Description
Proto-oncogene tyrosine-protein kinase MER (MERTK) is a member of the MER/AXL/TYRO3 receptor kinase family and encodes a transmembrane protein with two fibronectin type-III domains, two Ig-like C2-type (immunoglobulin-like) domains, and one tyrosine kinase domain. MERTK is localized in the membrane and is no expressed in normal B-and T-lymphocytes but is expressed in numerous neoplastic B-and T-cell lines. This protein is highly expressed in the testis, ovary, prostate, lung, and kidney, with lower expression in the spleen, small intestine, colon, and liver. MERTK 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. MERTK signaling plays a role in various processes such as macrophage clearance of apoptotic cells, platelet aggregation, cytoskeleton reorganization, and engulfment. MERTK plays also an important role in the inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces the production of suppressors of cytokine signaling SOCS1 and SOCS3. Defects in MERTK are the cause of retinitis pigmentosa type 38.
Form
Lyophilized from sterile 100mM NaCl, 50mM Tris, pH 7.5, 5 % trehalose, 5% mannitol and 0.01% Tween80.
Molecular Mass
The recombinant human Mer consists of 485 amino acids and predicts a molecular mass of 54 kDa. As a result of glycosylation, the rhMer migrates as approximately 110-120 kDa band in SDS-PAGE under reducing conditions.
