Recombinant Mouse Pro-EGF (aa 29-1029) Protein


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Reactivity MuSpecies Glossary
Applications Bioactivity

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Recombinant Mouse Pro-EGF (aa 29-1029) Protein 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 1-5 ng/mL.
Mouse myeloma cell line, NS0-derived mouse EGF protein
Trp29-Arg1029, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Proteins
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.


Theoretical MW
110 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.
160 kDa, reducing conditions
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4095-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 with BSA as a carrier protein.
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 50 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.


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

Alternate Names for Recombinant Mouse Pro-EGF (aa 29-1029) Protein

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


EGF is the prototypic member of a family of growth factors that also includes amphiregulin, betacellulin, epigen, epiregulin, HB-EGF, neuregulins-1 through -6, and TGF-alpha (1). These proteins contain EGF-like domains with three intramolecular disulfide bonds between conserved cysteines (2). EGF family members are synthesized as transmembrane preproproteins with varying numbers of EGF-like domains (3). The extracellular region of mouse pro-EGF contains eight LDL R class B repeats and nine EGF-like domains (4). Mature EGF is derived from the juxtamembrane EGF-like domain. EGF binds ErbB1 and induces the formation of homodimers or heterodimers containing ErbB2 (5). Pro-EGF is most highly expressed in the submaxillary gland and kidney (6). In the kidney, the 190 kDa preproprotein is cleaved by membrane-associated serine proteases, liberating the extracellular region which is subsequently processed into smaller fragments including the 6 kDa mature EGF (7 - 10). The various cleavage products produced in the kidney also are present in urine (9 - 11). In the submaxillary gland, however, nearly all EGF is processed intracellularly and stored in secretory vesicles (6, 12). The soluble precursor binds ErbB1 and induces cellular proliferation, although it is significantly less potent than mature EGF (8, 9). In human thyroid carcinoma cells, a splice variant of pro-EGF with a deletion in the cytoplasmic domain induces increased proliferative activity relative to wild-type pro-EGF (13). Within the extracellular region, mouse pro-EGF shares 79% amino acid sequence identity with rat pro-EGF and 67% - 69% with human, canine, feline, and porcine pro-EGF.

  1. Singh, A.B. and R.C. Harris (2005) Cell. Signal. 17:1183.
  2. Wouters, M.A. et al. (2005) Prot. Sci. 14:1091.
  3. Sanderson, M.P. et al. (2006) Growth Factors 24:121.
  4. Gray, A. et al. (1983) Nature 303:722.
  5. Jorissen, R.N. et al. (2003) Exp. Cell Res. 284:31.
  6. Rall, L.B. et al. (1985) Nature 313:228.
  7. Le Gall, S.M. et al. (2004) Regul. Pept. 122:119.
  8. Breyer, J.A. and S. Cohen (1990) J. Biol. Chem. 265:16564.
  9. Parries, G. et al. (1995) J. Biol. Chem. 270:27954.
  10. Le Gall, S.M. et al. (2003) J. Biol. Chem. 278:45255.
  11. Lakshmanan, J. et al. (1990) Biochem. Biophys. Res. Commun. 173:902.
  12. Pasquini, F. et al. (1974) Exp. Cell Res. 86:233.
  13. Pyka, J. et al. (2005) Cancer Res. 65:1343.

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Publications for EGF (4095-EG)(1)

We have publications tested in 1 confirmed species: Mouse.

We have publications tested in 1 application: Bioassay.

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Gene Symbol Egf