Recombinant Human EGF Protein, CF

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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 (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.
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.
iPSC-derived human intestinal organoids were cultured using Cultrex™ UltiMatrix RGF Basement Membrane Extract (BME001-05) and intestinal organoid culture medium, which includes Recombinant Human EGF (Catalog # ...read more
Adult stem cells isolated from human descending colon were embedded in Cultrex UltiMatrix RGF Basement Membrane Extract (BME001-05) and cultured for 30 days in intestinal organoid culture medium, which includes ...read more
D3 mouse embryonic stem cells were expanded in KO-ES Media supplemented with Bovine Fibronectin Protein (1030-FN) to support cell attachment and spreading, the ITS and N-2 Plus Media Supplements (AR013 and AR003), and a ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

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Catalog# & Formulation Size Price

Recombinant Human EGF Protein, CF Summary

Additional Information
Analyzed by SEC-MALS
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 20-100 pg/mL.
Source
E. coli-derived human EGF protein
Asn971-Arg1023, with an N-terminal Met
Accession #
N-terminal Sequence
Met
Protein/Peptide Type
Recombinant Proteins
Gene
EGF
Purity
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
6 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
6 kDa, reducing conditions
Publications
Read Publications using
236-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.
Purity
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Human EGF Protein, CF

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

Background

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.

  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.

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Publications for EGF (236-EG)(872)

We have publications tested in 17 confirmed species: Human, Mouse, Rat, Bovine, Canine, Chicken, Equine, Feline, N/A, Porcine, Primate, Primate - Macaca fascicularis (Crab-eating Monkey or Cynomolgus Macaque), Rabbit, Transgenic Mouse, Xenograft, Zebrafish,  Human.

We have publications tested in 9 applications: Bioassay, Cell Culture, Differentiation, In Vivo, Organoid Culture, Spheroid Culture, Stimulation, Surface Plasmon Resonance (SPR), Tissue Culture.


Filter By Application
Bioassay
(769)
Cell Culture
(81)
Differentiation
(7)
In Vivo
(10)
Organoid Culture
(1)
Spheroid Culture
(1)
Stimulation
(1)
Surface Plasmon Resonance (SPR)
(1)
Tissue Culture
(2)
All Applications
Filter By Species
Human
(773)
Mouse
(68)
Rat
(8)
Bovine
(2)
Canine
(3)
Chicken
(3)
Equine
(1)
Feline
(2)
N/A
(1)
Porcine
(6)
Primate
(1)
Primate - Macaca fascicularis (Crab-eating Monkey or Cynomolgus Macaque)
(1)
Rabbit
(1)
Transgenic Mouse
(6)
Xenograft
(5)
Zebrafish
(1)
 Human
(1)
All Species
Showing Publications 1 - 10 of 872. Show All 872 Publications.
Publications using 236-EG Applications Species
Goswami, Y;Baghel, A;Sharma, G;Sharma, PK;Biswas, S;Yadav, R;Garg, PK;Shalimar, ;Tandon, R; Liver Organoids From Hepatocytes of Healthy Humans and Non-alcoholic Fatty Liver Disease (NAFLD) Patients Display Multilineage Architecture and can be Used to Develop an In Vitro Model of Steatohepatitis Journal of clinical and experimental hepatology 2024-12-03 [PMID: 39872219] (Bioassay, Human) Bioassay Human
Lee, SM;Smela, MP;Surani, MA; The role of KLF4 in human primordial germ cell development Open biology 2025-01-01 [PMID: 39837498] (Bioassay, Human) Bioassay Human
Ruffilli, C;Röth, S;Zelcer, N;Moreau, K; Orthogonal validation of PROTAC mediated degradation of the integral membrane proteins EGFR and c-MET Scientific reports 2025-01-02 [PMID: 39748066] (Bioassay, Human) Bioassay Human
Tang, M;Dirks, K;Kim, SY;Qiu, Z;Gao, Y;Sun, D;Peruggia, G;Sallavanti, J;Li, W; Inhibition of thioredoxin reductase 1 sensitizes glucose-starved glioblastoma cells to disulfidptosis Cell death and differentiation 2024-12-23 [PMID: 39715824] (Bioassay, Human) Bioassay Human
Stefanski, KM;Huang, H;Luu, DD;Hutchison, JM;Saksena, N;Fisch, AJ;Hasaka, TP;Bauer, JA;Kenworthy, AK;Van Horn, WD;Sanders, CR; Small-Molecule Modulators of Lipid Raft Stability and Protein-Raft Partitioning bioRxiv : the preprint server for biology 2024-12-11 [PMID: 39713458] (Bioassay, Human) Bioassay Human
Hammond, T;Choi, JB;Membreño, MW;Demeter, J;Ng, R;Bhattacharya, D;Nguyen, TN;Hartmann, GG;Bossard, C;Skotheim, JM;Jackson, PK;Pasca, A;Rubin, SM;Sage, J; THE FAM53C/DYRK1A axis regulates the G1/S transition of the cell cycle bioRxiv : the preprint server for biology 2024-12-11 [PMID: 39713326] (Bioassay, Human) Bioassay Human
Harel, K;Czamanski-Cohen, J;Cohen, M;Lane, RD;Dines, M;Caspi, O;Weihs, KL; Differences in Emotional Awareness Moderate Cytokine-Symptom Associations Among Breast Cancer Survivors Brain, behavior, and immunity 2024-12-12 [PMID: 39674559] (Bioassay, Human) Bioassay Human
Zhao, C;Inada, Y;Motoike, S;Kamiya, D;Hino, K;Ikeya, M; BMP-9 mediates fibroproliferation in fibrodysplasia ossificans progressiva through TGF-? signaling EMBO molecular medicine 2024-12-03 [PMID: 39627568] (Bioassay, Human) Bioassay Human
Ounadjela, JR;Zhang, K;Kobayashi-Kirschvink, KJ;Jin, K;J C Russell, A;Lackner, AI;Callahan, C;Viggiani, F;Dey, KK;Jagadeesh, K;Maxian, T;Prandstetter, AM;Nadaf, N;Gong, Q;Raichur, R;Zvezdov, ML;Hui, M;Simpson, M;Liu, X;Min, W;Knöfler, M;Chen, F;Haider, S;Shu, J; Spatial multiomic landscape of the human placenta at molecular resolution Nature medicine 2024-11-20 [PMID: 39567716] (Bioassay, Human) Bioassay Human
He, C;Chen, Y;Zhang, X;Feng, H;Rao, Y;Ji, T;Wang, W; Down-regulation of ESRP2 inhibits breast cancer cell proliferation via inhibiting cyclinD1 Scientific reports 2024-11-18 [PMID: 39557898] (Bioassay, Human) Bioassay Human
Show All 872 Publications.

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Bioinformatics

Gene Symbol EGF
Uniprot