Measured in a cell proliferation assay using 4MBr‑5 rhesus monkey epithelial cells. Rubin, J.S. et al. (1989) Proc. Natl. Acad. Sci. USA 86:802. The ED50 for this effect is typically 6-60 ng/mL. The specific activity of recombinant human KGF/FGF-7 is approximately 1.3 x 103 U/μg, which is calibrated against recombinant human KGF/FGF-7 WHO Standard (NIBSC code: 03/150).
E. coli-derived human KGF/FGF-7 protein Cys32-Thr194, with an N-terminal Met
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
19 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
KGF (keratinocyte growth factor), also known as FGF-7 (fibroblast growth factor-7), is one of 22 known members of the mouse FGF family of secreted proteins that plays a key role in development, morphogenesis, angiogenesis, wound healing, and tumorigenesis (1-4). KGF expression is restricted to cells of mesenchymal origin. When secreted, it acts as a paracrine growth factor for nearby epithelial cells (1). KGF speeds wound healing by being dramatically upregulated in response to damage to skin or internal structures that results in high local concentrations of inflammatory mediators such as IL-1 and TNF-alpha. (2, 5). KGF promotes cell migration and invasion, and mediates melanocyte transfer to keratinocytes upon UVB radiation (6, 7). It has been used ectopically to avoid chemotherapy-induced oral mucositis in patients with hematological malignancies (1). Deletion of KGF affects kidney development, producing abnormally small ureteric buds and fewer nephrons (8). It also impedes hair follicle differentiation (9). The 194 amino acid (aa) KGF precursor contains a 31 aa signal sequence and, like all other FGFs, an ~120 aa beta -trefoil scaffold that includes receptor- and heparin-binding sites. KGF signals only through the IIIb splice form of the tyrosine kinase receptor, FGF R2 (FGF R2-IIIb/KGF R) (10). Receptor dimerization requires an octameric or larger heparin or heparin sulfate proteoglycan (11). FGF-10, also called KGF2, shares 51% aa identity and similar function to KGF, but shows more limited expression than KGF and uses an additional receptor, FGF R2-IIIc (12). Following receptor engagement, KGF is typically degraded, while FGF-10 is recycled (12). Mature human KGF, which is active across species, shares 98% aa sequence identity with bovine, equine, ovine and canine, 96% with mouse and porcine, and 92% with rat KGF, respectively.
Finch, P.W. and J.S. Rubin (2006) J. Natl. Cancer Inst. 98:812.
Werner, S. et al. (2007) J. Invest. Dermatol. 127:998.
Werner, S. (1998) Cytokine Growth Factor Rev. 9:153.
Mason, I.J. et al. (1994) Mech. Dev. 45:15.
Geer, D.J. et al. (2005) Am. J. Pathol. 167:1575.
Niu, J. et al. (2007) J. Biol. Chem. 282:6001.
Cardinali, G. et al. (2005) J. Invest. Dermatol. 125:1190.
Qiao, J. et al. (1999) Development 126:547.
Guo, L. et al. (1996) Genes Dev. 10:165.
de Georgi, V. et al. (2007) Dermatol. Clin. 25:477.
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