Analytical Data
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Gene name
FGF7
- Application
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Alternative Names
FGF7；KGF；Fibroblast growth factor 7
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P21781
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Expression Region
32-194aa
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AA Sequence
CNDMTPEQMATNVNCSSPERHTRSYDYMEGGDIRVRRLFCRTQWYLRIDK RGKVKGTQEMKNNYNIMEIRTVAVGIVAIKGVESEFYLAMNKEGKLYAKK ECNEDCNFKELILENHYNTYASAKWTHNGGEMFVALNQKGIPVRGKKTKK EQKTAHFLPMAIT
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Molecular Weight
19 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Fibroblast growth factor 7 (FGF7), also known as keratinocyte growth factor (KGF), is a member of the fibroblast growth factor family that plays a crucial role in various biological processes, including embryonic development, tissue repair, and cell survival. It primarily acts on epithelial cells, promoting their proliferation and differentiation, making it significant in skin and lung development. FGF7 is particularly important in wound healing and has been implicated in tissue regeneration following injury. Research into recombinant FGF7 proteins has gained traction due to their therapeutic potential in treating skin disorders, enhancing wound healing, and mitigating the effects of radiotherapy or chemotherapy on epithelial tissues. Recent studies have focused on the production of recombinant FGF7 in various expression systems, aiming to optimize yield, bioactivity, and stability for clinical applications. Understanding the structure-function relationship of FGF7 has also been a vital area of research, as it can lead to the development of more effective therapeutic agents. Furthermore, FGF7’s interactions with its receptor, FGFR2, and the downstream signaling pathways involved in cell growth and differentiation are crucial for developing targeted therapies in regenerative medicine. As research progresses, recombinant FGF7 holds promise for applications in dermatology and oncology, presenting a potential avenue for enhancing recovery and improving patient outcomes in conditions associated with epithelial tissue damage.
