Skip to main content

Novus Biologicals products are now on bio-techne.com

Better as one

Recombinant Human EGF Protein, CF Best Seller

Bio-Techne includes R&D Systems | Catalog # 236-EG

Catalog #
Availability
Size / Price
Qty
Loading...
236-EG-01M
236-EG-200

Key Product Details

Source

E. coli

Accession #

Conjugate

Unconjugated

Applications

Bioactivity

Product Specifications

Source

E. coli-derived human EGF protein
Asn971-Arg1023, with an N-terminal Met

Purity

>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met

Predicted Molecular Mass

6 kDa

SDS-PAGE

6 kDa, reducing conditions

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 20-100 pg/mL.

Scientific Data Images for Recombinant Human EGF Protein, CF

Recombinant Human EGF Protein SEC-MALS.

Recombinant Human EGF Protein (Catalog # 236-EG) has a molecular weight (MW) of 6.7 kDa as analyzed by SEC-MALS, suggesting that this protein is a monomer.
Recombinant Human EGF Protein Bioactivity

Recombinant Human EGF Protein Bioactivity

Recombinant Human EGF (Catalog # 236‑EG) stimulates cell proliferation of the Balb/3T3 mouse embryonic fibroblast cell line. The ED50 for this effect is 20‑100 pg/mL.
Recombinant Human EGF Protein SDS-PAGE

Recombinant Human EGF Protein SDS-PAGE

1 µg/lane of Recombinant Human EGF was resolved with SDS-PAGE and visualized by silver staining under reducing (R) conditions, showing a single band at 6 kDa.

Formulation, Preparation and Storage

236-EG
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 500 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. 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.

Background: EGF

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.

References

  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. Bell, G.I. et al. (1986) Nucl. Acids Res. 14:8427.
  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.

Long Name

Epidermal Growth Factor

Alternate Names

HOMG4, URG, Urogastrone

Entrez Gene IDs

1950 (Human); 13645 (Mouse); 25313 (Rat)

Gene Symbol

EGF

UniProt

Additional EGF Products

Product Documents for Recombinant Human EGF Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human EGF Protein, CF

For research use only

Citations for Recombinant Human EGF Protein, CF (775)

Showing  1 - 10 of 775 publications Showing All
Filter By:
Search Title:

Citations are publications that use Bio-Techne products. Selected citations for Recombinant Human EGF Protein, CF include: