Recombinant Human Pro-EGF (aa 21-1023) Protein

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human Pro-EGF (aa 21-1023) 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.
Source
Mouse myeloma cell line, NS0-derived human EGF protein
Met1-Arg1023, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Ser21
Protein/Peptide Type
Recombinant Proteins
Gene
EGF
Purity
>90%, 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.

Applications/Dilutions

Theoretical MW
112 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.
SDS-PAGE
138-145 kDa, reducing conditions
Publications
Read Publication using
4289-EG in the following applications:

Packaging, Storage & Formulations

Storage
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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.

Notes

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

Alternate Names for Recombinant Human Pro-EGF (aa 21-1023) Protein

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

Background

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 human Pro-EGF contains nine LDL R class B repeats and nine EGF-like domains (4). Within this region, human Pro-EGF shares 69% amino acid sequence identity with mouse and rat Pro-EGF and 82% with canine, feline, and porcine Pro-EGF. Mature epidermal growth factor 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 160 kDa preproprotein is shed 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 EGF R 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).

  1. Singh, A.B. and R.C. Harris (2005) Cell. Signal. 17:1183.
  2. Wouters, M.A. et al. (2005) Protein Sci. 14:1091.
  3. Sanderson, M.P. et al. (2006) Growth Factors 24:121.
  4. Bell, G.I. et al. (1986) Nucleic Acids Res. 14:8427. 
  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 (4289-EG)(1)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: Enzyme Assay.


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Bioinformatics

Gene Symbol EGF
Uniprot