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

Carrier Free

Catalog # Availability Size / Price Qty
4289-EG-025/CF

With Carrier

Catalog # Availability Size / Price Qty
4289-EG-025
R&D Systems Recombinant Proteins and Enzymes
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Recombinant Human Pro-EGF (aa 21-1023) Protein Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
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 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
Analysis
Ser21
Predicted Molecular Mass
112 kDa
SDS-PAGE
138-145 kDa, reducing conditions

Product Datasheets

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4289-EG (with carrier)

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4289-EG/CF (carrier free)

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

4289-EG

Formulation Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

4289-EG/CF

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: EGF

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).

References
  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.
Long Name
Epidermal Growth Factor
Entrez Gene IDs
1950 (Human); 13645 (Mouse); 25313 (Rat)
Alternate Names
beta-urogastrone; EGF; epidermal growth factor (beta-urogastrone); epidermal growth factor; hEGF; HOMG4; pro-epidermal growth factor; URG; Urogastrone

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

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

1 Citation: Showing 1 - 1

  1. SMOC Binds to Pro-EGF, but Does Not Induce Erk Phosphorylation via the EGFR
    Authors: JT Thomas, L Chhuy-Hy, KR Andrykovic, M Moos
    PLoS ONE, 2016-04-21;11(4):e0154294.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Enzyme Assay

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