Recombinant human epidermal growth factor is 6.2kDa globular protein comprosed of 53 amino acids. EGF is a polypeptide growth factor which stimulates the proliferation of a wide range of epidermal and epithelial cells.
- Target Species
- Species Cross-Reactivity
|Target Species||Cross Reactivity|
- N.B. Antibody reactivity and working conditions may vary between species.
- Product Form
- Purified recombinant protein - lyophilized
- Reconstitute with 0.5ml distilled water
Care should be taken during reconstitution as the protein may appear as a film at the bottom of the vial. Bio-Rad recommend that the vial is gently mixed after reconstitution. For extended storage, the addition of 5% trehalose is recommended
- Purified recombinant human EGF expressed in E. coli
- Preservative Stabilisers
- None present
- Carrier Free
- 1 x 107 units/mg
- >98% by SDS PAGE and HPLC analysis
- Approx. Protein Concentrations
- 1.0 mg/ml after reconstitution.
- Protein Molecular Weight
- 6.2 kD (53 Amino acid sequence)
- Endotoxin Level
- < 0.1 ng/ug
- Prior to reconstitution store at -20oC. Following reconstitution store at -20oC if preferred.
This product should be stored undiluted.
Storage in frost free freezers is not recommended. Avoid repeated freezing and thawing as this may denature the protein. Should this product contain a precipitate we recommend microcentrifugation before use.
- Guaranteed for 3 months from the date of reconstitution or until the date of expiry, whichever comes first. Please see label for expiry date.
- Entrez Gene
- GO Terms
calcium ion binding
integral to membrane
epidermal growth factor receptor binding
transmembrane receptor protein tyrosine kinase activator activity
positive regulation of epidermal growth factor receptor activity
epidermal growth factor receptor signaling pathway
growth factor activity
platelet alpha granule lumen
positive regulation of catenin import into nucleus
negative regulation of epidermal growth factor receptor signaling pathway
positive regulation of MAP kinase activity
positive regulation of mitosis
negative regulation of secretion
regulation of calcium ion import
regulation of protein localization at cell surface
- For research purposes only
This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit the antibody protocols page.
Where this protein has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the protein for use in their own system using appropriate postive/negative controls.
- Recombinant human EGF may be used as athe standard in ELISA applications with either a purified human EGF antibody (AHP767) or a biotinylated human EGF antibody (AHP767B).
- Western Blotting
- Recombinant human EGF may be used as the positive control for Wester Blotting application with either a purified human EGF antibody (AHP767) or a biotinylated human EGF antibody (AHP767B)
Copyright © 2021 Bio-Rad Antibodies (formerly AbD Serotec)
Product Specific References
References for EGF
Tomlins, C. & Storey, A. (2010) Cutaneous HPV5 E6 causes increased expression of Osteoprotegerin and Interleukin 6 which contribute to evasion of UV-induced apoptosis.
Carcinogenesis. 31 (12): 2155-64.
Wray, H. et al. (2012) α6 Integrin and CD44 enrich for a primary keratinocyte population that displays resistance to UV-induced apoptosis.
PLoS One. 7 (10): e46968.
Chen, W. et al. (2016) Tissue Kallikrein Inhibitors Based on the Sunflower Trypsin Inhibitor Scaffold - A Potential Therapeutic Intervention for Skin Diseases.
PLoS One. 11 (11): e0166268.
Zhang, X. et al. (2015) Wnt signaling regulates the stemness of lung cancer stem cells and its inhibitors exert anticancer effect on lung cancer SPC-A1 cells.
Med Oncol. 32 (4): 95.
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