Analytics cookies help us understand what works in the catalog. Accept all, reject non-essential ones, or choose categories below. Privacy policy
Recombinant human hepatocyte growth factor, a two-chain glycoprotein of ~90 kDa and the only known ligand of the c-Met receptor. Not a peptide. A research reagent (RUO) for work on liver regeneration, anti-fibrosis and c-Met signalling.
Size: 10 µg
No published analyses yet.
Titration schedule · reference
The information below is provided from public sources for reference only. It is not advice or instructions for use; products are intended for laboratory research only and not for human consumption.
| Period / condition | Dose | Escalation |
|---|---|---|
| Phase I/II clinical (IV infusion ~3 h, daily 12–14 days) | 0.6 mg/m² per day | Only studied dose |
| Planned escalation in the same protocol | up to 1.2–2.4 mg/m² per day | Not reached in the trial |
| Preclinical reference (rats, SC / IM / IV) | 0.25–2.5 mg/kg | Preclinical data only |
Share your experience
No reviews yet. Tell others what you think of this product.
HGF (hepatocyte growth factor) is the only known ligand of the c-Met (MET) receptor and one of the key tools for researchers working on tissue regeneration, anti-fibrosis and cell-proliferation signalling. Chemically it is not a peptide or a peptide analogue at all, but a large two-chain glycoprotein of about 90 kDa: an α- and a β-chain joined by a disulfide bridge, formed from an inactive single-chain precursor (pro-HGF) by proteolytic cleavage.
Structurally HGF is about one third identical to plasminogen and carries four kringle domains and a serine-protease-like domain. However, that protease domain is catalytically inactive: it has lost the residues of the catalytic triad. HGF is, in essence, a protease scaffold that evolution has repurposed into a growth factor.
That link to c-Met is exactly what makes HGF difficult: activation of c-Met launches an "invasive growth" programme (proliferation, cell scattering, morphogenesis, angiogenesis), and the same axis is a target for oncology drugs that inhibit it.
Mice lacking HGF or Met die in utero with defects of the placenta, liver and migration of muscle precursors. This is not a subtle modifier but an essential developmental gene.
Development status, honestly. There is no approved HGF agonist anywhere in the world. The recombinant protein is almost unusable as a systemic drug: a very short plasma half-life, strong binding to heparan sulfates, rapid hepatic clearance, and complex, expensive manufacture of a glycosylated two-chain protein. So clinical development took two roundabout routes: gene therapy with a plasmid encoding HGF (VM202/Engensis; phase 2 positive, phase 3 in diabetic neuropathy did not meet the primary endpoint), and local delivery of the recombinant protein (intrathecal KP-100IT in acute spinal cord injury).
A detailed analysis of the mechanism, the evidence base and the limitations is in the HGF monograph. Related catalogue directions: healing and regeneration, in particular B7-33 (an antifibrotic relaxin analogue on a different receptor axis, RXFP1) and ARA-290 (neuroregeneration).
