Recombinant Human FGF-7

Keratinocyte growth factor (KGF), also known as FGF-7 and HBGF-7, is a member of the fibroblast growth factor (FGF) family. The family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion.¹ KGF is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells.² When secreted, KGF acts as a paracrine growth factor for nearby epithelial cells. KGF will only signal through the FGF R2-IIIb receptor.³ For signaling to occur, receptor dimerization is required with an octameric or larger heparin or heparin sulfate proteoglycan. Studies of mouse and rat homologs of this gene implicated roles in morphogenesis of epithelium, re-epithelialization of wounds, hair development and early lung organogenesis.^4,5 Instillation of KGF into the lungs of animals protects them from oxidant-induced injury to the lung epithelium.

Measured in a cell proliferation assay using 4MBr‑5 rhesus monkey epithelial cells.⁶ The ED₅₀ for this effect is typically 6-60 ng/mL. The specific activity of Recombinant Human FGF-7 is approximately 1.3 x 10³ U/μg, which is calibrated against Recombinant Human FGF-7 WHO Standard (NIBSC code: 03/150).

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Lyophilized

The predicted molecular weight of Recombinant Human FGF-7 is Mr 19 kDa.

19

This recombinant protein was 0.2 µm filtered and lyophilized from modified Dulbecco’s phosphate buffered saline (1X PBS) pH 7.2 – 7.3 with no calcium, magnesium, or preservatives.

This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.

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1. Finch, PW. et al. (2006) J. Natl. Cancer Inst. 98:812
2. Aaronson, SA. et al. (1991) Ann. N. Y. Acad. Sci. 638:62
3. Bottaro, DP. et al. (1993) J. Biol. Chem. 268:9180
4. Werner, S. et al. (1992) Proc. Natl. Acad. Sci. (USA) 89:6896
5. Simonet, WS. et al. (1995) Proc. Natl. Acad. Sci. (USA) 92:12461
6. Rubin, JS. et al. (1989) Proc. Natl. Acad. Sci. USA 86:802.