Recombinant Mouse MERTK Protein

Beta LifeScience SKU/CAT #: BLA-9956P

Recombinant Mouse MERTK Protein

Beta LifeScience SKU/CAT #: BLA-9956P
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Product Overview

Host Species Mouse
Accession Q60805
Synonym c MER c mer proto oncogene tyrosine kinase c-mer cMER cmer protooncogene tyrosine kinase Eyk MER MER receptor tyrosine kinase MERK MERPEN Mertk MERTK c-mer proto-oncogene tyrosine kinase MERTK_HUMAN MGC133349 nmf12 Nyk Proto oncogene tyrosine protein kinase MER Proto oncogene tyrosine protein kinase MER precursor Proto-oncogene c-Mer Receptor tyrosine kinase MerTK RP38 STK kinase Tyrosine-protein kinase Mer
Description Recombinant Mouse MERTK Protein was expressed in Baculovirus infected Sf9 cells. It is a Protein fragment
Source Baculovirus infected Sf9 cells
Purity >80% SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity The specific activity of this protein was 32 nmol/min/mg in a kinase assay using Poly (4:1 Glu, Tyr) synthetic peptide as substrate.
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped on Dry Ice. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.

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
Tissue Specificity Expressed predominantly in the hematopoietic lineages: macrophages, NK cells, NKT cells, dendritic cells and platelets.

