EGF Mouse, His
Description
Production and Purification
EGF Mouse, His is typically produced in E. coli or HEK293 cells, followed by purification via immobilized metal ion affinity chromatography (IMAC) .
| Parameter | Details |
|---|---|
| Expression Host | HEK293 or E. coli |
| Purification | His-tag enables >90% purity via IMAC |
| Formulation | Lyophilized in phosphate buffer (pH 7.4–7.5); reconstituted in sterile PBS |
Biological Activity and Mechanisms
EGF Mouse, His binds the epidermal growth factor receptor (EGFR/ErbB1), activating downstream signaling pathways (e.g., MAPK, PI3K-AKT) . Key findings include:
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Bioactivity:
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Mechanistic Insights:
Research Applications
Comparative Analysis with Other EGF Variants
Therapeutic Potential and Challenges
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Regenerative Medicine: Promotes muscle regeneration in DMD models and epithelial repair .
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Cancer Research: Modulates tumor microenvironments, though prolonged EGFR activation risks oncogenic signaling .
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Challenges:
Future Directions
Product Specs
Product Science Overview
Epidermal Growth Factor (EGF) is a protein that plays a crucial role in regulating cell growth, proliferation, and differentiation. It is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The recombinant form of EGF from mice, tagged with a Histidine (His) sequence, is widely used in research to study its biological effects and potential therapeutic applications.
The mouse recombinant EGF is produced in Escherichia coli (E. coli) as a single polypeptide chain containing 77 amino acids. The molecular mass of this recombinant protein is approximately 8.6 kDa. The EGF is fused to a 24 amino acid His-tag at the N-terminus, which facilitates its purification through affinity chromatography techniques .
The His-tagged EGF is purified using proprietary chromatographic techniques to achieve a purity greater than 90%, as determined by SDS-PAGE. The purified protein is typically formulated in a sterile filtered colorless solution containing 20 mM Tris-HCl buffer (pH 8.0), 100 mM NaCl, 2 mM DTT, and 10% glycerol .
EGF has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for various epidermal and epithelial tissues. It stimulates the growth of some fibroblasts in cell culture and is believed to exist as a membrane-bound molecule that is proteolytically cleaved to generate the active peptide hormone .
The recombinant EGF with a His-tag is used extensively in laboratory research to study its molecular attributes and therapeutic potential. It is employed in cellular assays to investigate its effects on cell growth and differentiation. Additionally, the His-tag facilitates the purification and detection of the protein in various experimental setups .
For short-term storage, the recombinant EGF can be kept at 4°C if it will be used within 2-4 weeks. For longer-term storage, it is recommended to store the protein frozen at -20°C. To ensure stability, it is advisable to add a carrier protein such as 0.1% Human Serum Albumin (HSA) or Bovine Serum Albumin (BSA) and avoid multiple freeze-thaw cycles .
