Product Type |
Recombinant Proteins |
Derivation |
Mouse EGF, 53 amino acids Asn977-Arg1029 (Accession# NP_034243) was expressed in E. coli. |
Purity |
>98%, as determined by Coomassie stained SDS-PAGE. |
Formulation |
0.22 µm filtered protein solution is in PBS. |
Concentration |
10-100 µg sizes are bottled at 200 µg/mL. 500 µg and larger sizes are bottled at the concentration indicated on the vial. |
Activity |
The ED50 is 1-2 ng/ml, corresponding to a specific activity 5x105 - 1x106 units/mg, as determined by a dose-dependent inhibition on A431 cells proliferation. |
Function |
EGF is a potent mitogen for many cells in culture, and in vivo, it induces the proliferation and differentiation of skin, cornea, lung, and trachea, among other tissues. Processing of pro EGF to mature EGF in different tissues is not equally efficient. The precursor is processed to mature EGF in the submaxillary gland, pancreas, small intestine, and mammary gland. In the submaxillary gland, EGF is fully processed, stored at secretory granules, and secreted in saliva. In kidney, EGF is present in unprocessed or intermediated forms on the cell surface. |
Applications |
Bioassay |
Application References |
1. Henson ES and Gibson SB. 2006. Cell Signal. 18:2089. 2. Burgess AW, et al. 2003. Mol. Cell. 12:541. 3. Imai Y, et al. 1982. Cancer Res. 42:4394. 4. Barnes DW. 1982. J. Cell. Biol. 93:1. 5. Heo JS, et al. 2006. Am. J. Physiol. Cell. Physiol. 290:C123. |
Description |
Epidermal growth factor (EGF) is a small 6 kD polypeptide and has six conserved cysteine residues that form three intramolecular disulfide bonds. Human and mouse EGF share 70% homology in amino acid structure. Mouse EGF is synthesized as a transmembrane precursor protein (1217 amino acids) which is proteolytically cleaved to generate the 53 amino acid mature EGF. Many different cells including mammary gland cells, macrophages, gut epithelial cells, and cells in the nervous system and the kidney can produce EGF. EGF plays important roles in the regulation of cell survival, proliferation, and differentiation by binding to its receptor EGFR. For example, EGF can stimulate the proliferation of mouse embryonic stem cells or induce the terminal differentiation/growth inhibition of A431 cells. The binding of EGF to EGFR will induce receptor dimerization, which is required for activating the tyrosine kinase in the receptor cytoplasmic domain. In addition, the binding of EGF to its receptor triggers several signal transduction pathways including JAK/STAT, Ras/ERK and PI3K/AKT pathways. Blocking of the EGF/EGFR pathway can suppress some tumor cell's proliferation. Other members of the EGF family (including transforming growth factor-α (TGF-α), heparin-binding EGF-like growth factor (HB-EGF), amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), and epigen) also bind to EGFR. |
Storage |
Unopened vial can be stored at 4°C for three months, at -20°C for six months, or at -70°C for one year. For maximum results, quick spin vial prior to opening. Stock solutions should be prepared at no less than 10 µg/mL in sterile buffer (PBS, HPBS, DPBS, and EBSS) containing carrier protein such as 1% BSA or HSA. After dilution, the cytokine can be stored at 4°C for one month or from -20°C to -70°C for up to 3 months. Avoid repeated freeze/thaw cycles. |