This is an unconjugated, non-therapeutic recombinant analog of rilotumumab, a fully human IgG2-kappa monoclonal antibody directed against hepatocyte growth factor (HGF). Supplied for research use only, it is built around the same HGF target as the originator drug and is intended to reproduce that binding specificity in the laboratory rather than in patients. It is not the clinical product and is not for human or veterinary use. The reagent is well suited to in-vitro and preclinical work: neutralization and ligand-blocking assays, competition and epitope-binning studies, ELISA and surface-plasmon-resonance characterization, as a positive or isotype-matched comparator control, and as a benchmark reference when developing or screening other anti-HGF or anti-MET agents. Because HGF signaling through the MET receptor is heavily implicated in tumor growth, invasion and angiogenesis, an HGF-neutralizing analog is a useful tool for interrogating the HGF/MET axis in cell-based models. Material is offered at research grade with low endotoxin (<1 EU/mg; ultra-low <0.5 EU/mg options), and in bulk milligram-to-gram quantities suitable for scale-up screening campaigns.
Hepatocyte growth factor (HGF, also called scatter factor; UniProt P14210) is a secreted, heparin-binding glycoprotein and the sole known ligand for the receptor tyrosine kinase MET (c-Met). It is produced as an inactive single-chain precursor that is proteolytically cleaved into a disulfide-linked alpha/beta heterodimer to become active. HGF is composed of an N-terminal PAN/hairpin domain, four kringle domains and a serine-protease-like beta chain that is catalytically inactive. Binding of mature HGF to MET drives receptor dimerization and autophosphorylation, activating downstream RAS-MAPK, PI3K-AKT and STAT pathways. Physiologically this controls epithelial proliferation, motility ("scattering"), morphogenesis, tissue regeneration and wound healing. Aberrant HGF/MET signaling promotes tumor proliferation, epithelial-mesenchymal transition, invasion, metastasis and angiogenesis, making HGF an important oncology target.