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Mouse Mertk Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
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- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | Q60805 |
| Reactivity | Mouse, Rat |
| Host | Rabbit |
| Clonality | polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 110157 Da |
| Gene ID | 17289 |
|---|---|
| Other Names | Tyrosine-protein kinase Mer, Proto-oncogene c-Mer, Receptor tyrosine kinase MerTK, Mertk, Mer |
| Target/Specificity | This Mouse Mertk antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 946-980 amino acids from the C-terminal region of mouse Mertk. |
| Dilution | WB~~1:1000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Mouse Mertk Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | Mertk |
|---|---|
| Synonyms | Mer |
| 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. Also plays 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. |
| Cellular Location | Cell membrane {ECO:0000250|UniProtKB:Q12866}; Single-pass type I membrane protein |
| Tissue Location | Expressed predominantly in the hematopoietic lineages: macrophages, NK cells, NKT cells, dendritic cells and platelets. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
References
Graham D.K.,et al.Oncogene 10:2349-2359(1995).
Dowds C.A.,et al.Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
Lu Q.,et al.Nature 398:723-728(1999).
Georgescu M.M.,et al.Mol. Cell. Biol. 19:1171-1181(1999).
Behrens E.M.,et al.Eur. J. Immunol. 33:2160-2167(2003).
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