Recombinant Human EGF (Animal-Free)

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Regulatory Status
Other Names
Urogastrone (URG), HOMG4
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Product Citations
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713008 500 µg £174
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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
Technical Data Sheet (pdf)

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.

Product Citations
  1. Revkova VA, et al. 2021. ACS Omega. 6:15264. PubMed
  2. Liu M, et al. 2021. Dev Cell. 56:2765. PubMed

Antigen Details

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

Related FAQs

Why choose BioLegend recombinant proteins?

     • Each lot of product is quality-tested for bioactivity as indicated on the data sheet.
     • Greater than 95% Purity or higher, tested on every lot of product.
     • 100% Satisfaction Guarantee for quality performance, stability, and consistency.
     • Ready-to-use liquid format saves time and reduces challenges associated with reconstitution.
     • Bulk and customization available. Contact us.
     • Learn more about our Recombinant Proteins.

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.

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.

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.

How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?

Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)

Go To Top Version: 4    Revision Date: 05/06/2014

For Research Use Only. Not for diagnostic or therapeutic use.


This product is supplied subject to the terms and conditions, including the limited license, located at ("Terms") and may be used only as provided in the Terms. Without limiting the foregoing, BioLegend products may not be used for any Commercial Purpose as defined in the Terms, resold in any form, used in manufacturing, or reverse engineered, sequenced, or otherwise studied or used to learn its design or composition without express written approval of BioLegend. Regardless of the information given in this document, user is solely responsible for determining any license requirements necessary for user’s intended use and assumes all risk and liability arising from use of the product. BioLegend is not responsible for patent infringement or any other risks or liabilities whatsoever resulting from the use of its products.


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