An ophthalmic formulation of epidermal growth factor (urogastrone) has been launched
for stimulation of healing of the corneal epithelium following various corneal diseases.
Endotoxin < 0.1 ng per μg (1EU/ug) of EGF
This product is used as a mitogen, triggering the cell to commence mitosis, in a variety of cell lines. In tissue cultures, EGF acts to reduce or eliminate the requirement for serum and can be used in conjunction with other media additives and hormones.
EGF (epidermal growth factor) human has been used in the culture medium for the maintenance of MCF10A cells (human mammary epithelial cells).
Epidermal Growth Factor, human, animal component free has been used:
- as a supplement in in LHC-8 medium to culture liver cell lines
- in the fetal bovine serum (FBS)-Dulbecco′s modified essential medium (DMEM) /F12 medium for primary culture of human glioma cells
- as an additive in the conditional medium of normal fibroblasts (NFs) to study its effect on the migration and invasion of endometrial cancer (EC) cells
- as a component in tumorsphere medium
Epidermal Growth Factor (EGF) is a human protein that is involved in the regulation of cell growth, differentiation and survival. Recombinant EGF is an antigen binding molecule that can be used as a cancer treatment. Recombinant EGF has been shown to stimulate cellular transformation by binding to the epidermal growth factor receptor. It also has been shown to inhibit the growth of breast cancer cells with the HER2 gene mutation. The molecular weight of rec EGF is approximately 25 kDa and is composed of 165 amino acids. Recombinant EGF can be used in immunoassays, as a model system for studying biological properties, or as an antibody production tool.
Epidermal Growth Factor (EGF) is a small mitogenic polypeptide (～6 kDa), which is present in many mammalian species and is distributed throughout a wide number of tissues and body fluids. Human EGF is identical to β-urogastrone, a polypeptide which was recognized and isolated on the basis of its ability to inhibit gastric acid secretion. EGF is a member of a growth factor family, which is characterized by the presence of 6 conserved cysteine motifs that form three disulfide bonds. The location of 3 intrachain disulfide bonds in recombinant human EGF is identical to that of mouse EGF. EGF is homologous to a sequence contained in a 19 kDa protein of vaccinia virus, which appears to utilize the EGF receptor to gain entry into cell EGF is mitogenic for a variety of epidermal and epithelial cells, including fibroblasts, glial cells, mammary epithelial cells, vascular and corneal endothelial cells, bovine granulosa, rabbit chondrocytes, HeLa cells, and SV40-3T3 cells.
Epidermal growth factor (EGF) helps to induce cell growth, proliferation and differentiation. It participates in the repairing of renal tissues in the kidney. It promotes the reabsorption of magnesium with the help of the transient receptor potential cation channel 6 (TRMP6). EGF is known to participate in the pathophysiology of drug-induced renal magnesium loss.
Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6.2kDa. The EGF is purified by proprietary chromatographic techniques.
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
