Mer Protein, Mouse (sf9, His-GST)

Mer protein is a receptor tyrosine kinase that transduces signals by binding to ligands such as LGALS3, TUB, TULP1 or GAS6. Mer is critical in processes such as cell survival, migration, differentiation, and phagocytosis of apoptotic cells, and autophosphorylation occurs upon ligand binding. Mer Protein, Mouse (sf9, His-GST) is the recombinant mouse-derived Mer protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag. The total length of Mer Protein, Mouse (sf9, His-GST) is 295 a.a., with molecular weight of ~58 kDa.

The Mer protein is a receptor tyrosine kinase that mediates cellular signaling from the extracellular matrix to the cytoplasm through binding to ligands such as LGALS3, TUB, TULP1, or GAS6. It plays a crucial role in various physiological processes, including cell survival, migration, differentiation, and the phagocytosis of apoptotic cells. Activation of Mer by ligand binding leads to autophosphorylation on its intracellular domain, creating binding sites for downstream signaling molecules. This, in turn, triggers interactions with GRB2 or PLCG2 and subsequent phosphorylation of MAPK1, MAPK2, FAK/PTK2, or RAC1. Mer signaling is involved in macrophage clearance of apoptotic cells, platelet aggregation, cytoskeleton reorganization, and engulfment. Notably, within the retinal pigment epithelium (RPE), Mer serves as a regulator of phagocytosis of rod outer segment fragments. Additionally, Mer plays a pivotal role in inhibiting the innate immune response triggered by Toll-like receptors (TLRs) by activating STAT1, which selectively induces the production of suppressors of cytokine signaling SOCS1 and SOCS3.

Mouse

Sf9 insect cells

N-His;N-GST

Q60805 (E573-Y867)

17289  [NCBI]

Approximately 58 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.