HGFR Protein, Human (Active, sf9, His-GST)

The HGFR protein, a receptor tyrosine kinase, functions as a signal transducer from the extracellular matrix by binding to hepatocyte growth factor/HGF ligand. It plays a pivotal role in regulating diverse physiological processes, including proliferation, scattering, morphogenesis, and cell survival. Upon ligand binding at the cell surface, HGFR undergoes autophosphorylation on its intracellular domain, creating docking sites for downstream signaling molecules. Upon activation by ligand, it interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3, or the adapter GAB1, leading to the activation of multiple signaling cascades, including RAS-ERK, PI3 kinase-AKT, and PLCgamma-PKC. RAS-ERK activation is associated with morphogenetic effects, while PI3K/AKT coordinates prosurvival effects. In embryonic development, HGFR signaling contributes to gastrulation, the development and migration of neuronal precursors, angiogenesis, and kidney formation. During skeletal muscle development, it is crucial for the migration of muscle progenitor cells and the proliferation of secondary myoblasts. In adults, it participates in wound healing, organ regeneration, tissue remodeling, and promotes the differentiation and proliferation of hematopoietic cells. Additionally, in the context of microbial infection, HGFR acts as a receptor for Listeria monocytogenes internalin InlB, mediating the entry of the pathogen into cells.