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Recombinant human EGF protein

QK011

Brand: Qkine

Human epidermal growth factor (EGF) protein is a potent EGF-family growth factor used in many human and mouse organoid and stem cell culture systems including intestinal and tumor organoid culture. EGF is also used in epithelial cell culture.

Qkine human EGF (Qk011) is a highly pure, animal origin-free, bioactive 6.3 kDa recombinant protein, making it ideal for use in chemically defined induced pluripotent stem cell (iPSC), embryonic stem cell (ESC) and organoid culture media.

Currency: 

Product name Catalog number Pack size Price Price (USD) Price (GBP) Price (EUR)
Recombinant human EGF protein, 100 µg QK011-0100 100 µg (select above) $ 80.00 £ 60.00 € 71.00
Recombinant human EGF protein, 500 µg QK011-0500 500 µg (select above) $ 195.00 £ 140.00 € 164.00
Recombinant human EGF protein, 1000 µg QK011-1000 1000 µg (select above) $ 260.00 £ 190.00 € 222.00

Note: prices shown do not include shipping and handling charges.

Qkine company name and logo are the property of Qkine Ltd. UK.

Alternative protein names
Epidermal growth factor, Pro-epidermal growth factor, HOMG4, Beta-urogastrone, Urogastrone (URG)
Species reactivity

Human

Species similarity:
Porcine – 85%
Mouse – 74%
Rat – 70%

Frequently used together with:

Summary

  • High purity human EGF protein (residues 971-1023, Uniprot: P01133)
  • >98%, by SDS-PAGE quantitative densitometry
  • 6.3 kDa
  • Expressed in E. coli
  • Animal origin-free (AOF) and carrier protein-free
  • Manufactured in Qkine's Cambridge, UK laboratories
  • Lyophilized from acetonitrile, TFA
  • Resuspend in 10 mM HCl at >100 µg/ml (provided with protein and free of charge), prepare single use aliquots, add carrier protein if desired and store frozen at -20°C or -80°C
Handling and Storage FAQ

Featured applications

  • Tumor organoid culture

Bioactivity

Human EGF Qk011 protein bioactivity lot #011

EGF activity is determined using the Promega serum response element luciferase reporter assay (*) in transfected HEK293T cells. Cells are treated in triplicate with a serial dilution of EGF for 3 hours. Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. EC50 = 11.6 pM (72.8 pg/mL). Data from Qk011 lot #10. *Promega pGL4.33[luc2P/SRE/Hygro] #E1340

Purity

Human EGF Qk011 protein purity SDS-PAGE lot #011

EGF protein migrates as a single band at ~12 kDa in non-reducing (NR) and 9 kDa in reducing (R) conditions. Purified recombinant protein (7 µg) was resolved using 15% w/v SDS-PAGE in reduced (+β-mercaptothanol, R) and non-reduced conditions (NR) and stained with Coomassie Brilliant Blue R250.  Data from Qk011 lot #011.

Further quality assays

  • Mass spectrometry: single species with expected mass
  • Endotoxin: <0.005 EU/μg protein (below level of detection)
  • Recovery from stock vial:  >95%

Qkine EGF is as biologically active as a comparable alternative supplier protein

Quantitative luciferase assay with Qkine EGF (Qk011, green) and alternative supplier EGF (Supplier B, black). Cells were treated in triplicate with a serial dilution of EGF for 3 hours. Firefly luciferase activity was measured and normalized to control Renilla luciferase activity. EC50s 0.11 ng/ml.

Qkine EGF remains stable and bioactive in conditioned media

Quantitative luciferase assay with Qkine EGF (Day 0, green) and (Day 2, black). Cells were treated in triplicate with a serial dilution of EGF for 3 hours after preincubation in conditioned media. Firefly luciferase activity was measured and normalized to control Renilla luciferase activity.

Protein background

Members of the human epidermal growth factor family are synthesized as type I transmembrane precursor proteins, often containing several EGF domains in the extracellular region. Proteolysis yields mature proteins that are released from the cell surface [1]. Epidermal growth factor binds to high-affinity EGF receptors (EGFRs) and promotes receptor dimerization and clustering leading to activation of downstream signaling pathways, including PI3K, ERK1/2, JAK/STAT, β-catenin, and calcium signaling [2].

Human epidermal growth factor (EGF) stimulates cell proliferation and differentiation. It is used extensively in induced-pluripotent stem cell (iPSC) and embryonic stem cell (ESC) culture systems for the successful expansion and differentiation of epithelial, neural, mesoderm and hematopoietic lineages [3]. EGF also stimulates the differentiation of mesenchymal stem cells (MSC) into bone-forming cells [4].

Recombinant EGF protein is a key component of many organoid media, along with other stem cell niche factors, R-Spondin 1, Noggin or Gremlin, Wnt3a and FGF10. In addition, recombinant EGF is used for establishing and maintaining intestine, stomach, liver, pancreas, brain and cancer organoids [5].

Background references

  1. R. C. Harris, E. Chung and R.J. Coffey. EGF receptor ligands. Experimental cell research 284, 2–13 (2003). doi.org/10.1093/nar/14.21.8427
  2. G. Carpenter and S. Cohen. Epidermal growth factor. Journal of biological chemistry 265, 7709–7712 (1990). doi.org/10.1016/S0021-9258(19)38983-5
  3. A. G. Efthymiou, G. Chen, M. Rao, G. Chen and M. Boehm, M. Self-renewal and cell lineage differentiation strategies in human embryonic stem cells and induced pluripotent stem cells. Expert Opinion on Biological Therapy, 14(9), 1333–1344 (2014). doi.org/10.1517/14712598.2014.922533
  4. I. Kratchmarova, B. Blagoev, M. Haack-Sorensen, M. Kassem and M. Mann. Mechanism of Divergent Growth Factor Effects in Mesenchymal Stem Cell Differentiation. Science 308,1472-1477 (2005). doi:10.1126/science.1107627
  5. H. E. Abud, W. H. Chan and T. Jardé. Source and Impact of the EGF Family of Ligands on Intestinal Stem Cells. Front Cell Dev Biol. 2021 Jul 19;9:685665. doi: 10.3389/fcell.2021.685665

Publications using recombinant human EGF protein (Qk011)

Generation of human iPSC-derived pancreatic organoids to study pancreas development and disease
bioRxiv preprint on 25 October 2024 by Darrigrand, J. et al.
View publication

Metabolic rewiring underpins human trophoblast induction.

Preprint on 18 March 2024 by Żylicz, J., van Nerum, K., Wenzel, A., Argemi Muntadas, L. et al.
View publication