AXL Protein, Human (Biotinylated, HEK293, His-Avi)

The AXL protein, a receptor tyrosine kinase, serves as a key mediator in transducing signals from the extracellular matrix into the cytoplasm by binding the growth factor GAS6, thereby regulating diverse physiological processes such as cell survival, proliferation, migration, and differentiation. Ligand binding at the cell surface induces AXL dimerization and autophosphorylation. Upon activation, AXL interacts with and induces the tyrosine phosphorylation of various downstream signaling molecules, including PI3-kinase subunits (PIK3R1, PIK3R2, and PIK3R3), GRB2, PLCG1, LCK, PTPN11, CBL, NCK2, SOCS1, and TNS2. This triggers the recruitment of GRB2 and regulatory subunits of phosphatidylinositol 3 kinase, leading to the downstream activation of the AKT kinase. The GAS6/AXL signaling axis plays a pivotal role in various processes such as endothelial cell survival, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, and the regulation of thrombotic responses. Additionally, AXL is involved in inhibiting Toll-like receptors (TLRs)-mediated innate immune responses, and in the context of microbial infection, it acts as a receptor for lassa virus and lymphocytic choriomeningitis virus, possibly through GAS6 binding to phosphatidyl-serine at the surface of the virion envelope.