Recombinant Human EGF, Animal-Free Protein

Catalog #: AFL236
4 Citations Datasheet / COA / SDS

Intended for preclinical researchers who may transition to GMP EGF for their clinical work

Catalog #	Availability	Size / Price	Qty
AFL236
AFL236-200

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R&D Systems Animal-Free Recombinant Proteins

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Citations (4)

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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human EGF, Animal-Free Protein Summary

Learn more about Animal-Free Recombinant Proteins

Animal Free Proteins
Animal-free proteins are particularly important for researchers concerned with experimental variables caused by trace animal components or mammalian pathogens. Our products generated under animal-free conditions share the same biological activities as those produced using our standard laboratory techniques.

Product Specifications

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.

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.
The specific activity of Recombinant Human EGF is >8.0 x 10⁵ IU/mg, which is calibrated against the human EGF WHO International Standard (NIBSC code: 91/530).

Source

E. coli-derived human EGF protein
Asn971-Arg1023, with an N-terminal Met
Produced using non-animal reagents in an animal-free laboratory.

Accession #

P01133

N-terminal Sequence
Analysis

Met

Predicted Molecular Mass

6 kDa

Product Datasheets

AFL236

Product Datasheet

COA

SDS

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.

AFL236

Formulation	Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution	Reconstitute at 200 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.

Reconstitution Calculator

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

Harris, R.C. et al. (2003) Exp. Cell Res. 284:2.
Carpenter, G. and Cohen, S. (1990) J. Biol. Chem. 265:7709.
Bell, G.I. et al. (1986) Nucl. Acids Res. 14:8427.
Carpenter, G. and Zendegui, J.G. (1986) Exp. Cell Res. 164:1.
Jorissen, R.N. et al. (2003) Exp. Cell Res. 284:31.
Gamett, D.C. et al. (1997) J. Biol. Chem. 272:12052.
Qian, X. et al. (1994) Proc. Natl. Acad. Sci. 91:1500.
Qian, X. et al. (1999) J. Biol. Chem. 274:574.

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

Manufacturing Specifications

Animal-Free Manufacturing Conditions
Our dedicated controlled-access animal-free laboratories ensure that at no point in production are the products exposed to potential contamination by animal components or byproducts. Every stage of manufacturing is conducted in compliance with R&D Systems' stringent Standard Operating Procedures (SOPs). Production and purification procedures use equipment and media that are confirmed animal-free.

Production

All molecular biology procedures use animal-free media and dedicated labware.
Dedicated fermentors are utilized in committed animal-free areas.

Purification

Protein purification columns are animal-free.
Bulk proteins are filtered using animal-free filters.
Purified proteins are stored in animal-free containers in a dedicated cold storage room.

Quality Assurance

Low Endotoxin Level.
No impairment of biological activity.
High quality product obtained under stringent conditions.
For ex vivo research or bioproduction, additional documentation can be provided.

Please read our complete Animal-Free Statement

Related Research Areas

Citations for Recombinant Human EGF, Animal-Free 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.

4 Citations: Showing 1 - 4
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Mutations in ALK signaling pathways conferring resistance to ALK inhibitor treatment lead to collateral vulnerabilities in neuroblastoma cells
Authors: M Berlak, E Tucker, M Dorel, A Winkler, A McGearey, E Rodriguez-, BM da Costa, K Barker, E Fyle, E Calton, S Eising, K Ober, D Hughes, E Koutrouman, P Carter, R Stankunait, P Proszek, N Jain, C Rosswog, H Dorado-Gar, JJ Molenaar, M Hubank, G Barone, J Anderson, P Lang, HE Deubzer, A Künkele, M Fischer, A Eggert, C Kloft, AG Henssen, M Boettcher, F Hertwig, N Blüthgen, L Chesler, JH Schulte
Molecular Cancer, 2022-06-10;21(1):126.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
Patient-derived micro-organospheres enable clinical precision oncology
Authors: S Ding, C Hsu, Z Wang, NR Natesh, R Millen, M Negrete, N Giroux, GO Rivera, A Dohlman, S Bose, T Rotstein, K Spiller, A Yeung, Z Sun, C Jiang, R Xi, B Wilkin, PM Randon, I Williamson, DA Nelson, D Delubac, S Oh, G Rupprecht, J Isaacs, J Jia, C Chen, JP Shen, S Kopetz, S McCall, A Smith, N Gjorevski, AC Walz, S Antonia, E Marrer-Ber, H Clevers, D Hsu, X Shen
Cell Stem Cell, 2022-05-03;0(0):.
Species: Human
Sample Types: Whole Tissue
Applications: Cell Culture
Evaluation of active Rac1 levels in cancer cells: a case of misleading conclusions from immunofluorescence analysis
Authors: MJ Baker, M Cooke, G Kreider-Le, R Garcia-Mat, PA Janmey, MG Kazanietz
J. Biol. Chem., 2020-08-14;0(0):.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay, Cell Culture
FBXL14 abolishes breast cancer progression by targeting CDCP1 for proteasomal degradation
Authors: YH Cui, H Kim, M Lee, JM Yi, RK Kim, N Uddin, KC Yoo, JH Kang, MY Choi, HJ Cha, OS Kwon, IH Bae, MJ Kim, N Kaushik, SJ Lee
Oncogene, 2018-07-04;0(0):.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay