Fibroblast growth factor 7 (FGF-7), also known as Keratinocyte Growth Factor (KGF), is a member of the fibroblast growth factor (FGF) family. It plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is essential for normal branching morphogenesis and is an active growth factor for keratinocytes. It may be the main paracrine factor for the proliferation of normal epithelial cells. The activity of recombinant KGF overexpressed in E. coli is about 10 times that of the natural protein, which may be related to the lack of glycosylation of recombinant KGF. The 122-132AA segment of KGF is the specific binding site for the KGF receptor. KGF is secreted by various sources of mesenchymal cells and has a strong affinity for heparin. Its receptor, KGFR, belongs to the family of protein tyrosine kinase receptors and is mainly distributed in epithelial cells. After KGF specifically binds to the receptor KGFR on the target cell membrane, it promotes the autophosphorylation of the receptor, thereby initiating a series of intracellular signaling cascades and playing various biological functions: participating in the development of tissues and organs, promoting cell proliferation, and tissue damage repair.
This product is a recombinant protein prepared by the E. coli prokaryotic expression system, and is made through steps such as separation and purification, filtration sterilization, and freeze-drying. It has the characteristics of high purity, high activity, tag-free, and low endotoxin.