Gene Functions References

  1. These results suggest that MerTK inhibition impaired phagocytic function of the retina PMID: 29310530
  2. MerTK does not play an essential role in the phagocytosis of S. aureus but attenuates inflammation induced by staphylococcal LTA through blocking NF-kappaB activation. PMID: 28528507
  3. Tumor macrophage expression of Mertk is a therapeutic target to prevent tumor recurrence following radiation therapy. PMID: 27602953
  4. Hypercapnic Acidosis Regulates Mer Tyrosine Kinase Receptor Shedding and Activity. PMID: 29286859
  5. GC B cell-intrinsic sensing of self-RNA, but not self-DNA, from dead cells in GCs drives enhanced GC responses in Mer(-/-) mice. Mer loss in dendritic cells promotes enhanced T cell activation and proinflammatory cytokine production. Mer immunoregulatory signaling in APCs regulates B cell selection and autoimmunity. The phagocytic and immunomodulatory functions of Mer regulate GC responses preventing autoimmunity. PMID: 29118245
  6. this study shows that viral infection sensitizes fetal membranes by MERTK Inhibition PMID: 28916522
  7. Monocyte-induced MerTK cleavage on proreparative MHCII(LO) cardiac macrophages is a novel contributor to myocardial ischemic reperfusion injury. PMID: 28851810
  8. 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
  9. these results suggest, for the first time, that MerTK is an intracellular negative feedback regulator that inhibits the inflammatory response of lipoteichoic acid -stimulated macrophages PMID: 27419619
  10. the reciprocal activation of Axl and Mer receptor tyrosine kinases has a major impact on the outcome of renal inflammation. PMID: 27527599
  11. Reduced transcription of Mertk, rather than differences in MERTK protein structure, determines the reduced efficiency of apoptotic cell clearance in the Aath4a(DBA/DBA) mice, which, in turn, contributes to their increased susceptibility to atherosclerosis. PMID: 28473436
  12. Axl, Mertk and Tyro3 receptors are not required for Zika virus entry and infection. PMID: 28423319
  13. Signaling through the Mer proto-oncogene tyrosine kinase (MerTK) receptor in cultured macrophages and in sterile inflammation in vivo promotes specialized proresolving mediator (SPM) biosynthesis by a mechanism involving an increase in the cytoplasmic:nuclear ratio of a key SPM biosynthetic enzyme, 5-lipoxygenase. PMID: 27199481
  14. These studies define the clearance of infected, apoptotic neutrophils by dendritic cells and Mer receptor signaling as central to the early immune evasion strategies of L. major. PMID: 26658192
  15. Tyro3 gene dosage modulates Mertk-associated retinal degeneration, provide strong evidence for a direct role for TYRO3 in RPE phagocytosis, and suggest that an eQTL can modify a recessive Inherited photoreceptor degenerations. PMID: 26656104
  16. Activation of Mertk synergized with interferon-beta to tighten cell junctions and prevent virus transit across brain microvascular endothelial cells. PMID: 26523970
  17. results establish TAM receptors as both controllers of microglial physiology and potential targets for therapeutic intervention in central nervous system disease PMID: 27049947
  18. Loss of Mertk alters expression of micrornas in retinal pigment epithelial cells. PMID: 25604732
  19. These results suggest that TAM receptors support NSCs survival, proliferation and differentiation by regulating expression of neurotrophins, especially the nerve growth factor. PMID: 25514676
  20. Mertk deficiency affects not only phagocytosis but also cell shape and migration PMID: 25617898
  21. The results indicate that Axl and Mer receptors cooperatively regulate the systemic immune tolerance to male germ cell antigens. PMID: 25403570
  22. Enhanced Mer signaling during the recovery phase increases the abundance and activity of LXR to inactivate the inflammatory response in macrophages PMID: 25714463
  23. nuclear receptor agonists increase MerTK and Axl expression on plaque-associated immune cells, consequently licensing their phagocytic activity and promoting plaque clearance. PMID: 25904803
  24. Mertk expression is required for optimal B-cell antigen presentation, which is, in turn, required in this model for optimal T cell activation and subsequent T cell-dependent B cell differentiation. PMID: 24768065
  25. adiponectin elicited Mer expression and Mer-dependent efferocytosis in macrophages similar to cells stimulated with C1q. PMID: 24942043
  26. Optimal TAM signaling requires coincident TAM ligand engagement of both its receptor and the phospholipid phosphatidylserine regulating TAM receptor tyrosine kinases Tyro3, Axl, and Mer and their ligands Gas6 and Protein S. PMID: 25265470
  27. data suggest that MerTK cleavage contributes to the acute regulation of RPE phagocytosis by limiting POS binding to the cell surface. PMID: 25538233
  28. Inhibition of the Gas6 receptor Mer or therapeutic targeting of Gas6 by warfarin reduced myeloma burden and improved survival in a systemic model of myeloma. PMID: 25102945
  29. Mer mediates quiescence and chemotherapy resistance in a CNS co-culture model and causes CNS infiltration in immunodeficient mice. PMID: 25428221
  30. Data indicate that TAM receptor tyrosine kinases Axl and Mer had distinct roles as phagocytic receptors. PMID: 25194421
  31. Data indicate that MerTK, a receptor kinase, was essential for the engulfment of pyrenocytes by the central macrophages at erythroblastic islands. PMID: 24659633
  32. Data collectively and directly link efferocytosis to wound healing in the heart and identify Mertk as a significant link between acute inflammation resolution and organ function. PMID: 23836795
  33. the engulfment of apoptotic cells by resident peritoneal macrophages proceeds in two steps: binding to Tim4, a PtdSer receptor, followed by MerTK-mediated cell engulfment PMID: 24515440
  34. Axl and Mer (TAM) receptor tyrosine kinases (RTKs) developed persistent inflammatory liver damage resembling AIH. Tyro3(-/-)Axl(-/-)Mer(-/-) triple mutant (TAM(-/-)) mice exhibited chronic hepatitis PMID: 23799121
  35. Adult brain neurogenesis is reduced in the hippocampus of the Tyro3-/-Axl-/-Mertk-/- triple-knockout & Axl-/-Mertk-/- double-knockout mouse brains, but not in single Mertk-/- knockouts. PMID: 24244024
  36. Chronic systemic inflammation and autoimmune disorders in the Tyro3, Axl and Mertk knockout mice cause neuronal damage and death. PMID: 23840307
  37. studies reveal a novel role for astrocytes in mediating synapse elimination in the developing and adult brain, identify MEGF10 and MERTK as critical proteins in the synapse remodelling underlying neural circuit refinement PMID: 24270812
  38. Data indicate the two phagocytic proteins, Mer receptor tyrosine kinase (MerTK) and Milk fat globule EGF-like factor 8 (MFG-E8), were transiently up-regulated by macrophages/microglia after focal brain ischemia in vivo. PMID: 24101459
  39. Data indicate that azoxymethane (AOM) and dextran sulfate sodium (DSS)-induced inflammation-associated cancer is exacerbated in mice lacking Axl and Mer receptor tyrosine kinases. PMID: 23878224
  40. MerTK signaling may suppress antitumor immunity through suppression of CD8+ T lymphocyte proliferation. PMID: 23867499
  41. Mer deficiency in knockout mice results in long-term accumulation of apoptotic cells primarily in germinal centers and not in the T cell zone, marginal zone, or red pulp areas of the spleen. PMID: 23319738
  42. Results demonstrate that Protein S and Gas6 function as independent, bona fide Mer ligands, and are, to a first approximation, interchangeable with respect to Mer-driven phagocytosis in the retina. PMID: 23259948
  43. Mer of the TAM-family receptors is responsible for mediating transcriptional HGF production through a RhoA-dependent pathway. PMID: 22740630
  44. These results suggest that tubby is a ligand to facilitate microglial phagocytosis through MerTK for the maintenance of CNS homeostasis. PMID: 22884297
  45. Inhibiting Mer receptor tyrosine kinase suppresses STAT1, SOCS1/3, and NF-kappaB activation and enhances inflammatory responses in lipopolysaccharide-induced acute lung injury. PMID: 22427680
  46. Novel insight into the mechanism of TAM RTKs (Tyro3, Axl, Mer receptor tyrosine kinases)in regulating male fertility. PMID: 19602523
  47. A TRIF-mediated pattern recognition receptor signaling cascade requires NADPH oxidase to activate PKCdelta and then p38, culminating in ADAM17-mediated proteolysis of MerTK. PMID: 21828049
  48. TNF family members play a role in protecting photoreceptors of Mertk(nmf12) homozygotes from cell death. PMID: 21436282
  49. ERG from mer(kd) mice of different ages showed inner retinal dysfunction in mer(kd) mice. This and faster degeneration in mer(kd) mice may produce retinal environment unresponsive to neuroprotection from subretinal electrical stimulation. PMID: 21467171
  50. disrupted expression leads to enhanced marginal zone B-cell responses PMID: 20822883


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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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