Recombinant Rat EGF Protein, CF


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Recombinant Rat 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 10-60 pg/mL.
E. coli-derived rat EGF protein
Asn974-Arg1026, with an N-terminal Met
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Proteins
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.


  • Bioactivity
Theoretical MW
6.3 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.
Read Publications using
3214-EG/CF 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 Acetonitrile and TFA.
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile 10 mM Acetic Acid.


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

Alternate Names for Recombinant Rat 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. Saggi, S.J. et al. (1992) DNA Cell Biol. 11:481.
  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.

Publications for EGF (3214-EG/CF)(12)

We have publications tested in 1 confirmed species: Rat.

We have publications tested in 3 applications: Bioassay, Cell Culture, In Vivo.

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Showing Publications 1 - 10 of 12. Show All 12 Publications.
Publications using 3214-EG/CF Applications Species
Z Berkova, K Zacharovov, A Patikova, I Leontovyc, Z Hladikova, D Cerveny, E Tihlarikov, V Nedela, P Girman, D Jirak, F Saudek Decellularized Pancreatic Tail as Matrix for Pancreatic Islet Transplantation into the Greater Omentum in Rats Journal of functional biomaterials, 2022-09-30;13(4):. 2022-09-30 [PMID: 36278640] (Cell Culture, Rat) Cell Culture Rat
A López-Márq, C Carrasco-L, A Martínez-C, P Lemoine, CE Pierreux, P Santisteba Sox9 is involved in the thyroid differentiation program and is regulated by crosstalk between TSH, TGFbeta and thyroid transcription factors Scientific Reports, 2022-02-09;12(1):2144. 2022-02-09 [PMID: 35140269] (Bioassay, Rat) Bioassay Rat
LT Frasson, B Dalmaso, PS Akamine, ET Kimura, DE Hamassaki, CB Del Debbio Let-7, Lin28 and Hmga2 Expression in Ciliary Epithelium and Retinal Progenitor Cells Investigative Ophthalmology & Visual Science, 2021-03-01;62(3):31. 2021-03-01 [PMID: 33749722] (Bioassay, Rat) Bioassay Rat
B Fan, W Pan, X Wang, M Wei, A He, A Zhao, M Chopp, ZG Zhang, XS Liu Long noncoding RNA mediates stroke-induced neurogenesis Stem Cells, 2020-05-02;0(0):. 2020-05-02 [PMID: 32346940] (Bioassay, Rat) Bioassay Rat
M Nakamura, H Nishida, K Yoshizaki, H Akiyoshi, S Hatoya, K Sugiura, T Inaba Canine mesenchymal stromal cell-conditioned medium promotes survival and neurite outgrowth of neural stem cells J. Vet. Med. Sci., 2020-04-06;0(0):. 2020-04-06 [PMID: 32249241] (Cell Culture, Rat) Cell Culture Rat
W Zhang, X Li, S Sun, X Zhang Implantation of engineered conduction tissue in the rat heart Mol Med Rep, 2019-02-05;0(0):. 2019-02-05 [PMID: 30720107] (Bioassay, Rat) Bioassay Rat
D Stöckmann, T Spannbruck, N Ale-Agha, P Jakobs, C Goy, N Dyballa-Ru, T Hornstein, A Kümper, A Kraegeloh, J Haendeler, K Unfried Non-Canonical Activation of the Epidermal Growth Factor Receptor by Carbon Nanoparticles Nanomaterials (Basel), 2018-04-23;8(4):. 2018-04-23 [PMID: 29690640] (Bioassay, Rat) Bioassay Rat
M Zhang, MH Jiang, DW Kim, W Ahn, E Chung, Y Son, G Chi Comparative Analysis of the Cell Fates of Induced Schwann Cells from Subcutaneous Fat Tissue and Na�ve Schwann Cells in the Sciatic Nerve Injury Model Biomed Res Int, 2017-06-20;2017(0):1252851. 2017-06-20 [PMID: 28713821] (Bioassay, Rat) Bioassay Rat
O Stojadinov, TC Wikramanay, AC Villasante, NC Yin, L Liang, E Hinde, J Escandon, M Tomic-Cani, DM Ansell, R Paus, JJ Jimenez Wound healing protects against chemotherapy-induced alopecia in young rats via up-regulating interleukin-1?-mediated signaling Heliyon, 2017-05-30;3(5):e00309. 2017-05-30 [PMID: 28607955] (In Vivo, Rat) In Vivo Rat
Kandasamy M, Lehner B, Kraus S, Sander P, Marschallinger J, Rivera F, Trumbach D, Ueberham U, Reitsamer H, Strauss O, Bogdahn U, Couillard-Despres S, Aigner L TGF-beta signalling in the adult neurogenic niche promotes stem cell quiescence as well as generation of new neurons. J Cell Mol Med, 2014-04-30;18(7):1444-59. 2014-04-30 [PMID: 24779367] (Bioassay, Rat) Bioassay Rat
Show All 12 Publications.

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Gene Symbol Egf