Recombinant Human KGF/FGF-7 Protein, CF Summary
Product Specifications
Cys32-Thr194
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
11340-KG
| Formulation | Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4 and EDTA with Trehalose. |
| Reconstitution | Reconstitute 10 μg size at 100 μg/mL and all the other sizes at 250 μg/mL in PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
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Recombinant Human KGF/FGF-7 Protein (Catalog # 11340-KG) stimulates cell proliferation of MCF-7 human breast cancer cells, The ED50 for this effect is 25.0-250 ng/mL.
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2 μg/lane of Recombinant Human KGF/FGF‑7 Protein (Catalog # 11340-KG) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 22-28 kDa.
Reconstitution Calculator
Background: KGF/FGF-7
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 (1-4,13). 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.
- Hsu, Y-R. et al. (1999) Biochemistry 38:2523.
- Belleudi, F. et al. (2007) Traffic 8:1854.
- Vadija R. et al. (2016) J Chem Biol. 9:69.
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