| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | HBGF-7, FGF7, FGF-7, KGF. |
| Biological Activity | |
| Cellular Localization | |
| Concentration | |
| Expression System | |
| Form | Sterile Filtered White lyophilized (freeze-dried) powder. |
| Formulation | |
| Product Type | |
| Protein Length | |
| Purity | |
| Solubility | It is recommended to reconstitute the lyophilized Keratinocyte Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. |
| Source | Escherichia Coli. |
| Species | |
| Storage | |
| Target |
Recombinant Human Keratinocyte Growth Factor is supplied as a recombinant protein for in vitro research use.
Background
KGF is a member of the fibroblast growth factor (FGF) family. FGF 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. FGF7 is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. Studies of mouse and rat homologs of this gene implicated roles in morphogenesis of epithelium, reepithelialization of wounds, hair development and early lung organogenesis.
FGF stands for fibroblast growth factor that have proteins encoded inside them. The FGF family possess broad mitogenetic activities and are involved in a lot of processes in the body. Some of the biological processes that they are included in are embryonic development, cell growth, tumor growth and tissue repair. FGF-7 is often also commonly referred to as keratinocyte growth factor or KGF and studies have focused on the link between the protein and certain tumor growth. Structure Studies have found that the crystal structure of FGF7 is comparatively similar to that of FGF10. For instance, FGF7 does interact with D2, linker as well as D3 of the receptor. Similar to other FGFs much of interaction to do with D2 is confined to conserved residues as well as the residue Arg 251 in the linker domain and the hydrophobic surface of D2. That said there are notable differences and some models predict that FGF7 actually interacts with three loops in D3. Mechanism A member of the FGF family, this factor acts completely exclusively through a subset of FGF receptor isoforms. These are mainly expressed by epithelial cells. Indeed, studies suggest that the factor specifically acts on epithelial cells. This in turn causes increased proliferation differentiation and migrations of the aforementioned cells. Interactions FGF7 and FGF10 can interact with one of the FGF receptors that is expressed by the epithelial cells. As such, it could be the case that this interaction could cause a protective factor for these epithelial tissues. The protein has also been shown to interact with Perlecan. Also referred to as basement membrane specific heparan sulfate proteoglycan core protein, this is encoded by the HSPG2 gene. A large multi domain this cross-links and binds to various extracellular matrix components as well as self surface molecules. Since FGF7 binds specifically with the perlecan protein, research suggests that i should be considered a novel biological ligand for FGF-7. This could mean that interaction has an influence on both tissue remodeling and cancer growth. Function Studies have shown that FGF-7 expression is completely unregulated during minor or even chronic injury. This has lead researchers to believe that the protein is used to heal or repair epithelial cells. Furthermore, FGF-1 also triggers the formation of apical ectodermal ridge throughout the development of limbs in the body. Recently, it has seemed to be the case that FGF-7 has been linked to skin injury repair, and has also been found to play some sort of role in breast cancer. As well as this, it is a vital regulator of HPC’s. It is vital because it can induce de novo activation of these HPCs. Further research has shown that FGF6 is a niche signal that is required for the stimulation of adult liver progenitor cells and this can support liver regeneration. This research has lead to the suggestion that FGF7 could be a possibility therapeutic target for those suffering from liver diseases. Studies like this are just one of the reasons why researchers continue to explore fgf-7, it’s functions and interactions.
Product format
Provided as a recombinant protein suitable for in vitro workflows such as binding studies, screening, and assay development. Refer to the specifications table for expression format and molecular properties.
Quality notes
Protein quantitation was carried out by two independent methods:
1. UV spectroscopy at 280 nm using the absorbency value of 0.9 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
2. Analysis by RP-HPLC, using a calibrated solution of KGF as a Reference Standard.
What is the purity of Recombinant Human Keratinocyte Growth Factor (Human)?
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE. BioHippo includes a Certificate of Analysis (CoA) confirming purity per lot with every order.
What buffer / formulation is this protein supplied in?
How should Recombinant Human Keratinocyte Growth Factor (Human) be stored?
What expression system was used to produce this protein?
Is this protein biologically active?
Is this protein approved for clinical or in vitro diagnostic use?
Can I request a custom size, tag variant, or formulation?
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.