Human CD136/MST1R (His Tag) recombinant protein

Human CD136/MST1R (His Tag) recombinant protein

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Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to MST1 ligand. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces autophosphorylation of RON on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1 or the adapter GAB1. Recruitment of these downstream effectors by RON leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. RON signaling activates the wound healing response by promoting epithelial cell migration, proliferation as well as survival at the wound site. Plays also a role in the innate immune response by regulating the migration and phagocytic activity of macrophages. Alternatively, RON can also promote signals such as cell migration and proliferation in response to growth factors other than MST1 ligand.

Macrophage-stimulating protein receptor

FV2; MST1R; RON; CDW136; FV-2; STK; CD136; PTK8

Q04912

MST1R; PTK8; RON

Human Cells

A DNA sequence encoding the amino acid sequence (Met 1-Leu 571) of human CD136 (Q04912) extracellular domain was fused with a polyhistidine tag at the C-terminus.

Human

The secreted recombinant human CD136 consists of 558 amino acids, including the ? chain (Glu 25-Arg 309) and the polyhistidine-tagged ? chain (Gly 310-Leu 517), and predictes a molecular mass of 60 kDa. (30+30 kDa). As a result of glycosylation, in SDS-PAGE under reducing conditions, the apparent molecular mass of rhCD136 is approximately 70 kDa and 37 kDa, corresponding to the single chain and the cleaved two subunits respectively.

> 98 % as determined by SDS-PAGE