuric diabetics. Increased clearance of sTyro3 and sMer was associated with loss of tubular Tyro3 and Mer expression in diabetic nephropathy tissue. During in vitro diabetes, human kidney cells had down-regulation of Tyro3 and Mer mRNA and increased shedding of sTyro3 and sMer. PMID: 28668213 evidence that proteolytic cleavage of the macrophage efferocytosis receptor c-Mer tyrosine kinase (MerTK) reduces efferocytosis and promotes plaque necrosis and defective resolution. PMID: 28067670 Small molecule and antibody inhibitors of AXL and MER have recently been described, and some of these have already entered clinical trials. The optimal design of treatment strategies to maximize the clinical benefit of these AXL and MER targeting agents are discussed in relation to the different cancer types and the types of resistance encountered. PMID: 28251492 A 48 bp insertion sequence was buried within the breakpoint; 18 bps shared homology to MIR4435-2HG and LINC00152, and 30 bp mapped to MERTK. The deletion cosegregated with arRP in the family. PMID: 28324114 In this paper, we review the biology of the Gas6/Tyro3, Axl, and MerTK(collectively named TAM system)and the current evidence supporting its potential role in the pathogenesis of multiple sclerosis . PMID: 27801848 The rs4374383 AA genotype, associated with lower intrahepatic expression of MERTK, is protective against F2-F4 fibrosis in patients with non-alcoholic fatty liver disease (NAFLD). PMID: 26596542 We report a novel missense mutation (c.3G>A, p.0?) in the MERTK gene that causes severe vision impairment in a patient. PMID: 27122965 Utilizing an ex vivo co-cultivation approach to model key cellular and molecular events found in vivo during infarction, cardiomyocyte phagocytosis was found to be inefficient, in part due to myocyte-induced shedding of macrophage MERTK PMID: 26316303 Upon differentiation of these iPSC towards RPE, patient-specific RPE cells exhibited defective phagocytosis, a characteristic phenotype of MERTK deficiency observed in human patients and animal models PMID: 26263531 The current study demonstrates the contribution of the TAM receptor MerTK to the phagocytosis of myelin by human adult microglia and monocyte-derived macrophages. PMID: 26962228 One of the associated variants was also found to be linked with increased expression of MERTK in monocytes and higher expression of MERTK was associated with either increased or decreased risk of developing MS, dependent upon HLA-DRB1*15:01 status. PMID: 26990204 Combined Mertk (and Mfge8) deficiency in macrophages blunted VEGFA release from infarcted hearts. PMID: 26819373 Studies indicate that c-Mer receptor tyrosine kinase MERTK mutations cause retinal degenerations. PMID: 26427420 Data indicate that AAV2-VMD2-c-mer proto-oncogene protein (hMERTK) provided up to 6.5 months photoreceptor rescue in the RCS rat, and also had a major protective effect in Mertk-null mice. PMID: 26427450 Data show that activated AMP-activated protein kinase (AMPK) limits retinal pigment epithelial cells (RPE) phagocytic activity by abolishing retinal photoreceptor cell outer segment (POS)-induced activation of c-mer proto-oncogene tyrosine kinase (MerTK). PMID: 26427488 The mRNA expression levels of Tyro-3, Axl were decreased in pSS patients. When considering the plasma level, increased levels of soluble Mer was observed with statistically significant difference. PMID: 25881761 Mer enhances malignant phenotype and pharmacological inhibition of Mer overcomes resistance of non-small cell lung cancer to EGFR-targeted agents. PMID: 25826078 results identify Mer as a receptor uniquely capable of both tethering ACs to the macrophage surface and driving their subsequent internalization. PMID: 25695599 UNC1666 is a novel potent small molecule tyrosine kinase inhibitor that decreases oncogenic signaling and myeloblast survival by dual Mer/Flt3 inhibition. PMID: 25762638 Significantly increased levels of sMer, sTyro3 and sAxl may be important factors contributing to the deficit in phagocytosis ability in systemic lupus erythematosus . PMID: 25878564 MERTK on DCs controls T cell activation and expansion through the competition for PROS1 interaction with MERTK in the T cells. MERTK is a potent suppressor of T cell response. PMID: 25624460 Inhibition of the Gas6 receptor Mer or therapeutic targeting of Gas6 by warfarin is a promising strategy for the treatment of multiple myeloma. PMID: 25102945 Mer expression correlates with CNS positivity upon initial diagnosis in t(1;19)-positive pediatric acute lymphoblastic leukemia patients. PMID: 25428221 Patients with ACLF have increased numbers of immunoregulatory monocytes and macrophages that express MERTK and suppress the innate immune response to microbes. The number of these cells correlates with disease severity and the inflammatory response. PMID: 25479139 The key role of the MERTK could be demonstrated in HMDM engulfing dying cells using gene silencing as well as blocking antibodies. Similar pathways were found upregulated in living ARPE-19 engulfing anoikic ARPE-19 cells. PMID: 25450174 These studies demonstrate that, despite their similarity, TYRO3, AXL, and MER are likely to perform distinct functions in both immunoregulation and the recognition and removal of apoptotic cells PMID: 25074926 These data collectively identify MERTK as a significant link between cancer progression and efferocytosis, and a potentially unrealized tumor-promoting event when MERTK is overexpressed in epithelial cells. PMID: 25074939 Both mMer and sMer levels significantly increased in SLE and positively correlated with disease activity and severity. The upregulation of MerTK expression may serve as a biomarker of the disease activity and severity of SLE. PMID: 24741600 The MER receptor pathway promotes wound repair in macrophages and epithelial cell growth. PMID: 24939420 MerTK expression in circulating innate immune cells is increased in patients with septic shock in comparison with healthy volunteers and trauma patients and its persistent overexpression after septic shock is associated with adverse outcome. PMID: 23835724 MERTK has a role in regulating melanoma cell migration and survival and differentially regulates cell behavior relative to AXL PMID: 23617806 data suggest a role for Mer in acute myeloid leukemogenesis and indicate that targeted inhibition of Mer may be an effective therapeutic strategy in pediatric and adult AML PMID: 23474756 [review] Receptor tyrosine kinases Tyro-3, Axl and Mer, collectively designated as TAM, are involved in the clearance of apoptotic cells. PMID: 23662598 These results indicate that Mer and Axl have complementary and overlapping roles in Non-small cell lung cancer PMID: 22890323 MERTK signaling in the retinal pigment epithelium involves a cohort of SH2-domain proteins with the potential to regulate both cytoskeletal rearrangement and membrane movement. PMID: 23390493

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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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