HGFR Protein, Canine (HEK293, Fc)

The HGFR protein is a receptor tyrosine kinase that transduces signals by binding to hepatocyte growth factor/HGF. It regulates proliferation, scattering, morphogenesis, and cell survival. HGFR Protein, Canine (HEK293, Fc) is the recombinant canine-derived HGFR protein, expressed by HEK293, with C-hFc labeled tag.

The HGFR protein, a receptor tyrosine kinase, serves as a critical transducer of signals from the extracellular matrix by binding to hepatocyte growth factor/HGF ligand. It plays a pivotal role in regulating various physiological processes, including proliferation, scattering, morphogenesis, and cell survival. Upon ligand binding at the cell surface, MET undergoes autophosphorylation on its intracellular domain, creating docking sites for downstream signaling molecules. Upon activation, HGFR interacts with PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3, or the adapter GAB1, leading to the activation of multiple signaling cascades, such as 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, muscle and neuronal precursor development and migration, angiogenesis, and kidney formation. 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, facilitating the entry of the pathogen into cells.

Canine

HEK293

C-hFc

Q75ZY9 (E25-L935)

403438

Approximately 35-40 kDa and 110-120 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.