HGFR Protein, Human (HEK293, hFc)

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

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.

1.This product does not contain protein kinase domain.
2.Measured by its binding ability in a functional ELISA. Immobilized MET at 2 μg/mL can bind Anti-MET recombinant antibody and the EC₅₀ is 0.8123-1.572 ng/mL.

Human

HEK293

C-hFc

P08581-1 (E25-T932)

4233  [NCBI]

Extracellular Domain

ECKEALAKSEMNVNMKYQLPNFTAETPIQNVILHEHHIFLGATNYIYVLNEEDLQKVAEYKTGPVLEHPDCFPCQDCSSKANLSGGVWKDNINMALVVDTYYDDQLISCGSVNRGTCQRHVFPHNHTADIQSEVHCIFSPQIEEPSQCPDCVVSALGAKVLSSVKDRFINFFVGNTINSSYFPDHPLHSISVRRLKETKDGFMFLTDQSYIDVLPEFRDSYPIKYVHAFESNNFIYFLTVQRETLDAQTFHTRIIRFCSINSGLHSYMEMPLECILTEKRKKRSTKKEVFNILQAAYVSKPGAQLARQIGASLNDDILFGVFAQSKPDSAEPMDRSAMCAFPIKYVNDFFNKIVNKNNVRCLQHFYGPNHEHCFNRTLLRNSSGCEARRDEYRTEFTTALQRVDLFMGQFSEVLLTSISTFIKGDLTIANLGTSEGRFMQVVVSRSGPSTPHVNFLLDSHPVSPEVIVEHTLNQNGYTLVITGKKITKIPLNGLGCRHFQSCSQCLSAPPFVQCGWCHDKCVRSEECLSGTWTQQICLPAIYKVFPNSAPLEGGTRLTICGWDFGFRRNNKFDLKKTRVLLGNESCTLTLSESTMNTLKCTVGPAMNKHFNMSIIISNGHGTTQYSTFSYVDPVITSISPKYGPMAGGTLLTLTGNYLNSGNSRHISIGGKTCTLKSVSNSILECYTPAQTISTEFAVKLKIDLANRETSIFSYREDPIVYEIHPTKSFISGGSTITGVGKNLNSVSVPRMVINVHEAGRNFTVACQHRSNSEIICCTTPSLQQLNLQLPLKTKAFFMLDGILSKYFDLIYVHNPVFKPFEKPVMISMGNENVLEIKGNDIDPEAVKGEVLKVGNKSCENIHLHSEAVLCTVPNDLLKLNSELNIEWKQAISSTVLGKVIVQPDQNFT

Approximately 110 (β chain Fc chimera)&45-50 (α chain) kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

≥ 90%, as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of PBS, 6% trehalose, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. /biology-dictionary/lox-imvi-cell.html