Recombinant Human Pro-EGF (aa 21-1023) Protein Summary
Product Specifications
Met1-Arg1023, with a C-terminal 6-His tag
Analysis
Product Datasheets
4289-EG (with carrier)
4289-EG/CF (carrier free)
Carrier Free
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.
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.
|
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.
|
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).
- Singh, A.B. and R.C. Harris (2005) Cell. Signal. 17:1183.
- Wouters, M.A. et al. (2005) Protein Sci. 14:1091.
- Sanderson, M.P. et al. (2006) Growth Factors 24:121.
- Bell, G.I. et al. (1986) Nucleic Acids Res. 14:8427.
- Jorissen, R.N. et al. (2003) Exp. Cell Res. 284:31.
- Rall, L.B. et al. (1985) Nature 313:228.
- Le Gall, S.M. et al. (2004) Regul. Pept. 122:119.
- Breyer, J.A. and S. Cohen (1990) J. Biol. Chem. 265:16564.
- Parries, G. et al. (1995) J. Biol. Chem. 270:27954.
- Le Gall, S.M. et al. (2003) J. Biol. Chem. 278:45255.
- Lakshmanan, J. et al. (1990) Biochem. Biophys. Res. Commun. 173:902.
- Pasquini, F. et al. (1974) Exp. Cell Res. 86:233.
- Pyka, J. et al. (2005) Cancer Res. 65:1343.
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
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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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