Recombinant Human EGF Protein, CF


1 µg/lane of Recombinant Human EGF was resolved with SDS-PAGE and visualized by silver staining under reducing (R) conditions, showing a single band at 6 kDa.
Recombinant Human EGF (Catalog # 236‑EG) stimulates cell proliferation of the Balb/3T3 mouse embryonic fibroblast cell line. The ED50 for this effect is 20‑100 pg/mL.

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Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human EGF Protein, CF Summary

Details of Functionality
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.
E. coli-derived human EGF protein
Asn971-Arg1023, with an N-terminal Met
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Proteins
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.


  • Bioactivity
Theoretical MW
6 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
6 kDa, reducing conditions
Read Publications using
236-EG in the following applications:

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS.
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in sterile PBS.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human EGF Protein, CF

  • beta-urogastrone
  • EGF
  • epidermal growth factor (beta-urogastrone)
  • epidermal growth factor
  • hEGF
  • HOMG4
  • pro-epidermal growth factor
  • URG
  • Urogastrone


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.

  1. Harris, R.C. et al. (2003) Exp. Cell Res. 284:2.
  2. Carpenter, G. and Cohen, S. (1990) J. Biol. Chem. 265:7709.
  3. Bell, G.I. et al. (1986) Nucl. Acids Res. 14:8427.
  4. Carpenter, G. and Zendegui, J.G. (1986) Exp. Cell Res. 164:1.
  5. Jorissen, R.N. et al. (2003) Exp. Cell Res. 284:31.
  6. Gamett, D.C. et al. (1997) J. Biol. Chem. 272:12052.
  7. Qian, X. et al. (1994) Proc. Natl. Acad. Sci. 91:1500.
  8. Qian, X. et al. (1999) J. Biol. Chem. 274:574.

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Publications for EGF (236-EG)(668)

We have publications tested in 13 confirmed species: Human, Mouse, Rat, Canine, Chicken, Equine, Feline, Porcine, Primate - Macaca fascicularis (Crab-eating Monkey or Cynomolgus Macaque), Rabbit, Transgenic Mouse, Xenograft, Zebrafish.

We have publications tested in 7 applications: Bioassay, Cell Culture, Differentiation, In Vivo, Organoid Culture, Stimulation, Tissue Culture.

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Primate - Macaca fascicularis (Crab-eating Monkey or Cynomolgus Macaque)
Transgenic Mouse
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Showing Publications 1 - 10 of 668. Show All 668 Publications.
Publications using 236-EG Applications Species
JE Kaserman, RB Werder, F Wang, T Matte, MI Higgins, M Dodge, J Lindstrom-, P Bawa, A Hinds, E Bullitt, IS Caballero, X Shi, RE Gerszten, N Brunetti-P, M Liesa, C Villacorta, AN Hollenberg, DN Kotton, AA Wilson Human iPSC-hepatocyte modeling of alpha-1 antitrypsin heterozygosity reveals metabolic dysregulation and cellular heterogeneity Cell Reports, 2022;41(10):111775. 2022 [PMID: 36476855] (Bioassay, Human) Bioassay Human
Z Tu, Y Hu, D Raizada, MA Bassal, DG Tenen, AE Karnoub Long noncoding RNA-mediated activation of PROTOR1/PRR5-AKT signaling shunt downstream of PI3K in�triple-negative breast cancer Proceedings of the National Academy of Sciences of the United States of America, 2022;119(43):e2203180119. 2022 [PMID: 36269860] (Bioassay, Human) Bioassay Human
W He, X Zhu, A Xin, H Zhang, Y Sun, H Xu, H Li, T Yang, D Zhou, H Yan, X Sun Long-term maintenance of human endometrial epithelial stem cells and their therapeutic effects on intrauterine adhesion Cell & bioscience, 2022;12(1):175. 2022 [PMID: 36258228] (Bioassay, Human) Bioassay Human
O Revah, F Gore, KW Kelley, J Andersen, N Sakai, X Chen, MY Li, F Birey, X Yang, NL Saw, SW Baker, ND Amin, S Kulkarni, R Mudipalli, B Cui, S Nishino, GA Grant, JK Knowles, M Shamloo, JR Huguenard, K Deisseroth, SP Pa?ca Maturation and circuit integration of transplanted human cortical organoids Nature, 2022;610(7931):319-326. 2022 [PMID: 36224417] (Bioassay, Human) Bioassay Human
DS Lee, YJ Song, HR Gug, JH Lee, HS Bae, JC Park Nuclear Factor I-C Regulates Stemness Genes and Proliferation of Stem Cells in Various Mineralized Tissue through Epithelial-Mesenchymal Interactions in Dental Epithelial Stem Cells Stem Cells International, 2022;2022(0):1092184. 2022 [PMID: 36213683] (Cell Culture, Mouse) Cell Culture Mouse
PC Kinnunen, GD Luker, KE Luker, JJ Linderman Computational modeling implicates protein scaffolding in p38 regulation of Akt Journal of theoretical biology, 2022;555(0):111294. 2022 [PMID: 36195198] (Bioassay, Human) Bioassay Human
H Marei, WK Tsai, YS Kee, K Ruiz, J He, C Cox, T Sun, S Penikalapa, P Dwivedi, M Choi, D Kan, P Saenz-Lope, K Dorighi, P Zhang, YT Kschonsak, N Kljavin, D Amin, I Kim, AG Mancini, T Nguyen, C Wang, E Janezic, A Doan, E Mai, H Xi, C Gu, M Heinlein, B Biehs, J Wu, I Lehoux, S Harris, L Comps-Agra, D Seshasayee, FJ de Sauvage, M Grimmer, J Li, NJ Agard, F de Sousa E Antibody targeting of E3 ubiquitin ligases for receptor degradation Nature, 2022;610(7930):182-189. 2022 [PMID: 36131013] (Bioassay, Human) Bioassay Human
GM Jowett, E Read, LB Roberts, D Coman, M Vilà Gonzá, T Zabinski, U Niazi, R Reis, TJ Trieu, D Danovi, E Gentleman, L Vallier, MA Curtis, GM Lord, JF Neves Organoids capture tissue-specific innate lymphoid cell development in mice and humans Cell Reports, 2022;40(9):111281. 2022 [PMID: 36044863] (Bioassay, Mouse) Bioassay Mouse
I Jun, YJ Choi, BR Kim, KY Seo, TI Kim Activation of ADRB2/PKA Signaling Pathway Facilitates Lipid Synthesis in Meibocytes, and Beta-Blocker Glaucoma Drug Impedes PKA-Induced Lipid Synthesis by Inhibiting ADRB2 International Journal of Molecular Sciences, 2022;23(16):. 2022 [PMID: 36012741] (Cell Culture, Human) Cell Culture Human
Y Hattori, K Kurozumi, Y Otani, A Uneda, N Tsuboi, K Makino, S Hirano, K Fujii, Y Tomita, T Oka, Y Matsumoto, Y Shimazu, H Michiue, H Kumon, I Date Combination of Ad-SGE-REIC and bevacizumab modulates glioma progression by suppressing tumor invasion and angiogenesis PLoS ONE, 2022;17(8):e0273242. 2022 [PMID: 36006934] (Bioassay, Human) Bioassay Human
Show All 668 Publications.

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Gene Symbol EGF