*Optimal dilutions/concentrations should be determined by the researcher.
Not tested in other applications.
recombinant human EGF
Specifically reacts with both native and recombinant human EGF. The antibody does not cross-react with mouse EGF.
0.01M PBS pH7.4
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
recombinant human EGF
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Epidermal Growth Factor,Homg4,Urg,Egf
Epidermal growth factor (EGF) is a single chain poly-peptide hormone (6 kDa) which was first isolated from the submandibular gland of the mouse and is a potent growth-promoting factor for a variety of tissue cells in vivo and in vitro. Human EGF (hEGF) has also been extracted from human urine and shown to be identical or closely related to -urogastrone, a potent inhibitor of gastric acid secretion. Human EGF is structurally homologous to human transforming growth factor-alpha (TGF-Alpha) which also exerts its actions through EGF receptors. It 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 cells. Cloning data for mouse and human EGF suggest that the 53 amino-acid EGF peptide is cleaved from a 125-130 kDa, 1217 amino-acid precursor containing an N-terminal 29 amino-acid signal sequence. Mouse and human EGF exhibit 70% similarity at the amino acid level and are highly species cross-reactive. Structures obtained for both mouse and human EGF suggest that the protein exists largely in a beta sheet conformation, with a C-terminal hairpin that may be involved in receptor binding. EGF acts through a specific cell surface receptor glycoprotein of approximately 170 kDa. EGF binding induces phosphatidylinositide hydrolysis and generation of diacylglycerol (DAG). DAG-dependent activation of protein kinase C, in turn, results in the phosphorylation of a threonine residue at position 654 of the receptor, in attenuation of the intrinsic tyrosine kinase activity, and subsequently alterations of receptor homeostasis. Cellular metabolic effects of EGF include stimulation of ion fluxes, glucose transport, glycolysis and synthesis of DNA, RNA and proteins. EGF acts on a variety of tissues and binding has been demonstrated in virtually all cell types tested, with the exception of those of the hematopoietic lineage. 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 and SV40-3T3 cells. Human EGF is found in body fluids such as urine, milk, saliva, sweat, and seminal fluid and has its highest concentration in alpha granules of blood platelets. It has a widespread distribution in human tissues and organs, including neoplasms. The biological role of EGF includes the inhibition of gastric acid secretion, support of growth and differentiation during fetal development, neuromodulation in the central nervous system and stimulation of epidermal growth and keratinization. Since EGF plays a role in the proliferation and/ or differentiation of normal as well as tumor cells derived from a variety of tissues, 5 and can contribute to pathological states, an in vitro assay for its detection and quantification is desirable. Monoclonal antibody reacting specifically with EGF may be used in the determination and quantification of the molecule in many in vitro systems and in vivo human models, and for studies on structure-function relationship of this factor in binding to the receptor molecule.