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Epidermal growth factor (EGF) is a small 6 kD polypeptide and has six conserved cysteine residues that form three intramolecular disulfide bonds. Human and mouse EGF share 70% homology in amino acid structure. Human EGF is synthesized as a transmembrane precursor protein (1207 amino acids) which is proteolytically cleaved to generate the 54 amino acid mature EGF. Many different cells including mammary gland cells, macrophages, gut epithelial cells, and cells in the nervous system and the kidney can produce EGF. EGF plays an important role in the regulation of cell survival, proliferation, and differentiation by binding to its receptor EGFR. For example, EGF can stimulate the proliferation of mouse embryonic stem cells or induce the terminal differentiation/growth inhibition of A431 cells. The binding of EGF to EGFR will induce receptor dimerization, which is required for activating the tyrosine kinase in the receptor cytoplasmic domain. In addition, the binding of EGF to its receptor triggers several signal transduction pathways including JAK/STAT, Ras/ERK and PI3K/AKT pathways. Blocking of the EGF/EGFR pathway can suppress tumor cell proliferation. Other members of the EGF family (including transforming growth factor-α (TGF-α), heparin-binding EGF-like growth factor (HB-EGF), amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), and epigen also bind to EGFR.Product Details
- Human EGF, 53 amino acids Asn971-Arg1023 (Accession# P01133), was expressed in E. coli.
- Molecular Mass
- The 53 amino acid recombinant protein has a predicted molecular mass of approximately 6.2 kD. The predicted N-terminal amino acid is Asn.
- >98%, as determined by Coomassie stained SDS-PAGE and HPLC analysis.
- Lyophilized, carrier-free.
- Endotoxin Level
- Less than 0.1 ng per µg of protein.
- Storage & Handling
- Unopened vial can be stored at -20°C or -70°C. For maximum results, quick spin vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. It is recommended to further dilute in a buffer, such as 5% Trehalose, and store working aliquots at -20°C to -80°C. Avoid repeated freeze/thaw cycles.
- ED50 ≤ 0.1 ng/ml, corresponding to a specific activity of ≥ 1.0 x 107 units/mg as determined by a cell proliferation assay using BALB/c 3T3 cells.
- Application Notes
This product is reactive with human, cow, hamster, monkey, mouse, pig, rabbit, rat, and chicken.
- Mammary gland cell, macrophage, gut epithelial cells, cells in the nervous system, kidney
- EGF is a potent mitogen for many cells in culture, and in vivo. It induces the proliferation and differentiation of skin, cornea, lung, and trachea, among other tissues. Processing of pro EGF to mature EGF in different tissues is not equally efficient. The precursor is processed to mature EGF in the submaxillary gland, pancreas, small intestine, and mammary gland. In the submaxillary gland, EGF is fully processed, stored at secretory granules, and secreted in saliva. In kidney, EGF is present in unprocessed or intermediate forms on the cell surface.
- Stimulation of Balb/3T3 proliferation
- Cell Type
- Neural Stem Cells, Mesenchymal Stem Cells, Hematopoietic stem and progenitors, Embryonic Stem Cells
- Biology Area
- Cell Biology, Neuroscience, Stem Cells, Synaptic Biology
- Molecular Family
- Growth Factors, Cytokines/Chemokines
- Antigen References
1. Henson ES and Gibson SB. 2006. Cell Signal. 18:2089.
2. Burgess AW, et al. 2003. Mol. Cell. 12:541.
3. Imai Y, et al. 1982. Cancer Res. 42:4394.
4. Barnes DW. 1982. J. Cell. Biol. 93:1.
5. Heo JS, et al. 2006. Am. J. Physiol. Cell. Physiol. 290:C123.
- Gene ID
- 1950 View all products for this Gene ID
- View information about EGF on UniProt.org
- Does specific activity of a recombinant protein vary between lots?
Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.
- Have your recombinants been tested for stability?
Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.
- How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
- Use formula Specific activity (Units/mg) = 10e6/ ED50 (ng/mL)
- How does the activity of your recombinant proteins compare to competitors?
We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!
- What is the specific activity or ED50 of my recombinant protein?
The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.