Epidermal growth factor (EGF) is a small, potent growth factor capable of inducing cell proliferation, differentiation, and survival. EGF is the founding member of the EGF family that also includes TGF-alpha, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin‑binding EGF‑like growth factor (HB‑EGF), epigen, and the neuregulins (NRG)-1 through -6 (1). Members of The EGF family are characterized by a shared structural motif, the EGF‑like domain, which contains three intramolecular disulfide bonds that are formed by six similarly spaced, conserved cysteine residues (2). These disulfide bonds are essential for proper protein conformation and receptor binding. All EGF family members are synthesized as type I transmembrane precursor proteins that may contain several EGF domains in the extracellular region. The mature proteins are released from the cell surface by regulated proteolysis (1). The full length EGF protein is 1207 amino acids (aa) (EGF precursor) containing nine EGF domains and nine LDLR class B repeats. However, the mature protein is much smaller, only 53 aa, and is generated by proteolytic cleavage of the EGF domain proximal to the transmembrane region (3). EGF is well conserved across mammals with mature human EGF 70% identical to mature mouse and rat EGF. Physiologically, EGF is found in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid (4). EGF is a high affinity ligand of the EGF receptor (ErbB). Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members (5). EGF binding induces dimerization of the EGF receptor resulting in activation of the protein tyrosine kinase signaling pathway. These receptors undergo a complex pattern of ligand-induced homo- or hetero-dimerization to transduce EGF family signals (6, 7). EGF binds ErbB1 and depending on the context, induces the formation of homodimers or heterodimers containing ErbB2. Dimerization results in autophosphorylation of the receptor at specific tyrosine residues to create docking sites for a variety of signaling molecules (5, 8). Biological activities ascribed to EGF include epithelial development, angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation of epidermal cells in culture.
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Recombinant Mouse EGF Protein, CF
R&D Systems | Catalog # 2028-EG
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Key Product Details
- R&D Systems E. coli-derived Recombinant Mouse EGF Protein (2028-EG)
- Quality control testing to verify active proteins with lot specific assays by in-house scientists
- All R&D Systems proteins are covered with a 100% guarantee
Source
E. coli
Accession Number
Applications
Bioactivity
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Product Specifications
Source
E. coli-derived mouse EGF protein
Asn977-Arg1029, with an N-terminal Met
Asn977-Arg1029, with an N-terminal Met
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
N-terminal Sequence Analysis
Met
Predicted Molecular Mass
6.2 kDa
Activity
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. Rubin, J.S. et al. (1991) Proc. Natl. Acad. Sci. USA 88:415.
The ED50 for this effect is 20-100 pg/mL.
The ED50 for this effect is 20-100 pg/mL.
Reviewed Applications
Read 8 reviews rated 4.8 using 2028-EG in the following applications:
Formulation, Preparation, and Storage
2028-EG
| Formulation | Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA. |
| Reconstitution | Reconstitute at 200 μg/mL in sterile PBS.
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| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Calculators
Background: EGF
References
- Harris, R.C. et al. (2003) Exp. Cell Res. 284:2.
- Carpenter, G. and Cohen, S. (1990) J. Biol. Chem. 265:7709.
- Gray, A. et al. (1983) Nature 303:722.
- Carpenter, G. and Zendegui, J.G. (1986) Exp. Cell Res. 164:1.
- Jorissen, R.N. et al. (2003) Exp. Cell Res. 284:31.
- Gamett, D.C. et al. (1997) J. Biol. Chem. 272:12052.
- Qian, X. et al. (1994) Proc. Natl. Acad. Sci. 91:1500.
- Qian, X. et al. (1999) J. Biol. Chem. 274:574.
Long Name
Epidermal Growth Factor
Alternate Names
HOMG4, URG, Urogastrone
Gene Symbol
EGF
UniProt
Additional EGF Products
Product Documents for Recombinant Mouse EGF Protein, CF
Certificate of Analysis
To download a Certificate of Analysis, please enter a lot or batch number in the search box below.
Note: Certificate of Analysis not available for kit components.
Product Specific Notices for Recombinant Mouse EGF Protein, CF
For research use only
Related Research Areas
Citations for Recombinant Mouse EGF Protein, CF
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Customer Reviews for Recombinant Mouse EGF Protein, CF (8)
4.8 out of 5
8 Customer Ratings
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Application: Cell ProliferationVerified Customer | Posted 07/22/2025
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Application: Cell ProliferationVerified Customer | Posted 09/17/2022
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Application: Cell ProliferationVerified Customer | Posted 08/23/2022EpiLc Culture
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Application: In vitro bioactivity in cell cultureVerified Customer | Posted 05/28/2020
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Application: Cell ProliferationVerified Customer | Posted 08/14/2018culture of murine intestinal cel line 10 ng/ml EGF
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Application: Stem/Immune cell maintenance or differentiationVerified Customer | Posted 05/16/2017
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Application: In vitro bioactivity in cell cultureVerified Customer | Posted 04/19/2017Growth of B-16 Mouse melanoma cells as spheroids in serum-free medium after treatment with Recombinant Mouse EGF protein (#2028-EG) for 48 hours.
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Verified Customer | Posted 05/16/2016
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