HGF stands for hepatocyte growth factor. Despite the name, its role reaches far beyond the liver: it is a signalling protein that governs the movement, survival and division of many cell types through a single receptor. Here is what the molecule is, what the literature says about it, and the status in which it ships.
What HGF is, briefly
HGF is a secreted protein, a two-chain α/β heterodimer. It is not a peptide but a full-size growth factor, and it acts through the c-Met (MET) receptor. The full mechanistic breakdown of c-Met signalling lives in the HGF monograph; here is the gist and where the interest came from.
How it was discovered
The molecule was cloned in the late 1980s: a 1989 paper described the molecular cloning and expression of human hepatocyte growth factor (Nature, 1989). Two years later its receptor was identified: the HGF receptor turned out to be the product of the c-met proto-oncogene (Science, 1991). That pair, ligand and receptor, became the centre of all later work.
A review by one of the original discoverers later summed up the significance of HGF for regenerative medicine and why a single molecule combines so many functions (Proc. Jpn. Acad., 2010).
Why HGF interests researchers
Through c-Met, HGF triggers what is called invasive growth: cells begin to move, survive stress and divide. In physiology this underlies tissue repair after injury. The same pathway in pathology is involved in tumour growth, which is why c-Met is also an oncology target. For a researcher HGF is a convenient tool to study regeneration, cell migration and receptor tyrosine kinase signalling under controlled conditions.
Downstream of the receptor, that signalling activates intracellular pathways that control cell survival and motility, the same machinery some tumours co-opt once the pathway loses its normal restraints. That overlap is why cell lines expressing c-Met are a standard model in cancer research, not an unrelated detail borrowed from a different field.
HGF is not HGH
The name invites a mix-up. HGH (human growth hormone) is a single-chain pituitary hormone that signals through the growth hormone receptor and drives much of its effect indirectly, via IGF-1. HGH Fragment 176-191, a short peptide derived from the tail of that same hormone, is a different material again. HGF shares none of that biology: it is produced locally by cells near an injury and signals through its own receptor, c-Met, unrelated to the growth hormone receptor. A search for growth hormone or a growth-hormone peptide fragment that landed here by mistake is looking for one of those other two materials in the catalog.
How HGF differs from short regeneration peptides
Researchers browsing HGF often also look at BPC-157 or TB-500, other materials studied for tissue repair. The difference is structural. Both of those are short synthetic peptides, compact molecules that are comparatively simple and inexpensive to produce. HGF sits in a different size class: a roughly 90 kDa two-chain glycoprotein made by recombinant expression, structurally related to plasminogen, acting on one specific receptor. That specificity makes it a precise tool for isolating a single signalling pathway in an experiment, and it also means storage and handling matter more than they do for a short peptide.
Handling HGF as a laboratory reagent
Like most recombinant growth factors, HGF ships as a lyophilized powder and is unstable once reconstituted. Standard laboratory practice for a protein of this class is to reconstitute in sterile buffer immediately before use, keep the reconstituted solution refrigerated rather than at room temperature, and avoid repeated freeze-thaw cycles, which degrade activity faster than a single cycle would. None of this is a usage protocol for humans or animals; it is basic handling guidance for a research reagent, the same practice that applies to any recombinant protein in a lab. The HGF catalogue page has the specifications and a dedicated handling reference for this batch format.
Research status
Longeva material is research use only. It is not a medicine or a supplement but a reagent for laboratory use. HGF has no approved indications in this format; the data above concern basic and clinical-research work, not a ready treatment, and are not a basis for self-administration.
See also: human research results for HGF and why phase 3 failed.
Lots come with a certificate of analysis from an independent third-party laboratory; you can look up a COA (certificate of analysis) by lot number in the open archive. For presentation and specifications, see the HGF catalogue page.
